ID 3MGA_HAEIN Reviewed; 185 AA. AC P44321; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=DNA-3-methyladenine glycosylase; DE EC=3.2.2.20; DE AltName: Full=3-methyladenine-DNA glycosidase; DE Short=TAG; GN Name=tag; OrderedLocusNames=HI_0654; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine from the damaged DNA polymer formed by CC alkylation lesions. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22313.1; -; Genomic_DNA. DR PIR; G64084; G64084. DR RefSeq; NP_438814.1; NC_000907.1. DR RefSeq; WP_005694489.1; NC_000907.1. DR PDB; 1V1N; Model; -; A=1-185. DR PDBsum; 1V1N; -. DR ProteinModelPortal; P44321; -. DR SMR; P44321; 4-182. DR STRING; 71421.HI0654; -. DR EnsemblBacteria; AAC22313; AAC22313; HI_0654. DR GeneID; 949931; -. DR KEGG; hin:HI0654; -. DR PATRIC; 20189923; VBIHaeInf48452_0683. DR eggNOG; ENOG4108R3E; Bacteria. DR eggNOG; COG2818; LUCA. DR KO; K01246; -. DR OMA; YVAYHDT; -. DR OrthoDB; EOG661HDB; -. DR PhylomeDB; P44321; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.340.30; -; 1. DR InterPro; IPR005019; Adenine_glyco. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004597; Tag. DR Pfam; PF03352; Adenine_glyco; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR TIGRFAMs; TIGR00624; tag; 1. PE 3: Inferred from homology; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Hydrolase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 185 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000194879. FT METAL 5 5 Zinc. {ECO:0000250}. FT METAL 19 19 Zinc. {ECO:0000250}. FT METAL 176 176 Zinc. {ECO:0000250}. FT METAL 180 180 Zinc. {ECO:0000250}. SQ SEQUENCE 185 AA; 21193 MW; 03AC41B636BD4321 CRC64; MTTRCPWVGE QSIYIDYHDK EWGKPEFDSQ KLFEKICLEG QQAGLSWITV LKKRESYREA FHQFDPKKIA KMTALDIDAC MQNSGLIRHR AKLEAIVKNA KAYLAMEKCG ENFSDFIWSF VNHKPIVNDV PDLRSVPTKT EVSKALSKAL KKRGFVFIGE TTCYAFMQSM GLVDDHLNDC PCKTS // ID 3PASE_HAEIN Reviewed; 352 AA. AC P45267; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Inorganic triphosphatase; DE Short=PPPase; DE EC=3.6.1.25; GN OrderedLocusNames=HI_1598; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the hydrolysis of the beta-gamma- CC phosphoanhydride linkage of triphosphate-containing substrates CC (inorganic or nucleoside-linked). Catalyzes the hydrolysis of CC inorganic triphosphate (PPPi), which could be cytotoxic because of CC its high affinity for calcium ion, thereby interfering with CC calcium signaling (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Triphosphate + H(2)O = diphosphate + CC phosphate. CC -!- SIMILARITY: Contains 1 CYTH domain. {ECO:0000255|PROSITE- CC ProRule:PRU01044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23243.1; -; Genomic_DNA. DR PIR; H64172; H64172. DR RefSeq; NP_439740.1; NC_000907.1. DR RefSeq; WP_005693613.1; NC_000907.1. DR STRING; 71421.HI1598; -. DR DNASU; 950454; -. DR EnsemblBacteria; AAC23243; AAC23243; HI_1598. DR GeneID; 950454; -. DR KEGG; hin:HI1598; -. DR PATRIC; 20191927; VBIHaeInf48452_1671. DR eggNOG; ENOG4105I7R; Bacteria. DR eggNOG; COG3025; LUCA. DR OMA; GAFFNLY; -. DR OrthoDB; EOG60PHBT; -. DR PhylomeDB; P45267; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050355; F:triphosphatase activity; ISS:UniProtKB. DR GO; GO:0008152; P:metabolic process; ISS:UniProtKB. DR Gene3D; 2.40.320.10; -; 1. DR InterPro; IPR033469; CYTH-like_dom. DR InterPro; IPR023577; CYTH_domain. DR Pfam; PF01928; CYTH; 1. DR SMART; SM01118; CYTH; 1. DR SUPFAM; SSF55154; SSF55154; 1. DR PROSITE; PS51707; CYTH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 352 Inorganic triphosphatase. FT /FTId=PRO_0000169407. FT DOMAIN 6 203 CYTH. {ECO:0000255|PROSITE- FT ProRule:PRU01044}. SQ SEQUENCE 352 AA; 41315 MW; E23487A3B0702316 CRC64; MENIMLQEIE LKLAISPQIG IELPQYLAKF TILEHQNLFL GNTYYDYPDH FLAKQKMGLR IRQEDQELTL TLKTNGKVVS GLHSRPEYNL PLIEKETPTN AQLRGLYPFE QLPSSTLQPI FSTDFNRTFW LVEFQQSKIE VAFDQGKIIA GEYEQPISEI EFELKSGNVQ DLFDFVETLP FERDIYFSSA SKAKRGYLLG SKQFLTDWLN KWRDFLKEER EESAVDFCAK FNAVLKMEQK LLEETLSFSP TLFSQDFMKT VERVGAFFNL YHYYDENGKI LEAMATEKQK ETRLPALLES NQKIFVEIRD LIRFHSETKD NEKTIEKLTA LLKSRVYFER MIKLMELSYD LG // ID 5NTD_HAEIN Reviewed; 603 AA. AC P44569; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=NAD 5'-nucleotidase; DE Short=NadN; DE EC=3.1.3.5; DE Flags: Precursor; GN OrderedLocusNames=HI_0206; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 26-38. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-603, FUNCTION, SUBSTRATE RP SPECIFICITY, COFACTOR, SUBSTRATE-BINDING SITES, ZINC-BINDING SITES, RP AND SUBCELLULAR LOCATION. RX PubMed=21933152; DOI=10.1042/BJ20111263; RA Garavaglia S., Bruzzone S., Cassani C., Canella L., Allegrone G., RA Sturla L., Mannino E., Millo E., De Flora A., Rizzi M.; RT "The high-resolution crystal structure of periplasmic Haemophilus RT influenzae NAD nucleotidase reveals a novel enzymatic function of RT human CD73 related to NAD metabolism."; RL Biochem. J. 441:131-141(2012). CC -!- FUNCTION: Degrades NAD into adenosine and nicotinamide riboside, CC the latter being subsequently internalized by a specific permease. CC Also endowed with NAD(P) pyrophosphatase activity. Exhibits a CC broad substrate specificity, recognizing either mono- or CC dinucleotide nicotinamides and different adenosine phosphates with CC a maximal activity on 5'-adenosine monophosphate. CC {ECO:0000269|PubMed:21933152}. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:21933152}; CC Note=Binds 2 Zn(2+) ions per subunit. CC {ECO:0000269|PubMed:21933152}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:21933152}. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase 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; L42023; AAC21874.1; -; Genomic_DNA. DR PIR; E64054; E64054. DR RefSeq; NP_438375.1; NC_000907.1. DR RefSeq; WP_010868956.1; NC_000907.1. DR PDB; 3ZTV; X-ray; 1.30 A; A=25-603. DR PDB; 3ZU0; X-ray; 2.00 A; A/B=25-603. DR PDBsum; 3ZTV; -. DR PDBsum; 3ZU0; -. DR ProteinModelPortal; P44569; -. DR STRING; 71421.HI0206; -. DR EnsemblBacteria; AAC21874; AAC21874; HI_0206. DR GeneID; 951116; -. DR KEGG; hin:HI0206; -. DR PATRIC; 20188909; VBIHaeInf48452_0211. DR eggNOG; ENOG4105CGH; Bacteria. DR eggNOG; COG0737; LUCA. DR KO; K01081; -. DR OMA; WAVIFVL; -. DR OrthoDB; EOG62RS7N; -. DR PhylomeDB; P44569; -. DR BioCyc; MetaCyc:MONOMER-8341; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase 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:0009166; P:nucleotide catabolic process; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.90.780.10; -; 1. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_CS. DR InterPro; IPR006179; 5_nucleotidase/apyrase. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR006420; NadN. DR PANTHER; PTHR11575; PTHR11575; 2. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR SUPFAM; SSF55816; SSF55816; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR01530; nadN; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; KW Metal-binding; Nucleotide-binding; Periplasm; Reference proteome; KW Signal; Zinc. FT SIGNAL 1 25 {ECO:0000269|PubMed:10675023}. FT CHAIN 26 603 NAD 5'-nucleotidase. FT /FTId=PRO_0000000026. FT REGION 540 546 Substrate binding. {ECO:0000250}. FT METAL 44 44 Zinc 1. FT METAL 46 46 Zinc 1. FT METAL 94 94 Zinc 1. FT METAL 94 94 Zinc 2. FT METAL 126 126 Zinc 2. FT METAL 227 227 Zinc 2. FT BINDING 397 397 Substrate. FT BINDING 437 437 Substrate. FT BINDING 456 456 Substrate. FT SITE 127 127 Transition state stabilizer. FT SITE 130 130 Transition state stabilizer. FT STRAND 35 42 {ECO:0000244|PDB:3ZTV}. FT STRAND 52 58 {ECO:0000244|PDB:3ZTV}. FT STRAND 61 67 {ECO:0000244|PDB:3ZTV}. FT HELIX 70 83 {ECO:0000244|PDB:3ZTV}. FT STRAND 84 91 {ECO:0000244|PDB:3ZTV}. FT HELIX 100 103 {ECO:0000244|PDB:3ZTV}. FT TURN 104 107 {ECO:0000244|PDB:3ZTV}. FT HELIX 108 116 {ECO:0000244|PDB:3ZTV}. FT STRAND 120 123 {ECO:0000244|PDB:3ZTV}. FT HELIX 127 129 {ECO:0000244|PDB:3ZTV}. FT HELIX 132 140 {ECO:0000244|PDB:3ZTV}. FT STRAND 150 154 {ECO:0000244|PDB:3ZTV}. FT TURN 159 162 {ECO:0000244|PDB:3ZTV}. FT STRAND 165 172 {ECO:0000244|PDB:3ZTV}. FT STRAND 175 183 {ECO:0000244|PDB:3ZTV}. FT HELIX 186 191 {ECO:0000244|PDB:3ZTV}. FT STRAND 198 200 {ECO:0000244|PDB:3ZTV}. FT HELIX 203 214 {ECO:0000244|PDB:3ZTV}. FT HELIX 215 217 {ECO:0000244|PDB:3ZTV}. FT STRAND 222 227 {ECO:0000244|PDB:3ZTV}. FT HELIX 230 239 {ECO:0000244|PDB:3ZTV}. FT STRAND 245 248 {ECO:0000244|PDB:3ZTV}. FT STRAND 254 256 {ECO:0000244|PDB:3ZTV}. FT HELIX 258 262 {ECO:0000244|PDB:3ZTV}. FT STRAND 267 276 {ECO:0000244|PDB:3ZTV}. FT STRAND 282 288 {ECO:0000244|PDB:3ZTV}. FT STRAND 294 302 {ECO:0000244|PDB:3ZTV}. FT STRAND 308 319 {ECO:0000244|PDB:3ZTV}. FT STRAND 325 327 {ECO:0000244|PDB:3ZTV}. FT STRAND 333 335 {ECO:0000244|PDB:3ZTV}. FT HELIX 338 349 {ECO:0000244|PDB:3ZTV}. FT STRAND 354 357 {ECO:0000244|PDB:3ZTV}. FT HELIX 361 377 {ECO:0000244|PDB:3ZTV}. FT STRAND 380 388 {ECO:0000244|PDB:3ZTV}. FT HELIX 394 396 {ECO:0000244|PDB:3ZTV}. FT HELIX 410 420 {ECO:0000244|PDB:3ZTV}. FT TURN 423 425 {ECO:0000244|PDB:3ZU0}. FT STRAND 428 432 {ECO:0000244|PDB:3ZTV}. FT HELIX 433 435 {ECO:0000244|PDB:3ZTV}. FT STRAND 442 446 {ECO:0000244|PDB:3ZTV}. FT HELIX 447 453 {ECO:0000244|PDB:3ZTV}. FT STRAND 459 466 {ECO:0000244|PDB:3ZTV}. FT HELIX 467 482 {ECO:0000244|PDB:3ZTV}. FT HELIX 487 489 {ECO:0000244|PDB:3ZTV}. FT STRAND 491 503 {ECO:0000244|PDB:3ZTV}. FT STRAND 506 508 {ECO:0000244|PDB:3ZU0}. FT STRAND 511 517 {ECO:0000244|PDB:3ZTV}. FT STRAND 524 526 {ECO:0000244|PDB:3ZTV}. FT STRAND 531 538 {ECO:0000244|PDB:3ZTV}. FT HELIX 539 542 {ECO:0000244|PDB:3ZTV}. FT HELIX 545 547 {ECO:0000244|PDB:3ZTV}. FT HELIX 549 554 {ECO:0000244|PDB:3ZTV}. FT HELIX 558 560 {ECO:0000244|PDB:3ZTV}. FT STRAND 563 568 {ECO:0000244|PDB:3ZTV}. FT HELIX 569 579 {ECO:0000244|PDB:3ZTV}. FT STRAND 582 584 {ECO:0000244|PDB:3ZTV}. FT STRAND 590 594 {ECO:0000244|PDB:3ZTV}. SQ SEQUENCE 603 AA; 66245 MW; B641C32A5A2B6AEA CRC64; MLLSKKSASF ALSAFAMLFT SVALAKEAPQ AHKAVELSIL HINDHHSYLE PHETRINLNG QQTKVDIGGF SAVNAKLNKL RKKYKNPLVL HAGDAITGTL YFTLFGGSAD AAVMNAGNFH YFTLGNHEFD AGNEGLLKLL EPLKIPVLSA NVIPDKNSIL YNKWKPYDIF TVDGEKIAII GLDTVNKTVN SSSPGKDVKF YDEIATAQIM ANALKQQGIN KIILLSHAGS EKNIEIAQKV NDIDVIVTGD SHYLYGNDEL RSLKLPVIYE YPLEFKNPNG DPVFVMEGWA YSAVVGDLGV KFSPEGIASI TRKIPHVLMS SHKLQVKNAE GKWTELTGDE RKKALDTLKS MKSISLDDHD AKTDMLISKY KSEKDRLAQE IVGVITGSAM PGGSANRIPN KAGSNPEGSI ATRFIAETMY NELKTVDLTI QNAGGVRADI LPGNVTFNDA YTFLPFGNTL YTYKMEGSLV KQVLEDAMQF ALVDGSTGAF PYGAGIRYEA NETPNAEGKR LVSVEVLNKQ TQQWEPIDDN KRYLVGTNAY VAGGKDGYKT FGKLFNDPKY EGVDTYLPDA ESFIKFMKKH PHFEAYTSSN VKFNASTDAL PKK // ID 6PGL_HAEIN Reviewed; 232 AA. AC Q57039; P96334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=6-phosphogluconolactonase; DE Short=6PGL; DE EC=3.1.1.31; GN Name=pgl; Synonyms=devB; OrderedLocusNames=HI_0556; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2/3. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22212.1; Type=Frameshift; Positions=29; 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; L42023; AAC22212.1; ALT_FRAME; Genomic_DNA. DR PIR; D64077; D64077. DR ProteinModelPortal; Q57039; -. DR SMR; Q57039; 1-228. DR STRING; 71421.HI0556; -. DR EnsemblBacteria; AAC22212; AAC22212; HI_0556. DR PATRIC; 20189667; VBIHaeInf48452_0576. DR eggNOG; COG0363; LUCA. DR OMA; YWGDERC; -. DR OrthoDB; EOG63FW46; -. DR UniPathway; UPA00115; UER00409. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 232 6-phosphogluconolactonase. FT /FTId=PRO_0000090094. SQ SEQUENCE 232 AA; 26307 MW; 4744738C62D3B11D CRC64; MNYISFPTAQ HAVDKIAQEF VIYSQLNHPV HISLSGGSTP KLLFKTLAKS PYAEQINWKN LHFWWGDDRM VPPSDPESNY GEVQKLLFDH IQIPAENIHR IRGENEPHFE LKRFEEELSA VIPNGVFDWI ILGMGIDGHT ASLFPHQTNF DDENLAVIAK HPESGQIRIS KTAKLIEQAK RITYLVTGES KADILKEIQT TPAENLPYPA AKIKAKNGVT EWYLDKAAVR LL // ID ACCD_HAEIN Reviewed; 296 AA. AC P43778; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395}; DE Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395}; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395}; DE EC=6.4.1.2 {ECO:0000255|HAMAP-Rule:MF_01395}; GN Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; GN OrderedLocusNames=HI_1260; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. Biotin carboxylase (BC) catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the transcarboxylase to acetyl-CoA to form malonyl- CC CoA. {ECO:0000255|HAMAP-Rule:MF_01395}. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01395}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01395}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01395}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) CC and two subunits each of ACCase subunit alpha (AccA) and ACCase CC subunit beta (AccD). {ECO:0000255|HAMAP-Rule:MF_01395}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01395}. CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP- CC Rule:MF_01395}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22913.1; -; Genomic_DNA. DR PIR; B64113; B64113. DR RefSeq; NP_439415.1; NC_000907.1. DR RefSeq; WP_005694317.1; NC_000907.1. DR ProteinModelPortal; P43778; -. DR SMR; P43778; 25-285. DR STRING; 71421.HI1260; -. DR PRIDE; P43778; -. DR EnsemblBacteria; AAC22913; AAC22913; HI_1260. DR GeneID; 950194; -. DR KEGG; hin:HI1260; -. DR PATRIC; 20191201; VBIHaeInf48452_1312. DR eggNOG; ENOG4107QTG; Bacteria. DR eggNOG; COG0777; LUCA. DR KO; K01963; -. DR OMA; PEGLWIK; -. DR OrthoDB; EOG6HQSSF; -. DR PhylomeDB; P43778; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1. DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su. DR InterPro; IPR000022; Carboxyl_trans. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011762; COA_CT_N. DR Pfam; PF01039; Carboxyl_trans; 1. DR PRINTS; PR01070; ACCCTRFRASEB. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00515; accD; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 296 Acetyl-coenzyme A carboxylase carboxyl FT transferase subunit beta. FT /FTId=PRO_0000199772. FT ZN_FING 29 51 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_01395}. FT METAL 29 29 Zinc. {ECO:0000255|HAMAP-Rule:MF_01395}. FT METAL 32 32 Zinc. {ECO:0000255|HAMAP-Rule:MF_01395}. FT METAL 48 48 Zinc. {ECO:0000255|HAMAP-Rule:MF_01395}. FT METAL 51 51 Zinc. {ECO:0000255|HAMAP-Rule:MF_01395}. SQ SEQUENCE 296 AA; 32635 MW; 3FEE316557FD4553 CRC64; MSWINRIFSK SPSSSTRKAN VPEGVWTKCT ACEQVLYSEE LKRNLYVCPK CGHHMRIDAR ERLLNLLDED SSQEIAADLE PKDILKFKDL KKYKDRINAA QKETGEKDAL ITMTGTLYNM PIVVAASNFA FMGGSMGSVV GAKFVKAAEK AMEMNCPFVC FSASGGARMQ EALFSLMQMA KTSAVLAQMR EKGVPFISVL TDPTLGGVSA SFAMLGDLNI AEPKALIGFA GPRVIEQTVR EKLPEGFQRS EFLLEKGAID MIVKRSEMRQ TLASVLSKLT NQPSPFVEPE LISEDE // ID ABGA_HAEIN Reviewed; 423 AA. AC P44765; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=p-aminobenzoyl-glutamate hydrolase subunit A homolog; DE EC=3.5.1.-; DE AltName: Full=PABA-GLU hydrolase; DE Short=PGH; GN Name=abgA; OrderedLocusNames=HI_0584; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the cleavage of p-aminobenzoyl-glutamate CC (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- MISCELLANEOUS: Unlike E.coli, AbgB is not present in H.influenza CC and therefore the multicomponent hydrolase AbgAB does not exist in CC this form. CC -!- SIMILARITY: Belongs to the peptidase M20 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; L42023; AAC22243.1; -; Genomic_DNA. DR PIR; B64079; B64079. DR RefSeq; NP_438742.1; NC_000907.1. DR RefSeq; WP_005694556.1; NC_000907.1. DR ProteinModelPortal; P44765; -. DR STRING; 71421.HI0584; -. DR MEROPS; M20.020; -. DR EnsemblBacteria; AAC22243; AAC22243; HI_0584. DR GeneID; 950603; -. DR KEGG; hin:HI0584; -. DR PATRIC; 20189725; VBIHaeInf48452_0605. DR eggNOG; ENOG4105CH2; Bacteria. DR eggNOG; COG1473; LUCA. DR KO; K12940; -. DR OMA; TKIDIRY; -. DR OrthoDB; EOG6BW4VH; -. DR PhylomeDB; P44765; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR017439; Amidohydrolase. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01891; amidohydrolases; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 423 p-aminobenzoyl-glutamate hydrolase FT subunit A homolog. FT /FTId=PRO_0000061959. SQ SEQUENCE 423 AA; 46554 MW; E5887A9FBAD15DD7 CRC64; MNLDLNQLVK WHREFHRFPE IGWSEFWTTS RIADYLEDLD CFEIFLGKQI INPDFVRGRK QAVVDKGLAN AKAYGANEKW LEKMEGYTGC VALFDSGKPG KTIALRFDID CVNVTETRSP EHIPNKEGFA SINDGFMHAC GHDSHITIGL GVALWIAQNK DKLTGKVKIV FQPAEEGVRG AAAIAQSGII DDADYFASSH ISFCANTGTV IANPRNFLST TKIDIRYKGK PAHAGAAPHL GRNALLAAAH TVTQLHGIAR HGKGMTRINV GVLKAGEGRN VIPSSAELQL EVRGENKAIN EYMTEQVMQI AKGISISFNV AYETEIVGEA VDMNNDVELI KLIEEISLEQ PQINNVNSDY AFNASEDATI LGRRVQEHGG KAIYFILGAD RTAGHHEAEF DFDENQLLTG VNIYTSLVQK LLS // ID ACCA_HAEIN Reviewed; 315 AA. AC P43872; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823}; DE EC=6.4.1.2 {ECO:0000255|HAMAP-Rule:MF_00823}; GN Name=accA {ECO:0000255|HAMAP-Rule:MF_00823}; GN OrderedLocusNames=HI_0406; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. First, biotin carboxylase catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the carboxyltransferase to acetyl-CoA to form CC malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) CC and two subunits each of ACCase subunit alpha (AccA) and ACCase CC subunit beta (AccD). {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}. CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP- CC Rule:MF_00823}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22065.1; -; Genomic_DNA. DR PIR; I64065; I64065. DR RefSeq; NP_438568.1; NC_000907.1. DR RefSeq; WP_005693763.1; NC_000907.1. DR ProteinModelPortal; P43872; -. DR SMR; P43872; 5-314. DR STRING; 71421.HI0406; -. DR EnsemblBacteria; AAC22065; AAC22065; HI_0406. DR GeneID; 949505; -. DR KEGG; hin:HI0406; -. DR PATRIC; 20189363; VBIHaeInf48452_0425. DR eggNOG; ENOG4107QM9; Bacteria. DR eggNOG; COG0825; LUCA. DR KO; K01962; -. DR OMA; HSVYTVA; -. DR OrthoDB; EOG6HQSSF; -. DR PhylomeDB; P43872; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1. DR InterPro; IPR001095; Acetyl_CoA_COase_a_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011763; COA_CT_C. DR Pfam; PF03255; ACCA; 1. DR PRINTS; PR01069; ACCCTRFRASEA. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00513; accA; 1. DR PROSITE; PS50989; COA_CT_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 315 Acetyl-coenzyme A carboxylase carboxyl FT transferase subunit alpha. FT /FTId=PRO_0000146779. SQ SEQUENCE 315 AA; 35126 MW; E3B0B498A2686B23 CRC64; MNQEYLDFEL PIAELEAKIE ALRAASDDKV DLTDEIKRLQ KKSNELTKKT FANLDAWQVS RMARHPNRPY TLDYIEHIFT EFEELAGDRA FADDKAIVGG LARLDGRPVM VIGHQKGRSV KEKVQRNFGM PAPEGYRKAL RLMEMAERFK LPIITFIDTP GAYPGIGAEE RGQAEAIARN LREMAQLTVP VICTVIGEGG SGGALAIGVG DKVNMLQYST YSVISPEGCA SILWKSAEKA STAAEVMGLT ASRLKELNLI DSIVQEPLGG AHRSYLEIAE NLKLRLKEDL AELDELSKEE LLNRRYERLM SYGYC // ID 5FCL_HAEIN Reviewed; 187 AA. AC P44905; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase; DE Short=5-FCL; DE EC=6.3.3.2; DE AltName: Full=5,10-methenyltetrahydrofolate synthetase; DE Short=MTHFS; GN OrderedLocusNames=HI_0858; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Involved in the removal of 5-formyltetrahydrofolate. In CC vitro, it is a potent inhibitor of various folate-dependent CC enzymes in the C1 metabolism network and in vivo it might function CC as a folate storage. 5-formyltetrahydrofolate is also used as an CC antifolate rescue agent in cancer chemotherapy. Catalyzes the CC irreversible ATP-dependent transformation of 5- CC formyltetrahydrofolate (5-CHO-THF) to form 5,10- CC methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is CC catalyzed by the serine hydroxymethyltransferase GlyA (SHMT) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 5-formyltetrahydrofolate = ADP + CC phosphate + 5,10-methenyltetrahydrofolate. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. 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; L42023; AAC22517.1; -; Genomic_DNA. DR PIR; D64160; D64160. DR RefSeq; NP_439018.1; NC_000907.1. DR RefSeq; WP_005693206.1; NC_000907.1. DR ProteinModelPortal; P44905; -. DR STRING; 71421.HI0858; -. DR EnsemblBacteria; AAC22517; AAC22517; HI_0858. DR GeneID; 949870; -. DR KEGG; hin:HI0858; -. DR PATRIC; 20190371; VBIHaeInf48452_0899. DR eggNOG; ENOG4105MK2; Bacteria. DR eggNOG; COG0212; LUCA. DR KO; K01934; -. DR OMA; DTPMKQN; -. DR OrthoDB; EOG6RVG1P; -. DR PhylomeDB; P44905; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IBA:GO_Central. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central. 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. DR TIGRFAMs; TIGR02727; MTHFS_bact; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 187 5-formyltetrahydrofolate cyclo-ligase. FT /FTId=PRO_0000200286. FT NP_BIND 6 10 ATP. {ECO:0000255}. FT NP_BIND 139 146 ATP. {ECO:0000255}. FT BINDING 178 178 ATP. {ECO:0000255}. SQ SEQUENCE 187 AA; 21821 MW; 01164CB8302A8C8A CRC64; MNTQKRQQIR TEIRKIRANL TALQQHQAEQ SVTQHALNLI EQRQAKNIAL YFSFDGEIST KALIQSLWMQ NKNVYLPVLH PFTKHYLLFL RYLPDTPMKQ NQFGIWEPKL NVQNVLPLNE LDILFTPLVA FDKKGNRLGM GGGFYDRTLQ NWQNKSFIPV GLAYQCQQVE NLPTEHWDVP LFDILVG // ID AAT_HAEIN Reviewed; 396 AA. AC P44425; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Aspartate aminotransferase; DE Short=AspAT; DE EC=2.6.1.1; DE AltName: Full=Transaminase A; GN Name=aspC; OrderedLocusNames=HI_1617; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate + CC L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23265.1; -; Genomic_DNA. DR PIR; I64132; I64132. DR RefSeq; NP_439759.1; NC_000907.1. DR RefSeq; WP_005693630.1; NC_000907.1. DR ProteinModelPortal; P44425; -. DR SMR; P44425; 1-396. DR STRING; 71421.HI1617; -. DR PRIDE; P44425; -. DR EnsemblBacteria; AAC23265; AAC23265; HI_1617. DR GeneID; 950841; -. DR KEGG; hin:HI1617; -. DR PATRIC; 20191967; VBIHaeInf48452_1691. DR eggNOG; ENOG4105CGF; Bacteria. DR eggNOG; COG1448; LUCA. DR KO; K00813; -. DR OMA; RVGACTI; -. DR OrthoDB; EOG6C2WBK; -. DR PhylomeDB; P44425; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR000796; Asp_trans. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11879; PTHR11879; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00799; TRANSAMINASE. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 396 Aspartate aminotransferase. FT /FTId=PRO_0000123841. FT BINDING 34 34 Aspartate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 130 130 Aspartate. {ECO:0000250}. FT BINDING 183 183 Aspartate. {ECO:0000250}. FT BINDING 374 374 Aspartate. {ECO:0000250}. FT MOD_RES 246 246 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 396 AA; 44321 MW; 9BDEA7C487CD8122 CRC64; MFEHIKAAPA DPILGLGEAF KSETRENKIN LGIGVYKDAQ GTTPIMHAVK EAEKRLFDKE KTKNYLTIDG IADYNEQTKA LLFGKDSEVI QSNRARTVQS LGGTGALRIA AEFIKRQTKA QNVWISTPTW PNHNAIFNAV GMTIREYRYY DAERKALDWE HLLEDLSQAS EGDVVLLHGC CHNPTGIDPT PEQWQELAAL SAKNGWLPLF DFAYQGLANG LDEDAYGLRA FAANHKELLV ASSFSKNFGL YNERVGAFTL VAENAEIAST SLTQVKSIIR TLYSNPASHG GATVATVLND AQLRQEWENE LTEMRERIKK MRHLFVQLLK EYGAEQDFSF IIEQNGMFSF SGLTGEQVDR LKNEFAIYAV RSGRINVAGI TEDNIRYLCE SIVKVL // ID ACCC_HAEIN Reviewed; 448 AA. AC P43873; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 118. DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14; DE AltName: Full=Acetyl-CoA carboxylase subunit A; DE Short=ACC; DE EC=6.4.1.2; GN Name=accC; OrderedLocusNames=HI_0972; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A CC carboxylase complex; first, biotin carboxylase catalyzes the CC carboxylation of the carrier protein and then the transcarboxylase CC transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] + CC HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier- CC protein]. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin CC carboxyl carrier protein, biotin carboxylase and the two subunits CC of carboxyl transferase in a 2:2 complex. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC -!- SIMILARITY: Contains 1 biotin carboxylation 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; L42023; AAC22632.1; -; Genomic_DNA. DR PIR; F64105; F64105. DR RefSeq; NP_439133.1; NC_000907.1. DR RefSeq; WP_005655956.1; NC_000907.1. DR PDB; 4MV1; X-ray; 1.91 A; A=1-448. DR PDB; 4MV3; X-ray; 1.69 A; A=1-448. DR PDB; 4MV4; X-ray; 1.61 A; A=1-448. DR PDB; 4MV6; X-ray; 1.77 A; A=1-448. DR PDB; 4MV7; X-ray; 1.73 A; A=1-448. DR PDB; 4MV8; X-ray; 2.06 A; A=1-448. DR PDB; 4MV9; X-ray; 1.98 A; A=1-448. DR PDB; 4RZQ; X-ray; 1.98 A; A=1-448. DR PDBsum; 4MV1; -. DR PDBsum; 4MV3; -. DR PDBsum; 4MV4; -. DR PDBsum; 4MV6; -. DR PDBsum; 4MV7; -. DR PDBsum; 4MV8; -. DR PDBsum; 4MV9; -. DR PDBsum; 4RZQ; -. DR ProteinModelPortal; P43873; -. DR SMR; P43873; 1-446. DR STRING; 71421.HI0972; -. DR EnsemblBacteria; AAC22632; AAC22632; HI_0972. DR GeneID; 949398; -. DR KEGG; hin:HI0972; -. DR PATRIC; 20190601; VBIHaeInf48452_1013. DR eggNOG; ENOG4105CER; Bacteria. DR eggNOG; COG0439; LUCA. DR KO; K01961; -. DR OMA; EAPSPIM; -. DR OrthoDB; EOG6CVV6Z; -. DR PhylomeDB; P43873; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005481; BC-like_N. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; Biotin_carb_N; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00514; accC; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS50979; BC; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Biotin; Complete proteome; KW Fatty acid biosynthesis; Fatty acid metabolism; Ligase; KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 448 Biotin carboxylase. FT /FTId=PRO_0000146793. FT DOMAIN 1 445 Biotin carboxylation. FT DOMAIN 120 317 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT ACT_SITE 292 292 {ECO:0000255}. FT BINDING 116 116 ATP. {ECO:0000250}. FT BINDING 201 201 ATP. {ECO:0000250}. FT BINDING 236 236 ATP. {ECO:0000250}. FT STRAND 4 7 {ECO:0000244|PDB:4MV4}. FT HELIX 11 24 {ECO:0000244|PDB:4MV4}. FT STRAND 27 33 {ECO:0000244|PDB:4MV4}. FT HELIX 34 36 {ECO:0000244|PDB:4MV4}. FT HELIX 40 44 {ECO:0000244|PDB:4MV4}. FT STRAND 45 55 {ECO:0000244|PDB:4MV4}. FT HELIX 56 58 {ECO:0000244|PDB:4MV4}. FT TURN 59 61 {ECO:0000244|PDB:4MV4}. FT HELIX 63 73 {ECO:0000244|PDB:4MV4}. FT STRAND 76 79 {ECO:0000244|PDB:4MV4}. FT TURN 84 87 {ECO:0000244|PDB:4MV4}. FT HELIX 89 97 {ECO:0000244|PDB:4MV4}. FT STRAND 101 104 {ECO:0000244|PDB:4MV4}. FT HELIX 107 114 {ECO:0000244|PDB:4MV4}. FT HELIX 116 126 {ECO:0000244|PDB:4MV4}. FT HELIX 142 152 {ECO:0000244|PDB:4MV4}. FT STRAND 154 160 {ECO:0000244|PDB:4MV4}. FT STRAND 169 172 {ECO:0000244|PDB:4MV4}. FT HELIX 175 192 {ECO:0000244|PDB:4MV4}. FT STRAND 198 202 {ECO:0000244|PDB:4MV4}. FT STRAND 208 216 {ECO:0000244|PDB:4MV4}. FT STRAND 222 234 {ECO:0000244|PDB:4MV4}. FT STRAND 237 244 {ECO:0000244|PDB:4MV4}. FT HELIX 250 267 {ECO:0000244|PDB:4MV4}. FT STRAND 271 280 {ECO:0000244|PDB:4MV4}. FT STRAND 283 290 {ECO:0000244|PDB:4MV4}. FT HELIX 297 304 {ECO:0000244|PDB:4MV4}. FT HELIX 308 316 {ECO:0000244|PDB:4MV4}. FT HELIX 325 327 {ECO:0000244|PDB:4MV4}. FT STRAND 332 342 {ECO:0000244|PDB:4MV4}. FT TURN 344 346 {ECO:0000244|PDB:4MV4}. FT STRAND 356 358 {ECO:0000244|PDB:4MV4}. FT STRAND 365 368 {ECO:0000244|PDB:4MV4}. FT STRAND 379 381 {ECO:0000244|PDB:4MV4}. FT STRAND 384 394 {ECO:0000244|PDB:4MV4}. FT HELIX 395 408 {ECO:0000244|PDB:4MV4}. FT STRAND 410 414 {ECO:0000244|PDB:4MV4}. FT HELIX 418 425 {ECO:0000244|PDB:4MV4}. FT HELIX 428 432 {ECO:0000244|PDB:4MV4}. FT HELIX 439 444 {ECO:0000244|PDB:4MV4}. SQ SEQUENCE 448 AA; 49108 MW; 2B497E2A31ED96D1 CRC64; MLEKVVIANR GEIALRILRA CKELGIKTVA VHSTADRDLK HVLLADETIC IGPAPSAKSY LNIPAIIAAA EVTGADAIHP GYGFLSENAD FAEQVERSGF TFIGPTADVI RLMGDKVSAI KAMKKAGVPC VPGSDGPVSN DIAKNKEIAK RIGYPIIIKA SGGGGGRGMR VVRSEDALEE SIAMTKAEAK AAFNNDMVYM EKYLENPRHV EIQVLADTHG NAVYLAERDC SMQRRHQKVV EEAPAPGITE EVRRDIGSRC ANACVEIGYR GAGTFEFLYE NGEFYFIEMN TRIQVEHPVT EMITGVDLVK EQLRIAAGLP ISFKQEDIKV KGHAMECRIN AEDPKTFLPS PGKVNHLHSP GGLGVRWDSH VYGGYTVPPH YDSMIAKLIT YGDTREVAIR RMQNALSETI IDGIKTNIPL HELILEDENF QKGGTNIHYL EKKLGMNE // ID 6PGD_HAEIN Reviewed; 484 AA. AC P43774; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=HI_0553; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22210.1; -; Genomic_DNA. DR PIR; C64077; C64077. DR RefSeq; NP_438711.1; NC_000907.1. DR RefSeq; WP_005649523.1; NC_000907.1. DR ProteinModelPortal; P43774; -. DR SMR; P43774; 4-475. DR STRING; 71421.HI0553; -. DR PRIDE; P43774; -. DR EnsemblBacteria; AAC22210; AAC22210; HI_0553. DR GeneID; 949604; -. DR KEGG; hin:HI0553; -. DR PATRIC; 20189661; VBIHaeInf48452_0573. DR eggNOG; ENOG4105C7Q; Bacteria. DR eggNOG; COG0362; LUCA. DR KO; K00033; -. DR OMA; EGEPCVT; -. DR OrthoDB; EOG6MSS4W; -. DR PhylomeDB; P43774; -. DR SABIO-RK; P43774; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 1.20.5.320; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR012284; 6PGD_dom_3. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006183; Pgluconate_DH. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt; Reference proteome. FT CHAIN 1 484 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090041. FT NP_BIND 11 16 NADP. {ECO:0000250}. FT NP_BIND 34 36 NADP. {ECO:0000250}. FT NP_BIND 76 78 NADP. {ECO:0000250}. FT REGION 130 132 Substrate binding. {ECO:0000250}. FT REGION 188 189 Substrate binding. {ECO:0000250}. FT ACT_SITE 185 185 Proton acceptor. {ECO:0000250}. FT ACT_SITE 192 192 Proton donor. {ECO:0000250}. FT BINDING 104 104 NADP. {ECO:0000250}. FT BINDING 104 104 Substrate. {ECO:0000250}. FT BINDING 193 193 Substrate. {ECO:0000250}. FT BINDING 262 262 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 289 289 Substrate. {ECO:0000250}. FT BINDING 447 447 Substrate; shared with dimeric partner. FT {ECO:0000250}. FT BINDING 453 453 Substrate; shared with dimeric partner. FT {ECO:0000250}. SQ SEQUENCE 484 AA; 53140 MW; 8381EEB3C704C5DA CRC64; MSVKGDIGVI GLAVMGQNLI LNMNDHGFKV VAYNRTTSKV DEFLQGAAKG TNIIGAYSLE DLAAKLEKPR KVMLMVRAGD VVDQFIEALL PHLEEGDIII DGGNSNYPDT NRRVKALAEK GIRFIGSGVS GGEEGARHGP SIMPGGNQEA WQYVKPIFQA ISAKTEQGEP CCDWVGGEGA GHFVKMVHNG IEYGDMQLIC EAYQFLKEGL GLSYEEMQAI FAEWKNTELD SYLIDITTDI LGYKDASGEP LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITESVFARC VSSFKDQRVA ANQLFGKTIT PVEGDKKVWI EAVRKALLAS KIISYAQGFM LIREASEQFG WDINYGATAL LWREGCIIRS RFLGNIRDAY EANPNLVFLG SDSYFKGILE NALSDWRKVV AKSIEVGIPM PCMASAITFL DGYTSARLPA NLLQAQRDYF GAHTYERTDK PRGEFFHTNW TGRGGNTAST TYDV // ID ACKA_HAEIN Reviewed; 401 AA. AC P44406; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 104. DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; GN OrderedLocusNames=HI_1204; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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. 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; L42023; AAC22858.1; -; Genomic_DNA. DR PIR; G64189; G64189. DR RefSeq; NP_439360.1; NC_000907.1. DR RefSeq; WP_005694241.1; NC_000907.1. DR ProteinModelPortal; P44406; -. DR STRING; 71421.HI1204; -. DR EnsemblBacteria; AAC22858; AAC22858; HI_1204. DR GeneID; 949638; -. DR KEGG; hin:HI1204; -. DR PATRIC; 20191087; VBIHaeInf48452_1256. DR eggNOG; ENOG4105C6H; Bacteria. DR eggNOG; COG0282; LUCA. DR KO; K00925; -. DR OMA; HRLKKYI; -. DR OrthoDB; EOG69975F; -. DR PhylomeDB; P44406; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000579; 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 1 401 Acetate kinase. FT /FTId=PRO_0000107565. FT NP_BIND 207 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 282 284 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT NP_BIND 333 337 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT ACT_SITE 147 147 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT METAL 9 9 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT METAL 388 388 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT BINDING 16 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}. FT BINDING 88 88 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00020}. FT SITE 179 179 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. FT SITE 240 240 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00020}. SQ SEQUENCE 401 AA; 43758 MW; 4E12E0F67D322E2C CRC64; MSKLVLILNC GSSSLKFAIL DPATGEEKLS GLAEAFFLPE ARIKWKLNGE KGNADLGAGA AHTEALNFIA SNILNDELKN SIAAIGHRIV HGGEKYTQSV IVTDEVVKGI EDAAQFAPLH NPAHLIGIRE AFKAFPHLKD KNVVVFDTAF HQTMPEEAFL YALPYSLYKE HGVRRYGAHG TSHYFVSREV AKYVGKPADQ VNAIICHLGN GGSVSVVRNG QCIDTSMGLT PLEGLVMGTR CGDIDPAIVF YLYKTLGMSM DQIEETLVKK SGLLGLTEVT SDCRYAEDNY DDESKPETRR ALNVYSYRLA KYIGAYMAVL GDDHLDAIAF TGGIGENSAH VRELALNHLK LFGIKIDNER NLATRFGKDG VITTDDSAFK AIVLPTNEEL VIAQDTAKLC F // ID ACP_HAEIN Reviewed; 76 AA. AC P43709; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217}; DE Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217}; GN Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217}; GN OrderedLocusNames=HI_0154; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}. CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific CC serine of apo-ACP by AcpS. This modification is essential for CC activity because fatty acids are bound in thioester linkage to the CC sulfhydryl of the prosthetic group. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|HAMAP- CC Rule:MF_01217}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21823.1; -; Genomic_DNA. DR PIR; C64051; C64051. DR RefSeq; NP_438324.1; NC_000907.1. DR RefSeq; WP_005544465.1; NC_000907.1. DR ProteinModelPortal; P43709; -. DR SMR; P43709; 2-76. DR STRING; 71421.HI0154; -. DR EnsemblBacteria; AAC21823; AAC21823; HI_0154. DR GeneID; 25059107; -. DR GeneID; 951065; -. DR KEGG; hin:HI0154; -. DR PATRIC; 20188803; VBIHaeInf48452_0158. DR eggNOG; ENOG4105VNB; Bacteria. DR eggNOG; COG0236; LUCA. DR KO; K02078; -. DR OMA; CEIPDDQ; -. DR OrthoDB; EOG6MWNJM; -. DR PhylomeDB; P43709; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000036; F:ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1200.10; -; 1. DR HAMAP; MF_01217; Acyl_carrier; 1. DR InterPro; IPR003231; Acyl_carrier. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR Pfam; PF00550; PP-binding; 1. DR ProDom; PD000887; PD000887; 1. DR SUPFAM; SSF47336; SSF47336; 1. DR TIGRFAMs; TIGR00517; acyl_carrier; 1. DR PROSITE; PS50075; ACP_DOMAIN; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Phosphopantetheine; Phosphoprotein; Reference proteome. FT CHAIN 1 76 Acyl carrier protein. FT /FTId=PRO_0000180142. FT MOD_RES 36 36 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|HAMAP-Rule:MF_01217}. SQ SEQUENCE 76 AA; 8584 MW; 92BE1125772036FB CRC64; MSIEERVKKI IVEQLGVKEE DVKPEASFVE DLGADSLDTV ELVMALEEEF DIEIPDEEAE KITTVQSAID YVQNNQ // ID AKH_HAEIN Reviewed; 815 AA. AC P44505; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 120. DE RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase; DE Short=AK-HD; DE Includes: DE RecName: Full=Aspartokinase; DE EC=2.7.2.4; DE Includes: DE RecName: Full=Homoserine dehydrogenase; DE EC=1.1.1.3; GN Name=thrA; OrderedLocusNames=HI_0089; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ACT domains. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21767.1; -; Genomic_DNA. DR PIR; A64048; A64048. DR RefSeq; NP_438262.1; NC_000907.1. DR RefSeq; WP_005693830.1; NC_000907.1. DR ProteinModelPortal; P44505; -. DR STRING; 71421.HI0089; -. DR PRIDE; P44505; -. DR EnsemblBacteria; AAC21767; AAC21767; HI_0089. DR GeneID; 950991; -. DR KEGG; hin:HI0089; -. DR PATRIC; 20188641; VBIHaeInf48452_0090. DR eggNOG; ENOG4105CFH; Bacteria. DR eggNOG; COG0460; LUCA. DR eggNOG; COG0527; LUCA. DR KO; K12524; -. DR OMA; QAYDESS; -. DR OrthoDB; EOG6M0T34; -. DR PhylomeDB; P44505; -. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR001341; Asp_kinase_dom. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR011147; Bifunc_aspartokin/hSer_DH. DR InterPro; IPR027795; GATS-like_ACT_dom. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000727; ThrA; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 2. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Amino-acid biosynthesis; ATP-binding; KW Complete proteome; Kinase; Multifunctional enzyme; NADP; KW Nucleotide-binding; Oxidoreductase; Reference proteome; Repeat; KW Threonine biosynthesis; Transferase. FT CHAIN 1 815 Bifunctional aspartokinase/homoserine FT dehydrogenase. FT /FTId=PRO_0000066687. FT DOMAIN 320 392 ACT 1. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT DOMAIN 401 478 ACT 2. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT NP_BIND 471 478 NADP. {ECO:0000255}. FT REGION 1 249 Aspartokinase. FT REGION 250 470 Interface. FT REGION 471 815 Homoserine dehydrogenase. SQ SEQUENCE 815 AA; 88221 MW; 7FD5512FCC4BE7F7 CRC64; MRVLKFGGTS LANPERFSQA AKLIEQAHLE EQAAGVLSAP AKITNHLVAL SEKAALNQST DTHFNEAIEI FYNIINGLHT ENNQFDLNGT KALIDAEFVQ IKGLLEEIRQ AGKVEDAVKA TIDCRGEKLS IAMMKAWFEA RGYSVHIVDP VKQLLAKGGY LESSVEIEES TKRVDAANIA KDKVVLMAGF TAGNEKGELV LLGRNGSDYS AACLAACLGA SVCEIWTDVD GVYTCDPRLV PDARLLPTLS YREAMELSYF GAKVIHPRTI GPLLPQNIPC VIKNTGNPSA PGSIIDGNVK SESLQVKGIT NLDNLAMFNV SGPGMQGMVG MASRVFSAMS GAGISVILIT QSSSEYSISF CVPVKSAEVA KTVLETEFAN ELNEHQLEPI EVIKDLSIIS VVGDGMKQAK GIAARFFSAL AQANISIVAI AQGSSERSIS AVVPQNKAIE AVKATHQALF NNKKVVDMFL VGVGGVGGEL IEQVKRQKEY LAKKNVEIRV CAIANSNRML LDENGLNLED WKNDLENATQ PSDFDVLLSF IKLHHVVNPV FVDCTSAESV AGLYARALKE GFHVVTPNKK ANTRELVYYN ELRQNAQASQ HKFLYETNVG AGLPVIENLQ NLLAAGDELE YFEGILSGSL SFIFGKLEEG LSLSEVTALA REKGFTEPDP RDDLSGQDVA RKLLILAREA GIELELSDVE VEGVLPKGFS DGKSADEFMA MLPQLDEEFK TRVATAKAEG KVLRYVGKIS EGKCKVSIVA VDLNNPLYKV KDGENALAFY TRYYQPIPLL LRGYGAGNAV TAAGIFADIL RTLQH // ID ALAA_HAEIN Reviewed; 404 AA. AC P71348; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Glutamate-pyruvate aminotransferase AlaA; DE EC=2.6.1.2; GN Name=alaA; OrderedLocusNames=HI_0286; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the biosynthesis of alanine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-alanine + 2-oxoglutarate = pyruvate + L- CC glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21948.1; -; Genomic_DNA. DR RefSeq; NP_438453.1; NC_000907.1. DR RefSeq; WP_005694022.1; NC_000907.1. DR ProteinModelPortal; P71348; -. DR STRING; 71421.HI0286; -. DR PRIDE; P71348; -. DR EnsemblBacteria; AAC21948; AAC21948; HI_0286. DR GeneID; 949411; -. DR KEGG; hin:HI0286; -. DR PATRIC; 20189111; VBIHaeInf48452_0302. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR KO; K14260; -. DR OMA; RIVFLPH; -. DR OrthoDB; EOG6X9MJ6; -. DR PhylomeDB; P71348; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0030632; P:D-alanine biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 404 Glutamate-pyruvate aminotransferase AlaA. FT /FTId=PRO_0000123869. FT BINDING 41 41 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 179 179 Substrate. {ECO:0000250}. FT BINDING 378 378 Substrate. {ECO:0000250}. FT MOD_RES 240 240 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 404 AA; 45160 MW; 7F2C3E24CC69FB46 CRC64; MRLFPKSDKL EHVCYDIRGP VHKEALRLEE EGNKILKLNI GNPAPFGFEA PDEILVDVLR NLPSAQGYCD SKGLYSARKA IVQYYQSKGI LGATVNDVYI GNGVSELITM AMQALLNDGD EVLVPMPDYP LWTAAVTLSG GKAVHYLCDE DANWFPTIDD IKAKVNAKTK AIVIINPNNP TGAVYSKELL QEIVEIARQN NLIIFADEIY DKILYDGAVH HHIAALAPDL LTVTLNGLSK AYRVAGFRQG WMILNGPKHN AKGYIEGLDM LASMRLCANV PMQHAIQTAL GGYQSINEFI LPGGRLLEQR NKAYDLITQI PGITCVKPMG AMYMFPKIDV KKFNIHSDEK MVLDLLRQEK VLLVHGKGFN WHSPDHFRIV TLPYVNQLEE AITKLARFLS DYRQ // ID ALR_HAEIN Reviewed; 360 AA. AC P45257; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201}; GN Name=alr; OrderedLocusNames=HI_1575; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D- CC alanine. May also act on other amino acids. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D- CC alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. CC {ECO:0000255|HAMAP-Rule:MF_01201}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23218.1; -; Genomic_DNA. DR PIR; E64130; E64130. DR RefSeq; NP_439721.1; NC_000907.1. DR RefSeq; WP_005693598.1; NC_000907.1. DR ProteinModelPortal; P45257; -. DR SMR; P45257; 4-360. DR STRING; 71421.HI1575; -. DR EnsemblBacteria; AAC23218; AAC23218; HI_1575. DR GeneID; 950435; -. DR KEGG; hin:HI1575; -. DR PATRIC; 20191881; VBIHaeInf48452_1648. DR eggNOG; ENOG4105CJ4; Bacteria. DR eggNOG; COG0787; LUCA. DR KO; K01775; -. DR OMA; PSDWVRP; -. DR OrthoDB; EOG6PP9NJ; -. DR PhylomeDB; P45257; -. DR BRENDA; 5.1.1.1; 2529. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_01201; Ala_racemase; 1. DR InterPro; IPR000821; Ala_racemase. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C; 1. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR00492; alr; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 360 Alanine racemase. FT /FTId=PRO_0000114522. FT ACT_SITE 36 36 Proton acceptor; specific for D-alanine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT ACT_SITE 256 256 Proton acceptor; specific for L-alanine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT BINDING 132 132 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01201}. FT BINDING 304 304 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01201}. FT MOD_RES 36 36 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01201}. SQ SEQUENCE 360 AA; 39705 MW; A9FF1283C56AD71B CRC64; MNVKPATAKI SSHALKQNLE IIKQKAPNSK IIAVVKANAY GHGVVFVAST LEQNVDCFGV ARLEEALALR SNGITKPILL LEGFFNEQDL PILAVNNIET VVHNHEQLDA LKRANLPSPI KVWLKIDTGM HRLGVALDEV DYFYQELKKL PQIQPHLGFV SHFSRADELE SDYTQLQINR FLSVTKDKQG ERTIAASGGI LFWPKSHLEC IRPGIIMYGI SPTDTIGKEF GLTPVMNLTS SLIAVRHHKQ GDPVGYGGIW TSPRDTKIGV VAMGYGDGYP RDVPEGTPVY LNGRLVPIVG RVSMDMLTVD LGADSQDLVG DEVILWGKEL PIETVAKFTG ILSYELITKL TPRVITEYVD // ID AMPA_HAEIN Reviewed; 491 AA. AC P45334; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=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=HI_1705; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23351.1; -; Genomic_DNA. DR PIR; C64137; C64137. DR RefSeq; NP_439847.1; NC_000907.1. DR RefSeq; WP_005694194.1; NC_000907.1. DR ProteinModelPortal; P45334; -. DR SMR; P45334; 1-490. DR STRING; 71421.HI1705; -. DR MEROPS; M17.003; -. DR EnsemblBacteria; AAC23351; AAC23351; HI_1705. DR GeneID; 949712; -. DR KEGG; hin:HI1705; -. DR PATRIC; 20192161; VBIHaeInf48452_1784. DR eggNOG; ENOG4105BZ6; Bacteria. DR eggNOG; COG0260; LUCA. DR KO; K01255; -. DR OMA; ANGMELT; -. DR OrthoDB; EOG6FV8B3; -. DR PhylomeDB; P45334; -. DR Proteomes; UP000000579; 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 InterPro; IPR008283; Peptidase_M17_N. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 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 1 491 Cytosol aminopeptidase. FT /FTId=PRO_0000165758. FT ACT_SITE 275 275 {ECO:0000255}. FT ACT_SITE 349 349 {ECO:0000255}. FT METAL 263 263 Manganese 2. {ECO:0000250}. FT METAL 268 268 Manganese 1. {ECO:0000250}. FT METAL 268 268 Manganese 2. {ECO:0000250}. FT METAL 286 286 Manganese 2. {ECO:0000250}. FT METAL 345 345 Manganese 1. {ECO:0000250}. FT METAL 347 347 Manganese 1. {ECO:0000250}. FT METAL 347 347 Manganese 2. {ECO:0000250}. SQ SEQUENCE 491 AA; 53529 MW; 71376DDB1B0076EB CRC64; MKYQAKNTAL SQATDCIVLG VYENNKFSKS FNEIDQLTQG YLNDLVKSGE LTGKLAQTVL LRDLQGLSAK RLLIVGCGKK GELTERQYKQ IIQAVLKTLK ETNTREVISY LTEIELKDRD LYWNIRFAIE TIEHTNYQFD HFKSQKAETS VLESFIFNTD CAQAQQAISH ANAISSGIKA ARDIANMPPN ICNPAYLAEQ AKNLAENSTA LSLKVVDEEE MAKLGMNAYL AVSKGSENRA YMSVLTFNNA PDKNAKPIVL VGKGLTFDAG GISLKPAADM DEMKYDMCGA ASVFGTMKTI AQLNLPLNVI GVLAGCENLP DGNAYRPGDI LTTMNGLTVE VLNTDAEGRL VLCDTLTYVE RFEPELVIDV ATLTGACVVA LGQHNSGLVS TDNNLANALL QAATETTDKA WRLPLSEEYQ EQLKSPFADL ANIGGRWGGA ITAGAFLSNF TKKYRWAHLD IAGTAWLQGA NKGATGRPVS LLTQFLINQV K // ID AMPD_HAEIN Reviewed; 184 AA. AC P44624; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD; DE EC=3.5.1.28; DE AltName: Full=N-acetylmuramoyl-L-alanine amidase; GN Name=ampD; OrderedLocusNames=HI_0300; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in both cell wall peptidoglycans recycling and CC beta-lactamase induction. Specifically cleaves the amide bond CC between the lactyl group of N-acetylmuramic acid and the alpha- CC amino group of the L-alanine in degradation products containing an CC anhydro N-acetylmuramyl moiety (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl CC residues and L-amino acid residues in certain cell-wall CC glycopeptides. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Zn(2+) is required for amidase activity. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 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; L42023; AAC21965.1; -; Genomic_DNA. DR PIR; F64060; F64060. DR RefSeq; NP_438467.1; NC_000907.1. DR RefSeq; WP_005694366.1; NC_000907.1. DR ProteinModelPortal; P44624; -. DR SMR; P44624; 6-183. DR STRING; 71421.HI0300; -. DR EnsemblBacteria; AAC21965; AAC21965; HI_0300. DR GeneID; 949420; -. DR KEGG; hin:HI0300; -. DR PATRIC; 20189141; VBIHaeInf48452_0317. DR eggNOG; ENOG4108VBV; Bacteria. DR eggNOG; COG3023; LUCA. DR KO; K03806; -. DR OMA; FNARPEG; -. DR OrthoDB; EOG60GRR5; -. DR PhylomeDB; P44624; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central. DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central. DR Gene3D; 3.40.80.10; -; 1. DR InterPro; IPR002502; Amidase_domain. DR Pfam; PF01510; Amidase_2; 1. DR SMART; SM00644; Ami_2; 1. DR SUPFAM; SSF55846; SSF55846; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 184 1,6-anhydro-N-acetylmuramyl-L-alanine FT amidase AmpD. FT /FTId=PRO_0000164414. FT ACT_SITE 120 120 Proton acceptor. {ECO:0000250}. FT METAL 38 38 Zinc; catalytic. {ECO:0000250}. FT METAL 159 159 Zinc; catalytic. {ECO:0000250}. FT METAL 169 169 Zinc; catalytic. {ECO:0000250}. FT SITE 167 167 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 184 AA; 21448 MW; B7A035527E328401 CRC64; MRKIKDIEKG LLTDCRQIQS PHFDKRPNPQ DISLLVIHYI SLPPEQFGGG YVDDFFQGKL DPKIHPYFAE IYQMRVSAHC LIERNGRITQ YVNFNDRAWH AGVSNFQGRE KCNDFAIGIE LEGSNEQPFT DAQYFSLQEL TNVIMKSYPK ITKDRIVGHC DISPKRKIDP GQYFDWERYL SSVK // ID ANMK_HAEIN Reviewed; 382 AA. AC P44861; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270}; DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270}; DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270}; GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; GN OrderedLocusNames=HI_0753; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N- CC acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of CC the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the CC utilization of anhMurNAc either imported from the medium or CC derived from its own cell wall murein, and thus plays a role in CC cell wall recycling. {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- CATALYTIC ACTIVITY: ATP + 1,6-anhydro-N-acetyl-beta-muramate + CC H(2)O = ADP + N-acetylmuramate 6-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01270}. CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate CC degradation. {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_01270}. CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase CC family. {ECO:0000255|HAMAP-Rule:MF_01270}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22412.1; -; Genomic_DNA. DR PIR; B64158; B64158. DR RefSeq; NP_438912.1; NC_000907.1. DR RefSeq; WP_005693152.1; NC_000907.1. DR ProteinModelPortal; P44861; -. DR STRING; 71421.HI0753; -. DR EnsemblBacteria; AAC22412; AAC22412; HI_0753. DR GeneID; 949467; -. DR KEGG; hin:HI0753; -. DR PATRIC; 20190151; VBIHaeInf48452_0791. DR eggNOG; ENOG4105ED7; Bacteria. DR eggNOG; COG2377; LUCA. DR KO; K09001; -. DR OMA; GCHGQTI; -. DR OrthoDB; EOG64N9WW; -. DR PhylomeDB; P44861; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006040; P:amino sugar metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01270; AnhMurNAc_kinase; 1. DR InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase. DR Pfam; PF03702; UPF0075; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 382 Anhydro-N-acetylmuramic acid kinase. FT /FTId=PRO_0000214822. FT NP_BIND 15 22 ATP. {ECO:0000255|HAMAP-Rule:MF_01270}. SQ SEQUENCE 382 AA; 42026 MW; D14E353287BC11A6 CRC64; MINMKPQYYL GMMSGTSLDG VDIVLVDFSQ DPQLILSDFF PMPEDLREKL TTLIQVGETT LQNLGELDHK LALLYSDCVN AFLQKNTFLP NQIQAIGCHG QTVWHSPNSQ FPFTMQLGDM NLLAAKTGIS VIGDFRRKDM AWGGQGAPLV PAFHEAVFSN SNFATAVLNI GGISNVSILF PNQAVIGFDT GPGNTLLDQW IEKHQGLRYD ENGEWAAKGN VNKVLLDELL NEPFFSLPAP KSTGRELFNL VWLNHKIAKI REKLTALSVE MSFRPEDVQA TLVELTVTSI VNALNQLQTD LPKRLLVCGG GAKNSLIMRG LHDNLLDWQV STTTEQGFDI DYVEAAAFAW LAYCRINNLP ANLPSVTGAK SAVSLGAIFP KD // ID ADPP_HAEIN Reviewed; 217 AA. AC P44684; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=ADP-ribose pyrophosphatase; DE EC=3.6.1.13; DE AltName: Full=ADP-ribose diphosphatase; DE AltName: Full=ADP-ribose phosphohydrolase; DE Short=ASPPase; DE AltName: Full=Adenosine diphosphoribose pyrophosphatase; DE Short=ADPR-PPase; GN Name=nudF; OrderedLocusNames=HI_0398; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP CHARACTERIZATION. RX PubMed=10542272; DOI=10.1074/jbc.274.45.32318; RA Dunn C.A., O'Handley S.F., Frick D.N., Bessman M.J.; RT "Studies on the ADP-ribose pyrophosphatase subfamily of the nudix RT hydrolases and tentative identification of trgB, a gene associated RT with tellurite resistance."; RL J. Biol. Chem. 274:32318-32324(1999). CC -!- FUNCTION: Acts on ADP-mannose and ADP-glucose as well as ADP- CC ribose. Prevents glycogen biosynthesis. The reaction catalyzed by CC this enzyme is a limiting step of the gluconeogenic process (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. 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 -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22057.1; -; Genomic_DNA. DR PIR; B64151; B64151. DR RefSeq; NP_438560.2; NC_000907.1. DR ProteinModelPortal; P44684; -. DR STRING; 71421.HI0398; -. DR EnsemblBacteria; AAC22057; AAC22057; HI_0398. DR GeneID; 949499; -. DR KEGG; hin:HI0398; -. DR PATRIC; 20189347; VBIHaeInf48452_0417. DR eggNOG; ENOG41087AY; Bacteria. DR eggNOG; ENOG410ZYVG; LUCA. DR KO; K01515; -. DR OMA; EQAYQWM; -. DR OrthoDB; EOG6SNDRS; -. DR BRENDA; 3.6.1.13; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR004385; NDP_pyrophosphatase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00052; TIGR00052; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 217 ADP-ribose pyrophosphatase. FT /FTId=PRO_0000057045. FT DOMAIN 58 204 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT REGION 31 32 Substrate binding. {ECO:0000250}. FT REGION 54 55 Substrate binding; shared with dimeric FT partner. {ECO:0000250}. FT REGION 139 141 Substrate binding; shared with dimeric FT partner. {ECO:0000250}. FT MOTIF 103 124 Nudix box. FT ACT_SITE 168 168 Proton acceptor. {ECO:0000250}. FT METAL 102 102 Magnesium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 118 118 Magnesium 2. {ECO:0000250}. FT METAL 118 118 Magnesium 3. {ECO:0000250}. FT METAL 122 122 Magnesium 1. {ECO:0000250}. FT METAL 122 122 Magnesium 3. {ECO:0000250}. FT METAL 170 170 Magnesium 3. {ECO:0000250}. FT BINDING 82 82 Substrate. {ECO:0000250}. FT BINDING 104 104 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 145 145 Substrate. {ECO:0000250}. SQ SEQUENCE 217 AA; 24580 MW; 6040146E71ABD400 CRC64; MQFWRKQMSE IQHFSQQDIE ILGEQTLYEG FFTLKRIQFK HKLFAGGQSG VVTRELLIKG AASAVIAYDP KEDSVILVEQ VRIGAAYHPE SHRSPWLLEL IAGMVEKGEK PEDVALRESE EEAGIQVKNL THCLSVWDSP GGIVERIHLF AGEVDSAQAK GIHGLAEENE DIKVHVVKRE QAYQWMCEGK IDNGIAVIGL QWLQLNYAQL QQSWKRS // ID ALF_HAEIN Reviewed; 359 AA. AC P44429; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. 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; OrderedLocusNames=HI_0524; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22182.1; -; Genomic_DNA. DR PIR; C64074; C64074. DR RefSeq; NP_438682.1; NC_000907.1. DR RefSeq; WP_005694127.1; NC_000907.1. DR ProteinModelPortal; P44429; -. DR SMR; P44429; 2-359. DR STRING; 71421.HI0524; -. DR PRIDE; P44429; -. DR EnsemblBacteria; AAC22182; AAC22182; HI_0524. DR GeneID; 949539; -. DR KEGG; hin:HI0524; -. DR PATRIC; 20189601; VBIHaeInf48452_0543. DR eggNOG; ENOG4105D2N; Bacteria. DR eggNOG; COG0191; LUCA. DR KO; K01624; -. DR OMA; RMSKMGM; -. DR OrthoDB; EOG69GZPB; -. DR PhylomeDB; P44429; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000579; 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:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006411; Fruct_bisP_bact. 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; TIGR01520; FruBisAldo_II_A; 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 1 359 Fructose-bisphosphate aldolase. FT /FTId=PRO_0000178716. FT REGION 266 268 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT REGION 287 290 Dihydroxyacetone phosphate binding. FT {ECO:0000250}. FT ACT_SITE 110 110 Proton donor. {ECO:0000250}. FT METAL 111 111 Zinc 1; catalytic. {ECO:0000250}. FT METAL 145 145 Zinc 2. {ECO:0000250}. FT METAL 175 175 Zinc 2. {ECO:0000250}. FT METAL 227 227 Zinc 1; catalytic. {ECO:0000250}. FT METAL 265 265 Zinc 1; catalytic. {ECO:0000250}. FT BINDING 62 62 Glyceraldehyde 3-phosphate. FT {ECO:0000250}. FT BINDING 228 228 Dihydroxyacetone phosphate; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 359 AA; 39340 MW; 1EDDFCDD0B69E32C CRC64; MAKLLDIVKP GVVTGEDVQK VFAYAKEHNF AIPAVNCVGS DSVNAVLETA ARVKAPVIIQ FSNGGAAFYA GKGIKPTSGT RPDVLGAIAG AKQVHTLAKE YGVPVILHTD HAAKKLLPWI DGLLDAGEKH FAETGRPLFS SHMIDLSEES MEENMAICRE YLARMDKMGM TLEIEIGITG GEEDGVDNSD VDESRLYTQP SDVLYVYDQL HPVSPNFTVA AAFGNVHGVY KPGNVKLKPS ILGESQEFVS KERNLPAKPI NFVFHGGSGS SREEIREAIG YGAIKMNIDT DTQWASWNGI LNFYKANEAY LQGQLGNPEG PDAPNKKYYD PRVWLRKMEE SMSKRLEQSF EDLNCVDVL // ID AMPN_HAEIN Reviewed; 869 AA. AC P45274; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 121. DE RecName: Full=Aminopeptidase N; DE EC=3.4.11.2; DE AltName: Full=Alpha-aminoacylpeptide hydrolase; GN Name=pepN; OrderedLocusNames=HI_1614; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129. RC STRAIN=Eagan / Serotype B; RX PubMed=7927773; RA McCrea K.W., Watson W.J., Gilsdorf J.R., Marrs C.F.; RT "Identification of hifD and hifE in the pilus gene cluster of RT Haemophilus influenzae type b strain Eagan."; RL Infect. Immun. 62:4922-4928(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28. RC STRAIN=AM30 (770235) / Serotype B; RX PubMed=7997179; DOI=10.1111/j.1365-2958.1994.tb00461.x; RA van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M.; RT "The fimbrial gene cluster of Haemophilus influenzae type b."; RL Mol. Microbiol. 13:673-684(1994). CC -!- FUNCTION: Aminopeptidase N is involved in the degradation of CC intracellular peptides generated by protein breakdown during CC normal growth as well as in response to nutrient starvation. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|- CC Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, CC but may be most amino acids including Pro (slow action). When a CC terminal hydrophobic residue is followed by a prolyl residue, the CC two may be released as an intact Xaa-Pro dipeptide. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M1 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; L42023; AAC23262.1; -; Genomic_DNA. DR EMBL; Z33502; CAA83910.1; -; Genomic_DNA. DR EMBL; U58657; AAB70877.1; -; Genomic_DNA. DR PIR; F64132; F64132. DR RefSeq; NP_439756.1; NC_000907.1. DR RefSeq; WP_005693625.1; NC_000907.1. DR ProteinModelPortal; P45274; -. DR SMR; P45274; 4-868. DR STRING; 71421.HI1614; -. DR PRIDE; P45274; -. DR EnsemblBacteria; AAC23262; AAC23262; HI_1614. DR GeneID; 950613; -. DR KEGG; hin:HI1614; -. DR PATRIC; 20191959; VBIHaeInf48452_1687. DR eggNOG; ENOG4105CD8; Bacteria. DR eggNOG; COG0308; LUCA. DR KO; K01256; -. DR OMA; FKRWYSQ; -. DR OrthoDB; EOG693GJ0; -. DR PhylomeDB; P45274; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central. DR GO; GO:0042277; F:peptide binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR Gene3D; 1.25.50.10; -; 1. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_N. DR InterPro; IPR012779; Peptidase_M1_pepN. DR InterPro; IPR024601; Peptidase_M1_pepN_C. DR PANTHER; PTHR11533; PTHR11533; 2. DR Pfam; PF11940; DUF3458; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR TIGRFAMs; TIGR02414; pepN_proteo; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Aminopeptidase; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Zinc. FT CHAIN 1 869 Aminopeptidase N. FT /FTId=PRO_0000095070. FT REGION 262 266 Substrate binding. {ECO:0000250}. FT ACT_SITE 299 299 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 298 298 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 302 302 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 321 321 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT BINDING 122 122 Substrate. {ECO:0000250}. FT SITE 382 382 Transition state stabilizer. FT {ECO:0000250}. FT CONFLICT 58 58 Q -> G (in Ref. 2). {ECO:0000305}. FT CONFLICT 93 93 I -> L (in Ref. 2). {ECO:0000305}. FT CONFLICT 121 121 C -> T (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 869 AA; 99786 MW; A00381DC6FB725D1 CRC64; MLAKAKYRKD YKQPDFTVTD IYLDFQLDPK HTVVTAITKF QRLNNEATSL CLDGHSFQFS SIKFNGEPFS DYQQDGESLT LDLKDKSADE FEIEIVTFLV PAENTSLQGL YQSGEGICTQ CEAEGFRQIT YMLDRPDVLA RYITKITADK TKYPFLLSNG NRIASGELED GRHWVEWNDP FPKPSYLFAL VAGDFDLLQD KFITKSGREV ALELYVDRGN LNRATWAMES LKKAMKWDED RFNLEYDLDI YMIVAVDFFN MGAMENKGLN IFNSKFVLAN PQTATDDDYL AIESVIAHEY FHNWTGNRVT CRDWFQLSLK EGLTVFRDQE FSSDTGSRAV NRINNVKFLR TVQFAEDASP MSHPIRPEKV IEMNNFYTVT VYEKGAEVIR MLHTLLGEQG FQKGMQLYIA ENDGKAATCE DFVSAMERAN NLDLNQFRRW YSQSGTPELL ISDAYDEKTH TYRLTVSQST PPTADQMEKV NLHIPLKVAL YDANGTKQML QHNGELLSDV LNVTEKDQVF EFHGIYGRPI PALLCDFSAP VKLDYDYKTE QLLGLLKFAD NQFIRWDAAQ MLFAQELRRN VVRFQQGEAL EISPEILTAL SYVLNHYEKD IELATLILTL PKEMEFAESF KTIDPDGISA ARAFMQAQIA ESLKDDFLRV YTHIRLNDYQ VTQQDIALRV MRNLCLTYLA YTNLGNNLVQ KHYNNANNMT DTLAALSVAT KAALLCRDVL LADFEQKWQH DGLVMDKWFA LQATRPDDNV LEIIQLLMDH PSFNFNNPNR LRSLVGSFAN HNLKAFHNVS GSGYRFLTDV LIRLNESNPQ VAARLIEPLI RFSRFDAQRQ TLMKRALERL SVVENLSKDL FEKIEKALQ // ID AMPP_HAEIN Reviewed; 430 AA. AC P44881; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=Xaa-Pro aminopeptidase; DE EC=3.4.11.9; DE AltName: Full=Aminoacylproline aminopeptidase; DE AltName: Full=Aminopeptidase P II; DE Short=APP-II; DE AltName: Full=X-Pro aminopeptidase; GN Name=pepP; OrderedLocusNames=HI_0816; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SUBUNIT: Homotetramer. {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; L42023; AAC22475.1; -; Genomic_DNA. DR PIR; B64096; B64096. DR RefSeq; NP_438976.1; NC_000907.1. DR RefSeq; WP_005693180.1; NC_000907.1. DR ProteinModelPortal; P44881; -. DR SMR; P44881; 7-429. DR STRING; 71421.HI0816; -. DR MEROPS; M24.004; -. DR EnsemblBacteria; AAC22475; AAC22475; HI_0816. DR GeneID; 949828; -. DR KEGG; hin:HI0816; -. DR PATRIC; 20190287; VBIHaeInf48452_0857. DR eggNOG; ENOG4107RAQ; Bacteria. DR eggNOG; COG0006; LUCA. DR KO; K01262; -. DR OMA; KDPLMET; -. DR OrthoDB; EOG6XHC3N; -. DR PhylomeDB; P44881; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. 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; IPR007865; Aminopep_P_N. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR028980; Creatinase/Aminopeptidase_P_N. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR Pfam; PF05195; AMP_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR SMART; SM01011; AMP_N; 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 1 430 Xaa-Pro aminopeptidase. FT /FTId=PRO_0000185076. FT METAL 254 254 Manganese 2. {ECO:0000250}. FT METAL 265 265 Manganese 1. {ECO:0000250}. FT METAL 265 265 Manganese 2. {ECO:0000250}. FT METAL 348 348 Manganese 1. {ECO:0000250}. FT METAL 377 377 Manganese 1. {ECO:0000250}. FT METAL 400 400 Manganese 1. {ECO:0000250}. FT METAL 400 400 Manganese 2. {ECO:0000250}. SQ SEQUENCE 430 AA; 49261 MW; 970C2CFFCB1FE2E6 CRC64; MELAYMAKLP KEEFEERRTR VFAQMQPNSA LLLFSEIEKR RNNDCTYPFR QDSYFWYLTG FNEPNAALLL LKTEQVEKAI IFLRPRDPLL ETWNGRRLGV ERAPQQLNVN EAYSIEEFAT VLPKILKNLT ALYHVPEIHT WGDTLVSESA VNFSEILDWR PMLSEMRLIK SPNEIRLMQQ AGQITALGHI KAMQTTRPNR FEYEIESDIL HEFNRHCARF PSYNSIVAGG SNACILHYTE NDRPLNDGDL VLIDAGCEFA MYAGDITRTF PVNGKFSQPQ REIYELVLKA QKRAIELLVP GNSIKQANDE VIRIKTQGLV DLGILKGDVD TLIEQQAYRQ FYMHGLGHWL GLDVHDVGSY GQDKQRILEI GMVITVEPGI YISEDADVPE QYKGIGVRIE DNLLMTEYGN KILTAAVPKE IADIENLMNF // ID ALKH_HAEIN Reviewed; 212 AA. AC P44480; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Putative KHG/KDPG aldolase; DE Includes: DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase; DE EC=4.1.3.16; DE AltName: Full=2-keto-4-hydroxyglutarate aldolase; DE Short=KHG-aldolase; DE Includes: DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase; DE EC=4.1.2.14; DE AltName: Full=2-keto-3-deoxy-6-phosphogluconate aldolase; DE Short=KDPG-aldolase; DE AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase; DE AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase; GN Name=eda; OrderedLocusNames=HI_0047; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-212. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- CATALYTIC ACTIVITY: 4-hydroxy-2-oxoglutarate = pyruvate + CC glyoxylate. CC -!- CATALYTIC ACTIVITY: 2-dehydro-3-deoxy-6-phosphate-D-gluconate = CC pyruvate + D-glyceraldehyde 3-phosphate. CC -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D- CC gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate CC from 2-dehydro-3-deoxy-D-gluconate: step 2/2. CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate CC metabolism. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the KHG/KDPG aldolase 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; L42023; AAC21725.1; -; Genomic_DNA. DR PIR; A64045; A64045. DR RefSeq; NP_438220.1; NC_000907.1. DR RefSeq; WP_005693874.1; NC_000907.1. DR PDB; 1VHC; X-ray; 1.89 A; A/B/C/D/E/F=2-212. DR PDBsum; 1VHC; -. DR ProteinModelPortal; P44480; -. DR SMR; P44480; 2-212. DR STRING; 71421.HI0047; -. DR EnsemblBacteria; AAC21725; AAC21725; HI_0047. DR GeneID; 950945; -. DR KEGG; hin:HI0047; -. DR PATRIC; 20188547; VBIHaeInf48452_0047. DR eggNOG; ENOG4108UHU; Bacteria. DR eggNOG; COG0800; LUCA. DR KO; K01625; -. DR OMA; SFRNRED; -. DR OrthoDB; EOG67DPKT; -. DR PhylomeDB; P44480; -. DR UniPathway; UPA00227; -. DR UniPathway; UPA00856; UER00829. DR EvolutionaryTrace; P44480; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR000887; Aldlse_KDPG_KHG. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR031337; KDPG/KHG_AS_1. DR InterPro; IPR031338; KDPG/KHG_AS_2. DR Pfam; PF01081; Aldolase; 1. DR TIGRFAMs; TIGR01182; eda; 1. DR PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1. DR PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lyase; KW Multifunctional enzyme; Reference proteome; Schiff base. FT CHAIN 1 212 Putative KHG/KDPG aldolase. FT /FTId=PRO_0000201041. FT ACT_SITE 45 45 {ECO:0000255|PROSITE-ProRule:PRU10118}. FT ACT_SITE 49 49 {ECO:0000255|PROSITE-ProRule:PRU10118}. FT ACT_SITE 133 133 Schiff-base intermediate with KHG or FT pyruvate. {ECO:0000255|PROSITE- FT ProRule:PRU10118}. FT HELIX 5 15 {ECO:0000244|PDB:1VHC}. FT STRAND 17 21 {ECO:0000244|PDB:1VHC}. FT HELIX 26 28 {ECO:0000244|PDB:1VHC}. FT HELIX 29 38 {ECO:0000244|PDB:1VHC}. FT STRAND 43 47 {ECO:0000244|PDB:1VHC}. FT HELIX 53 63 {ECO:0000244|PDB:1VHC}. FT STRAND 68 73 {ECO:0000244|PDB:1VHC}. FT HELIX 77 86 {ECO:0000244|PDB:1VHC}. FT STRAND 89 92 {ECO:0000244|PDB:1VHC}. FT HELIX 98 106 {ECO:0000244|PDB:1VHC}. FT HELIX 118 126 {ECO:0000244|PDB:1VHC}. FT STRAND 131 134 {ECO:0000244|PDB:1VHC}. FT TURN 135 141 {ECO:0000244|PDB:1VHC}. FT HELIX 142 150 {ECO:0000244|PDB:1VHC}. FT TURN 151 155 {ECO:0000244|PDB:1VHC}. FT STRAND 157 163 {ECO:0000244|PDB:1VHC}. FT TURN 166 168 {ECO:0000244|PDB:1VHC}. FT HELIX 169 173 {ECO:0000244|PDB:1VHC}. FT STRAND 181 183 {ECO:0000244|PDB:1VHC}. FT HELIX 185 187 {ECO:0000244|PDB:1VHC}. FT HELIX 189 193 {ECO:0000244|PDB:1VHC}. FT HELIX 197 211 {ECO:0000244|PDB:1VHC}. SQ SEQUENCE 212 AA; 22861 MW; 1D920F34AB4C14E3 CRC64; MSYTTQQIIE KLRELKIVPV IALDNADDIL PLADTLAKNG LSVAEITFRS EAAADAIRLL RANRPDFLIA AGTVLTAEQV VLAKSSGADF VVTPGLNPKI VKLCQDLNFP ITPGVNNPMA IEIALEMGIS AVKFFPAEAS GGVKMIKALL GPYAQLQIMP TGGIGLHNIR DYLAIPNIVA CGGSWFVEKK LIQSNNWDEI GRLVREVIDI IK // ID APAH_HAEIN Reviewed; 275 AA. AC P44751; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical; DE EC=3.6.1.41; DE AltName: Full=Ap4A hydrolase; DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase; DE AltName: Full=Diadenosine tetraphosphatase; GN Name=apaH; OrderedLocusNames=HI_0551; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to CC yield ADP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate + CC H(2)O = 2 ADP. CC -!- SIMILARITY: Belongs to the Ap4A hydrolase 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; L42023; AAC22209.1; -; Genomic_DNA. DR PIR; B64077; B64077. DR RefSeq; NP_438709.1; NC_000907.1. DR RefSeq; WP_005664434.1; NC_000907.1. DR ProteinModelPortal; P44751; -. DR SMR; P44751; 2-268. DR STRING; 71421.HI0551; -. DR EnsemblBacteria; AAC22209; AAC22209; HI_0551. DR GeneID; 950805; -. DR KEGG; hin:HI0551; -. DR PATRIC; 20189657; VBIHaeInf48452_0571. DR eggNOG; ENOG4105DDT; Bacteria. DR eggNOG; COG0639; LUCA. DR KO; K01525; -. DR OMA; INAFTRM; -. DR OrthoDB; EOG66B3WP; -. DR PhylomeDB; P44751; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 2. DR HAMAP; MF_00199; ApaH; 1. DR InterPro; IPR004617; ApaH. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00668; apaH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 275 Bis(5'-nucleosyl)-tetraphosphatase, FT symmetrical. FT /FTId=PRO_0000197993. SQ SEQUENCE 275 AA; 31908 MW; 95D6C22779DFDAA9 CRC64; MATYFVGDLQ GCYDELQLLL ERVDFNPTQD KLYLVGDLVA RGDKSLECLR FVKSLGNAAQ TVLGNHDLHL IATALDIKKV KPRDRVDAIF NAPDFDELIH WLRHQPLLVH NEKLNFLMSH AGISPDWDLK TAKSCAAEVE QILQHGDFHY LIENMYSEQP DRWSPDLQGL ARHRYIINAF TRMRFCYLDH RFDFACKSPL KDAPAELTPW FNLDNPLYKQ IPIVFGHWAS LVDEPTPKGI YALDTGCVWN NRMTMLRWED KQFFTQSAVK NYSDF // ID APBC_HAEIN Reviewed; 370 AA. AC P45135; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 17-FEB-2016, entry version 91. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040}; GN Name=mrp; OrderedLocusNames=HI_1277; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to CC target apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP- CC Rule:MF_02040}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {ECO:0000255|HAMAP-Rule:MF_02040}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22925.1; 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; L42023; AAC22925.1; ALT_INIT; Genomic_DNA. DR PIR; A64114; A64114. DR RefSeq; NP_439430.2; NC_000907.1. DR RefSeq; WP_010869171.1; NC_000907.1. DR ProteinModelPortal; P45135; -. DR STRING; 71421.HI1277; -. DR EnsemblBacteria; AAC22925; AAC22925; HI_1277. DR GeneID; 950197; -. DR KEGG; hin:HI1277; -. DR PATRIC; 20191233; VBIHaeInf48452_1328. DR eggNOG; ENOG4105D1F; Bacteria. DR eggNOG; COG0489; LUCA. DR KO; K03593; -. DR OMA; ATDCKLI; -. DR OrthoDB; EOG64XXQJ; -. DR PhylomeDB; P45135; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR000808; Mrp_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23264; PTHR23264; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01215; MRP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Iron; Iron-sulfur; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 370 Iron-sulfur cluster carrier protein. FT /FTId=PRO_0000184934. FT NP_BIND 115 122 ATP. {ECO:0000255|HAMAP-Rule:MF_02040}. SQ SEQUENCE 370 AA; 40046 MW; CA530C487D8B582B CRC64; MATYFSDNLT ADQQNQVQQI IQQFQHPTLQ KDLIVLNTLK KVEKGGDTLR IELQLPFAWN SGAEQLKQAV SDALLKATDC KLIKWAVAYQ IATLKRANNQ PAVKGVKNII AVSSGKGGVG KSSVSVNLAL ALQAQGARVG ILDADIYGPS IPHMLGAADQ RPTSPDNQHI TPIKAHGLSA NSIGFLMNED SATIWRGPMA SSALSQLLNE TLWDSLDYLV IDMPPGTGDI QLTLSQQIPV TGAVVVTTPQ DIALLDAVKG ISMFERVSVP VLGIVENMSM HICSECGHHE AIFGTGGAEK MAEKYNVKVL AQLPLHIRIR EDLDAGNPTV VRVPENEISQ AFLQLAEKVS TELYWQGSVI PSEILFKEVK // ID APHA_HAEIN Reviewed; 236 AA. AC P44009; P44730; P77869; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Class B acid phosphatase; DE Short=CBAP; DE EC=3.1.3.2 {ECO:0000250|UniProtKB:Q540U1}; DE Flags: Precursor; GN Name=aphA; Synonyms=napA; OrderedLocusNames=HI_0494/HI_0495; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CCUG 7317/A; RA Rossolini G.M., Bonci A., Schippa S., Iori P., Thaller M.C.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Dephosphorylates several organic phosphate monoesters. CC Also has a phosphotransferase activity catalyzing the transfer of CC low-energy phosphate groups from organic phosphate monoesters to CC free hydroxyl groups of various organic compounds (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol + CC phosphate. {ECO:0000250|UniProtKB:Q540U1}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q540U1}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:Q540U1}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class B bacterial acid phosphatase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22151.1; Type=Frameshift; Positions=66; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; CC Sequence=AAC22152.1; Type=Frameshift; Positions=66; Note=Produces two separate ORFs.; 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; L42023; AAC22151.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC22152.1; ALT_FRAME; Genomic_DNA. DR EMBL; Y07615; CAA68889.1; -; Genomic_DNA. DR PIR; T09434; T09434. DR RefSeq; NP_438653.1; NC_000907.1. DR ProteinModelPortal; P44009; -. DR STRING; 71421.HI0495m; -. DR EnsemblBacteria; AAC22151; AAC22151; HI_0494. DR EnsemblBacteria; AAC22152; AAC22152; HI_0495. DR GeneID; 950561; -. DR KEGG; hin:HI0495m; -. DR PATRIC; 20189539; VBIHaeInf48452_0512. DR eggNOG; ENOG4105F0S; Bacteria. DR eggNOG; COG3700; LUCA. DR KO; K03788; -. DR OrthoDB; EOG6HTNVZ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR005519; Acid_phosphat_B-like. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR010025; HAD-SF_ppase_IIIB_AphA. DR Pfam; PF03767; Acid_phosphat_B; 1. DR PIRSF; PIRSF017818; Acid_Ptase_B; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01672; AphA; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Periplasm; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 236 Class B acid phosphatase. FT /FTId=PRO_0000024005. FT REGION 136 137 Substrate binding. FT {ECO:0000250|UniProtKB:Q540U1}. FT ACT_SITE 67 67 Nucleophile. FT {ECO:0000250|UniProtKB:Q540U1}. FT ACT_SITE 69 69 Proton donor. FT {ECO:0000250|UniProtKB:Q540U1}. FT METAL 67 67 Magnesium. FT {ECO:0000250|UniProtKB:Q540U1}. FT METAL 69 69 Magnesium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:Q540U1}. FT METAL 191 191 Magnesium. FT {ECO:0000250|UniProtKB:Q540U1}. FT BINDING 176 176 Substrate. FT {ECO:0000250|UniProtKB:Q540U1}. FT CONFLICT 73 73 Missing (in Ref. 2; CAA68889). FT {ECO:0000305}. SQ SEQUENCE 236 AA; 26271 MW; D5D7091AC6BB4418 CRC64; MKNVMKLSVI ALLTAAAVPA MAGKTEPYTQ SGTNAREMLQ EQAIHWISVD QIKQSLEGKA PINVSFDIDD TVMLFSSPCF YHGQQKFSPG KHDYLKNQDF WNEVNAGCDK YSIPKQIAID LINMHQARGD QVYFFTGRTA GKVDGVTPIL EKTFNIKNMH PVEFMGSRER TTKYNKTPAI ISHKVSIHYG DSDDDVLAAK EAGVRGIRLM RAANSTYQPM PTLGGYGEEV LINSSY // ID ARCA_HAEIN Reviewed; 236 AA. AC P44918; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 108. DE RecName: Full=Aerobic respiration control protein ArcA homolog; GN Name=arcA; OrderedLocusNames=HI_0884; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Member of the two-component regulatory system ArcB/ArcA. CC Represses a wide variety of aerobic enzymes under anaerobic CC conditions (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- PTM: Phosphorylated by ArcB. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 OmpR/PhoB-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01091}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22542.1; -; Genomic_DNA. DR PIR; I64099; I64099. DR RefSeq; NP_439045.1; NC_000907.1. DR RefSeq; WP_005651417.1; NC_000907.1. DR ProteinModelPortal; P44918; -. DR SMR; P44918; 1-122. DR STRING; 71421.HI0884; -. DR PRIDE; P44918; -. DR EnsemblBacteria; AAC22542; AAC22542; HI_0884. DR GeneID; 949839; -. DR KEGG; hin:HI0884; -. DR PATRIC; 20190425; VBIHaeInf48452_0926. DR eggNOG; ENOG41065U4; Bacteria. DR eggNOG; COG0745; LUCA. DR KO; K07773; -. DR OMA; TDGSEMH; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P44918; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CACAO. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; Phosphoprotein; KW Reference proteome; Repressor; Transcription; KW Transcription regulation; Two-component regulatory system. FT CHAIN 1 236 Aerobic respiration control protein ArcA FT homolog. FT /FTId=PRO_0000081012. FT DOMAIN 5 118 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DNA_BIND 133 233 OmpR/PhoB-type. {ECO:0000255|PROSITE- FT ProRule:PRU01091}. FT MOD_RES 54 54 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 236 AA; 27424 MW; 3FB2AE2980E27F01 CRC64; MTTPKILVVE DEIVTRNTLK GIFEAEGYDV FEAENGVEMH HILANHNINL VVMDINLPGK NGLLLARELR EELSLPLIFL TGRDNEVDKI LGLEIGADDY LTKPFNPREL TIRARNLLHR AMPHQEKENT FGREFYRFNG WKLDLNSHSL ITPEGQEFKL PRSEFRAMLH FCENPGKLQT REELLKKMTG RELKPQDRTV DVTIRRIRKH FEDHPNTPNI IMTIHGEGYR FCGDIE // ID AMIB_HAEIN Reviewed; 432 AA. AC P44493; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Probable N-acetylmuramoyl-L-alanine amidase AmiB; DE EC=3.5.1.28; DE Flags: Precursor; GN Name=amiB; OrderedLocusNames=HI_0066; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during CC cell division. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl CC residues and L-amino acid residues in certain cell-wall CC glycopeptides. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan CC binding. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 LysM domains. {ECO:0000255|PROSITE- CC ProRule:PRU01118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21744.1; -; Genomic_DNA. DR PIR; D64046; D64046. DR RefSeq; NP_438239.1; NC_000907.1. DR RefSeq; WP_005693856.1; NC_000907.1. DR ProteinModelPortal; P44493; -. DR STRING; 71421.HI0066; -. DR EnsemblBacteria; AAC21744; AAC21744; HI_0066. DR GeneID; 950965; -. DR KEGG; hin:HI0066; -. DR PATRIC; 20188587; VBIHaeInf48452_0067. DR eggNOG; ENOG4105C5C; Bacteria. DR eggNOG; COG0860; LUCA. DR eggNOG; COG1388; LUCA. DR KO; K01448; -. DR OMA; NNRTSEQ; -. DR OrthoDB; EOG6CP3X3; -. DR PhylomeDB; P44493; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.10.350.10; -; 2. DR Gene3D; 3.40.630.40; -; 2. DR InterPro; IPR002508; CW_Hdrlase/autolysin_cat. DR InterPro; IPR018392; LysM_dom. DR Pfam; PF01520; Amidase_3; 1. DR Pfam; PF01476; LysM; 2. DR SMART; SM00646; Ami_3; 1. DR SMART; SM00257; LysM; 2. DR SUPFAM; SSF54106; SSF54106; 2. DR PROSITE; PS51782; LYSM; 2. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation; Complete proteome; Hydrolase; KW Periplasm; Reference proteome; Repeat; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 432 Probable N-acetylmuramoyl-L-alanine FT amidase AmiB. FT /FTId=PRO_0000006464. FT DOMAIN 292 335 LysM 1. {ECO:0000255|PROSITE- FT ProRule:PRU01118}. FT DOMAIN 385 429 LysM 2. {ECO:0000255|PROSITE- FT ProRule:PRU01118}. SQ SEQUENCE 432 AA; 49109 MW; 008D918A0E1EE81D CRC64; MKTKILFFLF FSTFSFSIFA APITIAIDPG HGGKDPGAIS RNLGIYEKNV TLSIAKELKA LLDKDPHFRG VLTRKSDYYI SVPERSEIAR KFKANYLISI HADSSKSPDR RGASVWVLSN RRANDEMGQW LEDDEKRSEL LGGAGKVLSH NNDKYLDQTV LDLQFGHSQR TGYVLGEHIL HHFAKVTTLS RSTPQHASLG VLRSPDIPSV LVETGFLSNS EEEKKLNSQT YRRRIAYMIY EGLVAFHSGK TNTLVKDNLV QNIKQNDIKK SGKNNRTSEQ NINEDNIKDS GIRHIVKKGE SLGSLSNKYH VKVSDIIKLN QLKRKTLWLN ESIKIPDNVE IKNKSLTIKE NDFHKKQNSL VNNTNKDLKK EKNTQTNNQK NIIPLYHKVT KNQTLYAISR EYNIPVNILL SLNPHLKNGK VITGQKIKLR EK // ID API_HAEIN Reviewed; 337 AA. AC P45313; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Probable arabinose 5-phosphate isomerase; DE Short=API; DE EC=5.3.1.13; GN OrderedLocusNames=HI_1678; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization CC between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate CC (A5P). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-arabinose 5-phosphate = D-ribulose 5- CC phosphate. CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23324.1; -; Genomic_DNA. DR PIR; C64136; C64136. DR RefSeq; NP_439820.1; NC_000907.1. DR RefSeq; WP_005694401.1; NC_000907.1. DR ProteinModelPortal; P45313; -. DR STRING; 71421.HI1678; -. DR EnsemblBacteria; AAC23324; AAC23324; HI_1678. DR GeneID; 950863; -. DR KEGG; hin:HI1678; -. DR PATRIC; 20192107; VBIHaeInf48452_1757. DR eggNOG; ENOG4105C2X; Bacteria. DR eggNOG; COG0517; LUCA. DR eggNOG; COG0794; LUCA. DR KO; K06041; -. DR OMA; ADFAKFH; -. DR OrthoDB; EOG6RFZWS; -. DR PhylomeDB; P45313; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR004800; KdsD/KpsF-type. DR InterPro; IPR001347; SIS. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01380; SIS; 1. DR PIRSF; PIRSF004692; KdsD_KpsF; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR00393; kpsF; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; CBS domain; Complete proteome; Isomerase; KW Metal-binding; Reference proteome; Repeat; Zinc. FT CHAIN 1 337 Probable arabinose 5-phosphate isomerase. FT /FTId=PRO_0000136582. FT DOMAIN 58 201 SIS. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT DOMAIN 227 284 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 292 337 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT REGION 92 93 Substrate binding. {ECO:0000250}. FT REGION 131 140 Substrate binding. {ECO:0000250}. FT REGION 165 167 Substrate binding. {ECO:0000250}. FT METAL 99 99 Zinc. {ECO:0000250}. FT BINDING 99 99 Substrate. {ECO:0000250}. FT BINDING 105 105 Substrate. {ECO:0000250}. FT BINDING 237 237 Substrate. {ECO:0000250}. FT BINDING 290 290 Substrate. {ECO:0000250}. FT SITE 76 76 Catalytically relevant. {ECO:0000250}. FT SITE 128 128 Catalytically relevant. {ECO:0000250}. FT SITE 169 169 Catalytically relevant. {ECO:0000250}. FT SITE 210 210 Catalytically relevant. {ECO:0000250}. SQ SEQUENCE 337 AA; 36655 MW; 6A12AC7A87DB061C CRC64; MPNFSFVFFY DSAKITPIST ALLGRRMNYL KIAQDSLSVE SNALLQLSQR LGDDFNQVID LILACEGRLV IGGIGKSGLI GKKMVATFAS TGTPSFFLHP TEAFHGDLGM LKPIDIVMLI SYSGETDDVN KLIPSLKNFG NKIIAVTSNK NSTLARHADY VLDITVEREV CPNNLAPTTS ALVTLALGDA LAVSLITARN FQPADFAKFH PGGSLGRRLL CKVKDQMQTR LPTILPTTNF TDCLTVMNEG RMGVALVMEN EQLKGIITDG DIRRALTANG AGTLNKTAKD FMTSSPKTIH QDEFLSKAED FMKAKKIHSL VVVNDENHVV GLVEFSS // ID ARGR_HAEIN Reviewed; 151 AA. AC P45110; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 111. DE RecName: Full=Arginine repressor; GN Name=argR; OrderedLocusNames=HI_1209; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis CC [regulation]. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22863.1; -; Genomic_DNA. DR PIR; B64110; B64110. DR RefSeq; NP_439365.1; NC_000907.1. DR RefSeq; WP_005691176.1; NC_000907.1. DR ProteinModelPortal; P45110; -. DR SMR; P45110; 3-73, 76-148. DR STRING; 71421.HI1209; -. DR EnsemblBacteria; AAC22863; AAC22863; HI_1209. DR GeneID; 950154; -. DR KEGG; hin:HI1209; -. DR PATRIC; 20191097; VBIHaeInf48452_1261. DR eggNOG; ENOG410682Y; Bacteria. DR eggNOG; COG1438; LUCA. DR KO; K03402; -. DR OMA; LNQERFG; -. DR OrthoDB; EOG6Z9B6J; -. DR PhylomeDB; P45110; -. DR UniPathway; UPA00068; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034618; F:arginine binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051259; P:protein oligomerization; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR HAMAP; MF_00173; Arg_repressor; 1. DR InterPro; IPR001669; Arg_repress. DR InterPro; IPR020899; Arg_repress_C. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR020900; Arg_repress_DNA-bd. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01316; Arg_repressor; 1. DR Pfam; PF02863; Arg_repressor_C; 1. DR PRINTS; PR01467; ARGREPRESSOR. DR ProDom; PD007402; Arg_repress; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55252; SSF55252; 1. DR TIGRFAMs; TIGR01529; argR_whole; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; DNA-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 151 Arginine repressor. FT /FTId=PRO_0000205093. SQ SEQUENCE 151 AA; 16720 MW; F7AD4FABA1B6E805 CRC64; MTENLTRAFK ELLNQERFGS QSEIVDALKK QGFTGINQSK ISRMLSKFGA VRTRNTKMEM VYCLPNELSV PNTSSPLKNL VLDVDHNAML IVIKTTPGAA QLIARLLDSI GKSEGILGTI AGDDTIFVTP TNNKPIDELL QNIQRLFENT L // ID APT_HAEIN Reviewed; 180 AA. AC P43856; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. 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=HI_1230; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22883.1; -; Genomic_DNA. DR PIR; G64111; G64111. DR RefSeq; NP_439386.1; NC_000907.1. DR RefSeq; WP_005650156.1; NC_000907.1. DR ProteinModelPortal; P43856; -. DR SMR; P43856; 4-180. DR STRING; 71421.HI1230; -. DR EnsemblBacteria; AAC22883; AAC22883; HI_1230. DR GeneID; 950707; -. DR KEGG; hin:HI1230; -. DR PATRIC; 20191139; VBIHaeInf48452_1282. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR PhylomeDB; P43856; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000579; 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_0000149391. SQ SEQUENCE 180 AA; 19710 MW; 1E00D7165FE55ABA CRC64; MTTQLDLIKS SIKSIPNYPK EGIIFRDITT LLEVPAAFKA TIDLIVEQYR DKGITKVLGT ESRGFIFGAP VALALGLPFE LVRKPKKLPR ETISQSYQLE YGQDTLEMHV DAISEGDNVL IIDDLLATGG TVEATVKLVQ RLGGAVKHAA FVINLPELGG EKRLNNLGVD CYTLVNFEGH // ID ARCB_HAEIN Reviewed; 325 AA. AC P44578; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Aerobic respiration control sensor protein ArcB homolog; DE EC=2.7.13.3; GN Name=arcB; OrderedLocusNames=HI_0220; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Member of the two-component regulatory system ArcB/ArcA. CC Activates ArcA by phosphorylation (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; G64055; G64055. DR ProteinModelPortal; P44578; -. DR OMA; RHTETIK; -. DR BRENDA; 2.7.13.3; 2529. DR Proteomes; UP000000579; 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 1.10.287.970; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR027460; ArcB_TM. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Transferase; Transmembrane; Transmembrane helix; KW Two-component regulatory system. FT CHAIN 1 325 Aerobic respiration control sensor FT protein ArcB homolog. FT /FTId=PRO_0000074686. FT TOPO_DOM 1 26 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TOPO_DOM 48 57 Periplasmic. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TOPO_DOM 79 325 Cytoplasmic. {ECO:0000255}. FT DOMAIN 128 325 Histidine kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00107}. FT MOD_RES 131 131 Phosphohistidine; by autocatalysis. FT {ECO:0000255|PROSITE-ProRule:PRU00107}. SQ SEQUENCE 325 AA; 37249 MW; 5D1E952870CCA21B CRC64; MKNFKYFAQS YVDWVIRLGR LRFSLLGVMI LAVLALCTQI LFSLFIVHQI SWVDIFRSVT FGLLTAPFVI YFFTLLVEKL EHSRLDLSSS VNRLENEVAE RIAAQKKLSQ ALEKLEKNSR DKSTLLATIS HEFRTPLNGI VGLSQILLDD ELDDLQRNYL KTINISAVSL GYIFSDIIDL EKIDASRIEL NRQPTDFPAL LNDIYNFASF LAKEKNLIFS LELEPNLPNW LNLDRVRLSQ ILWNLISNAV KFTDQGNIIL KIMRNQDCYH FIVKDTGMGI SPEEQKHIFE MYYQVKESRQ QSAGSGIGLA ISKNLAQLMG RGFNS // ID APBE_HAEIN Reviewed; 346 AA. AC P44550; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=FAD:protein FMN transferase {ECO:0000250|UniProtKB:A5F5Y3}; DE EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3}; DE AltName: Full=Flavin transferase {ECO:0000250|UniProtKB:A5F5Y3}; DE Flags: Precursor; GN Name=apbE; OrderedLocusNames=HI_0172; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the CC FMN moiety of FAD and its covalent binding to the hydroxyl group CC of a threonine residue in a target flavoprotein such as NqrB and CC NqrC, two subunits of the NQR complex. CC {ECO:0000250|UniProtKB:A5F5Y3}. CC -!- CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L- CC threonine + AMP. {ECO:0000250|UniProtKB:A5F5Y3}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:A5F5Y3}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000250|UniProtKB:P41780, CC ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side CC {ECO:0000250|UniProtKB:P41780}. CC -!- SIMILARITY: Belongs to the ApbE 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; L42023; AAC21842.1; -; Genomic_DNA. DR PIR; C64144; C64144. DR RefSeq; NP_438340.1; NC_000907.1. DR RefSeq; WP_005668096.1; NC_000907.1. DR ProteinModelPortal; P44550; -. DR STRING; 71421.HI0172; -. DR EnsemblBacteria; AAC21842; AAC21842; HI_0172. DR GeneID; 951081; -. DR KEGG; hin:HI0172; -. DR PATRIC; 20188839; VBIHaeInf48452_0176. DR eggNOG; ENOG4105CJ2; Bacteria. DR eggNOG; COG1477; LUCA. DR KO; K03734; -. DR OMA; INIKAYG; -. DR OrthoDB; EOG6CGCF7; -. DR PhylomeDB; P44550; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0017013; P:protein flavinylation; IEA:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like. DR Pfam; PF02424; ApbE; 1. DR PIRSF; PIRSF006268; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; FAD; KW Flavoprotein; Lipoprotein; Magnesium; Membrane; Metal-binding; KW Palmitate; Reference proteome; Signal; Transferase. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 346 FAD:protein FMN transferase. FT /FTId=PRO_0000001749. FT NP_BIND 115 117 FAD. {ECO:0000250|UniProtKB:P41780}. FT METAL 180 180 Magnesium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P0AB85}. FT METAL 295 295 Magnesium. FT {ECO:0000250|UniProtKB:O83774}. FT METAL 299 299 Magnesium. FT {ECO:0000250|UniProtKB:O83774}. FT BINDING 34 34 FAD; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P41780}. FT BINDING 73 73 FAD. {ECO:0000250|UniProtKB:P41780}. FT BINDING 177 177 FAD. {ECO:0000250|UniProtKB:P41780}. FT BINDING 183 183 FAD. {ECO:0000250|UniProtKB:O83774}. FT BINDING 269 269 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250|UniProtKB:P41780}. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 346 AA; 37780 MW; 6A9D0E5DF5877B61 CRC64; MKKLISGIIA VAMALSLAAC QKETKVISLS GKTMGTTYHV KYLDDGSITA TSEKTHEEIE AILKDVNAKM STYKKDSELS RFNQNTQVNT PIEISADFAK VLAEAIRLNK VTEGALDVTV GPVVNLWGFG PEKRPEKQPT PEQLAERQAW VGIDKITLDT NKEKATLSKA LPQVYVDLSS IAKGFGVDQV AEKLEQLNAQ NYMVEIGGEI RAKGKNIEGK PWQIAIEKPT TTGERAVEAV IGLNNMGMAS SGDYRIYFEE NGKRFAHEID PKTGYPIQHH LASITVLAPT SMTADGLSTG LFVLGEDKAL EVAEKNNLAV YLIIRTDNGF VTKSSSAFKK LTETKE // ID ARCC_HAEIN Reviewed; 310 AA. AC P44769; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Carbamate kinase; DE EC=2.7.2.2; GN Name=arcC; OrderedLocusNames=HI_0595; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + NH(3) + CO(2) = ADP + carbamoyl CC phosphate. CC -!- PATHWAY: Metabolic intermediate metabolism; carbamoyl phosphate CC degradation; CO(2) and NH(3) from carbamoyl phosphate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the carbamate 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; L42023; AAC22252.1; -; Genomic_DNA. DR PIR; G64079; G64079. DR RefSeq; NP_438752.1; NC_000907.1. DR RefSeq; WP_005694569.1; NC_000907.1. DR ProteinModelPortal; P44769; -. DR STRING; 71421.HI0595; -. DR EnsemblBacteria; AAC22252; AAC22252; HI_0595. DR GeneID; 949637; -. DR KEGG; hin:HI0595; -. DR PATRIC; 20189747; VBIHaeInf48452_0616. DR eggNOG; ENOG4105C5B; Bacteria. DR eggNOG; COG0549; LUCA. DR KO; K00926; -. DR OMA; QIAKIHP; -. DR OrthoDB; EOG65QWKX; -. DR PhylomeDB; P44769; -. DR UniPathway; UPA00996; UER00366. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008804; F:carbamate kinase activity; IBA:GO_Central. DR GO; GO:0019546; P:arginine deiminase pathway; IBA:GO_Central. DR GO; GO:0035975; P:carbamoyl phosphate catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR003964; Carb_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000723; Carbamate_kin; 1. DR PRINTS; PR01469; CARBMTKINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00746; arcC; 1. PE 3: Inferred from homology; KW Arginine metabolism; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 310 Carbamate kinase. FT /FTId=PRO_0000185125. SQ SEQUENCE 310 AA; 33440 MW; E86DB86848377425 CRC64; MRIVIALGGN ALLRRGEPMT AENQRQNVRI ACEQIAKIWP NNELVIAHGN GPQVGLLALQ GAAYTDVPTY PLDVLGAETA GMIGYMIQQE LGNLVPFEVP FATLLSQVEV DINDPAFKNP TKPIGPVYTK EEAERLAKEK NWSIAQDGDK YRRVVPSPLP KRIFEIRPVK WLLEKGSIVI CAGGGGIPTY YDEHHNLQGV EAVIDKDLCS ALLAENLDAD LFIIATDVSA TFVDWGKPNQ KAISVASPEA ISELGFASGS MGPKVQAAIN FAKQTGKDAV IGSLSDIVDI VKGKAGTRIT KKTEGISYYA // ID ARFA_HAEIN Reviewed; 69 AA. AC P44588; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Alternative ribosome-rescue factor A; GN Name=arfA; OrderedLocusNames=HI_0235; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Rescues the ribosomes stalled at the 3' end of non-stop CC mRNAs. May induce hydrolysis of the ribosome-bound peptidyl-tRNA CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with the 50S ribosomal subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the alternative ribosome-rescue factor A 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; L42023; AAC21905.1; -; Genomic_DNA. DR PIR; I64145; I64145. DR RefSeq; NP_438406.1; NC_000907.1. DR RefSeq; WP_005648813.1; NC_000907.1. DR STRING; 71421.HI0235; -. DR DNASU; 951152; -. DR EnsemblBacteria; AAC21905; AAC21905; HI_0235. DR GeneID; 951152; -. DR KEGG; hin:HI0235; -. DR PATRIC; 20188995; VBIHaeInf48452_0250. DR eggNOG; COG3036; LUCA. DR KO; K09890; -. DR OMA; WEANDDN; -. DR OrthoDB; EOG6V1M8M; -. DR PhylomeDB; P44588; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR InterPro; IPR005589; DUF331. DR Pfam; PF03889; DUF331; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Translation regulation. FT CHAIN 1 69 Alternative ribosome-rescue factor A. FT /FTId=PRO_0000169495. SQ SEQUENCE 69 AA; 8154 MW; 786EC512B63540B1 CRC64; MRKKQKSAVE NETVYLHTRG VIKDNAVMAL LGDKLFRQRV EKKRKGKGSY QRKAKHPGKI FEKPDYKFF // ID AROK_HAEIN Reviewed; 180 AA. AC P43880; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00109}; DE Short=SK {ECO:0000255|HAMAP-Rule:MF_00109}; DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00109}; GN Name=aroK {ECO:0000255|HAMAP-Rule:MF_00109}; GN OrderedLocusNames=HI_0207; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00109}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00109}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21875.1; -; Genomic_DNA. DR PIR; F64054; F64054. DR RefSeq; NP_438376.1; NC_000907.1. DR RefSeq; WP_005648746.1; NC_000907.1. DR ProteinModelPortal; P43880; -. DR SMR; P43880; 3-171. DR STRING; 71421.HI0207; -. DR EnsemblBacteria; AAC21875; AAC21875; HI_0207. DR GeneID; 951112; -. DR KEGG; hin:HI0207; -. DR PATRIC; 20188911; VBIHaeInf48452_0212. DR eggNOG; ENOG4105KHV; Bacteria. DR eggNOG; COG0703; LUCA. DR KO; K00891; -. DR OMA; FEQHGEA; -. DR OrthoDB; EOG6SJJGD; -. DR PhylomeDB; P43880; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000000579; 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; IBA:GO_Central. DR GO; GO:0004765; F:shikimate kinase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR InterPro; IPR023000; Shikimate_kinase_CS. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 180 Shikimate kinase. FT /FTId=PRO_0000192385. FT NP_BIND 14 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00109}. FT METAL 18 18 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 36 36 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 60 60 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 82 82 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00109}. FT BINDING 120 120 ATP. {ECO:0000255|HAMAP-Rule:MF_00109}. FT BINDING 140 140 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00109}. FT BINDING 157 157 ATP. {ECO:0000255|HAMAP-Rule:MF_00109}. SQ SEQUENCE 180 AA; 20292 MW; E430C65F542B0C84 CRC64; MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM DFIDSDAVIE ERTGADISWI FDLEGEDGFR KREERIINEL TQMQGIVLST GGGAVLSKEN RNYLSARGIV IYLETTVEKQ FQRTQRDKKR PLLQDAENPR QVLEDLAKIR NPLYEEIADI TLPTDEQNAK IMVNQIVDLI DNMNGLNGAL // ID AROG_HAEIN Reviewed; 362 AA. AC P44303; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase; DE EC=2.5.1.54; DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase; DE AltName: Full=DAHP synthase; DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase; GN Name=aroG; OrderedLocusNames=HI_1547; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) CC and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D- CC arabino-heptulosonate-7-phosphate (DAHP). CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + D-erythrose 4-phosphate CC + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + CC phosphate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 1/7. CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23197.1; -; Genomic_DNA. DR PIR; I64128; I64128. DR RefSeq; NP_439696.1; NC_000907.1. DR RefSeq; WP_010869242.1; NC_000907.1. DR ProteinModelPortal; P44303; -. DR SMR; P44303; 12-357. DR STRING; 71421.HI1547; -. DR PRIDE; P44303; -. DR EnsemblBacteria; AAC23197; AAC23197; HI_1547. DR GeneID; 950411; -. DR KEGG; hin:HI1547; -. DR PATRIC; 20191819; VBIHaeInf48452_1618. DR eggNOG; ENOG4105E99; Bacteria. DR eggNOG; COG0722; LUCA. DR KO; K01626; -. DR OMA; DGCIDWA; -. DR OrthoDB; EOG63JR9W; -. DR PhylomeDB; P44303; -. DR UniPathway; UPA00053; UER00084. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR InterPro; IPR006219; DHAP_synth_1. DR PANTHER; PTHR21225; PTHR21225; 1. DR Pfam; PF00793; DAHP_synth_1; 1. DR PIRSF; PIRSF001361; DAHP_synthase; 1. DR TIGRFAMs; TIGR00034; aroFGH; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 362 Phospho-2-dehydro-3-deoxyheptonate FT aldolase. FT /FTId=PRO_0000140830. SQ SEQUENCE 362 AA; 39937 MW; 533B76F7B379CD2D CRC64; MAKEKIEIVV ANDDTRIEKV DQVLPPIALL EKYPASEQAA ALVKQTRHEA HNIIHGKDDR LLVVIGPCSI HDPKAAIEYA TRLKPLREKY KDSLEIIMRV YFEKPRTTVG WKGLINEPYL NDTYRLNDGL RIARKLLSDI NDLGVPAAGE FLDMITPQYL ADFMSWGAIG ARTTESQVHR ELASGLSCAV GFKNATNGGV KVALDAIGAA EAPHYFLSVT KFGHSAIVST KGNEDCHIIL RGGDKGPNYS AEDVEKVCAD IEKTGRIPHV MVDFSHANSS KQYKKQMDVC QDVCNQIAFG SKQIFGVMVE SHLVEGRQDL VDGKAQTYGQ SITDACIGWE DSERLLQQLS DAVIARRKAT SN // ID ARTI_HAEIN Reviewed; 239 AA. AC P45091; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=ABC transporter arginine-binding protein; DE Flags: Precursor; GN Name=artI; OrderedLocusNames=HI_1179; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). RN [3] RP PROTEIN SEQUENCE OF 20-24. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the ABC transporter complex ArtPIQM involved in CC arginine transport. {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute- CC binding protein (ArtI). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 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; L42023; AAC22830.1; -; Genomic_DNA. DR EMBL; U17295; AAA95978.1; -; Genomic_DNA. DR PIR; C64188; C64188. DR RefSeq; NP_439335.1; NC_000907.1. DR RefSeq; WP_005694262.1; NC_000907.1. DR ProteinModelPortal; P45091; -. DR STRING; 71421.HI1179; -. DR EnsemblBacteria; AAC22830; AAC22830; HI_1179. DR GeneID; 950269; -. DR KEGG; hin:HI1179; -. DR PATRIC; 20191035; VBIHaeInf48452_1230. DR eggNOG; ENOG4106PMH; Bacteria. DR eggNOG; COG0834; LUCA. DR KO; K09997; -. DR OMA; CKFKSET; -. DR OrthoDB; EOG62VNJH; -. DR PhylomeDB; P45091; -. DR PRO; PR:P45091; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR InterPro; IPR005768; Lys_Arg_Orn-bd. DR InterPro; IPR018313; SBP_3_CS. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00062; PBPb; 1. DR TIGRFAMs; TIGR01096; 3A0103s03R; 1. DR PROSITE; PS01039; SBP_BACTERIAL_3; 1. PE 1: Evidence at protein level; KW Amino-acid transport; Complete proteome; Direct protein sequencing; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 19 {ECO:0000269|PubMed:10675023}. FT CHAIN 20 239 ABC transporter arginine-binding protein. FT /FTId=PRO_0000031753. SQ SEQUENCE 239 AA; 26022 MW; F8A25DF801E697F3 CRC64; MKKTLLTAIL LGASVAASAQ ELTFAMQPSY PPFETTNAKG EIIGFDVDVT NAICQEIQAT CKFKSETFDA LIPNLKAKRF DAAISAIDIT DARAKQVLFS DAYYDSSASY VALKGKATLE SAKNIGVQNG TTFQQYTVAE TKQYSPKSYA SLQNAILDLK SGRIDIIFGD TAVLADMISK EPEIQFIGEK VTNKKYFGNG LGIAMHKSNK DLAAQLNKGL AAIKANGEYQ KIYDKWITK // ID ARTM_HAEIN Reviewed; 227 AA. AC P45089; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Arginine ABC transporter permease protein ArtM; GN Name=artM; OrderedLocusNames=HI_1177; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the ABC transporter complex ArtPIQM involved in CC arginine transport. Probably responsible for the translocation of CC the substrate across the membrane (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute- CC binding protein (ArtI). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. HisMQ 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; L42023; AAC22828.1; -; Genomic_DNA. DR EMBL; U17295; AAA95980.1; -; Genomic_DNA. DR PIR; A64188; A64188. DR RefSeq; NP_439333.1; NC_000907.1. DR RefSeq; WP_005694264.1; NC_000907.1. DR ProteinModelPortal; P45089; -. DR STRING; 71421.HI1177; -. DR EnsemblBacteria; AAC22828; AAC22828; HI_1177. DR GeneID; 950131; -. DR KEGG; hin:HI1177; -. DR PATRIC; 20191031; VBIHaeInf48452_1228. DR eggNOG; ENOG4105DMR; Bacteria. DR eggNOG; COG4160; LUCA. DR KO; K09998; -. DR OMA; MNEQHVW; -. DR OrthoDB; EOG6MM1R5; -. DR PhylomeDB; P45089; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 227 Arginine ABC transporter permease protein FT ArtM. FT /FTId=PRO_0000059964. FT TRANSMEM 17 37 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 51 71 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 78 98 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 155 175 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 188 208 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 13 209 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT CONFLICT 99 99 A -> R (in Ref. 2; AAA95980). FT {ECO:0000305}. SQ SEQUENCE 227 AA; 25213 MW; 6AC67F3B9F5464B1 CRC64; MFQEYLSVIV KGIPTSLLLT VVSLLIAFFL ALFLTFLLSM ENKWIKSAVN LYLTLFTGTP LLVQFFLIYA GPGQFQWIID SPLWYVLSNA WFCAALALAL NSAAYSTQLF HGAVKAIPKG QWESCGALGL NRIQTLKILI PYALKRALPS YSNEIILVFK GTALASTITI MDIMGYARQL YGTEYDALTI YGIAGGIYLI ITGIATLLLR KLEKKVLAFE RFEVSKA // ID ARLY_HAEIN Reviewed; 457 AA. AC P44314; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 119. DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006}; DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006}; DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006}; DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006}; GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; GN OrderedLocusNames=HI_0811; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate + CC L-arginine. {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 3/3. CC {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22470.1; -; Genomic_DNA. DR PIR; F64095; F64095. DR RefSeq; NP_438971.1; NC_000907.1. DR RefSeq; WP_005693177.1; NC_000907.1. DR ProteinModelPortal; P44314; -. DR SMR; P44314; 3-457. DR STRING; 71421.HI0811; -. DR EnsemblBacteria; AAC22470; AAC22470; HI_0811. DR GeneID; 949824; -. DR KEGG; hin:HI0811; -. DR PATRIC; 20190277; VBIHaeInf48452_0852. DR eggNOG; ENOG4105CH7; Bacteria. DR eggNOG; COG0165; LUCA. DR KO; K01755; -. DR OMA; AHHLMAY; -. DR OrthoDB; EOG6P5ZF8; -. DR PhylomeDB; P44314; -. DR UniPathway; UPA00068; UER00114. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR HAMAP; MF_00006; Arg_succ_lyase; 1. DR InterPro; IPR029419; Arg_succ_lyase_C. DR InterPro; IPR009049; Argininosuccinate_lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1. DR Pfam; PF14698; ASL_C2; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00838; argH; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Lyase; Reference proteome. FT CHAIN 1 457 Argininosuccinate lyase. FT /FTId=PRO_0000137776. SQ SEQUENCE 457 AA; 51217 MW; 51272D516BC1FE6B CRC64; MALWGGRFTQ AADKRFKDFN DSLRFDYRLA EQDIQGSIGW SKALVKVNVL TIEEQHQLEQ ALNELLVEVR SNPQAILQDD AEDIHSWVES KLIDKVGNLG KKLHTGRSRN DQVAVDIKLW CKQRVIELQE SVRNLQRHLV QTAENTQQAV MPGYTHLQRA QPITFAHWCM AYVEMFDRDY SRLTDAYNRM NTCPLGSGAL AGTAYAVDRD SLAHDLSFAF ATRNSLDSVS DRDHIVELLS IASLSMAHLS RFAEDMIIFN SGEANFVELS DRVTSGSSLM PQKKNPDACE LIRGKTGRVI GSLTSMLITL KGLPLAYNKD MQEDKEGIFD ALDTWQNCVD MATFVLDELK VNVERTREAA LKGYSNATEL ADYLVSKGVP FRDSHHIVGE TVVYAIEKGK GLEDLTIPEF RQFSEVVGDD VYEILSLQSC LDKRCAKGGV SPLRVAEAIA EAKTRFA // ID AROC_HAEIN Reviewed; 357 AA. AC P43875; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; GN OrderedLocusNames=HI_0196; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21865.1; -; Genomic_DNA. DR PIR; G64053; G64053. DR RefSeq; NP_438365.1; NC_000907.1. DR RefSeq; WP_005694095.1; NC_000907.1. DR ProteinModelPortal; P43875; -. DR STRING; 71421.HI0196; -. DR EnsemblBacteria; AAC21865; AAC21865; HI_0196. DR GeneID; 951107; -. DR KEGG; hin:HI0196; -. DR PATRIC; 20188889; VBIHaeInf48452_0201. DR eggNOG; ENOG4105D10; Bacteria. DR eggNOG; COG0082; LUCA. DR KO; K01736; -. DR OMA; MLSINAV; -. DR OrthoDB; EOG6WDSHT; -. DR PhylomeDB; P43875; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP; KW Reference proteome. FT CHAIN 1 357 Chorismate synthase. FT /FTId=PRO_0000140594. FT NP_BIND 125 127 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 243 244 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 298 302 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 48 48 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 54 54 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 283 283 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 324 324 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. SQ SEQUENCE 357 AA; 38691 MW; 4504562BADF68164 CRC64; MAGNTIGQLF RVTTFGESHG IALGCIVDGV PPNLELSEKD IQPDLDRRKP GTSRYTTPRR EDDEVQILSG VFEGKTTGTS IGMIIKNGDQ RSQDYGDIKD RFRPGHADFT YQQKYGIRDY RGGGRSSARE TAMRVAAGAI AKKYLREHFG IEVRGFLSQI GNIKIAPQKV GQIDWEKVNS NPFFCPDESA VEKFDELIRE LKKEGDSIGA KLTVIAENVP VGLGEPVFDR LDADLAHALM GINAVKGVEI GDGFAVVEQR GSEHRDEMTP NGFESNHAGG ILGGISSGQP IIATIALKPT SSITIPGRSI NLNGEAVEVV TKGRHDPCVG IRAVPIAEAM VAIVLLDHLL RFKAQCK // ID ASNC_HAEIN Reviewed; 150 AA. AC P44337; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Regulatory protein AsnC; GN Name=asnC; OrderedLocusNames=HI_0563; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activator of asnA transcription. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH asnC-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00319}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22221.1; -; Genomic_DNA. DR PIR; G64077; G64077. DR RefSeq; NP_438720.1; NC_000907.1. DR RefSeq; WP_005649540.1; NC_000907.1. DR ProteinModelPortal; P44337; -. DR SMR; P44337; 4-150. DR STRING; 71421.HI0563; -. DR EnsemblBacteria; AAC22221; AAC22221; HI_0563. DR GeneID; 950765; -. DR KEGG; hin:HI0563; -. DR PATRIC; 20189681; VBIHaeInf48452_0583. DR eggNOG; ENOG4108VVK; Bacteria. DR eggNOG; COG1522; LUCA. DR KO; K03718; -. DR OMA; ENARIPY; -. DR OrthoDB; EOG6F29D2; -. DR PhylomeDB; P44337; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR Pfam; PF13404; HTH_AsnC-type; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 150 Regulatory protein AsnC. FT /FTId=PRO_0000111723. FT DOMAIN 4 65 HTH asnC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. FT DNA_BIND 23 42 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. SQ SEQUENCE 150 AA; 17060 MW; 1DC36CB301A25146 CRC64; MHNIDSLDQK ILRVLTKDAR TPYAEMAKNF GVSPGTIHVR VEKMRQSGII KGTKVIIDER KLGYDVCCFI GIILKSAKDY EKVIKKLESF DEVVEAYYTT GNYSIFLKVM THTIAELHSV LATKIQLIDE IQSTETLISM QNPILRDIKP // ID ASPA_HAEIN Reviewed; 475 AA. AC P44324; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Aspartate ammonia-lyase; DE Short=Aspartase; DE EC=4.3.1.1; GN Name=aspA; OrderedLocusNames=HI_0534; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-aspartate = fumarate + NH(3). CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Aspartase 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; L42023; AAC22191.1; -; Genomic_DNA. DR PIR; C64075; C64075. DR RefSeq; NP_438692.1; NC_000907.1. DR RefSeq; WP_010869000.1; NC_000907.1. DR ProteinModelPortal; P44324; -. DR SMR; P44324; 8-461. DR STRING; 71421.HI0534; -. DR EnsemblBacteria; AAC22191; AAC22191; HI_0534. DR GeneID; 949597; -. DR KEGG; hin:HI0534; -. DR PATRIC; 20189621; VBIHaeInf48452_0553. DR eggNOG; ENOG4108IJ0; Bacteria. DR eggNOG; COG1027; LUCA. DR KO; K01744; -. DR OMA; EICENYV; -. DR OrthoDB; EOG6V1M4M; -. DR PhylomeDB; P44324; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IBA:GO_Central. DR GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IBA:GO_Central. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR004708; ApsA. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00839; aspA; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 475 Aspartate ammonia-lyase. FT /FTId=PRO_0000161341. FT REGION 145 147 Substrate binding. {ECO:0000250}. FT BINDING 106 106 Substrate. {ECO:0000250}. SQ SEQUENCE 475 AA; 51483 MW; E89F8041436EB9EA CRC64; MITMTQFRKE VDLLGERDVP AEAYWGIHTL RAVENFNISN VTISDVPEFV RGMVMVKKAT ALANGELGAI PSDIAKAIVA ACDEILTTGK CLDQFPSDVY QGGAGTSVNM NTNEVVANLA LEKIGHKKGE YNVINPMDHV NASQSTNDAY PTGFRIAVYN SILKLIDKIQ YLHDSFDNKA KEFANILKMG RTQLQDAVPM TVGQEFKAFA VLLEEEVRNL KRTAGLLLEV NLGATAIGTG LNTPQGYTEL VVKHLAEVTG LACVPAENLI EATSDCGAYV MVHGALKRTA VKLSKVCNDL RLLSSGPRAG LKEINLPELQ AGSSIMPAKV NPVVPEVVNQ VCFKVIGNDT TVTFASEAGQ LQLNVMEPVI GQAMFESIDI LTNACVNLRD KCVDGITVNK EICENYVFNS IGIVTYLNPF IGHHNGDLVG KICAQTGKGV REVVLEKGLL TEEQLDDILS VENLMNPTYK AKLNK // ID AROE_HAEIN Reviewed; 272 AA. AC P43876; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, AND RP SUBUNIT. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=12837789; DOI=10.1128/JB.185.14.4144-4151.2003; RA Ye S., Von Delft F., Brooun A., Knuth M.W., Swanson R.V., McRee D.E.; RT "The crystal structure of shikimate dehydrogenase (AroE) reveals a RT unique NADPH binding mode."; RL J. Bacteriol. 185:4144-4151(2003). CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which CC leads to the biosynthesis of aromatic amino acids. Catalyzes the CC reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to CC yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222, CC ECO:0000269|PubMed:12837789}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00222}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22314.1; -; Genomic_DNA. DR PIR; H64084; H64084. DR RefSeq; NP_438815.1; NC_000907.1. DR RefSeq; WP_005694487.1; NC_000907.1. DR PDB; 1P74; X-ray; 2.40 A; A/B=1-272. DR PDB; 1P77; X-ray; 1.95 A; A=1-272. DR PDBsum; 1P74; -. DR PDBsum; 1P77; -. DR ProteinModelPortal; P43876; -. DR SMR; P43876; 1-272. DR STRING; 71421.HI0655; -. DR EnsemblBacteria; AAC22314; AAC22314; HI_0655. DR GeneID; 949697; -. DR KEGG; hin:HI0655; -. DR PATRIC; 20189925; VBIHaeInf48452_0684. DR eggNOG; ENOG4105E2X; Bacteria. DR eggNOG; COG0169; LUCA. DR KO; K00014; -. DR OMA; FWRGVRP; -. DR OrthoDB; EOG6RRKMV; -. DR PhylomeDB; P43876; -. DR BRENDA; 1.1.1.25; 2529. DR SABIO-RK; P43876; -. DR UniPathway; UPA00053; UER00087. DR EvolutionaryTrace; P43876; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR011342; Shikimate_DH. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00507; aroE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 272 Shikimate dehydrogenase (NADP(+)). FT /FTId=PRO_0000136006. FT NP_BIND 126 130 NADP. {ECO:0000255|HAMAP-Rule:MF_00222, FT ECO:0000269|PubMed:12837789}. FT NP_BIND 149 154 NADP. {ECO:0000255|HAMAP-Rule:MF_00222, FT ECO:0000269|PubMed:12837789}. FT REGION 14 16 Shikimate binding. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT ACT_SITE 65 65 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 61 61 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 86 86 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 102 102 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 189 189 NADP. {ECO:0000269|PubMed:12837789}. FT BINDING 213 213 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT BINDING 215 215 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 238 238 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT STRAND 2 10 {ECO:0000244|PDB:1P77}. FT HELIX 16 26 {ECO:0000244|PDB:1P77}. FT STRAND 31 37 {ECO:0000244|PDB:1P77}. FT TURN 40 42 {ECO:0000244|PDB:1P77}. FT HELIX 43 52 {ECO:0000244|PDB:1P77}. FT STRAND 57 60 {ECO:0000244|PDB:1P77}. FT HELIX 65 71 {ECO:0000244|PDB:1P77}. FT STRAND 73 75 {ECO:0000244|PDB:1P77}. FT HELIX 77 82 {ECO:0000244|PDB:1P77}. FT STRAND 86 90 {ECO:0000244|PDB:1P77}. FT STRAND 92 94 {ECO:0000244|PDB:1P74}. FT STRAND 96 99 {ECO:0000244|PDB:1P77}. FT HELIX 102 112 {ECO:0000244|PDB:1P77}. FT STRAND 121 125 {ECO:0000244|PDB:1P77}. FT HELIX 129 132 {ECO:0000244|PDB:1P77}. FT HELIX 135 140 {ECO:0000244|PDB:1P77}. FT STRAND 144 151 {ECO:0000244|PDB:1P77}. FT HELIX 152 162 {ECO:0000244|PDB:1P77}. FT HELIX 163 165 {ECO:0000244|PDB:1P77}. FT STRAND 168 172 {ECO:0000244|PDB:1P77}. FT HELIX 173 175 {ECO:0000244|PDB:1P77}. FT STRAND 182 186 {ECO:0000244|PDB:1P77}. FT HELIX 201 206 {ECO:0000244|PDB:1P77}. FT STRAND 210 213 {ECO:0000244|PDB:1P77}. FT STRAND 217 219 {ECO:0000244|PDB:1P74}. FT HELIX 222 229 {ECO:0000244|PDB:1P77}. FT HELIX 239 254 {ECO:0000244|PDB:1P77}. FT HELIX 260 271 {ECO:0000244|PDB:1P77}. SQ SEQUENCE 272 AA; 29760 MW; 3B7A92AF22D4470B CRC64; MDLYAVWGNP IAQSKSPLIQ NKLAAQTHQT MEYIAKLGDL DAFEQQLLAF FEEGAKGCNI TSPFKERAYQ LADEYSQRAK LAEACNTLKK LDDGKLYADN TDGIGLVTDL QRLNWLRPNQ HVLILGAGGA TKGVLLPLLQ AQQNIVLANR TFSKTKELAE RFQPYGNIQA VSMDSIPLQT YDLVINATSA GLSGGTASVD AEILKLGSAF YDMQYAKGTD TPFIALCKSL GLTNVSDGFG MLVAQAAHSF HLWRGVMPDF VSVYEQLKKA ML // ID ATPA_HAEIN Reviewed; 513 AA. AC P43714; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 123. DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE EC=3.6.3.14 {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; GN OrderedLocusNames=HI_0481; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01346}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01346}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01346}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01346}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22139.1; -; Genomic_DNA. DR PIR; F64071; F64071. DR RefSeq; NP_438641.1; NC_000907.1. DR RefSeq; WP_005688698.1; NC_000907.1. DR ProteinModelPortal; P43714; -. DR SMR; P43714; 29-507. DR STRING; 71421.HI0481; -. DR PRIDE; P43714; -. DR EnsemblBacteria; AAC22139; AAC22139; HI_0481. DR GeneID; 950615; -. DR KEGG; hin:HI0481; -. DR PATRIC; 20189515; VBIHaeInf48452_0500. DR eggNOG; ENOG4105CDG; Bacteria. DR eggNOG; COG0056; LUCA. DR KO; K02111; -. DR OMA; PVFCIYV; -. DR OrthoDB; EOG67X1S1; -. DR PhylomeDB; P43714; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR005294; ATPase_F1-cplx_asu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR15184:SF3; PTHR15184:SF3; 1. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 513 ATP synthase subunit alpha. FT /FTId=PRO_0000144329. FT NP_BIND 169 176 ATP. {ECO:0000255|HAMAP-Rule:MF_01346}. FT SITE 373 373 Required for activity. FT {ECO:0000255|HAMAP-Rule:MF_01346}. SQ SEQUENCE 513 AA; 55591 MW; 34B580C74524FA00 CRC64; MQLNSTEISE LIKKRIAQFD VVSEARNTGT IVSVSDGIIR IHGLSDVMQG EMIALPGNRY AMALNLERDS VGAVVMGPYA DLAEGMEVQC TGRILEVPVG RGLLGRVVNT LGQPIDGKGE IENDGFSPVE VIAPGVIDRR SVDQPVQTGY KAVDSMVPIG RGQRELIIGD RQTGKTALAI DAIINQRNSG IKCIYVAIGQ KASTIANVVR KLEEHGALAN TIVVAASASE SAALQYLAPY AGCAMGEYFR DRGEDALIVY DDLSKQAVAY RQISLLLRRP PGREAYPGDV FYLHSRLLER ASRVNEDYVE KFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLESNLF NSGIRPAVNP GISVSRVGGS AQTKVIKKLA GGIRTALAQY RELAAFAQFA SDLDDATRKQ LSHGEKVTEL LKQKQFTPLS VAEQAVILFA VEFGYLDDVE LSKIASFETA LLDYSNRNHA EFMQELNKTG NYNDEIKDTL KSILDGFKAN SAW // ID AROA_HAEIN Reviewed; 432 AA. AC Q03421; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 122. DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210}; DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210}; GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; GN OrderedLocusNames=HI_1589; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8335255; DOI=10.1016/0378-1119(93)90713-D; RA Maskell D.J.; RT "Cloning and sequencing of the Haemophilus influenzae aroA gene."; RL Gene 129:155-156(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- CC phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and CC inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L04686; AAA24943.1; -; Genomic_DNA. DR EMBL; L42023; AAC23237.1; -; Genomic_DNA. DR PIR; JN0758; JN0758. DR RefSeq; NP_439734.1; NC_000907.1. DR RefSeq; WP_005693605.1; NC_000907.1. DR ProteinModelPortal; Q03421; -. DR STRING; 71421.HI1589; -. DR EnsemblBacteria; AAC23237; AAC23237; HI_1589. DR GeneID; 950448; -. DR KEGG; hin:HI1589; -. DR PATRIC; 20191911; VBIHaeInf48452_1663. DR eggNOG; ENOG4105CMY; Bacteria. DR eggNOG; COG0128; LUCA. DR KO; K00800; -. DR OMA; IGRNSVQ; -. DR OrthoDB; EOG6Z6FZ4; -. DR PhylomeDB; Q03421; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00210; EPSP_synth; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 432 3-phosphoshikimate 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000088258. FT REGION 22 23 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT REGION 94 97 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT REGION 173 175 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT ACT_SITE 316 316 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT ACT_SITE 344 344 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 27 27 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 127 127 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 201 201 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 339 339 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 343 343 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 347 347 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 391 391 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 416 416 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT CONFLICT 75 75 V -> I (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 81 81 T -> A (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 111 112 KT -> NH (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 114 114 S -> V (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 218 218 Q -> K (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 328 328 A -> S (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 330 330 S -> G (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 364 364 G -> E (in Ref. 1; AAA24943). FT {ECO:0000305}. FT CONFLICT 375 375 P -> A (in Ref. 1; AAA24943). FT {ECO:0000305}. SQ SEQUENCE 432 AA; 47413 MW; D1EA2D787AC03FAC CRC64; MEKITLAPIS AVEGTINLPG SKSLSNRALL LAALAKGTTK VTNLLDSDDI RHMLNALKAL GVRYQLSDDK TICEVEGLGG TFNIQDNLSL FLGNAGTAMR PLTAALCLKG KTESEIILTG EPRMKERPIL HLVDALRQAG ADIRYLENEG YPPLAIRNKG IKGGKVKIDG SISSQFLTAL LMSAPLAEND TEIEIIGELV SKPYIDITLA MMRDFGVQVE NHHYQKFQVK GNQSYISPNK YLVEGDASSA SYFLAAGAIK GKVKVTGIGK NSIQGDRLFA DVLEKMGAKI TWGEDFIQAE HAELNGIDMD MNHIPDAAMT IATTALFANS ETVIRNIYNW RVKETDRLTA MATELRKVGA EVEGGEDFIR IQPLPLNQFK HANIETYNDH RMAMCFSLIA LSNTPVTILD PKCTAKTFPT FFNEFEKICL KN // ID AROB_HAEIN Reviewed; 362 AA. AC P43879; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=3-dehydroquinate synthase; DE EC=4.2.3.4; GN Name=aroB; OrderedLocusNames=HI_0208; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate CC = 3-dehydroquinate + phosphate. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 divalent metal cation per subunit. Can use either CC Co(2+) or Zn(2+). {ECO:0000250}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 2/7. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dehydroquinate synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21876.1; -; Genomic_DNA. DR PIR; G64054; G64054. DR RefSeq; NP_438377.1; NC_000907.1. DR RefSeq; WP_005694088.1; NC_000907.1. DR ProteinModelPortal; P43879; -. DR STRING; 71421.HI0208; -. DR EnsemblBacteria; AAC21876; AAC21876; HI_0208. DR GeneID; 951118; -. DR KEGG; hin:HI0208; -. DR PATRIC; 20188913; VBIHaeInf48452_0213. DR eggNOG; ENOG4105D49; Bacteria. DR eggNOG; COG0337; LUCA. DR KO; K01735; -. DR OMA; IERSCAA; -. DR OrthoDB; EOG6SJJGD; -. DR PhylomeDB; P43879; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. DR HAMAP; MF_00110; DHQ_synthase; 1. DR InterPro; IPR016037; DHQ_synth_AroB. DR InterPro; IPR030963; DHQ_synth_fam. DR InterPro; IPR030960; DHQS/DOIS. DR Pfam; PF01761; DHQ_synthase; 1. DR PIRSF; PIRSF001455; DHQ_synth; 1. DR TIGRFAMs; TIGR01357; aroB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cobalt; KW Complete proteome; Cytoplasm; Lyase; NAD; Reference proteome; Zinc. FT CHAIN 1 362 3-dehydroquinate synthase. FT /FTId=PRO_0000140743. SQ SEQUENCE 362 AA; 39919 MW; F787324C1428A110 CRC64; MLCVNVELQE RRYPILIGSG LLQDERSYPI KRGDRVMIVT NPTVAQFYLD TVIYALEKRG CVVDHVLLPD GEKYKTLESL NLIFTALLQG NHGRDTTIIA LGGGVIGDVA GFAAASYQRG VRLIQIPTTL LSQVDSSVGG KTAVNHELGK NMIGAFYQPS MVIIDTLTLN TLPKREVNAG LAEVIKYGAI LDYEFFEWLE QHIDELVALH PEALQHCISR CCQIKADVVA RDETEKGDRA LLNLGHTFGH AIETHLGYGN WLHGEAVSTG MMMAAALSEE LGDISIADVS RLEKLLARAN LPTVSPDTMQ PEDYLPHMMR DKKVLSGKLR LVLLKSLGQA YVANDTEHTL VLNAIRRCTQ TD // ID AROQ_HAEIN Reviewed; 149 AA. AC P43878; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=3-dehydroquinate dehydratase; DE Short=3-dehydroquinase; DE EC=4.2.1.10; DE AltName: Full=Type II DHQase; GN Name=aroQ; OrderedLocusNames=HI_0970; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate CC intermediate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. CC -!- SUBUNIT: Homododecamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22627.1; -; Genomic_DNA. DR PIR; D64105; D64105. DR RefSeq; NP_439131.1; NC_000907.1. DR RefSeq; WP_010869097.1; NC_000907.1. DR ProteinModelPortal; P43878; -. DR SMR; P43878; 6-148. DR STRING; 71421.HI0970; -. DR EnsemblBacteria; AAC22627; AAC22627; HI_0970. DR GeneID; 949969; -. DR KEGG; hin:HI0970; -. DR PATRIC; 20190597; VBIHaeInf48452_1011. DR eggNOG; ENOG4108Z38; Bacteria. DR eggNOG; COG0757; LUCA. DR KO; K03786; -. DR OMA; IPTIEVH; -. DR OrthoDB; EOG66MQVT; -. DR PhylomeDB; P43878; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.9100; -; 1. DR HAMAP; MF_00169; AroQ; 1. DR InterPro; IPR001874; DHquinase_II. DR InterPro; IPR018509; DHquinase_II_CS. DR PANTHER; PTHR21272; PTHR21272; 1. DR Pfam; PF01220; DHquinase_II; 1. DR PIRSF; PIRSF001399; DHquinase_II; 1. DR ProDom; PD004527; DHquinase_II; 1. DR SUPFAM; SSF52304; SSF52304; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 149 3-dehydroquinate dehydratase. FT /FTId=PRO_0000159903. FT REGION 104 105 Substrate binding. {ECO:0000250}. FT ACT_SITE 26 26 Proton acceptor. {ECO:0000250}. FT ACT_SITE 103 103 Proton donor. {ECO:0000250}. FT BINDING 77 77 Substrate. {ECO:0000250}. FT BINDING 83 83 Substrate. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT BINDING 114 114 Substrate. {ECO:0000250}. FT SITE 21 21 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 149 AA; 16766 MW; BB070AAF36F4C4BA CRC64; MSQTHRILLL NGPNLNMLGA REPKHYGSIS LESIEEKIQT LATQHNVKVE CFQANSEGKL INKIHESFQQ VDFILINPAA YTHTSVALRD ALLAVSIPFV EIHLSNVHKR EPFRHHSYFS DVAEGVICGL GAKGYEFAFL FAMDYLAKK // ID ASNA_HAEIN Reviewed; 330 AA. AC P44338; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Aspartate--ammonia ligase {ECO:0000255|HAMAP-Rule:MF_00555}; DE EC=6.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00555}; DE AltName: Full=Asparagine synthetase A {ECO:0000255|HAMAP-Rule:MF_00555}; GN Name=asnA {ECO:0000255|HAMAP-Rule:MF_00555}; GN OrderedLocusNames=HI_0564; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + NH(3) = AMP + diphosphate CC + L-asparagine. {ECO:0000255|HAMAP-Rule:MF_00555}. CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L- CC asparagine from L-aspartate (ammonia route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00555}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00555}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. AsnA subfamily. {ECO:0000255|HAMAP-Rule:MF_00555}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22222.1; -; Genomic_DNA. DR PIR; H64077; H64077. DR RefSeq; NP_438721.1; NC_000907.1. DR RefSeq; WP_005654693.1; NC_000907.1. DR ProteinModelPortal; P44338; -. DR SMR; P44338; 5-330. DR STRING; 71421.HI0564; -. DR EnsemblBacteria; AAC22222; AAC22222; HI_0564. DR GeneID; 949631; -. DR KEGG; hin:HI0564; -. DR PATRIC; 20189683; VBIHaeInf48452_0584. DR eggNOG; ENOG4105CU9; Bacteria. DR eggNOG; COG2502; LUCA. DR KO; K01914; -. DR OMA; QSRICMF; -. DR OrthoDB; EOG64V2FB; -. DR PhylomeDB; P44338; -. DR UniPathway; UPA00134; UER00194. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro. DR GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro. DR HAMAP; MF_00555; AsnA; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004618; AsnA. DR Pfam; PF03590; AsnA; 1. DR PIRSF; PIRSF001555; Asp_ammon_ligase; 1. DR TIGRFAMs; TIGR00669; asnA; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 330 Aspartate--ammonia ligase. FT /FTId=PRO_0000195878. SQ SEQUENCE 330 AA; 37432 MW; 3C8D32400A77FF41 CRC64; MKKTFILQQQ EISFVKNTFT QNLIEQLGII EVQGPILSQV GNGMQDNLSG IEKAVQVNVK CIPNAVFEVV HSLAKWKRHT LARFNFKEDE GLFVHMKALR PDEDSLDPTH SVYVDQWDWE KVIPEGRRNF AYLKETVNSI YRAIRLTELA VEARFDIPSI LPKQITFVHS EDLVKRYPDL SSKERENAIC KEYGAVFLIG IGGKLSDGKP HDGRAPDYDD WTTESENGYK GLNGDILVWN DQLGKAFELS SMGIRVDESA LRLQVGLTGD EDHLKMDWHQ DLLNGKLPLT IGGGIGQSRL AMLLLRKKHI GEVQSSVWPK EMLEEFSNIL // ID ASPG2_HAEIN Reviewed; 349 AA. AC P43843; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Probable L-asparaginase periplasmic; DE Short=L-ASNase; DE EC=3.5.1.1; DE AltName: Full=L-asparagine amidohydrolase; DE Flags: Precursor; GN Name=ansB; OrderedLocusNames=HI_0745; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 22-26. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- CATALYTIC ACTIVITY: L-asparagine + H(2)O = L-aspartate + NH(3). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 asparaginase/glutaminase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22403.1; -; Genomic_DNA. DR PIR; A64090; A64090. DR RefSeq; NP_438904.1; NC_000907.1. DR RefSeq; WP_005652322.1; NC_000907.1. DR ProteinModelPortal; P43843; -. DR SMR; P43843; 24-349. DR STRING; 71421.HI0745; -. DR EnsemblBacteria; AAC22403; AAC22403; HI_0745. DR GeneID; 949675; -. DR KEGG; hin:HI0745; -. DR PATRIC; 20190133; VBIHaeInf48452_0782. DR eggNOG; ENOG4105HDK; Bacteria. DR eggNOG; COG0252; LUCA. DR KO; K01424; -. DR OMA; NFGPLGY; -. DR OrthoDB; EOG6VTK47; -. DR PhylomeDB; P43843; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC. DR GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1170; -; 1. DR Gene3D; 3.40.50.40; -; 1. DR InterPro; IPR004550; AsnASE_II. DR InterPro; IPR006034; Asparaginase/glutaminase. DR InterPro; IPR020827; Asparaginase/glutaminase_AS1. DR InterPro; IPR027475; Asparaginase/glutaminase_AS2. DR InterPro; IPR027473; L-asparaginase_C. DR InterPro; IPR027474; L-asparaginase_N. DR Pfam; PF00710; Asparaginase; 1. DR PIRSF; PIRSF001220; L-ASNase_gatD; 1. DR PRINTS; PR00139; ASNGLNASE. DR SMART; SM00870; Asparaginase; 1. DR SUPFAM; SSF53774; SSF53774; 1. DR TIGRFAMs; TIGR00520; asnASE_II; 1. DR PROSITE; PS00144; ASN_GLN_ASE_1; 1. DR PROSITE; PS00917; ASN_GLN_ASE_2; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Hydrolase; Periplasm; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000269|PubMed:10675023}. FT CHAIN 22 349 Probable L-asparaginase periplasmic. FT /FTId=PRO_0000002357. FT DOMAIN 25 349 Asparaginase/glutaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01068}. FT REGION 112 113 Substrate binding. {ECO:0000250}. FT ACT_SITE 35 35 O-isoaspartyl threonine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU10099, FT ECO:0000255|PROSITE-ProRule:PRU10100}. FT BINDING 81 81 Substrate. {ECO:0000250}. FT DISULFID 100 128 {ECO:0000250}. SQ SEQUENCE 349 AA; 37212 MW; 45EA79CAC215F8A9 CRC64; MKLTKLALCT LFGLGVSIAN AADLPNITIL ATGGTIAGSG QSSVNSAYKA GQLSIDTLIE AVPEMKNIAN IKGEQIVKIG SQDMNDEVWL KLAKAINAQC KSTDGFVITH GTDTMEETAY FLDLTVKCEK PVVLVGAMRP ATEKSADGPL NLYNAVVVAA DKKSSGRGVL VAMNNEVLGA RDVTKTSTTA VQTFHSPNYG SLGYIHNSKV DYERSPESKH TINTPFNVEK LDSLPKVGII YAYSNAPVEP LNALLNAGYQ GIVSAGVGNG NVNAAHLDRL EKAAKDSVVV VRSSRVPTGY TTRDAEVDDS KYGFVASGTL NPQKARVLLQ LALTQTKDPK VIQQYFEDF // ID ASSY_HAEIN Reviewed; 444 AA. AC P44315; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=HI_1727; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 2 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; L42023; AAC23373.1; -; Genomic_DNA. DR PIR; F64138; F64138. DR RefSeq; NP_439868.1; NC_000907.1. DR RefSeq; WP_005694213.1; NC_000907.1. DR ProteinModelPortal; P44315; -. DR SMR; P44315; 4-441. DR STRING; 71421.HI1727; -. DR EnsemblBacteria; AAC23373; AAC23373; HI_1727. DR GeneID; 950537; -. DR KEGG; hin:HI1727; -. DR PATRIC; 20192207; VBIHaeInf48452_1806. DR eggNOG; ENOG4105CDH; Bacteria. DR eggNOG; COG0137; LUCA. DR KO; K01940; -. DR OMA; AFHIRSG; -. DR OrthoDB; EOG6K9QCV; -. DR PhylomeDB; P44315; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 1.10.287.400; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00581; Arg_succ_synth_type2; 1. DR InterPro; IPR023437; Arg_succ_synth_type2_subfam. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR024073; AS_multimer_C_tail. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00764; Arginosuc_synth; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 444 Argininosuccinate synthase. FT /FTId=PRO_0000148700. FT NP_BIND 18 26 ATP. {ECO:0000250}. FT BINDING 44 44 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 100 100 Citrulline. {ECO:0000250}. FT BINDING 130 130 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 132 132 Aspartate. {ECO:0000250}. FT BINDING 132 132 ATP. {ECO:0000250}. FT BINDING 136 136 Aspartate. {ECO:0000250}. FT BINDING 136 136 Citrulline. {ECO:0000250}. FT BINDING 137 137 Aspartate. {ECO:0000250}. FT BINDING 137 137 ATP. {ECO:0000250}. FT BINDING 140 140 Citrulline. {ECO:0000250}. FT BINDING 193 193 Citrulline. {ECO:0000250}. FT BINDING 195 195 ATP. {ECO:0000250}. FT BINDING 202 202 Citrulline. {ECO:0000250}. FT BINDING 204 204 Citrulline. {ECO:0000250}. FT BINDING 281 281 Citrulline. {ECO:0000250}. SQ SEQUENCE 444 AA; 49289 MW; F833EDD718199098 CRC64; MSNTILQNLP KGQKVGIAFS GGLDTSAALL WMRQKGAVPY AYTANLGQPD EDDYNAIPKK AMAYGAENAR LIDCRAQLAH EGIAAIQCGA FHISTGGIPY FNTTPLGRAV TGTMLVAAMK EDDVNIWGDG STFKGNDIER FYRYGLLTNP NLKIYKPWLD VQFIEELGGR LEMSQFLIEN GFDYKMSVEK AYSTDSNMLG ATHEAKDLEQ LSTGMKIVKP IMGVAFWDEK VEIKPETVTV TFEDGVPVAL NGKHFDNAVD LILEANRIGG RHGLGMSDQI ENRIIEAKSR GIYEAPGMAL LHIAYERLVT GIHNEDTIEQ YRINGIRLGR LLYQGRWFDP QALMLRETAQ RWVAKAITGT VTLELRRGND FTILNTESPN LTYEAERLSM EKVEDAPFDP IDRIGQLTMR NLDVSDTRGK LGIYAQTGLL SAIKDSVLPQ LGKK // ID ARTQ_HAEIN Reviewed; 221 AA. AC P45090; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Arginine ABC transporter permease protein ArtQ; GN Name=artQ; OrderedLocusNames=HI_1178; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the ABC transporter complex ArtPIQM involved in CC arginine transport. Probably responsible for the translocation of CC the substrate across the membrane (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute- CC binding protein (ArtI). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. HisMQ 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; L42023; AAC22829.1; -; Genomic_DNA. DR EMBL; U17295; AAA95979.1; -; Genomic_DNA. DR PIR; B64188; B64188. DR RefSeq; NP_439334.1; NC_000907.1. DR RefSeq; WP_005694263.1; NC_000907.1. DR ProteinModelPortal; P45090; -. DR STRING; 71421.HI1178; -. DR EnsemblBacteria; AAC22829; AAC22829; HI_1178. DR GeneID; 950141; -. DR KEGG; hin:HI1178; -. DR PATRIC; 20191033; VBIHaeInf48452_1229. DR eggNOG; ENOG4105GBT; Bacteria. DR eggNOG; COG4215; LUCA. DR KO; K09999; -. DR OMA; WAWIEAR; -. DR OrthoDB; EOG6MM1R5; -. DR PhylomeDB; P45090; -. DR BioCyc; RETL1328306-WGS:GSTH-6366-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 221 Arginine ABC transporter permease protein FT ArtQ. FT /FTId=PRO_0000059965. FT TRANSMEM 17 37 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 49 69 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 82 102 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 121 141 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 186 206 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 13 206 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 221 AA; 24291 MW; 7C4DC4F7C5B7FF47 CRC64; MFSDFLSLMF TAALMTLGLA VCSLLLGLFL SLIFAVLEAN RFVGKPMTVF VALLRGLPEI IVVLLVYFGS TELVEMLTGE YIEFGAFGCG VLALSLIFAA YASQTLRGAI QAIPKGQWES GAALGLSKSY TFIHIVMPQV WRHALPGLST QWLVLLKDTA LVSLIGVDDL MHQADLINTN THQPFTWYGI AALIYLAVTL ISQVGIRKLE LRFTRFERGV K // ID ARSC_HAEIN Reviewed; 116 AA. AC P44589; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative arsenate reductase; DE EC=1.20.4.1; GN Name=arsC; Synonyms=arsG; OrderedLocusNames=HI_0236; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reduction of arsenate [As(V)] to arsenite [As(III)]. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite + CC glutaredoxin disulfide + H(2)O. 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; L42023; AAC21906.1; -; Genomic_DNA. DR PIR; G64056; G64056. DR RefSeq; NP_438407.1; NC_000907.1. DR RefSeq; WP_005664106.1; NC_000907.1. DR ProteinModelPortal; P44589; -. DR STRING; 71421.HI0236; -. DR EnsemblBacteria; AAC21906; AAC21906; HI_0236. DR GeneID; 951153; -. DR KEGG; hin:HI0236; -. DR PATRIC; 20188997; VBIHaeInf48452_0251. DR eggNOG; ENOG4105K89; Bacteria. DR eggNOG; COG1393; LUCA. DR KO; K00537; -. DR OMA; VSHGQAR; -. DR OrthoDB; EOG6PP9QC; -. DR PhylomeDB; P44589; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR006659; Arsenate_reductase. DR InterPro; IPR006660; Arsenate_reductase-like. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF03960; ArsC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00014; arsC; 1. DR PROSITE; PS51353; ARSC; 1. PE 3: Inferred from homology; KW Arsenical resistance; Complete proteome; Oxidoreductase; KW Reference proteome. FT CHAIN 1 116 Putative arsenate reductase. FT /FTId=PRO_0000162539. SQ SEQUENCE 116 AA; 13228 MW; 4780A59D04C4247E CRC64; MSVIIYHNPH CSKSRETLAL LENKGIQPII ELYLQKQYSV NELQSIAKKL GIDDVRQMMR TKDELYKSLN LDNLDLSQAE LFKAISEHSA LIERPIVING DKAKIGRPPE TVLEIL // ID ARTP_HAEIN Reviewed; 243 AA. AC P45092; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Arginine transport ATP-binding protein ArtP; DE EC=3.6.3.-; GN Name=artP; OrderedLocusNames=HI_1180; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the ABC transporter complex ArtPIQM involved in CC arginine transport. Probably responsible for energy coupling to CC the transport system (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute- CC binding protein (ArtI). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22831.1; -; Genomic_DNA. DR EMBL; U17295; AAA95977.1; -; Genomic_DNA. DR PIR; D64188; D64188. DR RefSeq; NP_439336.1; NC_000907.1. DR RefSeq; WP_005694261.1; NC_000907.1. DR ProteinModelPortal; P45092; -. DR STRING; 71421.HI1180; -. DR EnsemblBacteria; AAC22831; AAC22831; HI_1180. DR GeneID; 950628; -. DR KEGG; hin:HI1180; -. DR PATRIC; 20191037; VBIHaeInf48452_1231. DR eggNOG; ENOG4105E5Z; Bacteria. DR eggNOG; COG4161; LUCA. DR KO; K10000; -. DR OMA; AMNHADI; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45092; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030679; ABC_ATPase_HisP-typ. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 243 Arginine transport ATP-binding protein FT ArtP. FT /FTId=PRO_0000091943. FT DOMAIN 3 242 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 35 42 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 243 AA; 27138 MW; 22A406FF0F1FAE3B CRC64; MAIRVKNLNF FYGSSQTLFD INLEAEEGDT VVLLGPSGAG KSTLIRTLNL LEVPKSGELS IANNEFNLSN AMANPKAIQQ LRQDVGMVFQ QYHLWPHLTV IENLIEAPMK VRGVSENEAK TDAMELLKRL RLEQLADRFP LHLSGGQQQR VAIARALMMK PQVLLFDEPT AALDPEITAQ VVDIIKELQE TGITQVIVTH EVNVAQKVAT KVVYMEQGKI VEMGSADCFE NPKTEQFKHY LSH // ID ATPF_HAEIN Reviewed; 156 AA. AC P43720; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398}; DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398}; GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; GN OrderedLocusNames=HI_0483; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01398}. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC {ECO:0000255|HAMAP-Rule:MF_01398}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22141.1; -; Genomic_DNA. DR PIR; H64071; H64071. DR RefSeq; NP_438643.1; NC_000907.1. DR RefSeq; WP_005629246.1; NC_000907.1. DR ProteinModelPortal; P43720; -. DR SMR; P43720; 1-33, 64-121. DR STRING; 71421.HI0483; -. DR EnsemblBacteria; AAC22141; AAC22141; HI_0483. DR GeneID; 949543; -. DR KEGG; hin:HI0483; -. DR PATRIC; 20189519; VBIHaeInf48452_0502. DR eggNOG; ENOG4107Z6K; Bacteria. DR eggNOG; COG0711; LUCA. DR KO; K02109; -. DR OMA; HFAWGPV; -. DR OrthoDB; EOG6DNTDK; -. DR PhylomeDB; P43720; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.5.620; -; 1. DR HAMAP; MF_01398; ATP_synth_b_bact; 1. DR InterPro; IPR028987; ATPase_B-like_membr. DR InterPro; IPR002146; ATPase_F0-cplx_b/b'su_bac. DR InterPro; IPR005864; ATPase_F0-cplx_bsu_bac. DR Pfam; PF00430; ATP-synt_B; 1. DR SUPFAM; SSF81573; SSF81573; 1. DR TIGRFAMs; TIGR01144; ATP_synt_b; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 156 ATP synthase subunit b. FT /FTId=PRO_0000082375. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. SQ SEQUENCE 156 AA; 17172 MW; 3D630396E07329B1 CRC64; MNLNATLIGQ LIAFALFVWF CMKFVWPPII NAIETRQSQI ANALASAEAA KKEQADTKNL VEQELSAAKL QAQDILDAAN KRRNEVLDEV KAEAEELKAK IIAQGYAEVE AERKRVQEEL RLKVASLAVA GAEKIVGRSI DEAANNDIID KLVAEL // ID ATOB_HAEIN Reviewed; 393 AA. AC P44873; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Acetyl-CoA acetyltransferase; DE EC=2.3.1.9; DE AltName: Full=Acetoacetyl-CoA thiolase; GN Name=atoB; Synonyms=thi, thl; OrderedLocusNames=HI_0771; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA. CC {ECO:0000255|PROSITE-ProRule:PRU10020}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the thiolase 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; L42023; AAC22430.1; -; Genomic_DNA. DR RefSeq; NP_438930.1; NC_000907.1. DR RefSeq; WP_005666204.1; NC_000907.1. DR ProteinModelPortal; P44873; -. DR SMR; P44873; 3-393. DR STRING; 71421.HI0771; -. DR EnsemblBacteria; AAC22430; AAC22430; HI_0771. DR GeneID; 950638; -. DR KEGG; hin:HI0771; -. DR PATRIC; 20190193; VBIHaeInf48452_0810. DR eggNOG; ENOG4105CHU; Bacteria. DR eggNOG; COG0183; LUCA. DR KO; K00626; -. DR OMA; MRMGARM; -. DR OrthoDB; EOG68M4GV; -. DR PhylomeDB; P44873; -. DR UniPathway; UPA00058; UER00101. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.47.10; -; 4. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020610; Thiolase_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Fatty acid metabolism; KW Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1 393 Acetyl-CoA acetyltransferase. FT /FTId=PRO_0000206407. FT ACT_SITE 88 88 Acyl-thioester intermediate. FT {ECO:0000250}. FT ACT_SITE 349 349 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10020}. FT ACT_SITE 379 379 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10020}. SQ SEQUENCE 393 AA; 40801 MW; 1C1FB6D1AE4D8410 CRC64; MENVVIVSAV RTPIGSFNGA LSSVSAVDLG AIVIQEAIKR ANIESALVNE VIMGNVLQAG LGQNPARQAA LKAGIEKEIP SLTINKVCGS GLKSVALGAQ SIISGDADIV VVGGMENMSQ APYLLDSKVR QGVKMGNLTL RDTMIEDGLT CASNHYHMGI TAENIAEQYG ISRQAQDELA LRSQTLASQA VQLGVFDKEI VPVMVKTRKG DIIVSRDEYP KADTTAEGLA KLKPAFKKEG TVTAGNASGI NDGAAALILV SESKAHALGL KAIAKIRSYA SGGVDPSVMG LGPVPATQKA LKKAGINLDD IDLIEANEAF ASQFLGVGKD LNLDMNKTNI HGGAIALGHP IGASGARILV TLLHNLIEKD KKLGLATLCI GGGQGISMIV ERL // ID ATP6_HAEIN Reviewed; 262 AA. AC P43719; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. 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}; GN OrderedLocusNames=HI_0485; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner 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; L42023; AAC22143.1; -; Genomic_DNA. DR PIR; A64072; A64072. DR RefSeq; NP_438645.1; NC_000907.1. DR RefSeq; WP_005629251.1; NC_000907.1. DR ProteinModelPortal; P43719; -. DR STRING; 71421.HI0485; -. DR EnsemblBacteria; AAC22143; AAC22143; HI_0485. DR GeneID; 949858; -. DR KEGG; hin:HI0485; -. DR PATRIC; 20189523; VBIHaeInf48452_0504. DR eggNOG; ENOG4105EE4; Bacteria. DR eggNOG; COG0356; LUCA. DR KO; K02108; -. DR OMA; QIMITFS; -. DR OrthoDB; EOG6K4054; -. DR PhylomeDB; P43719; -. DR Proteomes; UP000000579; 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 TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 262 ATP synthase subunit a. FT /FTId=PRO_0000082056. FT TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 86 106 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 130 150 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 204 226 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. FT TRANSMEM 240 260 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01393}. SQ SEQUENCE 262 AA; 29333 MW; 2089A134611010F4 CRC64; MSGQTTSEYI SHHLSFLKTG DGFWNVHIDT LFFSILAAVI FLFVFSRVGK KATTGVPGKM QCLVEIVVEW VNGIVKENFH GPRNVVAPLA LTIFCWVFIM NAIDLIPVDF LPQFAGLFGI HYLRAVPTAD ISATLGMSIC VFFLILFYTI KSKGFKGLVK EYTLHPFNHW AFIPVNFILE TVTLLAKPIS LAFRLFGNMY AGELIFILIA VMYSANMAIA ALGIPLHLAW AIFHILVITL QAFIFMMLTV VYLSIAYNKA DH // ID ATPL_HAEIN Reviewed; 84 AA. AC P43721; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396}; DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396}; GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; GN OrderedLocusNames=HI_0484; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner 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 aspartate 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; L42023; AAC22142.1; -; Genomic_DNA. DR PIR; I64071; I64071. DR RefSeq; NP_438644.1; NC_000907.1. DR RefSeq; WP_005652035.1; NC_000907.1. DR ProteinModelPortal; P43721; -. DR SMR; P43721; 7-76. DR STRING; 71421.HI0484; -. DR EnsemblBacteria; AAC22142; AAC22142; HI_0484. DR GeneID; 949568; -. DR KEGG; hin:HI0484; -. DR PATRIC; 20189521; VBIHaeInf48452_0503. DR eggNOG; ENOG4105KY6; Bacteria. DR eggNOG; COG0636; LUCA. DR KO; K02110; -. DR OMA; MEIVMET; -. DR OrthoDB; EOG68H8G3; -. DR PhylomeDB; P43721; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR Gene3D; 1.20.20.10; -; 1. DR HAMAP; MF_01396; ATP_synth_c_bact; 1. DR InterPro; IPR000454; ATPase_F0-cplx_csu. DR InterPro; IPR005953; ATPase_F0-cplx_csu_bac/chlpt. DR InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS. DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR SUPFAM; SSF81333; SSF81333; 1. DR TIGRFAMs; TIGR01260; ATP_synt_c; 1. DR PROSITE; PS00605; ATPASE_C; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(0); KW Complete proteome; Hydrogen ion transport; Ion transport; KW Lipid-binding; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 84 ATP synthase subunit c. FT /FTId=PRO_0000112148. FT TRANSMEM 9 29 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT TRANSMEM 54 74 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01396}. FT SITE 60 60 Reversibly protonated during proton FT transport. {ECO:0000255|HAMAP- FT Rule:MF_01396}. SQ SEQUENCE 84 AA; 8641 MW; E57C8B223498ED02 CRC64; METVITATII GASILLAFAA LGTAIGFAIL GGKFLESSAR QPELASSLQT KMFIVAGLLD AIAMIAVGIS LLFIFANPFI GLLN // ID ATPD_HAEIN Reviewed; 177 AA. AC P43717; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416}; GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; GN OrderedLocusNames=HI_0482; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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_01416}. CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CC CF(1). It either transmits conformational changes from CF(0) to CC CF(1) or is implicated in proton conduction. {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic CC core - and F(0) - the membrane proton channel. F(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) CC has three main subunits: a(1), b(2) and c(10-14). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. F(1) is attached to F(0) by a central stalk formed by CC the gamma and epsilon chains, while a peripheral stalk is formed CC by the delta and b chains. {ECO:0000255|HAMAP-Rule:MF_01416}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01416}. CC -!- SIMILARITY: Belongs to the ATPase delta chain family. CC {ECO:0000255|HAMAP-Rule:MF_01416}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22140.1; -; Genomic_DNA. DR PIR; G64071; G64071. DR RefSeq; NP_438642.1; NC_000907.1. DR RefSeq; WP_005642563.1; NC_000907.1. DR ProteinModelPortal; P43717; -. DR SMR; P43717; 2-105. DR STRING; 71421.HI0482; -. DR EnsemblBacteria; AAC22140; AAC22140; HI_0482. DR GeneID; 949424; -. DR KEGG; hin:HI0482; -. DR PATRIC; 20189517; VBIHaeInf48452_0501. DR eggNOG; ENOG4107S15; Bacteria. DR eggNOG; COG0712; LUCA. DR KO; K02113; -. DR OMA; TMQRVLK; -. DR OrthoDB; EOG6DNTDK; -. DR PhylomeDB; P43717; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.520.20; -; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR026015; ATPase_OSCP/delta_N. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR PANTHER; PTHR11910; PTHR11910; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; SSF47928; 1. DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 177 ATP synthase subunit delta. FT /FTId=PRO_0000193465. SQ SEQUENCE 177 AA; 19451 MW; 3834112589211D60 CRC64; MSELTTIARP YAKAAFDFAI EQSAVEKWTE MLGFAAAVAE DETVKAYLSS SLSAQKLADT VISICGEQLD QYGQNLIRLM AENKRLSAIP AVFEEFKHHV EEHQAIAEVE VTSAQPLNAT QIEKIAAAME KRLARKVKLN CNVDNALIAG VIVRTEDFVI DGSSRGQLTR LANELQL // ID BAMD_HAEIN Reviewed; 262 AA. AC P44553; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=Outer membrane protein assembly factor BamD {ECO:0000255|HAMAP-Rule:MF_00922}; DE Flags: Precursor; GN Name=bamD {ECO:0000255|HAMAP-Rule:MF_00922}; GN OrderedLocusNames=HI_0177; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. {ECO:0000255|HAMAP- CC Rule:MF_00922}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_00922}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_00922}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00922}. CC -!- SIMILARITY: Belongs to the BamD family. {ECO:0000255|HAMAP- CC Rule:MF_00922}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21847.1; -; Genomic_DNA. DR PIR; G64144; G64144. DR RefSeq; NP_438345.1; NC_000907.1. DR RefSeq; WP_005694110.1; NC_000907.1. DR STRING; 71421.HI0177; -. DR EnsemblBacteria; AAC21847; AAC21847; HI_0177. DR GeneID; 951089; -. DR KEGG; hin:HI0177; -. DR PATRIC; 20188849; VBIHaeInf48452_0181. DR eggNOG; ENOG4106SNF; Bacteria. DR eggNOG; COG4105; LUCA. DR KO; K05807; -. DR OMA; DMFINLH; -. DR OrthoDB; EOG6WHNPP; -. DR PhylomeDB; P44553; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR Gene3D; 1.25.40.10; -; 1. DR HAMAP; MF_00922; OM_assembly_BamD; 1. DR InterPro; IPR017689; BamD. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR03302; OM_YfiO; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255|HAMAP-Rule:MF_00922}. FT CHAIN 19 262 Outer membrane protein assembly factor FT BamD. FT /FTId=PRO_0000036228. FT LIPID 19 19 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_00922}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_00922}. SQ SEQUENCE 262 AA; 29348 MW; 1DD9FFFE568D2B7B CRC64; MRKIKSLALL AVAALVIGCS SGSKDVEQAS VNELYTKGTT SLQEGSYSEA IRYLKATTER FPGSVYQEQA MLDLIYANYK TQDYTQVLLM VDSFLHQFTQ SPNQAYAVYM AGLTNAATGD NFIQDFFGID RATRETTSMR TAFSNFQNLV RVFPNSPYSQ DALARMAYIK DALARHELEI AKFYAKRKAW VAVANRVVGM LKQYPDTKAT YEGLFLMQEA YEKMGLTALA NDTQKIIDAN KDKTFAPIEK PNEPDLKVPA VK // ID ATOA_HAEIN Reviewed; 223 AA. AC P44874; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Acetate CoA-transferase subunit beta; DE EC=2.8.3.8; DE AltName: Full=Acetyl-CoA:acetoacetate CoA-transferase subunit beta; GN Name=atoA; OrderedLocusNames=HI_0773; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acetate = a fatty acid anion + CC acetyl-CoA. CC -!- PATHWAY: Lipid metabolism; short-chain fatty acid metabolism. CC -!- SUBUNIT: Heterodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B 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; L42023; AAC22432.1; -; Genomic_DNA. DR PIR; G64158; G64158. DR RefSeq; NP_438932.1; NC_000907.1. DR RefSeq; WP_005693164.1; NC_000907.1. DR ProteinModelPortal; P44874; -. DR STRING; 71421.HI0773; -. DR EnsemblBacteria; AAC22432; AAC22432; HI_0773. DR GeneID; 949789; -. DR KEGG; hin:HI0773; -. DR PATRIC; 20190197; VBIHaeInf48452_0812. DR eggNOG; ENOG4107QNJ; Bacteria. DR eggNOG; COG2057; LUCA. DR KO; K01035; -. DR OMA; DDHYDPT; -. DR OrthoDB; EOG6HMXJG; -. DR PhylomeDB; P44874; -. DR UniPathway; UPA00656; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC. DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B. DR InterPro; IPR004165; CoA_trans_fam_I. DR InterPro; IPR004164; CoA_transf_AS. DR PANTHER; PTHR13707; PTHR13707; 1. DR Pfam; PF01144; CoA_trans; 1. DR SMART; SM00882; CoA_trans; 1. DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1. DR PROSITE; PS01274; COA_TRANSF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid metabolism; Lipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 223 Acetate CoA-transferase subunit beta. FT /FTId=PRO_0000157916. FT ACT_SITE 46 46 {ECO:0000255|PROSITE-ProRule:PRU10034}. SQ SEQUENCE 223 AA; 23750 MW; EC56D6684708C851 CRC64; MNAKELIARR IAMELHDGDI VNLGIGLPTQ VVNYLPDNVN ITLQSENGFL GLTAFDPENA NSNLVNAGGQ PCGIKKGGST FDSAFSFALI RGGHVDACVL GGLEVDQEAN LANWMVPGKM VPGMGGAMDL VTGAKKVIIG MEHCAKSGSS KILKKCTLPL TASKKVAMVV TELAVFNFIE GRLVLKEHAP HVDLETIKAK TEADFIVADD FKEMQISQKG LEL // ID ATOD_HAEIN Reviewed; 217 AA. AC P44875; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Acetate CoA-transferase subunit alpha; DE EC=2.8.3.8; DE AltName: Full=Acetyl-CoA:acetoacetate-CoA transferase subunit alpha; GN Name=atoD; OrderedLocusNames=HI_0774; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + acetate = a fatty acid anion + CC acetyl-CoA. CC -!- PATHWAY: Lipid metabolism; short-chain fatty acid metabolism. CC -!- SUBUNIT: Heterodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A 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; L42023; AAC22433.1; -; Genomic_DNA. DR PIR; B64092; B64092. DR RefSeq; NP_438933.1; NC_000907.1. DR RefSeq; WP_005693165.1; NC_000907.1. DR ProteinModelPortal; P44875; -. DR SMR; P44875; 1-217. DR STRING; 71421.HI0774; -. DR EnsemblBacteria; AAC22433; AAC22433; HI_0774. DR GeneID; 949792; -. DR KEGG; hin:HI0774; -. DR PATRIC; 20190199; VBIHaeInf48452_0813. DR eggNOG; ENOG4107QP7; Bacteria. DR eggNOG; COG1788; LUCA. DR KO; K01034; -. DR OMA; VKAHRAD; -. DR OrthoDB; EOG6HMXJG; -. DR PhylomeDB; P44875; -. DR UniPathway; UPA00656; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:UniProtKB-EC. DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A. DR InterPro; IPR004165; CoA_trans_fam_I. DR InterPro; IPR004163; CoA_transf_BS. DR PANTHER; PTHR13707; PTHR13707; 1. DR Pfam; PF01144; CoA_trans; 1. DR SMART; SM00882; CoA_trans; 1. DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1. DR PROSITE; PS01273; COA_TRANSF_1; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid metabolism; Lipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 217 Acetate CoA-transferase subunit alpha. FT /FTId=PRO_0000157905. FT REGION 24 30 CoA-binding. {ECO:0000255}. SQ SEQUENCE 217 AA; 23090 MW; 6FAA18F32047F910 CRC64; MTQKHLKLNN LNQHLHDGMS IMFGGFMGIG TPAKLVQQIL DSGVKDLTLI GNDTAFIDTG VGPLIVNNRV KRLITSHIGT NPETGKKMIA GEIDVELVPQ GTLAERIRAG GAGLGGILTP TGVGTVVEEG KQKIQIDGRE YLLELPLKAD IAIIHAQKGD MNGNLAYELS ARNFNPLVAL AAKTVIAQVD NLLEVGQLPP DEVITPAALI DYIVCSE // ID ATOE_HAEIN Reviewed; 447 AA. AC P44051; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Short-chain fatty acids transporter; GN Name=atoE; OrderedLocusNames=HI_0772; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for the intake of short-chain fatty acids. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22431.1; -; Genomic_DNA. DR PIR; F64013; F64013. DR RefSeq; NP_438931.1; NC_000907.1. DR RefSeq; WP_005693163.1; NC_000907.1. DR STRING; 71421.HI0772; -. DR EnsemblBacteria; AAC22431; AAC22431; HI_0772. DR GeneID; 949788; -. DR KEGG; hin:HI0772; -. DR PATRIC; 20190195; VBIHaeInf48452_0811. DR eggNOG; ENOG4105CRW; Bacteria. DR eggNOG; COG2031; LUCA. DR KO; K02106; -. DR OMA; YSGFVIW; -. DR OrthoDB; EOG6DVJMZ; -. DR PhylomeDB; P44051; -. DR Proteomes; UP000000579; 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; IPR006161; CHP00366. DR InterPro; IPR006160; SCFA_transpt_AtoE. DR Pfam; PF02667; SCFA_trans; 1. DR TIGRFAMs; TIGR00366; TIGR00366; 1. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 447 Short-chain fatty acids transporter. FT /FTId=PRO_0000064734. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. FT TRANSMEM 284 304 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT TRANSMEM 359 379 Helical. {ECO:0000255}. FT TRANSMEM 402 422 Helical. {ECO:0000255}. FT TRANSMEM 427 447 Helical. {ECO:0000255}. SQ SEQUENCE 447 AA; 48443 MW; C6551EDA82517DF7 CRC64; MISRVSRFMT TFVSKYLPDP LIFAVLLTFV TFICAWGLTD STPVDLVNMW GNGFWNLLGF GMQMALIVVT GNALATSPQI RKFLSTIASI AKTPAQGVVL VTFMGSIACI INWGFGLVVG AMFAKEVARR IKGSDYALLI ACAYIAFMTW GGGFSGSMPL LAATPGNPVA HLMMSESNPQ GIIPAVSTLF SGYNIFITLS LVICLPFITY MMMPKNGETK SIDPKLIAPD PTFDKKLDKD ATLAEKMEES RFLAYTIGAL GYSYLGMYFY KNGFNLTINN VNLIFLITGI VLHGSPMAYM RAIINATRST AGILVQFPFY AGVQLMMEHS GLGGLITEFF INVANKDSFP LLTFFSSAFI NFAVPSGGGH WVIQGPFVIP AAQALGADLG KSTMAIAYGE QWMNMAQPFW ALPALGIAGL GVRDIMGFCM TALIFTAPIF IIGLYFL // ID ATPB_HAEIN Reviewed; 457 AA. AC P43715; DT 01-NOV-1995, 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}; GN OrderedLocusNames=HI_0479; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The catalytic sites are hosted CC primarily by the beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {ECO:0000255|HAMAP-Rule:MF_01347}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a(1), b(2) and c(9-12). The alpha and CC beta chains form an alternating ring which encloses part of the CC gamma chain. CF(1) is attached to CF(0) by a central stalk formed CC by the gamma and epsilon chains, while a peripheral stalk is CC formed by the delta and b chains. {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01347}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000255|HAMAP-Rule:MF_01347}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22137.1; -; Genomic_DNA. DR RefSeq; NP_438639.1; NC_000907.1. DR RefSeq; WP_005649402.1; NC_000907.1. DR ProteinModelPortal; P43715; -. DR SMR; P43715; 4-457. DR STRING; 71421.HI0479; -. DR PRIDE; P43715; -. DR EnsemblBacteria; AAC22137; AAC22137; HI_0479. DR GeneID; 950675; -. DR KEGG; hin:HI0479; -. DR PATRIC; 20189511; VBIHaeInf48452_0498. DR eggNOG; ENOG4105C4J; Bacteria. DR eggNOG; COG0055; LUCA. DR KO; K02112; -. DR OMA; FKESGVI; -. DR OrthoDB; EOG6HQSP3; -. DR PhylomeDB; P43715; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1140.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01347; ATP_synth_beta_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR005722; ATPase_F1-cplx_bsu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR024034; ATPase_F1_bsu/V1_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Hydrolase; Ion transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 457 ATP synthase subunit beta. FT /FTId=PRO_0000144443. FT NP_BIND 147 154 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 457 AA; 49835 MW; F202789770B963FE CRC64; MSAGKIVQII GAVIDVEFPQ DAVPKVYDAL KVESGLTLEV QQQLGGGVVR CIALGTSDGL KRGLKVENTN NPIQVPVGTK TLGRIMNVLG EPIDEQGAIG EEERWAIHRS APSYEEQSNS TELLETGIKV IDLICPFAKG GKVGLFGGAG VGKTVNMMEL IRNIAIEHSG YSVFAGVGER TREGNDFYHE MKDSNVLDKV SLVYGQMNEP PGNRLRVALT GLTMAEKFRD EGRDVLFFVD NIYRYTLAGT EVSALLGRMP SAVGYQPTLA EEMGVLQERI TSTKTGSITS VQAVYVPADD LTDPSPATTF AHLDSTVVLS RQIASLGIYP AVDPLDSTSR QLDPLVVGQE HYDVARGVQG ILQRYKELKD IIAILGMDEL SEEDKLVVAR ARKIERFLSQ PFFVAEVFTG SPGKYVTLKD TIRGFKGILD GEYDHIPEQA FYMVGSIDEV LEKAKNM // ID BIOA_HAEIN Reviewed; 430 AA. AC P44426; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE EC=2.6.1.62 {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00834}; GN Name=bioA {ECO:0000255|HAMAP-Rule:MF_00834}; GN OrderedLocusNames=HI_1554; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S- CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only CC animotransferase known to utilize SAM as an amino donor. CC {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7- CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8- CC diaminononanoate. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00834}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8- CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00834}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23203.1; -; Genomic_DNA. DR PIR; E64129; E64129. DR RefSeq; NP_439703.1; NC_000907.1. DR RefSeq; WP_005693582.1; NC_000907.1. DR ProteinModelPortal; P44426; -. DR SMR; P44426; 6-425. DR STRING; 71421.HI1554; -. DR EnsemblBacteria; AAC23203; AAC23203; HI_1554. DR GeneID; 950608; -. DR KEGG; hin:HI1554; -. DR PATRIC; 20191833; VBIHaeInf48452_1625. DR eggNOG; ENOG4108JPX; Bacteria. DR eggNOG; COG0161; LUCA. DR KO; K00833; -. DR OMA; YPWQERR; -. DR OrthoDB; EOG6QVRHN; -. DR PhylomeDB; P44426; -. DR UniPathway; UPA00078; UER00160. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00834; BioA; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR005815; BioA. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00508; bioA; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 430 Adenosylmethionine-8-amino-7-oxononanoate FT aminotransferase. FT /FTId=PRO_0000120369. FT REGION 114 115 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT REGION 311 312 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT BINDING 54 54 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 147 147 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 248 248 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 277 277 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 310 310 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT BINDING 394 394 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT SITE 19 19 Participates in the substrate recognition FT with KAPA and in a stacking interaction FT with the adenine ring of SAM. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT MOD_RES 277 277 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00834}. SQ SEQUENCE 430 AA; 47606 MW; 0E391250BC3B0602 CRC64; MVDEQSLLAF DTQHIWHPYS SVSSDMPLYA VERADGVMIT LKDGRRLIDG MSSWWAALHG YNHPRLNAAA QNQLAKMSHI MFGGFTHDPA VELAQLLVQI LPNGLDKIFF ADSGSVAVEV AMKMAIQYQH AKGEVQRQKF ATIRSGYHGD TWNAMSVCDP TTGMHHLFHH SLPVQYFLPQ PNIPFNESWN DCAIEPLADL LKKKGNEIAA LILEPVVQGA GGMYFYSPTY LVKAQALCKQ YGILLIFDEI ATGFGRTGKL FAAEHAGISP DIMCIGKALT GGYLTLSASI TTTEIAQTIC SGEAKCFMHG PTFMANPLAC AIAAESIRLL LESPWQQNIQ RIESSLKQQL SPLSEKDYVK EVRALGAIGV VEMKSAVNMK TLVPRFVEQG VWIRPFGKLV YVMPPFVIKD DELQKLTEGM ILALTQEYEH // ID ATPE_HAEIN Reviewed; 142 AA. AC P43718; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. 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=HI_0478; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000250}; CC Peripheral 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; L42023; AAC22136.1; -; Genomic_DNA. DR PIR; C64071; C64071. DR RefSeq; NP_438638.1; NC_000907.1. DR RefSeq; WP_005649396.1; NC_000907.1. DR ProteinModelPortal; P43718; -. DR SMR; P43718; 2-136. DR STRING; 71421.HI0478; -. DR EnsemblBacteria; AAC22136; AAC22136; HI_0478. DR GeneID; 950629; -. DR KEGG; hin:HI0478; -. DR PATRIC; 20189509; VBIHaeInf48452_0497. DR eggNOG; ENOG4105KNM; Bacteria. DR eggNOG; COG0355; LUCA. DR KO; K02114; -. DR OMA; HHRAEVA; -. DR OrthoDB; EOG690MN9; -. DR PhylomeDB; P43718; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.15.10; -; 1. DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1. DR InterPro; IPR001469; ATPase_F1-cplx_dsu/esu. DR InterPro; IPR020546; ATPase_F1-cplx_dsu/esu_N. DR InterPro; IPR020547; ATPase_F1_dsu/esu_C. DR PANTHER; PTHR13822; PTHR13822; 1. DR Pfam; PF02823; ATP-synt_DE_N; 1. DR ProDom; PD000944; ATPase_F1-cplx_dsu/esu; 1. DR SUPFAM; SSF46604; SSF46604; 1. DR SUPFAM; SSF51344; SSF51344; 1. DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 142 ATP synthase epsilon chain. FT /FTId=PRO_0000188142. SQ SEQUENCE 142 AA; 15591 MW; E5BBDE1DA34A9039 CRC64; MATFNLTIVS AEQKIFEGEV KQIQVTGVEG ELGILPGHTP LLTAIKPGIV KFTLKDGNEE VIYVSGGFLE VQPNIVTVLA DIAIRGSELD ADRIHEAKRK AEENIVSRGS DADHDLLVAK LSKELAKLRA YELTEKLLKT RR // ID ATPG_HAEIN Reviewed; 289 AA. AC P43716; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. 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}; GN OrderedLocusNames=HI_0480; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 inner 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; L42023; AAC22138.1; -; Genomic_DNA. DR PIR; E64071; E64071. DR RefSeq; NP_438640.1; NC_000907.1. DR RefSeq; WP_005693686.1; NC_000907.1. DR ProteinModelPortal; P43716; -. DR SMR; P43716; 19-250. DR STRING; 71421.HI0480; -. DR EnsemblBacteria; AAC22138; AAC22138; HI_0480. DR GeneID; 949567; -. DR KEGG; hin:HI0480; -. DR PATRIC; 20189513; VBIHaeInf48452_0499. DR eggNOG; ENOG4105J80; Bacteria. DR eggNOG; COG0224; LUCA. DR KO; K02115; -. DR OMA; DRGMCGG; -. DR OrthoDB; EOG6R5C97; -. DR PhylomeDB; P43716; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1. DR InterPro; IPR000131; ATPase_F1-cplx_gsu. DR InterPro; IPR023632; ATPase_F1_gsu_CS. DR InterPro; IPR023633; ATPase_F1_gsu_dom. DR PANTHER; PTHR11693; PTHR11693; 1. DR Pfam; PF00231; ATP-synt; 1. DR PRINTS; PR00126; ATPASEGAMMA. DR SUPFAM; SSF52943; SSF52943; 1. DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1. DR PROSITE; PS00153; ATPASE_GAMMA; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Complete proteome; Hydrogen ion transport; Ion transport; Membrane; KW Reference proteome; Transport. FT CHAIN 1 289 ATP synthase gamma chain. FT /FTId=PRO_0000073292. SQ SEQUENCE 289 AA; 32069 MW; 622CBA682F37FD00 CRC64; MAGAKEIKTK IASVQSTQKI TKAMEMVATS KMRKTQDRMA ASRPYSETIR NVISHVSKAS IGYKHPFLVE REVKKIGILV ISTDRGMCGG LNVNLFKTTL NQIKNWKEQN ISTDLGLIGS KGISFFRSFG FNIKGQLSGL GDTPALEELI GVANTMFDAY RNGEIDAVYI AYNKFVNTMS QKPVVQQLVP LPESKDDHLN ERQQTWDYLY EPEPKVLLDS LLVRYLESQI YQAVVDNVAS EQAARMVAMK AATDNAGNLI NDLRLVYNKA RQASITNELN EIVAGAAAI // ID BAMA_HAEIN Reviewed; 795 AA. AC P44935; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 100. DE RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000255|HAMAP-Rule:MF_01430}; DE AltName: Full=80 kDa D15 antigen; DE Short=D-15-Ag; DE AltName: Full=Outer membrane protein D15; DE AltName: Full=Protective surface antigen D15; DE Flags: Precursor; GN Name=bamA {ECO:0000255|HAMAP-Rule:MF_01430}; GN OrderedLocusNames=HI_0917; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SIMILARITY: Belongs to the BamA family. {ECO:0000255|HAMAP- CC Rule:MF_01430}. CC -!- SIMILARITY: Contains 5 POTRA domains. {ECO:0000255|PROSITE- CC ProRule:PRU01115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22575.1; -; Genomic_DNA. DR RefSeq; NP_439077.1; NC_000907.1. DR RefSeq; WP_005693264.1; NC_000907.1. DR ProteinModelPortal; P44935; -. DR STRING; 71421.HI0917; -. DR EnsemblBacteria; AAC22575; AAC22575; HI_0917. DR GeneID; 949634; -. DR KEGG; hin:HI0917; -. DR PATRIC; 20190489; VBIHaeInf48452_0958. DR eggNOG; ENOG4105E1Z; Bacteria. DR eggNOG; COG4775; LUCA. DR KO; K07277; -. DR OMA; NLDRGYF; -. DR OrthoDB; EOG6F81K6; -. DR PhylomeDB; P44935; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01430; OM_assembly_BamA; 1. DR InterPro; IPR000184; Bac_surfAg_D15. DR InterPro; IPR023707; OM_assembly_BamA. DR InterPro; IPR010827; Surface_Ag_variable_number. DR Pfam; PF01103; Bac_surface_Ag; 1. DR Pfam; PF07244; POTRA; 4. DR PIRSF; PIRSF006076; OM_assembly_OMP85; 1. DR TIGRFAMs; TIGR03303; OM_YaeT; 1. DR PROSITE; PS51779; POTRA; 5. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 19 {ECO:0000255|HAMAP-Rule:MF_01430}. FT CHAIN 20 795 Outer membrane protein assembly factor FT BamA. FT /FTId=PRO_0000033468. FT DOMAIN 22 89 POTRA 1. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 90 170 POTRA 2. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 173 259 POTRA 3. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 262 341 POTRA 4. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. FT DOMAIN 344 418 POTRA 5. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 795 AA; 87479 MW; B85691FC22E6ED44 CRC64; MKKLLIASLL FGTTTTVFAA PFVAKDIRVD GVQGDLEQQI RASLPVRAGQ RVTDNDVANI VRSLFVSGRF DDVKAHQEGD VLVVSVVAKS IISDVKIKGN SIIPTEALKQ NLDANGFKVG DVLIREKLNE FAKSVKEHYA SVGRYNATVE PIVNTLPNNR AEILIQINED DKAKLASLTF KGNESVSSST LQEQMELQPD SWWKLWGNKF EGAQFEKDLQ SIRDYYLNNG YAKAQITKTD VQLNDEKTKV NVTIDVNEGL QYDLRSARII GNLGGMSAEL EPLLSALHLN DTFRRSDIAD VENAIKAKLG ERGYGSATVN SVPDFDDANK TLAITLVVDA GRRLTVRQLR FEGNTVSADS TLRQEMRQQE GTWYNSQLVE LGKIRLDRTG FFETVENRID PINGSNDEVD VVYKVKERNT GSINFGIGYG TESGISYQAS VKQDNFLGTG AAVSIAGTKN DYGTSVNLGY TEPYFTKDGV SLGGNVFFEN YDNSKSDTSS NYKRTTYGSN VTLGFPVNEN NSYYVGLGHT YNKISNFALE YNRNLYIQSM KFKGNGIKTN DFDFSFGWNY NSLNRGYFPT KGVKASLGGR VTIPGSDNKY YKLSADVQGF YPLDRDHLWV VSAKASAGYA NGFGNKRLPF YQTYTAGGIG SLRGFAYGSI GPNAIYAEHG NGNGTFKKIS SDVIGGNAIT TASAELIVPT PFVSDKSQNT VRTSLFVDAA SVWNTKWKSD KSGLDNNVLK SLPDYGKSSR IRASTGVGFQ WQSPIGPLVF SYAKPIKKYE NDDVEQFQFS IGGSF // ID BCR_HAEIN Reviewed; 398 AA. AC P45123; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Bicyclomycin resistance protein homolog; GN Name=bcr; OrderedLocusNames=HI_1242; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in sulfonamide (sulfathiazole) and bicyclomycin CC resistance. Probable membrane translocase (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Bcr/CmlA 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; L42023; AAC22894.1; -; Genomic_DNA. DR PIR; E64112; E64112. DR RefSeq; NP_439398.1; NC_000907.1. DR RefSeq; WP_005694302.1; NC_000907.1. DR ProteinModelPortal; P45123; -. DR STRING; 71421.HI1242; -. DR EnsemblBacteria; AAC22894; AAC22894; HI_1242. DR GeneID; 949578; -. DR KEGG; hin:HI1242; -. DR PATRIC; 20191163; VBIHaeInf48452_1294. DR eggNOG; ENOG4105C2C; Bacteria. DR eggNOG; ENOG410XNNX; LUCA. DR KO; K07552; -. DR OMA; CEAEIEL; -. DR OrthoDB; EOG6RJV6T; -. DR PhylomeDB; P45123; -. DR Proteomes; UP000000579; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004812; Efflux_drug-R_Bcr/CmlA. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00710; efflux_Bcr_CflA; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 398 Bicyclomycin resistance protein homolog. FT /FTId=PRO_0000173316. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 102 122 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TRANSMEM 343 363 Helical. {ECO:0000255}. FT TRANSMEM 369 389 Helical. {ECO:0000255}. SQ SEQUENCE 398 AA; 43459 MW; F681C5C654675216 CRC64; MNQQKSTFIF ILTLGILSML PPFGVDMYLP SFLEIAKDLD VSPEQVQHTL TSFAYGMAFG QLFWGPFGDS FGRKPIILLG VIVGALTALV LTEINSVGNF TALRFVQGFF GAAPVVLSGA LLRDLFSKDQ LSKVMSTITL VFMLAPLVAP IIGGYIVKFF HWHAIFYVIS LVGLLAAALV FFIIPETHKK ENRIPLRLNI IARNFLLLWK QKEVLGYMFA ASFSFGGLFA FVTAGSIVYI GIYGVPVDQF GYFFMMNIVT MIFASFLNSR FVTKVGAETM LRIALAIQFL SGMWLILTAL LDLGFWPMAI GVAFFVGPNP VISSNAMASA LERCPQMAGT ANSLIGSVRF AVGAIMGSLV ASMKMDTAAP MLFTMGACVV ISVLAYYFLT SRNLKSRG // ID BCP_HAEIN Reviewed; 155 AA. AC P44411; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative peroxiredoxin bcp; DE EC=1.11.1.15; DE AltName: Full=Bacterioferritin comigratory protein homolog; DE AltName: Full=Thioredoxin reductase; GN Name=bcp; OrderedLocusNames=HI_0254; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SIMILARITY: Belongs to the AhpC/TSA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21920.1; -; Genomic_DNA. DR PIR; I64057; I64057. DR RefSeq; NP_438423.1; NC_000907.1. DR RefSeq; WP_005694049.1; NC_000907.1. DR ProteinModelPortal; P44411; -. DR STRING; 71421.HI0254; -. DR EnsemblBacteria; AAC21920; AAC21920; HI_0254. DR GeneID; 949377; -. DR KEGG; hin:HI0254; -. DR PATRIC; 20189033; VBIHaeInf48452_0269. DR eggNOG; ENOG4108YXY; Bacteria. DR eggNOG; COG1225; LUCA. DR KO; K03564; -. DR OMA; YDSYGLK; -. DR OrthoDB; EOG6ZH2P1; -. DR PhylomeDB; P44411; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00578; AhpC-TSA; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Peroxidase; Redox-active center; KW Reference proteome. FT CHAIN 1 155 Putative peroxiredoxin bcp. FT /FTId=PRO_0000135137. FT DOMAIN 4 155 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT ACT_SITE 46 46 {ECO:0000250}. SQ SEQUENCE 155 AA; 17553 MW; 0E7AC12651107EA2 CRC64; MNPLSVGNQA PAFTLLNQQE KFVSLSDFRG KKVLIYFYPK ALTPGCTTQA CGLRDSKSEL DVLGLVVLGI SPDAPKKLAQ FIEKKELNFT LLSDPDHQVA EQFGVWGEKK FMGRTYDGIH RISFLINESG TIMQVFDKFK IKDHHQMIID YLRSL // ID AZOR_HAEIN Reviewed; 194 AA. AC P43013; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 92. 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}; GN OrderedLocusNames=HI_1366; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6; RA Chandler M.S., Smith R.A.; RT "Characterization of the Haemophilus influenzae topA locus: DNA RT topoisomerase I is required for genetic competence."; RL Gene 169:25-31(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20964; AAC43728.1; -; Genomic_DNA. DR EMBL; L42023; AAC23013.1; -; Genomic_DNA. DR PIR; G64026; G64026. DR RefSeq; NP_439517.1; NC_000907.1. DR RefSeq; WP_005693994.1; NC_000907.1. DR ProteinModelPortal; P43013; -. DR SMR; P43013; 1-193. DR STRING; 71421.HI1366; -. DR EnsemblBacteria; AAC23013; AAC23013; HI_1366. DR GeneID; 950279; -. DR KEGG; hin:HI1366; -. DR PATRIC; 20191419; VBIHaeInf48452_1420. DR eggNOG; ENOG4108V3G; Bacteria. DR eggNOG; COG1182; LUCA. DR KO; K01118; -. DR OMA; EVNPNTE; -. DR OrthoDB; EOG6QRW9T; -. DR PhylomeDB; P43013; -. DR Proteomes; UP000000579; 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 1 194 FMN-dependent NADH-azoreductase. FT /FTId=PRO_0000166320. SQ SEQUENCE 194 AA; 21208 MW; A8AEC9D00829522C CRC64; MSNVLVLKSS ISGNNSQTNQ LADYVIEKLQ GNNIVVRDLS QQPLPYFDTA AAIAVRGEPK TTEEKQLLAL SDKLIEELKN AQTLIIGAPM YNLNVPTQLK SYFDFIARPR VTFQYTANGS EGLLKGKKAI LLCAFGGLYD EENLVTQYMK SILGFIGITD VQFVYAQGIG FGPEAIEKAQ ASAKNKINEI VAAL // ID BAMCH_HAEIN Reviewed; 215 AA. AC P43973; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Outer membrane protein assembly factor BamC homolog; DE Flags: Precursor; GN OrderedLocusNames=HI_0256; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the BamC family. {ECO:0000305}. CC -!- CAUTION: This sequence is shorter than orthologs. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21922.1; -; Genomic_DNA. DR PIR; I64004; I64004. DR RefSeq; NP_438425.1; NC_000907.1. DR RefSeq; WP_005694048.1; NC_000907.1. DR STRING; 71421.HI0256; -. DR DNASU; 949378; -. DR EnsemblBacteria; AAC21922; AAC21922; HI_0256. DR GeneID; 949378; -. DR KEGG; hin:HI0256; -. DR PATRIC; 20189037; VBIHaeInf48452_0271. DR eggNOG; COG3317; LUCA. DR KO; K07287; -. DR OMA; DKQRYAS; -. DR OrthoDB; EOG6QVRD3; -. DR PhylomeDB; P43973; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR010653; NlpB/DapX. DR Pfam; PF06804; Lipoprotein_18; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 16 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 17 215 Outer membrane protein assembly factor FT BamC homolog. FT /FTId=PRO_0000077903. FT LIPID 17 17 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 17 17 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 215 AA; 24012 MW; 1CABB7F749E35FB5 CRC64; MKKIILNLVT AIILAGCSSN PETLKATNDS FQKSETSIPH FSPLATGGVQ LPKADDSYSL PNIEVKKGED IDIRPPLIPL AIIQNSITKF DGERSLIVYP KQQAKLYNLQ QVERLLKEEG ISSTTDGSIL TTDWAKTERI GDKSIEIKYQ IEQVMTADVS ALTVSILHMR RDGIIFTPNV SDKQYYTSER LNRIVLTLTT AYNKQLRDLS STLIQ // ID BIOD1_HAEIN Reviewed; 242 AA. AC P45209; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE Short=DTBS 1 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase 1 {ECO:0000255|HAMAP-Rule:MF_00336}; GN Name=bioD1 {ECO:0000255|HAMAP-Rule:MF_00336}; Synonyms=bioD-A; GN OrderedLocusNames=HI_1445; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP + CC phosphate + dethiobiotin. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23095.1; -; Genomic_DNA. DR PIR; I64123; I64123. DR RefSeq; NP_439597.1; NC_000907.1. DR RefSeq; WP_005693920.1; NC_000907.1. DR ProteinModelPortal; P45209; -. DR STRING; 71421.HI1445; -. DR EnsemblBacteria; AAC23095; AAC23095; HI_1445. DR GeneID; 950720; -. DR KEGG; hin:HI1445; -. DR PATRIC; 20191595; VBIHaeInf48452_1507. DR eggNOG; ENOG4105E78; Bacteria. DR eggNOG; COG0132; LUCA. DR KO; K01935; -. DR OMA; ANRINPC; -. DR OrthoDB; EOG66B3XT; -. DR PhylomeDB; P45209; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00347; bioD; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 242 ATP-dependent dethiobiotin synthetase FT BioD 1. FT /FTId=PRO_0000187969. FT NP_BIND 12 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 184 185 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 213 215 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT METAL 12 12 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 16 16 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 66 66 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 124 124 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 66 66 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT BINDING 220 220 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. SQ SEQUENCE 242 AA; 26967 MW; 94FCC0501CFAF262 CRC64; MSSFFVAGTD TNVGKTTAAR AMIQALQGQG VQVVGYKPIA CCGEESIYPV AQSENTSDYD HFVNADVLTL MHSTKENVSY QDINSYTFSH CAPMLTQDKM RIKLDKINCD LTRLNQTYQS VVVEGSFGLM TPMAEGKSFA DWIAQQKMPV VLVVGIKDGC VNHALLTVKV IQQLGVPLLG WIANRINPLL SHYAEIVDLL VEHIDAPLLG KIPYLHKPEE QELGHYLTNI DRLMYMQTEF IK // ID BAME_HAEIN Reviewed; 137 AA. AC P44057; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 09-DEC-2015, entry version 90. DE RecName: Full=Outer membrane protein assembly factor BamE {ECO:0000255|HAMAP-Rule:MF_00925}; DE Flags: Precursor; GN Name=bamE {ECO:0000255|HAMAP-Rule:MF_00925}; Synonyms=smpA; GN OrderedLocusNames=HI_0838; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the outer membrane protein assembly complex, CC which is involved in assembly and insertion of beta-barrel CC proteins into the outer membrane. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_00925}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00925}. CC -!- SIMILARITY: Belongs to the BamE family. {ECO:0000255|HAMAP- CC Rule:MF_00925}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22496.1; 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; L42023; AAC22496.1; ALT_INIT; Genomic_DNA. DR PIR; C64014; C64014. DR RefSeq; NP_438998.2; NC_000907.1. DR RefSeq; WP_005693190.1; NC_000907.1. DR ProteinModelPortal; P44057; -. DR STRING; 71421.HI0838; -. DR EnsemblBacteria; AAC22496; AAC22496; HI_0838. DR GeneID; 949852; -. DR KEGG; hin:HI0838; -. DR PATRIC; 20190331; VBIHaeInf48452_0879. DR eggNOG; ENOG4105YRI; Bacteria. DR eggNOG; COG2913; LUCA. DR KO; K06186; -. DR OMA; QPGHEKV; -. DR OrthoDB; EOG6J48RK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0051205; P:protein insertion into membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00925; OM_assembly_BamE; 1. DR InterPro; IPR026592; BamE. DR InterPro; IPR007450; Lipoprotein_SmpA/OmlA. DR Pfam; PF04355; SmpA_OmlA; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255|HAMAP-Rule:MF_00925}. FT CHAIN 19 137 Outer membrane protein assembly factor FT BamE. FT /FTId=PRO_0000032812. FT LIPID 19 19 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_00925}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_00925}. SQ SEQUENCE 137 AA; 15647 MW; B411EC3B6BE0C4FE CRC64; MQVKTLLGAT FLALSLASCS TVEKVVYRID VPQGNYLEAT TVAQVKEGMT AQQVQYLLGT PVLVDPYNSQ TWYYVFLQQR AYETPVQHTF TVKFDQRGIV TETHLDKPLP QVSQQGENNT IIETGEKPKS SWWKFWK // ID BCCP_HAEIN Reviewed; 155 AA. AC P43874; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase; DE Short=BCCP; GN Name=accB; Synonyms=fabE; OrderedLocusNames=HI_0971; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 1-10. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A CC carboxylase complex; first, biotin carboxylase catalyzes the CC carboxylation of the carrier protein and then the transcarboxylase CC transfers the carboxyl group to form malonyl-CoA. {ECO:0000250}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 biotinyl-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; L42023; AAC22631.1; -; Genomic_DNA. DR PIR; E64105; E64105. DR RefSeq; NP_439132.1; NC_000907.1. DR RefSeq; WP_005693317.1; NC_000907.1. DR ProteinModelPortal; P43874; -. DR SMR; P43874; 76-155. DR STRING; 71421.HI0971; -. DR PRIDE; P43874; -. DR EnsemblBacteria; AAC22631; AAC22631; HI_0971. DR GeneID; 949974; -. DR KEGG; hin:HI0971; -. DR PATRIC; 20190599; VBIHaeInf48452_1012. DR eggNOG; ENOG4105KM4; Bacteria. DR eggNOG; COG0511; LUCA. DR KO; K02160; -. DR OMA; KMFNQIE; -. DR OrthoDB; EOG6CVV6Z; -. DR PhylomeDB; P43874; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001249; AcCoA_biotinCC. DR InterPro; IPR001882; Biotin_BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR PRINTS; PR01071; ACOABIOTINCC. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR00531; BCCP; 1. DR PROSITE; PS00188; BIOTIN; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. PE 1: Evidence at protein level; KW Biotin; Complete proteome; Direct protein sequencing; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Reference proteome. FT CHAIN 1 155 Biotin carboxyl carrier protein of FT acetyl-CoA carboxylase. FT /FTId=PRO_0000146808. FT DOMAIN 72 155 Biotinyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT MOD_RES 121 121 N6-biotinyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. SQ SEQUENCE 155 AA; 16247 MW; 696F19B4429A03CD CRC64; MDIRKIKKLI ELVEESGITE LEVQEEEGTV RISRAAPVIA PAAVQYAAAP VVAPTPAAAP AQVPAAATTA PAASDELSGH LVRSPMVGTF YRSPSPEAKA FVEVGQSVKV GDALCIVEAM KMMNRIEADK AGVVKAILIN DGNAVEFDEP LIVIE // ID BIOB_HAEIN Reviewed; 333 AA. AC P44987; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694}; DE EC=2.8.1.6 {ECO:0000255|HAMAP-Rule:MF_01694}; GN Name=bioB {ECO:0000255|HAMAP-Rule:MF_01694}; GN OrderedLocusNames=HI_1022; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin CC by the insertion of a sulfur atom into dethiobiotin via a radical- CC based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S- CC adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + CC (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. {ECO:0000255|HAMAP-Rule:MF_01694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22682.1; -; Genomic_DNA. DR PIR; F64108; F64108. DR RefSeq; NP_439182.1; NC_000907.1. DR RefSeq; WP_005655985.1; NC_000907.1. DR ProteinModelPortal; P44987; -. DR SMR; P44987; 19-326. DR STRING; 71421.HI1022; -. DR DNASU; 950009; -. DR EnsemblBacteria; AAC22682; AAC22682; HI_1022. DR GeneID; 950009; -. DR KEGG; hin:HI1022; -. DR PATRIC; 20190707; VBIHaeInf48452_1066. DR eggNOG; ENOG4105CZF; Bacteria. DR eggNOG; COG0502; LUCA. DR KO; K01012; -. DR OMA; PFDFIRM; -. DR OrthoDB; EOG622PMP; -. DR PhylomeDB; P44987; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01694; BioB; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR002684; Biotin_synth/BioAB. DR InterPro; IPR024177; Biotin_synthase. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF001619; Biotin_synth; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 333 Biotin synthase. FT /FTId=PRO_0000185554. FT METAL 66 66 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 70 70 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 73 73 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 110 110 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 141 141 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 201 201 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 273 273 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. SQ SEQUENCE 333 AA; 36785 MW; AD9F3A676878E1DB CRC64; MLAEKLQINS ITPHPSVEYW SVCKVEALFE TPFLELVYRA TQVHRKHFNP RAIQLSTLMS IKTGGCPEDC SYCPQSARYH TGVQNQQLLD VDEIVAKAKI AKARGAGRFC MGAAWRGPKP KDIEKVTEII KAVKSLGLET CGTFGLLQDG MAEDLKEAGL DYYNHNLDTA PEHYAEVIGT RRFDDRLSTL GKVRKAGLKV CCGGIVGMNE TRKERAGLIA SLANLDPQPE SVPINQLVKV EGTPLADAEE LDWTEFVRTI AVARITMPKS YVRLSAGRSG MTEEMQAMCF MAGANSIFYG DKLLVTDNPE EDGDQLLMAK LDLEPETAEN KKL // ID BIOD2_HAEIN Reviewed; 191 AA. AC P45248; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD 2 {ECO:0000255|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00336}; DE Short=DTBS 2 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase 2 {ECO:0000255|HAMAP-Rule:MF_00336}; GN Name=bioD2 {ECO:0000255|HAMAP-Rule:MF_00336}; Synonyms=bioD-B; GN OrderedLocusNames=HI_1550; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP + CC phosphate + dethiobiotin. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23200.1; -; Genomic_DNA. DR PIR; B64129; B64129. DR RefSeq; NP_439699.1; NC_000907.1. DR RefSeq; WP_010869244.1; NC_000907.1. DR ProteinModelPortal; P45248; -. DR STRING; 71421.HI1550; -. DR EnsemblBacteria; AAC23200; AAC23200; HI_1550. DR GeneID; 950414; -. DR KEGG; hin:HI1550; -. DR PATRIC; 20191825; VBIHaeInf48452_1621. DR eggNOG; ENOG4105E78; Bacteria. DR eggNOG; COG0132; LUCA. DR KO; K01935; -. DR OMA; NGYPEYD; -. DR OrthoDB; EOG66B3XT; -. DR PhylomeDB; P45248; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00347; bioD; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 191 ATP-dependent dethiobiotin synthetase FT BioD 2. FT /FTId=PRO_0000187970. FT NP_BIND 13 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 115 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT METAL 13 13 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 17 17 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 50 50 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 115 115 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 42 42 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 50 50 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. SQ SEQUENCE 191 AA; 21097 MW; 7C899BEC3FE60406 CRC64; MGKVIFISGI DTDVGKTIAT GIYAKKLMEQ GCSVITQKMI QTGCKNIADD LLVHRKIQGI DLTEEDLQGK TCPYVFEYPC SPHLAAKRES RKIEAKIIEK STALLAEKYD YVLLEGAGGL MVPYCEEATT LDYIQLNNYP LILVTSGKLG SINHTLLSLE ACRTRGISVL SVMYNGYPEY DLLLVKKPNA I // ID BIOC_HAEIN Reviewed; 260 AA. AC P45249; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835}; DE Short=Malonyl-ACP O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835}; DE EC=2.1.1.197 {ECO:0000255|HAMAP-Rule:MF_00835}; DE AltName: Full=Biotin synthesis protein BioC {ECO:0000255|HAMAP-Rule:MF_00835}; GN Name=bioC {ECO:0000255|HAMAP-Rule:MF_00835}; GN OrderedLocusNames=HI_1551; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester CC to its methyl ester by transfer of a methyl group from S-adenosyl- CC L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the CC fatty acid synthetic pathway. {ECO:0000255|HAMAP-Rule:MF_00835}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + malonyl-[acyl- CC carrier protein] = S-adenosyl-L-homocysteine + malonyl-[acyl- CC carrier protein] methyl ester. {ECO:0000255|HAMAP-Rule:MF_00835}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00835}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000255|HAMAP-Rule:MF_00835}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23201.1; -; Genomic_DNA. DR PIR; C64129; C64129. DR RefSeq; NP_439700.1; NC_000907.1. DR RefSeq; WP_005693577.1; NC_000907.1. DR ProteinModelPortal; P45249; -. DR STRING; 71421.HI1551; -. DR DNASU; 950415; -. DR EnsemblBacteria; AAC23201; AAC23201; HI_1551. DR GeneID; 950415; -. DR KEGG; hin:HI1551; -. DR PATRIC; 20191827; VBIHaeInf48452_1622. DR eggNOG; ENOG41090JN; Bacteria. DR eggNOG; ENOG4111P8N; LUCA. DR KO; K02169; -. DR OMA; SADYWLF; -. DR OrthoDB; EOG6GXTQ5; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00835; BioC; 1. DR InterPro; IPR011814; BioC. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02072; BioC; 1. PE 3: Inferred from homology; KW Biotin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 260 Malonyl-[acyl-carrier protein] O- FT methyltransferase. FT /FTId=PRO_0000204418. SQ SEQUENCE 260 AA; 29676 MW; 654C546338645F06 CRC64; MGSLTSVDKS RIRQAFQKAL NDYDRHALIQ QKMTINLMAH LQDYLPNGSL DSVLELGCGS GMLSSLLQKQ ISADYWLFND LCDVQTQLAE KLPQSFDFYC GDAEHFLFLQ QFDLIASASA VQWFHQPDAF IAHCKTGLKT NGLLAVATFG EDNLKEVRQI TNIGLNYPTL SQWQTWLAKD FELLWCEDFK VILDFDTPLD VLKHLKYTGV TATNQKNWTR KNLNGFIGDY LSAFGMPSGK VRLTYHPLFF IARYSHIENQ // ID BIRA_HAEIN Reviewed; 302 AA. AC P46363; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Bifunctional ligase/repressor BirA {ECO:0000255|HAMAP-Rule:MF_00978}; DE AltName: Full=Biotin operon repressor {ECO:0000255|HAMAP-Rule:MF_00978}; DE AltName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000255|HAMAP-Rule:MF_00978}; DE EC=6.3.4.15 {ECO:0000255|HAMAP-Rule:MF_00978}; DE AltName: Full=Biotin--protein ligase {ECO:0000255|HAMAP-Rule:MF_00978}; DE AltName: Full=Biotin-[acetyl-CoA carboxylase] synthetase {ECO:0000255|HAMAP-Rule:MF_00978}; GN Name=birA {ECO:0000255|HAMAP-Rule:MF_00978}; GN OrderedLocusNames=HI_0220.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Acts both as a biotin--[acetyl-CoA-carboxylase] ligase CC and a biotin-operon repressor. In the presence of ATP, BirA CC activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio- CC 5'-AMP or holoBirA) complex. HoloBirA can either transfer the CC biotinyl moiety to the biotin carboxyl carrier protein (BCCP) CC subunit of acetyl-CoA carboxylase, or bind to the biotin operator CC site and inhibit transcription of the operon. {ECO:0000255|HAMAP- CC Rule:MF_00978}. CC -!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide CC ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon- CC dioxide ligase (ADP-forming)]. {ECO:0000255|HAMAP-Rule:MF_00978}. CC -!- SIMILARITY: Belongs to the biotin--protein ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00978}. 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; L42023; AAC21889.1; -; Genomic_DNA. DR RefSeq; NP_438391.1; NC_000907.1. DR RefSeq; WP_005694072.1; NC_000907.1. DR ProteinModelPortal; P46363; -. DR STRING; 71421.HI0220.1; -. DR EnsemblBacteria; AAC21889; AAC21889; HI_0220.1. DR GeneID; 951136; -. DR KEGG; hin:HI0220.1; -. DR PATRIC; 20188959; VBIHaeInf48452_0232. DR eggNOG; ENOG4105HJX; Bacteria. DR eggNOG; COG0340; LUCA. DR eggNOG; COG1654; LUCA. DR KO; K03524; -. DR OMA; VEIANHK; -. DR OrthoDB; EOG6DNTBX; -. DR PhylomeDB; P46363; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009305; P:protein biotinylation; 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 HAMAP; MF_00978; Bifunct_BirA; 1. DR InterPro; IPR030855; Bifunct_BirA. DR InterPro; IPR004408; Biotin_CoA_COase_ligase. DR InterPro; IPR004409; Biotin_operon_repress_HTH. DR InterPro; IPR003142; BPL_C. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR008988; Transcriptional_repressor_C. DR PANTHER; PTHR12835; PTHR12835; 1. DR Pfam; PF02237; BPL_C; 1. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR SUPFAM; SSF50037; SSF50037; 1. DR TIGRFAMs; TIGR00121; birA_ligase; 1. DR TIGRFAMs; TIGR00122; birA_repr_reg; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin; Complete proteome; DNA-binding; Ligase; KW Nucleotide-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 302 Bifunctional ligase/repressor BirA. FT /FTId=PRO_0000064933. FT DOMAIN 62 236 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT DNA_BIND 14 33 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00978}. FT REGION 80 82 Biotin binding. {ECO:0000255|HAMAP- FT Rule:MF_00978}. FT REGION 107 109 Biotin binding. {ECO:0000255|HAMAP- FT Rule:MF_00978}. FT BINDING 103 103 Biotin. {ECO:0000255|HAMAP- FT Rule:MF_00978}. FT BINDING 167 167 Biotin. {ECO:0000255|HAMAP- FT Rule:MF_00978}. SQ SEQUENCE 302 AA; 34342 MW; 50EE9D6E9820378B CRC64; MMNFTLLTYL ADCQPKVRSE LEKFSKNLEE DIQQLREIGL DILVDGQDYR LVPMLPLLNP QQISTALFPY SIHYQPIISS TNEWILQNIL SLKKGDLCVA EYQTAGRGRR GRQWLSPFAG QIMFSFYWAF DPKKSIEGLS LVIGLAIAEV LNVQVKWPND ILFDERKLGG ILVEIANHKN GMLNLVIGIG INVSLSKQTE ISQPYAEVCE IDPDVERQTL LPKLIQHLYT RLNIFEQNGI DEEFQQAWQS YNAFSNSEIN VLTEQGVISG IEQGIDERGY LKVLCGNKIQ MFNGGEVSLR KK // ID BOLA_HAEIN Reviewed; 103 AA. AC P43780; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=DNA-binding transcriptional regulator BolA {ECO:0000250|UniProtKB:P0ABE2}; GN Name=bolA; OrderedLocusNames=HI_0163; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transcriptional regulator that plays an important role CC in general stress response. {ECO:0000250|UniProtKB:P0ABE2}. CC -!- SIMILARITY: Belongs to the BolA/IbaG 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; U20229; AAA62135.1; -; Genomic_DNA. DR EMBL; L42023; AAC21835.1; -; Genomic_DNA. DR PIR; B64052; B64052. DR RefSeq; NP_438333.1; NC_000907.1. DR RefSeq; WP_005668108.1; NC_000907.1. DR ProteinModelPortal; P43780; -. DR STRING; 71421.HI0163; -. DR EnsemblBacteria; AAC21835; AAC21835; HI_0163. DR GeneID; 951075; -. DR KEGG; hin:HI0163; -. DR PATRIC; 20188825; VBIHaeInf48452_0169. DR eggNOG; ENOG4105M85; Bacteria. DR eggNOG; COG0271; LUCA. DR KO; K05527; -. DR OMA; INESHNH; -. DR OrthoDB; EOG6VMTQ7; -. DR PhylomeDB; P43780; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.300.90; -; 1. DR InterPro; IPR002634; BolA. DR Pfam; PF01722; BolA; 1. DR PIRSF; PIRSF003113; BolA; 1. DR SUPFAM; SSF82657; SSF82657; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Stress response; KW Transcription; Transcription regulation. FT CHAIN 1 103 DNA-binding transcriptional regulator FT BolA. FT /FTId=PRO_0000201215. SQ SEQUENCE 103 AA; 12057 MW; EF0DF80DE747FA90 CRC64; MSIQQIIEQK IQKEFQPHFL AIENESHLHH SNRGSESHFK CVIVSADFKN IRKVQRHQRI YQLLNEELNH SIHALALHLF TPEEWKAQNE TVPHSTKCAG IGR // ID CAN_HAEIN Reviewed; 229 AA. AC P45148; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 103. DE RecName: Full=Carbonic anhydrase 2; DE EC=4.2.1.1 {ECO:0000269|PubMed:16584170}; DE AltName: Full=Carbonate dehydratase 2; GN Name=can; OrderedLocusNames=HI_1301; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ZINC ION, RP CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=16584170; DOI=10.1021/bi052272q; RA Cronk J.D., Rowlett R.S., Zhang K.Y., Tu C., Endrizzi J.A., Lee J., RA Gareiss P.C., Preiss J.R.; RT "Identification of a novel noncatalytic bicarbonate binding site in RT eubacterial beta-carbonic anhydrase."; RL Biochemistry 45:4351-4361(2006). CC -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O. CC {ECO:0000269|PubMed:16584170}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:16584170}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16584170}; CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase 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; L42023; AAC22946.1; -; Genomic_DNA. DR PIR; F64170; F64170. DR RefSeq; NP_439452.1; NC_000907.1. DR RefSeq; WP_005631770.1; NC_000907.1. DR PDB; 2A8C; X-ray; 2.30 A; A/B/C/D/E/F=1-229. DR PDB; 2A8D; X-ray; 2.20 A; A/B/C/D/E/F=1-229. DR PDB; 3E1V; X-ray; 2.80 A; A/B=1-229. DR PDB; 3E1W; X-ray; 2.60 A; A/B=1-229. DR PDB; 3E24; X-ray; 2.30 A; A/B=1-229. DR PDB; 3E28; X-ray; 2.50 A; A/B/C/D/E/F=1-229. DR PDB; 3E2A; X-ray; 2.30 A; A/B/C/D/E/F=1-229. DR PDB; 3E2W; X-ray; 2.30 A; A/B/C/D/E/F=1-229. DR PDB; 3E2X; X-ray; 2.55 A; A/B=1-229. DR PDB; 3E31; X-ray; 2.95 A; A/B=1-229. DR PDB; 3E3F; X-ray; 2.30 A; A/B=1-229. DR PDB; 3E3G; X-ray; 2.30 A; A/B/C/D/E/F=1-229. DR PDB; 3E3I; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-229. DR PDB; 3MF3; X-ray; 2.50 A; A/B/C/D/E/F=1-221. DR PDB; 4WAJ; X-ray; 2.70 A; A/B=1-229. DR PDB; 4WAK; X-ray; 2.49 A; A/B=1-229. DR PDB; 4WAM; X-ray; 2.20 A; A/B=1-229. DR PDBsum; 2A8C; -. DR PDBsum; 2A8D; -. DR PDBsum; 3E1V; -. DR PDBsum; 3E1W; -. DR PDBsum; 3E24; -. DR PDBsum; 3E28; -. DR PDBsum; 3E2A; -. DR PDBsum; 3E2W; -. DR PDBsum; 3E2X; -. DR PDBsum; 3E31; -. DR PDBsum; 3E3F; -. DR PDBsum; 3E3G; -. DR PDBsum; 3E3I; -. DR PDBsum; 3MF3; -. DR PDBsum; 4WAJ; -. DR PDBsum; 4WAK; -. DR PDBsum; 4WAM; -. DR ProteinModelPortal; P45148; -. DR STRING; 71421.HI1301; -. DR EnsemblBacteria; AAC22946; AAC22946; HI_1301. DR GeneID; 950229; -. DR KEGG; hin:HI1301; -. DR PATRIC; 20191285; VBIHaeInf48452_1353. DR eggNOG; ENOG41077A9; Bacteria. DR eggNOG; COG0288; LUCA. DR KO; K01673; -. DR OMA; RASMQDR; -. DR OrthoDB; EOG6FFSB8; -. DR PhylomeDB; P45148; -. DR BRENDA; 4.2.1.1; 2529. DR EvolutionaryTrace; P45148; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0015976; P:carbon utilization; IDA:UniProtKB. DR Gene3D; 3.40.1050.10; -; 1. DR InterPro; IPR001765; Carbonic_anhydrase. DR InterPro; IPR015892; Carbonic_anhydrase_CS. DR PANTHER; PTHR11002; PTHR11002; 1. DR Pfam; PF00484; Pro_CA; 1. DR SMART; SM00947; Pro_CA; 1. DR SUPFAM; SSF53056; SSF53056; 1. DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1. DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 229 Carbonic anhydrase 2. FT /FTId=PRO_0000077467. FT METAL 42 42 Zinc. {ECO:0000244|PDB:2A8C, FT ECO:0000244|PDB:2A8D, FT ECO:0000269|PubMed:16584170}. FT METAL 44 44 Zinc. {ECO:0000244|PDB:2A8C, FT ECO:0000244|PDB:2A8D, FT ECO:0000269|PubMed:16584170}. FT METAL 98 98 Zinc; via tele nitrogen. FT {ECO:0000244|PDB:2A8C, FT ECO:0000244|PDB:2A8D, FT ECO:0000269|PubMed:16584170}. FT METAL 101 101 Zinc. {ECO:0000244|PDB:2A8C, FT ECO:0000244|PDB:2A8D, FT ECO:0000269|PubMed:16584170}. FT HELIX 2 20 {ECO:0000244|PDB:3E3I}. FT TURN 21 24 {ECO:0000244|PDB:4WAJ}. FT HELIX 25 31 {ECO:0000244|PDB:2A8D}. FT STRAND 37 42 {ECO:0000244|PDB:3E3I}. FT TURN 43 45 {ECO:0000244|PDB:3E31}. FT HELIX 49 53 {ECO:0000244|PDB:3E3I}. FT STRAND 59 65 {ECO:0000244|PDB:3E3I}. FT HELIX 66 68 {ECO:0000244|PDB:3E2X}. FT HELIX 75 86 {ECO:0000244|PDB:3E3I}. FT STRAND 92 100 {ECO:0000244|PDB:3E3I}. FT HELIX 102 108 {ECO:0000244|PDB:3E3I}. FT HELIX 116 129 {ECO:0000244|PDB:3E3I}. FT HELIX 131 135 {ECO:0000244|PDB:3E3I}. FT HELIX 139 141 {ECO:0000244|PDB:3E3I}. FT HELIX 142 159 {ECO:0000244|PDB:3E3I}. FT HELIX 162 169 {ECO:0000244|PDB:3E3I}. FT STRAND 175 181 {ECO:0000244|PDB:3E3I}. FT TURN 183 185 {ECO:0000244|PDB:3E3I}. FT STRAND 188 197 {ECO:0000244|PDB:3E3I}. FT HELIX 198 212 {ECO:0000244|PDB:3E3I}. FT HELIX 217 219 {ECO:0000244|PDB:2A8D}. SQ SEQUENCE 229 AA; 26250 MW; 4EB20478BC9EB6C9 CRC64; MDKIKQLFAN NYSWAQRMKE ENSTYFKELA DHQTPHYLWI GCSDSRVPAE KLTNLEPGEL FVHRNVANQV IHTDFNCLSV VQYAVDVLKI EHIIICGHTN CGGIHAAMAD KDLGLINNWL LHIRDIWFKH GHLLGKLSPE KRADMLTKIN VAEQVYNLGR TSIVKSAWER GQKLSLHGWV YDVNDGFLVD QGVMATSRET LEISYRNAIA RLSILDEENI LKKDHLENT // ID BIOF_HAEIN Reviewed; 380 AA. AC P44422; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Putative 8-amino-7-oxononanoate synthase; DE Short=AONS; DE EC=2.3.1.47; DE AltName: Full=7-keto-8-amino-pelargonic acid synthase; DE Short=7-KAP synthase; DE AltName: Full=8-amino-7-ketopelargonate synthase; GN Name=bioF; OrderedLocusNames=HI_1553; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl- CC [acyl-carrier protein] and L-alanine to produce 8-amino-7- CC oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] + L-alanine = CC 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein]. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. BioF 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; L42023; AAC23202.1; -; Genomic_DNA. DR PIR; D64129; D64129. DR RefSeq; NP_439702.1; NC_000907.1. DR RefSeq; WP_005693580.1; NC_000907.1. DR ProteinModelPortal; P44422; -. DR STRING; 71421.HI1553; -. DR EnsemblBacteria; AAC23202; AAC23202; HI_1553. DR GeneID; 950334; -. DR KEGG; hin:HI1553; -. DR PATRIC; 20191831; VBIHaeInf48452_1624. DR eggNOG; ENOG4107EEK; Bacteria. DR eggNOG; COG0156; LUCA. DR KO; K00652; -. DR OMA; FECENDI; -. DR OrthoDB; EOG6PZX7V; -. DR PhylomeDB; P44422; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004723; AONS_Archaea/Proteobacteria. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00858; bioF; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Biotin biosynthesis; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 380 Putative 8-amino-7-oxononanoate synthase. FT /FTId=PRO_0000163813. FT REGION 106 107 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 205 208 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 236 239 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 18 18 Substrate. {ECO:0000250}. FT BINDING 131 131 Substrate. {ECO:0000250}. FT BINDING 179 179 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 352 352 Substrate. {ECO:0000250}. FT MOD_RES 239 239 N6-(pyridoxal phosphate)lysine. FT {ECO:0000305}. SQ SEQUENCE 380 AA; 43212 MW; B04083718BCEE470 CRC64; MDAFKQQLEQ LSAKNQYRSI PDLVHQGRYI TRENRKMLNM SSNDYLGLAS NENLRQSFLQ QYGGNFPSFT SSSSRLLTGN FPIYTDLEEL VAQRFQRESA LLFNSGYHAN IGILPALTTT KSLILADKLV HASMIDGIRL SQCEFFRYRH NDYEHLKNLL EKNVGKFDRT FIVTESVFSM DGDVADLKQL VQLKKQFPNT YLYVDEAHAV GVYGQNGLGI AERANVIADI DLLVGTFGKA LASMGAYVVC DQILKECLIN QMRPLIFSTA LPPFNVAWTH FIFERLPQLS KERTHLEQLS AFLRQEVEHR TQIMPSQTCI VPYILGENEA TLAKAKDLQE QGYYCLPIRP PTVPKNTSRI RLSLTADMTA DEVRQFAVHL // ID BRNQ_HAEIN Reviewed; 436 AA. AC P71345; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Branched-chain amino acid transport system carrier protein; DE AltName: Full=Branched-chain amino acid uptake carrier; GN Name=brnQ; OrderedLocusNames=HI_0226; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Component of the transport system for branched-chain CC amino acids (leucine, isoleucine and valine) Which is coupled to a CC proton motive force. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the branched chain amino acid transporter 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; L42023; AAC21896.1; -; Genomic_DNA. DR PIR; D64056; D64056. DR RefSeq; NP_438398.1; NC_000907.1. DR RefSeq; WP_005694065.1; NC_000907.1. DR STRING; 71421.HI0226; -. DR EnsemblBacteria; AAC21896; AAC21896; HI_0226. DR GeneID; 951144; -. DR KEGG; hin:HI0226; -. DR PATRIC; 20188975; VBIHaeInf48452_0240. DR eggNOG; ENOG4105CWM; Bacteria. DR eggNOG; COG1114; LUCA. DR KO; K03311; -. DR OMA; VWIATIG; -. DR OrthoDB; EOG60KN4N; -. DR PhylomeDB; P71345; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005304; F:L-valine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0098655; P:cation transmembrane transport; IBA:GOC. DR GO; GO:0015818; P:isoleucine transport; IBA:GO_Central. DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IBA:GOC. DR GO; GO:0015807; P:L-amino acid transport; IBA:GOC. DR GO; GO:1903785; P:L-valine transmembrane transport; IBA:GOC. DR GO; GO:0015820; P:leucine transport; IBA:GO_Central. DR InterPro; IPR004685; Brnchd-chn_aa_trnsp_Livcs. DR PANTHER; PTHR30588; PTHR30588; 1. DR Pfam; PF05525; Branch_AA_trans; 1. DR TIGRFAMs; TIGR00796; livcs; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 436 Branched-chain amino acid transport FT system carrier protein. FT /FTId=PRO_0000099769. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 277 297 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 339 359 Helical. {ECO:0000255}. FT TRANSMEM 411 431 Helical. {ECO:0000255}. SQ SEQUENCE 436 AA; 47039 MW; FA37EDF6C2193FDF CRC64; MFSRKDIIVL GMMIFALFLG AGNIIFPPME GFSSGQHWTS ASLGFVLTGV LMPFITLVVV AILGRGEELT KDLPKWAGTG FLVILYLTIG STFAMPRITN VAYEMAWLPL GLTENNANVR FVFSLIFNLI AMGFMISPNT IISSVGKFMT PALLVLLIAV AITVFISPLS EIQAPSNAYE NSHSLLIGLT SGYQTMDVLA AIAFGGIVAR ALSAKNVTKT KDIVKYTISA GFVSVILLAG LYFSLFYLGA TSAAVAEGAT NGGQIFSRYV NVLFGSAGTW IMAGIIVLAS LTTLVGVTSA SADYFSKFSV RFSYPFWAAL FTAMTITVSQ YGLTDLLRIT IPALLLIYPV AIVLVLLQFL RKKLPSIKFT YNSTLLVTVC FSLCDSLNNV KMLPESINSL LKHFPLSSEG MAWLVPTLVM LVASIFIGKA LHKTHS // ID CAPP_HAEIN Reviewed; 879 AA. AC P43920; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 108. DE RecName: Full=Phosphoenolpyruvate carboxylase; DE Short=PEPC; DE Short=PEPCase; DE EC=4.1.1.31; GN Name=ppc; OrderedLocusNames=HI_1636; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid CC source for the tricarboxylic acid cycle. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + HCO(3)(-). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23281.1; -; Genomic_DNA. DR PIR; I64133; I64133. DR RefSeq; NP_439778.1; NC_000907.1. DR RefSeq; WP_005693644.1; NC_000907.1. DR ProteinModelPortal; P43920; -. DR SMR; P43920; 4-879. DR STRING; 71421.HI1636; -. DR PRIDE; P43920; -. DR EnsemblBacteria; AAC23281; AAC23281; HI_1636. DR GeneID; 950481; -. DR KEGG; hin:HI1636; -. DR PATRIC; 20192017; VBIHaeInf48452_1712. DR eggNOG; ENOG4105CCA; Bacteria. DR eggNOG; COG2352; LUCA. DR KO; K01595; -. DR OMA; IAEAWHT; -. DR OrthoDB; EOG6TJ7T8; -. DR PhylomeDB; P43920; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP. DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR HAMAP; MF_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR033129; PEPCASE_His_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; SSF51621; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. PE 3: Inferred from homology; KW Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; KW Reference proteome. FT CHAIN 1 879 Phosphoenolpyruvate carboxylase. FT /FTId=PRO_0000166597. FT ACT_SITE 138 138 {ECO:0000250}. FT ACT_SITE 545 545 {ECO:0000250}. SQ SEQUENCE 879 AA; 100055 MW; 3E45E42C2D62DF40 CRC64; MTQEYSTLRN NISMLGRFLG ETINDAQGED ILELIENIRK LSRNSRAGDD KARQALLDTL GSISNENIIP VARAFSQFLN LTNIAEQYQT ISREHSLAQS SSQSLSELFK RLKEQNASVE EVHKTVEKLL IELVLTAHPT ETTRRSLIHK HIEINKCLSK LEHHDLTEKE RNIIERLLLR LIAEAWHTNE IRTVRPTPFD EAKWGFAMLE NSLWQAVPEF LRQLNETARE FLGYDLSVGL KPVRISSWMG GDRDGNPFVT AQITKKVLYF ARWKAADLFL QDISKLADEL SMMKCSDEFR DKYGEHLEPY RFVVKNLRNQ LTATLAYFDD HLSNRTPRVS ESEIILEDNQ LWEPLYDCYQ SLIQCGMRII ANGSLLNILH RISCFGVTLS QMDIRQESTR HTDAIAEITR YIGLGDYSQW MEDDKQAFLI RELSSRRPLI PQNWTPSPET KEILDTCKVI AQQKQGVIAC YVISMARSAS DVLAVHLLLK ESGVPYHIPV VPLFETLEDL DAAEKVMTQL FNVGWYRGVI NNRQMVMIGY SDSAKDAGMM AASWAQYRAQ EALVNLTEKL GIELTLFHGR GGTIGRGGAP AHAALLSQPP RSLKNGLRVT EQGEMIRFKL GLPAVAVETF DLYASAILEA NLLPPPEPKP EWRTIMDELS TISCDIYRGV VRGDKDFVPY FRSATPEQEL SKLPLGSRPA KRNPNGGVES LRAIPWIFAW MQNRLMLPAW LGAGAAIRQV IEQGKGDIIH KMCENWPFFS TRIGMLEMVF SKSDTWLSQQ YDQRLVKKEL WYLGENLRKQ LEDDIQTVLS LSHQSELMSD LPWIADSIAL RNIYTDPLNL LQVELLHRFR ENPEQVNPDV EQALMITITG IAAGMRNTG // ID CCMD_HAEIN Reviewed; 67 AA. AC P45035; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Heme exporter protein D; DE AltName: Full=Cytochrome c-type biogenesis protein CcmD; GN Name=ccmD; OrderedLocusNames=HI_1092; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the export of heme to the periplasm for the CC biogenesis of c-type cytochromes. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmD/CycX/HelD 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; L42023; AAC22749.1; -; Genomic_DNA. DR PIR; H64166; H64166. DR RefSeq; NP_439249.1; NC_000907.1. DR RefSeq; WP_005693416.1; NC_000907.1. DR STRING; 71421.HI1092; -. DR EnsemblBacteria; AAC22749; AAC22749; HI_1092. DR GeneID; 950064; -. DR KEGG; hin:HI1092; -. DR PATRIC; 20190849; VBIHaeInf48452_1137. DR eggNOG; ENOG4105X3C; Bacteria. DR eggNOG; COG3114; LUCA. DR KO; K02196; -. DR OMA; QQMENTL; -. DR OrthoDB; EOG60391X; -. DR PhylomeDB; P45035; -. DR Proteomes; UP000000579; 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:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR GO; GO:0015886; P:heme transport; IEA:InterPro. DR InterPro; IPR007078; Haem_export_protD_CcmD. DR Pfam; PF04995; CcmD; 1. DR TIGRFAMs; TIGR03141; cytochro_ccmD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 67 Heme exporter protein D. FT /FTId=PRO_0000201567. FT TRANSMEM 17 35 Helical. {ECO:0000255}. SQ SEQUENCE 67 AA; 7847 MW; A6F78561DB5C3114 CRC64; MFFQTWSDFF NMGGYGFYVW LSYAVSLVAV IALIVQSVKQ RKTVLQNVLR EKQREERLQQ ANKGNTL // ID CCME_HAEIN Reviewed; 173 AA. AC P45036; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Cytochrome c-type biogenesis protein CcmE {ECO:0000255|HAMAP-Rule:MF_01959}; DE AltName: Full=Cytochrome c maturation protein E {ECO:0000255|HAMAP-Rule:MF_01959}; DE AltName: Full=Heme chaperone CcmE {ECO:0000255|HAMAP-Rule:MF_01959}; GN Name=ccmE {ECO:0000255|HAMAP-Rule:MF_01959}; GN Synonyms=cycJ {ECO:0000255|HAMAP-Rule:MF_01959}; GN OrderedLocusNames=HI_1093; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Heme chaperone required for the biogenesis of c-type CC cytochromes. Transiently binds heme delivered by CcmC and CC transfers the heme to apo-cytochromes in a process facilitated by CC CcmF and CcmH. {ECO:0000255|HAMAP-Rule:MF_01959}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01959}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01959}; Periplasmic side CC {ECO:0000255|HAMAP-Rule:MF_01959}. CC -!- SIMILARITY: Belongs to the CcmE/CycJ family. {ECO:0000255|HAMAP- CC Rule:MF_01959}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22750.1; -; Genomic_DNA. DR PIR; I64166; I64166. DR RefSeq; NP_439250.1; NC_000907.1. DR RefSeq; WP_005693417.1; NC_000907.1. DR ProteinModelPortal; P45036; -. DR SMR; P45036; 30-144. DR STRING; 71421.HI1093; -. DR EnsemblBacteria; AAC22750; AAC22750; HI_1093. DR GeneID; 950065; -. DR KEGG; hin:HI1093; -. DR PATRIC; 20190851; VBIHaeInf48452_1138. DR eggNOG; ENOG4108ZKK; Bacteria. DR eggNOG; COG2332; LUCA. DR KO; K02197; -. DR OMA; HVEFAVH; -. DR OrthoDB; EOG69D3JN; -. DR PhylomeDB; P45036; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR GO; GO:0017003; P:protein-heme linkage; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01959; CcmE; 1. DR InterPro; IPR004329; CcmE. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF03100; CcmE; 1. DR SUPFAM; SSF82093; SSF82093; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Heme; Iron; Membrane; Metal-binding; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 173 Cytochrome c-type biogenesis protein FT CcmE. FT /FTId=PRO_0000201578. FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01959}. FT TRANSMEM 9 29 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255|HAMAP- FT Rule:MF_01959}. FT TOPO_DOM 30 173 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01959}. FT METAL 135 135 Iron (heme axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01959}. FT BINDING 131 131 Heme (covalent; via pros nitrogen). FT {ECO:0000255|HAMAP-Rule:MF_01959}. SQ SEQUENCE 173 AA; 19149 MW; 0505AC6B99709156 CRC64; MNPRRKSRFK LVIFVVLGIA IASGLMLYAL RQNIDLFYTP SEVIQGKDNN PNQKPEVGQR IRVGGMVVEG TVVRDPKSLK VRFDLNDIGP AITVEYEGIL PDLFREGQGI VAQGVLTQPT VLTATEVLAK HDENYVPPEL GEKMQKVHKP MGIEAADLKG ESARDRQEKE GAK // ID CCMC_HAEIN Reviewed; 246 AA. AC P45034; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Heme exporter protein C; DE AltName: Full=Cytochrome c-type biogenesis protein CcmC; GN Name=ccmC; OrderedLocusNames=HI_1091; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the export of heme to the periplasm for the CC biogenesis of c-type cytochromes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmC/CycZ/HelC 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; L42023; AAC22748.1; -; Genomic_DNA. DR PIR; G64166; G64166. DR RefSeq; NP_439248.1; NC_000907.1. DR RefSeq; WP_005693415.1; NC_000907.1. DR STRING; 71421.HI1091; -. DR EnsemblBacteria; AAC22748; AAC22748; HI_1091. DR GeneID; 950063; -. DR KEGG; hin:HI1091; -. DR PATRIC; 20190847; VBIHaeInf48452_1136. DR eggNOG; ENOG41060IM; Bacteria. DR eggNOG; COG0755; LUCA. DR KO; K02195; -. DR OMA; PSIATPM; -. DR OrthoDB; EOG6BCSQK; -. DR PhylomeDB; P45034; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0015232; F:heme transporter activity; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR GO; GO:0015886; P:heme transport; IBA:GO_Central. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR InterPro; IPR002541; Cyt_c_assembly. DR InterPro; IPR003557; Cyt_c_biogenesis_CcmC. DR Pfam; PF01578; Cytochrom_C_asm; 1. DR PRINTS; PR01386; CCMCBIOGNSIS. DR TIGRFAMs; TIGR01191; ccmC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 246 Heme exporter protein C. FT /FTId=PRO_0000201555. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. SQ SEQUENCE 246 AA; 27716 MW; 8CAACF95E74B1945 CRC64; MWKWLHPYAK PETQYRICGK LSPLFAFLTL VLLGVGIVWG LAFAPADYQQ GNSFRIMYVH APTAIWSMGV YGSMAIAAVV ALVWQIKQAH LAMIAMAPIG ALFTFLSLVT GAIWGKPMWG TWWVWDARLT AELILFFLYL GILALYSAFS DRNIGAKAAG ILCITTVVIL PIIHFSVEWW NTLHQGASIT KLEKPSIAIP MLVPLILCIF GFLTLYIWLT LVRYRMELLK EDAKRPWVKA LAQTLK // ID CATA_HAEIN Reviewed; 508 AA. AC P44390; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Catalase; DE EC=1.11.1.6; GN Name=katA; Synonyms=hktE; OrderedLocusNames=HI_0928; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8188593; RA Bishai W.R., Smith H.O., Barcak G.J.; RT "A peroxide/ascorbate-inducible catalase from Haemophilus influenzae RT is homologous to the Escherichia coli katE gene product."; RL J. Bacteriol. 176:2914-2921(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; CC serves to protect cells from the toxic effects of hydrogen CC peroxide. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC {ECO:0000255|PROSITE-ProRule:PRU10013}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- INDUCTION: By hydrogen peroxide. CC -!- SIMILARITY: Belongs to the catalase 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; U02682; AAA20441.1; -; Genomic_DNA. DR EMBL; L42023; AAC22587.1; -; Genomic_DNA. DR PIR; D64103; D64103. DR RefSeq; NP_439088.1; NC_000907.1. DR RefSeq; WP_005693274.1; NC_000907.1. DR ProteinModelPortal; P44390; -. DR SMR; P44390; 12-491. DR STRING; 71421.HI0928; -. DR PRIDE; P44390; -. DR EnsemblBacteria; AAC22587; AAC22587; HI_0928. DR GeneID; 949926; -. DR KEGG; hin:HI0928; -. DR PATRIC; 20190513; VBIHaeInf48452_0969. DR eggNOG; ENOG4105CH6; Bacteria. DR eggNOG; COG0753; LUCA. DR KO; K03781; -. DR OMA; PVAHNQN; -. DR OrthoDB; EOG6P5Z9F; -. DR PhylomeDB; P44390; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004096; F:catalase activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0098869; P:cellular oxidant detoxification; IBA:GOC. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central. DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central. DR Gene3D; 2.40.180.10; -; 1. DR InterPro; IPR018028; Catalase. DR InterPro; IPR020835; Catalase-like_dom. DR InterPro; IPR024708; Catalase_AS. DR InterPro; IPR024711; Catalase_clade1/3. DR InterPro; IPR011614; Catalase_core. DR InterPro; IPR002226; Catalase_haem_BS. DR InterPro; IPR010582; Catalase_immune_responsive. DR PANTHER; PTHR11465; PTHR11465; 1. DR Pfam; PF00199; Catalase; 1. DR Pfam; PF06628; Catalase-rel; 1. DR PIRSF; PIRSF038928; Catalase_clade1-3; 1. DR PRINTS; PR00067; CATALASE. DR SMART; SM01060; Catalase; 1. DR SUPFAM; SSF56634; SSF56634; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. DR PROSITE; PS51402; CATALASE_3; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron; KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome. FT CHAIN 1 508 Catalase. FT /FTId=PRO_0000084986. FT ACT_SITE 63 63 {ECO:0000255|PROSITE-ProRule:PRU10013}. FT ACT_SITE 136 136 {ECO:0000255|PROSITE-ProRule:PRU10013}. FT METAL 346 346 Iron (heme axial ligand). {ECO:0000250}. FT CONFLICT 357 357 N -> C (in Ref. 1; AAA20441). FT {ECO:0000305}. FT CONFLICT 384 384 N -> T (in Ref. 1; AAA20441). FT {ECO:0000305}. FT CONFLICT 413 413 N -> S (in Ref. 1; AAA20441). FT {ECO:0000305}. FT CONFLICT 423 423 N -> T (in Ref. 1; AAA20441). FT {ECO:0000305}. SQ SEQUENCE 508 AA; 57680 MW; 4FAFC16DB44043B0 CRC64; MSSQCPFSHL AATNLTMGNG APVADNQNSL TAGPRGPLLA QDLWLNEKLA DFVREVIPER RMHAKGSGAF GTFTVTHDIT KYTRAKIFSE VGKKTEMFAR FTTVAGERGA ADAERDIRGF ALKFYTEEGN WDLVGNNTPV FFLRDPRKFP DLNKAVKRDP RTNMRSATNN WDFWTLLPEA LHQVTVVMSD RGIPASYRHM HGFGSHTYSF WNEAGERFWV KFHFRTQQGI KNLTDAEAAE IIANDRESHQ RDLYEAIERG DFPKWTLFVQ IMPEADAEKV PYHPFDLTKV WSKKDYPLIE VGEFELNRNP ENFFADVEQS AFAPSNLVPG IGASPDRMLQ ARLFNYADAQ RYRLGVNYRQ IPVNRPRCPV HSNQRDGQGR VDGNYGSLPH YEPNSFSQWQ QQPDFAEPPL RINGDAAHWD YRNDDNDYFS QPRALFNLMN AEQKQSLFNN TAAAMGDAPD FIKYRHIRNC HWCDAAYGEG VAKALGLTVE DALKARDTDP ALGQGGLL // ID CCA_HAEIN Reviewed; 416 AA. AC P45269; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Multifunctional CCA protein {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261}; DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2'-nucleotidase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01261}; DE Includes: DE RecName: Full=Phosphatase {ECO:0000255|HAMAP-Rule:MF_01261}; DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261}; GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01261}; OrderedLocusNames=HI_1606; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'- CC terminal CCA sequence in tRNAs without using a nucleic acid CC template. Adds these three nucleotides in the order of C, C, and A CC to the tRNA nucleotide-73, using CTP and ATP as substrates and CC producing inorganic pyrophosphate. Also shows phosphatase, 2'- CC nucleotidase and 2',3'-cyclic phosphodiesterase activities. These CC phosphohydrolase activities are probably involved in the repair of CC the tRNA 3'-CCA terminus degraded by intracellular RNases. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a CC 3' CCA end + 3 diphosphate. {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261}; CC Note=Magnesium is required for nucleotidyltransferase activity. CC {ECO:0000255|HAMAP-Rule:MF_01261}; CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261}; CC Note=Nickel for phosphatase activity. {ECO:0000255|HAMAP- CC Rule:MF_01261}; CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the CC nucleotidyltransferase activity and a C-terminal HD domain CC associated with both phosphodiesterase and phosphatase activities. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- MISCELLANEOUS: A single active site specifically recognizes both CC ATP and CTP and is responsible for their addition. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. Bacterial CCA-adding enzyme type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01261}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23250.1; -; Genomic_DNA. DR PIR; B64132; B64132. DR RefSeq; NP_439748.1; NC_000907.1. DR RefSeq; WP_005693619.1; NC_000907.1. DR ProteinModelPortal; P45269; -. DR STRING; 71421.HI1606; -. DR DNASU; 950839; -. DR EnsemblBacteria; AAC23250; AAC23250; HI_1606. DR GeneID; 950839; -. DR KEGG; hin:HI1606; -. DR PATRIC; 20191943; VBIHaeInf48452_1679. DR eggNOG; ENOG4105D4J; Bacteria. DR eggNOG; COG0617; LUCA. DR KO; K00974; -. DR OMA; SEWPSHK; -. DR OrthoDB; EOG651SRP; -. DR PhylomeDB; P45269; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW. DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01261; CCA_bact_type1; 1. DR HAMAP; MF_01262; CCA_bact_type2; 1. DR InterPro; IPR012006; CCA_bact. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR Pfam; PF01966; HD; 1. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR PIRSF; PIRSF000813; CCA_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nickel; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding; KW Transferase; tRNA processing. FT CHAIN 1 416 Multifunctional CCA protein. FT /FTId=PRO_0000138980. FT METAL 21 21 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT METAL 23 23 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 8 8 ATP or CTP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01261}. FT BINDING 11 11 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 91 91 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 137 137 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. FT BINDING 140 140 ATP or CTP. {ECO:0000255|HAMAP- FT Rule:MF_01261}. SQ SEQUENCE 416 AA; 47247 MW; C6144ABFF03ED54C CRC64; MKVYLVGGAV RDQLLGLPVK DRDWIVVGAD PATLLSLGYQ QVGKDFPVFL NPKTKEEYAL ARTERKSSAG YTGFICDFSP TITLEQDLIR RDLTINAMAQ SEDGEIIDPY GGKQDLENRI LRHISPAFSE DPLRVLRVAR FAARYHSLGF KIASETLALM AELAQSGELQ HLTAERIWLE TEKALNEKNP EIYFETLHKT GALSVLFSEI DALYGVPNPV KHHPEVDSFI HTMLVLKQAV NLTENNPILN KSAVRFAAIC HDLGKALTPQ NILPHHYGHE QAGIKPTRSL CKRLKVPSYF QELAELTCEF HTHIHKAFEL RAETVITLFN RFDVWRKPQR FQEFLQVCLA DTRGRTGFET KDYPQIDYIN QLLHAANEVD VQQVIADGFE KQAIKNELTK RRILAVKQTK TNYPTN // ID CCMB_HAEIN Reviewed; 221 AA. AC P45033; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Heme exporter protein B; DE AltName: Full=Cytochrome c-type biogenesis protein CcmB; GN Name=ccmB; OrderedLocusNames=HI_1090; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the export of heme to the periplasm for the CC biogenesis of c-type cytochromes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmB/CycW/HelB 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; L42023; AAC22747.1; -; Genomic_DNA. DR PIR; F64166; F64166. DR RefSeq; NP_439247.1; NC_000907.1. DR RefSeq; WP_005637214.1; NC_000907.1. DR STRING; 71421.HI1090; -. DR EnsemblBacteria; AAC22747; AAC22747; HI_1090. DR GeneID; 950092; -. DR KEGG; hin:HI1090; -. DR PATRIC; 20190845; VBIHaeInf48452_1135. DR eggNOG; ENOG4105CA5; Bacteria. DR eggNOG; COG2386; LUCA. DR KO; K02194; -. DR OMA; GPAIVWI; -. DR OrthoDB; EOG64FKHN; -. DR PhylomeDB; P45033; -. DR Proteomes; UP000000579; 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:0015232; F:heme transporter activity; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR InterPro; IPR003544; Cyt_c_biogenesis_CcmB. DR InterPro; IPR026031; Cyt_c_CcmB_bac. DR PANTHER; PTHR30070:SF1; PTHR30070:SF1; 1. DR Pfam; PF03379; CcmB; 1. DR PIRSF; PIRSF002764; CcmB; 1. DR PRINTS; PR01414; CCMBBIOGNSIS. DR TIGRFAMs; TIGR01190; ccmB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 221 Heme exporter protein B. FT /FTId=PRO_0000201542. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. SQ SEQUENCE 221 AA; 23644 MW; 2FF8EAFDC5228EF8 CRC64; MIFLEIIKRE LQIAMRKNAE ILNPLWFFLL VITLFPLVIG PDPKLLSRIA PGIAWVAALL SALLSFERLF RDDFIDGSLE QLMLTAQPLP MTALAKVVAH WLLTGLPLIL LSPIAALLLS LEVNIWWALV LTLLLGTPVL SCIGAIGVAL TVGLRKGGVL LSLLVVPLFI PVLIFASSVL EAAGLNVPYG GQLAILGAMM VGAVTLSPFA IAAALRISLD N // ID CCMF_HAEIN Reviewed; 648 AA. AC P45037; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Cytochrome c-type biogenesis protein CcmF; GN Name=ccmF; OrderedLocusNames=HI_1094; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the biogenesis of c-type cytochromes. CC Possible subunit of a heme lyase. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA 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; L42023; AAC22751.1; -; Genomic_DNA. DR PIR; A64167; A64167. DR RefSeq; NP_439251.1; NC_000907.1. DR RefSeq; WP_005693418.1; NC_000907.1. DR STRING; 71421.HI1094; -. DR EnsemblBacteria; AAC22751; AAC22751; HI_1094. DR GeneID; 950066; -. DR KEGG; hin:HI1094; -. DR PATRIC; 20190853; VBIHaeInf48452_1139. DR eggNOG; ENOG4105DA4; Bacteria. DR eggNOG; COG1138; LUCA. DR KO; K02198; -. DR OMA; QRATHRE; -. DR OrthoDB; EOG6RRKJ4; -. DR PhylomeDB; P45037; -. DR Proteomes; UP000000579; 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:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0015232; F:heme transporter activity; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR InterPro; IPR032523; CcmF_C. DR InterPro; IPR002541; Cyt_c_assembly. DR InterPro; IPR003567; Cyt_c_biogenesis. DR InterPro; IPR003568; Cyt_c_biogenesis_CcmF. DR PANTHER; PTHR30009:SF0; PTHR30009:SF0; 2. DR Pfam; PF16327; CcmF_C; 1. DR Pfam; PF01578; Cytochrom_C_asm; 1. DR PRINTS; PR01410; CCBIOGENESIS. DR PRINTS; PR01411; CCMFBIOGNSIS. DR TIGRFAMs; TIGR00353; nrfE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 648 Cytochrome c-type biogenesis protein FT CcmF. FT /FTId=PRO_0000201584. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. FT TRANSMEM 312 332 Helical. {ECO:0000255}. FT TRANSMEM 352 372 Helical. {ECO:0000255}. FT TRANSMEM 394 414 Helical. {ECO:0000255}. FT TRANSMEM 424 444 Helical. {ECO:0000255}. FT TRANSMEM 448 468 Helical. {ECO:0000255}. FT TRANSMEM 490 510 Helical. {ECO:0000255}. FT TRANSMEM 616 636 Helical. {ECO:0000255}. SQ SEQUENCE 648 AA; 72353 MW; ABE434B80F4B92B6 CRC64; MIAELGNYAL ALSLAVSLML AIFPLWGAEK GNAQLMALAR PMTYGLFASL SIAFAALFYL FAVNDFSVQY IVNNSNTTLP IYYRLSAVWG SHEGSLLLWI WLLAVWSFAV ALLSKHLPQE AVARVLGIMG IISVGFVLFV LFTSNPFTRT FPDFPVDGKE LNPMLQDVGL IFHPPLLYMG YVGFSVAFAF AIASLMTGKL DSAWARWSRP WTLAAWVFLT LGIVLGSWWA YYELGWGGWW FWDPVENSSF MPWLAGTALI HSLSVTEKRG SFKAWTVLLA ILAFSLCLLG TFLVRSGILV SVHAFASDPT RGLYILAYLV VVIGGSLALY AYKGSQIRSR DNAERYSRES MLLLNNILLM TALCVVFLGT LLPLVHKQLG LGSISIGAPF FDQMFLIIMT PFALLLGIGP LVKWRRDQFS AIRTPVVICV FVMLIAGFAL PYFLQDKITV SSVLGSMMTV IIALLALYEL QQRATHRESF FVGVRKLSRS HWGMMLAHLG VAMTVWGIAF SQNFSVERDV RMKVGESAQI GRYDFKFTGV TDENGPNYIG GKAQIDISKD GQPEASLFAE KRFYTVSRMS MTEAAIAGGL TRDLYVALGE KLEDNSWALR LYYKPFIRWI WIGGLFMALG GLLCMFDRRY RFNVLLKK // ID CDSA_HAEIN Reviewed; 288 AA. AC P44937; O32623; O32627; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Phosphatidate cytidylyltransferase; DE EC=2.7.7.41; DE AltName: Full=CDP-DAG synthase; DE AltName: Full=CDP-DG synthase; DE AltName: Full=CDP-diacylglycerol synthase; DE Short=CDS; DE AltName: Full=CDP-diglyceride pyrophosphorylase; DE AltName: Full=CDP-diglyceride synthase; DE AltName: Full=CTP:phosphatidate cytidylyltransferase; GN Name=cdsA; Synonyms=cds; OrderedLocusNames=HI_0919; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=33, and Eagan / Serotype B; RA Loosmore S.M., Yang Y., Coleman D.C., Shortreed J.M., England D.M., RA Klein M.H.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. 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 inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22577.1; -; Genomic_DNA. DR EMBL; U60831; AAB61967.1; -; Genomic_DNA. DR EMBL; U60832; AAB61972.1; -; Genomic_DNA. DR PIR; G64102; G64102. DR RefSeq; NP_439079.1; NC_000907.1. DR RefSeq; WP_005693266.1; NC_000907.1. DR STRING; 71421.HI0919; -. DR EnsemblBacteria; AAC22577; AAC22577; HI_0919. DR GeneID; 949391; -. DR KEGG; hin:HI0919; -. DR PATRIC; 20190493; VBIHaeInf48452_0960. DR eggNOG; ENOG4105KNE; Bacteria. DR eggNOG; COG0575; LUCA. DR KO; K00981; -. DR OMA; YVFILVW; -. DR OrthoDB; EOG6TBHJT; -. DR PhylomeDB; P44937; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IBA:GO_Central. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IBA:GO_Central. DR InterPro; IPR000374; PC_trans. DR PROSITE; PS01315; CDS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipid biosynthesis; Lipid metabolism; Membrane; KW Nucleotidyltransferase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 288 Phosphatidate cytidylyltransferase. FT /FTId=PRO_0000090736. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT VARIANT 16 16 V -> F (in strain: Eagan). FT VARIANT 59 59 T -> A (in strain: 33). FT VARIANT 81 81 R -> H (in strain: Eagan). SQ SEQUENCE 288 AA; 32247 MW; 67FFBF29997FAFA5 CRC64; MLKQRVLSAI VLIAAVLCAL FLFTPFYFAL ALGAVAILGI WEWTQFARLK QPLIRFFVTT FLGVFIFLWL YTEGNYLDAG RVFEQHLQLL LINAVSWWGL ALLLVISYPK SAKFWSKNPL LQLLFAFSTL IPFVAGVLRL RLEHYTHDPY HGLFLLLYVF ILVWAADSGA YFSGRAFGKR KLAPKVSPGK SWEGVIGGLI TALVLAFIFI HFSNNTLVGD RNITGFIILS VATVAISVLG DLTESMFKRE SGVKDSSQLI PGHGGVLDRI DSLTAAVPFF SYFYFFVL // ID CH10_HAEIN Reviewed; 96 AA. AC P43734; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=10 kDa chaperonin; DE AltName: Full=GroES protein; DE AltName: Full=Protein Cpn10; GN Name=groS; Synonyms=groES, mopB; OrderedLocusNames=HI_0542; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22200.1; -; Genomic_DNA. DR PIR; B64076; B64076. DR RefSeq; NP_438700.1; NC_000907.1. DR RefSeq; WP_005687043.1; NC_000907.1. DR ProteinModelPortal; P43734; -. DR SMR; P43734; 1-96. DR STRING; 71421.HI0542; -. DR EnsemblBacteria; AAC22200; AAC22200; HI_0542. DR GeneID; 949601; -. DR KEGG; hin:HI0542; -. DR PATRIC; 20189637; VBIHaeInf48452_0561. DR eggNOG; ENOG4105K5Y; Bacteria. DR eggNOG; COG0234; LUCA. DR KO; K04078; -. DR OMA; VMGENEI; -. DR OrthoDB; EOG6GFGSD; -. DR PhylomeDB; P43734; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.33.40; -; 1. DR HAMAP; MF_00580; CH10; 1. DR InterPro; IPR020818; Chaperonin_GroES. DR InterPro; IPR018369; Chaprnonin_Cpn10_CS. DR InterPro; IPR011032; GroES-like. DR PANTHER; PTHR10772; PTHR10772; 1. DR Pfam; PF00166; Cpn10; 1. DR PRINTS; PR00297; CHAPERONIN10. DR SMART; SM00883; Cpn10; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR PROSITE; PS00681; CHAPERONINS_CPN10; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW Stress response. FT CHAIN 1 96 10 kDa chaperonin. FT /FTId=PRO_0000174761. SQ SEQUENCE 96 AA; 10340 MW; C2AEC18E85EF50DD CRC64; MNIRPLHDRV IIKREEVETR SAGGIVLTGS AATKSTRAKV LAVGKGRILE NGTVQPLDVK VGDIVIFNDG YGVKSEKIDG EEVLIISEND ILAIVE // ID CCMA_HAEIN Reviewed; 212 AA. AC P45032; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=Cytochrome c biogenesis ATP-binding export protein CcmA {ECO:0000255|HAMAP-Rule:MF_01707}; DE EC=3.6.3.41 {ECO:0000255|HAMAP-Rule:MF_01707}; DE AltName: Full=Heme exporter protein A {ECO:0000255|HAMAP-Rule:MF_01707}; GN Name=ccmA {ECO:0000255|HAMAP-Rule:MF_01707}; GN OrderedLocusNames=HI_1089; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex CcmAB involved in CC the biogenesis of c-type cytochromes; once thought to export heme, CC this seems not to be the case, but its exact role is uncertain. CC Responsible for energy coupling to the transport system. CC {ECO:0000255|HAMAP-Rule:MF_01707}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + heme(In) = ADP + phosphate + CC heme(Out). {ECO:0000255|HAMAP-Rule:MF_01707}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (CcmA) and two transmembrane proteins (CcmB). {ECO:0000255|HAMAP- CC Rule:MF_01707}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01707}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01707}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CcmA CC exporter (TC 3.A.1.107) family. {ECO:0000255|HAMAP-Rule:MF_01707}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01707}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22746.1; -; Genomic_DNA. DR PIR; E64166; E64166. DR RefSeq; NP_439246.1; NC_000907.1. DR RefSeq; WP_005693414.1; NC_000907.1. DR ProteinModelPortal; P45032; -. DR STRING; 71421.HI1089; -. DR EnsemblBacteria; AAC22746; AAC22746; HI_1089. DR GeneID; 949617; -. DR KEGG; hin:HI1089; -. DR PATRIC; 20190843; VBIHaeInf48452_1134. DR eggNOG; ENOG4107EV4; Bacteria. DR eggNOG; COG4133; LUCA. DR KO; K02193; -. DR OMA; RWDSEAI; -. DR OrthoDB; EOG6SNDS1; -. DR PhylomeDB; P45032; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015439; F:heme-transporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0017004; P:cytochrome complex assembly; 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; IPR005895; ABC_transptr_haem_export_CcmA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01189; ccmA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51243; CCMA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 212 Cytochrome c biogenesis ATP-binding FT export protein CcmA. FT /FTId=PRO_0000092182. FT DOMAIN 7 209 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01707}. FT NP_BIND 39 46 ATP. {ECO:0000255|HAMAP-Rule:MF_01707}. SQ SEQUENCE 212 AA; 24009 MW; BEDD2B7F3CE633D2 CRC64; MFEQHKLSLQ NLSCQRGERV LFRALTCDFN SGDFVQIEGH NGIGKTSLLR ILAGLVRPLE GEVRWDSEAI SKQREQYHQN LLYLGHLSGV KPELTAWENL QFYQRISQAE QNTDMLWDLL EKVGLLGRED LPAAQLSAGQ QKRIALGRLW LSQAPLWILD EPFTAIDKKG VEILTALFDE HAQRGGIVLL TSHQEVPSSH LQKLNLAAYK AE // ID CCMH_HAEIN Reviewed; 459 AA. AC P46458; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Putative cytochrome c-type biogenesis protein CcmH; DE Flags: Precursor; GN Name=ccmH; OrderedLocusNames=HI_1096; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May be required for the biogenesis of c-type CC cytochromes. Possible subunit of a heme lyase (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmH/CycL/Ccl2/NrfF family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Erroneous termination; Positions=154; Note=Translated as Xaa.; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P46458; -. DR SMR; P46458; 17-97. DR STRING; 71421.HI1097m; -. DR eggNOG; ENOG4108M1T; Bacteria. DR eggNOG; COG4235; LUCA. DR OMA; GYVAYLP; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005616; CcmH/CycL/Ccl2/NrfF. DR InterPro; IPR017560; Cyt_c_biogenesis_CcmI. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF03918; CcmH; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR03142; cytochro_ccmI; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 5: Uncertain; KW Complete proteome; Cytochrome c-type biogenesis; Heme; Iron; KW Metal-binding; Periplasm; Reference proteome; Repeat; Signal; KW TPR repeat. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 459 Putative cytochrome c-type biogenesis FT protein CcmH. FT /FTId=PRO_0000006613. FT REPEAT 322 355 TPR 1. FT REPEAT 393 426 TPR 2. FT BINDING 44 44 Heme (covalent). {ECO:0000255}. FT BINDING 47 47 Heme (covalent). {ECO:0000255}. SQ SEQUENCE 459 AA; 52516 MW; C9362E35D2E3B143 CRC64; MKKTWLFLTA LLFSSVAFSA IDALNFSSPQ QESDYHQLTQ SLRCPQCQNN NIADSNATIA VDMRGKVFEL LQEGKSKNDV VDYMVARYGN FVTYDPPITA STLVLWIAPL LLVLLGVVFL LRRKPKTQSA VKSQEILTDE DNARLAELLN KDKXMNFTLI FILTTLVVAL ICFYPLLCQF KAKHGQKRDD LNKALYFSRL EEIEQDNSQG LVENVEQLKQ ELQKTLLDDV PSKVQENVDY SGKSYGKIWF ISGVLALGII AGPSYFMVGS WQAESMLEQT YAKLPYFFDR MKNEDKNPFS DTEMQQFSTA LRIDLQKNPT DAKKWWMLGQ IGMNLGDARL AFDSYQKANK LEPDNVQYKL GYARILMFSE DATDKLKGGN LLREVIRQEH TNIEALSLLA FRYFETEDYK MAAVTWAMML RLMPKDDERV PLIEKSIRTA RDALEAQNEE KSKSITPEK // ID CILA_HAEIN Reviewed; 500 AA. AC P44459; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Citrate lyase alpha chain; DE Short=Citrase alpha chain; DE EC=4.1.3.6; DE AltName: Full=Citrate (pro-3S)-lyase alpha chain; DE AltName: Full=Citrate CoA-transferase subunit; DE EC=2.8.3.10; GN Name=citF; OrderedLocusNames=HI_0022; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Represents a citrate:acetyl-ACP transferase. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Citrate = acetate + oxaloacetate. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + citrate = acetate + (3S)-citryl- CC CoA. CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta, CC gamma)6. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21700.1; -; Genomic_DNA. DR PIR; C64043; C64043. DR RefSeq; NP_438195.1; NC_000907.1. DR RefSeq; WP_005663293.1; NC_000907.1. DR ProteinModelPortal; P44459; -. DR SMR; P44459; 32-499. DR STRING; 71421.HI0022; -. DR EnsemblBacteria; AAC21700; AAC21700; HI_0022. DR GeneID; 950920; -. DR KEGG; hin:HI0022; -. DR PATRIC; 20188495; VBIHaeInf48452_0022. DR eggNOG; ENOG4105CHY; Bacteria. DR eggNOG; COG3051; LUCA. DR KO; K01643; -. DR OMA; KGSVINQ; -. DR OrthoDB; EOG61KBGM; -. DR PhylomeDB; P44459; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009346; C:citrate lyase complex; IEA:InterPro. DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-EC. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR InterPro; IPR006472; Citrate_lyase_asu. DR Pfam; PF04223; CitF; 1. DR PIRSF; PIRSF009451; Citrt_lyas_alpha; 1. DR TIGRFAMs; TIGR01584; citF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lyase; Reference proteome; Transferase. FT CHAIN 1 500 Citrate lyase alpha chain. FT /FTId=PRO_0000089753. SQ SEQUENCE 500 AA; 54134 MW; F7D1EF303C446913 CRC64; MTTREQRIEK YHADRSVYQA VPKSESLSRT AKDRKLCTSL EEAIKRSGLK DGMTVSFHHA FRGGDFVVNM VMNKIAEMGF KNLTLASSSL IDSHFPIVEH IKNGVVTKIY SSGLRGELAE QISRGLLNEP VNIHSHGGRV HLVKSGELKI DVAFLGVPCC DTFGNANGFT GKSKCGSLGY ARVDAEYADK VVLLTEEFVE YPHHPISIAQ DQVDLIVQVE AVGDPKKIGG GATRMTTNPR ELLIARKCAE VIFASGYFKD GFSLQTGSGG AALAVTRFLE EKMRRENITA DFALGGITAS MVALHEAGLI KKLLDVQSFD SVAAESLARN PNHIEVSANQ YANYSSKGAS VERLDMVILS ALEIDTKFNV NVLTGSDGVI RGASGGHCDT AASAQVAIIV APLVRGRIPT VVENVITCVT PGENVDILVT DHGVAVNPKR PDLIEALSKT DIPLFTIEQL CERAYSITGK PKEIEFTNKP VAVVRYRDGS VIDTVYQVKD // ID CDD_HAEIN Reviewed; 292 AA. AC P44325; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Cytidine deaminase {ECO:0000255|HAMAP-Rule:MF_01558}; DE EC=3.5.4.5 {ECO:0000255|HAMAP-Rule:MF_01558}; DE AltName: Full=Cytidine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01558}; DE Short=CDA {ECO:0000255|HAMAP-Rule:MF_01558}; GN Name=cdd {ECO:0000255|HAMAP-Rule:MF_01558}; Synonyms=cda; GN OrderedLocusNames=HI_1350; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine CC and 2'-deoxycytidine for UMP synthesis. {ECO:0000255|HAMAP- CC Rule:MF_01558}. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- CATALYTIC ACTIVITY: 2'deoxycytidine + H(2)O = 2'-deoxyuridine + CC NH(3). {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01558}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_01558}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000255|HAMAP-Rule:MF_01558}. CC -!- SIMILARITY: Contains 2 CMP/dCMP-type deaminase domains. 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; L42023; AAC22997.1; -; Genomic_DNA. DR PIR; D64118; D64118. DR RefSeq; NP_439501.1; NC_000907.1. DR RefSeq; WP_010869187.1; NC_000907.1. DR ProteinModelPortal; P44325; -. DR STRING; 71421.HI1350; -. DR EnsemblBacteria; AAC22997; AAC22997; HI_1350. DR GeneID; 950271; -. DR KEGG; hin:HI1350; -. DR PATRIC; 20191385; VBIHaeInf48452_1403. DR eggNOG; ENOG4107T42; Bacteria. DR eggNOG; COG0295; LUCA. DR KO; K01489; -. DR OMA; NQSHAPY; -. DR OrthoDB; EOG6XDH25; -. DR PhylomeDB; P44325; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0009972; P:cytidine deamination; IBA:GO_Central. DR HAMAP; MF_01558; Cyt_deam; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd. DR InterPro; IPR006263; Cyt_deam_dimer. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR020797; Cytidine_deaminase_bacteria. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF08211; dCMP_cyt_deam_2; 1. DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 1. DR SUPFAM; SSF53927; SSF53927; 2. DR TIGRFAMs; TIGR01355; cyt_deam_dimer; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 292 Cytidine deaminase. FT /FTId=PRO_0000171653. FT DOMAIN 47 167 CMP/dCMP-type deaminase 1. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT DOMAIN 186 292 CMP/dCMP-type deaminase 2. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT REGION 88 90 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01558}. FT ACT_SITE 103 103 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01558}. FT METAL 101 101 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01558}. FT METAL 128 128 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01558}. FT METAL 131 131 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01558}. SQ SEQUENCE 292 AA; 32571 MW; 9EAAC949E96BA7B9 CRC64; MQDLIKRTLP QDDALNQAIV NDLRSQNWAG FLNYSQVQQL CHNFELTTLK LAMHLLPLAA SYSHTAISHF NVGAIAIGEQ GDFYFGANQE FANSAIQQTI HAEQSAISHA WLRNERRISD MVVNYTPCGH CRQFMNELHG AEKISIHLPH SQNNPLHSYL PDAFGPKDLD IAAHLLAEEN HDLVADHQDD LVNQAILAAN QSHCPYSNSP HGIAILFKNS DVVTGRYAEN AAFNPSLPAL QTALNFAYLN DKKLSDIERI VMAEKALKLS HKTMAETLLS TLTSVELEYY SL // ID CH60_HAEIN Reviewed; 548 AA. AC P43733; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Protein Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groEL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA; GN OrderedLocusNames=HI_0543; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Prevents misfolding and promotes the refolding and CC proper assembly of unfolded polypeptides generated under stress CC conditions. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBUNIT: Oligomer of 14 subunits composed of two stacked rings of CC 7 subunits. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22201.1; -; Genomic_DNA. DR PIR; C64076; C64076. DR RefSeq; NP_438701.1; NC_000907.1. DR RefSeq; WP_010869002.1; NC_000907.1. DR ProteinModelPortal; P43733; -. DR SMR; P43733; 2-527. DR STRING; 71421.HI0543; -. DR EnsemblBacteria; AAC22201; AAC22201; HI_0543. DR GeneID; 950072; -. DR KEGG; hin:HI0543; -. DR PATRIC; 20189639; VBIHaeInf48452_0562. DR eggNOG; ENOG4105CJ9; Bacteria. DR eggNOG; COG0459; LUCA. DR KO; K04077; -. DR OMA; KKQMDET; -. DR OrthoDB; EOG6JDWBZ; -. DR PhylomeDB; P43733; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 548 60 kDa chaperonin. FT /FTId=PRO_0000063387. SQ SEQUENCE 548 AA; 57577 MW; CA4066AAC1B62159 CRC64; MAAKDVKFGN DARVKMLKGV NVLADAVKVT LGPKGRHVIL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI DKAVSAVVSE LKNLSKPCET AKEIEQVGTI SANSDSIVGQ LISQAMEKVG KEGVITVEDG TGLEDELDVV EGMQFDRGYL SPYFINKPET ATVELDNPYL LLVDKKISNI RELLPVLEGV AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIAILTAGTV ISEEIGMELE KATLEDLGQA KRVVINKDNT TIIDGIGDEA QIKGRVAQIR QQIEESTSDY DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVDDAL HATRAAVEEG IVAGGGVALV RAAAKVAASL KGDNEEQNVG IKLALRAMEA PLRQIVTNAG EEASVVASAV KNGEGNFGYN AGTEQYGDMI EMGILDPTKV TRSALQFAAS VAGLMITTEC MVTDLPKDDK ADLGAAGMGG MGGMGGMM // ID CITD_HAEIN Reviewed; 95 AA. AC P44461; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Citrate lyase acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_00805}; DE AltName: Full=Citrate lyase gamma chain {ECO:0000255|HAMAP-Rule:MF_00805}; GN Name=citD {ECO:0000255|HAMAP-Rule:MF_00805}; GN OrderedLocusNames=HI_0024; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Covalent carrier of the coenzyme of citrate lyase. CC {ECO:0000255|HAMAP-Rule:MF_00805}. CC -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta, CC gamma)6. {ECO:0000255|HAMAP-Rule:MF_00805}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00805}. CC -!- SIMILARITY: Belongs to the CitD family. {ECO:0000255|HAMAP- CC Rule:MF_00805}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21702.1; -; Genomic_DNA. DR PIR; E64043; E64043. DR RefSeq; NP_438197.1; NC_000907.1. DR RefSeq; WP_005668023.1; NC_000907.1. DR STRING; 71421.HI0024; -. DR EnsemblBacteria; AAC21702; AAC21702; HI_0024. DR GeneID; 950921; -. DR KEGG; hin:HI0024; -. DR PATRIC; 20188499; VBIHaeInf48452_0024. DR eggNOG; ENOG4105XGS; Bacteria. DR eggNOG; COG3052; LUCA. DR KO; K01646; -. DR OMA; YNWKEID; -. DR OrthoDB; EOG6S52TW; -. DR PhylomeDB; P44461; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR HAMAP; MF_00805; CitD; 1. DR InterPro; IPR006495; CitD. DR InterPro; IPR023439; Mal_deCO2ase/Cit_lyase_ACP. DR Pfam; PF06857; ACP; 1. DR PIRSF; PIRSF002736; Citrt_lyas_gamma; 1. DR ProDom; PD015389; CitD; 1. DR TIGRFAMs; TIGR01608; citD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. FT CHAIN 1 95 Citrate lyase acyl carrier protein. FT /FTId=PRO_0000214700. FT MOD_RES 14 14 O-(phosphoribosyl dephospho-coenzyme FT A)serine. {ECO:0000255|HAMAP- FT Rule:MF_00805}. SQ SEQUENCE 95 AA; 10184 MW; 1F4DD150008E2471 CRC64; MKITKVAVAG TLESSDVQVR VQPFDSLDIE INSSVAKQFG EQIEATVREV LAKLGITAAQ VIVEDKGALD CVLQARVKAA AMRATDEAIN WEAVL // ID CLPP_HAEIN Reviewed; 193 AA. AC P43867; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 108. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444}; DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444}; DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444}; GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; GN OrderedLocusNames=HI_0714; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cleaves peptides in various proteins in a process that CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a CC major role in the degradation of misfolded proteins. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- CC and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP- CC Rule:MF_00444}. CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings CC which stack back to back to give a disk-like structure with a CC central cavity, resembling the structure of eukaryotic CC proteasomes. {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}. CC -!- SIMILARITY: Belongs to the peptidase S14 family. CC {ECO:0000255|HAMAP-Rule:MF_00444}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22371.1; -; Genomic_DNA. DR PIR; D64088; D64088. DR RefSeq; NP_438872.3; NC_000907.1. DR RefSeq; WP_005694635.1; NC_000907.1. DR ProteinModelPortal; P43867; -. DR SMR; P43867; 2-193. DR STRING; 71421.HI0714; -. DR MEROPS; S14.001; -. DR EnsemblBacteria; AAC22371; AAC22371; HI_0714. DR GeneID; 949737; -. DR KEGG; hin:HI0714; -. DR PATRIC; 20190051; VBIHaeInf48452_0746. DR eggNOG; ENOG4105CCQ; Bacteria. DR eggNOG; COG0740; LUCA. DR KO; K01358; -. DR OMA; ARMNELM; -. DR OrthoDB; EOG6Z3KQ0; -. DR PhylomeDB; P43867; -. DR BRENDA; 3.4.21.92; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_00444; ClpP; 1. DR InterPro; IPR001907; ClpP. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR033135; ClpP_His_AS. DR InterPro; IPR018215; ClpP_Ser_AS. DR PANTHER; PTHR10381; PTHR10381; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; KW Serine protease. FT CHAIN 1 193 ATP-dependent Clp protease proteolytic FT subunit. FT /FTId=PRO_0000179566. FT ACT_SITE 98 98 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00444}. FT ACT_SITE 123 123 {ECO:0000255|HAMAP-Rule:MF_00444}. SQ SEQUENCE 193 AA; 21373 MW; FDA4DCD8D2628181 CRC64; MSVIPMVVEQ TSRGERSYDI YSRLLKERVI FLSGEVEDRM ANLIVAQLLF LESEDPTKDI NIYINSPGGS VTAGMAIYDT MQFIKPDIRT LCIGQACSMG AFLLAGGTAG KRAALPNARV MIHQPLGGFR GQASDIQIHA QEILKIKHTL NDRLAFHTGQ GIERIEKDTD RDNFMSAEEA QAYGLVDEVL VKR // ID CITC_HAEIN Reviewed; 335 AA. AC P44462; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=[Citrate [pro-3S]-lyase] ligase; DE EC=6.2.1.22; DE AltName: Full=Acetate:SH-citrate lyase ligase; DE AltName: Full=Citrate lyase synthetase; GN Name=citC; OrderedLocusNames=HI_0025; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)- CC 3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase. CC -!- CATALYTIC ACTIVITY: ATP + acetate + [citrate (pro-3S)-lyase](thiol CC form) = AMP + diphosphate + [citrate (pro-3S)-lyase](acetyl form). CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21703.1; -; Genomic_DNA. DR PIR; F64043; F64043. DR RefSeq; NP_438198.1; NC_000907.1. DR RefSeq; WP_005668021.1; NC_000907.1. DR ProteinModelPortal; P44462; -. DR STRING; 71421.HI0025; -. DR DNASU; 950918; -. DR EnsemblBacteria; AAC21703; AAC21703; HI_0025. DR GeneID; 950918; -. DR KEGG; hin:HI0025; -. DR PATRIC; 20188501; VBIHaeInf48452_0025. DR eggNOG; ENOG4105DUA; Bacteria. DR eggNOG; COG3053; LUCA. DR KO; K01910; -. DR OMA; KGHQYLV; -. DR OrthoDB; EOG6WHNRS; -. DR PhylomeDB; P44462; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR005216; Citrate_lyase_ligase. DR InterPro; IPR013166; Citrate_lyase_ligase_C. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF08218; Citrate_ly_lig; 1. DR PIRSF; PIRSF005751; Acet_citr_lig; 1. DR SMART; SM00764; Citrate_ly_lig; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR00124; cit_ly_ligase; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 335 [Citrate [pro-3S]-lyase] ligase. FT /FTId=PRO_0000089771. FT DOMAIN 1 131 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 335 AA; 38495 MW; BF7CE241C725C8EC CRC64; MQFERISTEQ KKLSLIQTFL HQNALKLDEQ IEYFVVGYND NEQIVVCGGL AGNIIKCVAI DESLRGSGVA LQLITELVDL AYTLKRPHLF IYTKPEYATL FKSCGFYIIS DANPYVVLLE NSATRLQKQC SLWEKMRVDG NRIGSIVMNA NPFTLGHRYL IEQALQQCDH LHLFIVGEDA SQFSYTERFE MIQQGIFDLS NITLHSGSDY IISRATFPNY FLKDQLITDE SYFEIDLKLF RLHIAQALGI THRFVGTELN CPVTAEYNRQ MHYWLMDAEM NAPKINVIEI PRKTASNHII SASTVRKHLA EKNWAQLAEF VPMTTLNYLQ KCGRF // ID CITE_HAEIN Reviewed; 291 AA. AC P44460; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 98. DE RecName: Full=Citrate lyase subunit beta; DE Short=Citrase beta chain; DE EC=4.1.3.6; DE AltName: Full=Citrate (pro-3S)-lyase subunit beta; DE AltName: Full=Citryl-CoA lyase subunit; DE EC=4.1.3.34; GN Name=citE; OrderedLocusNames=HI_0023; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Represents a citryl-ACP lyase. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Citrate = acetate + oxaloacetate. CC -!- CATALYTIC ACTIVITY: (3S)-citryl-CoA = acetyl-CoA + oxaloacetate. 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 -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta, CC gamma)6. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. Citrate CC lyase beta subunit 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; L42023; AAC21701.1; -; Genomic_DNA. DR PIR; D64043; D64043. DR RefSeq; NP_438196.2; NC_000907.1. DR ProteinModelPortal; P44460; -. DR STRING; 71421.HI0023; -. DR EnsemblBacteria; AAC21701; AAC21701; HI_0023. DR GeneID; 950915; -. DR KEGG; hin:HI0023; -. DR PATRIC; 20188497; VBIHaeInf48452_0023. DR eggNOG; ENOG4105CI0; Bacteria. DR eggNOG; COG2301; LUCA. DR KO; K01644; -. DR OMA; FAPTQKD; -. DR OrthoDB; EOG6DVJVX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009346; C:citrate lyase complex; IEA:InterPro. DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.60; -; 1. DR InterPro; IPR005000; Aldolase/citrate-lyase_domain. DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2. DR InterPro; IPR006475; Citrate_lyase_beta_bac. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR32308; PTHR32308; 1. DR Pfam; PF03328; HpcH_HpaI; 1. DR PIRSF; PIRSF015582; Cit_lyase_B; 1. DR SUPFAM; SSF51621; SSF51621; 1. DR TIGRFAMs; TIGR01588; citE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lyase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 291 Citrate lyase subunit beta. FT /FTId=PRO_0000089758. FT METAL 129 129 Magnesium. {ECO:0000250}. FT METAL 156 156 Magnesium. {ECO:0000250}. FT BINDING 66 66 Substrate. {ECO:0000250}. FT BINDING 129 129 Substrate. {ECO:0000250}. SQ SEQUENCE 291 AA; 31855 MW; 9DB1B9D202CF221F CRC64; MKLRRSMLFV PGSNAAMLSN SFIYKPDSIM FDLEDAVALK EKDSARLLVA HALQHPLYKE IETVVRVNPL DSEFGLLDLN SVVRAGVDVV RMPKTESAQD VLDMDHAITE IEKACGREAG STKMLAAIES PLGITQANQI AFASKRLIGI ALGAEDYVRN LKTERSPEGI ELLFARCSIL QAARAAGIQA FDTVYSNANN EEGFLKEAAL IKQLGFDGKS LINPRQIELL HNLFAPTQKD VEQAKRIIEA AVEAERQGAG VVSLNGKMID APIIDRAKLV LERAKSGIRE E // ID CMOA_HAEIN Reviewed; 241 AA. AC P43985; P43986; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 118. DE RecName: Full=Carboxy-S-adenosyl-L-methionine synthase {ECO:0000255|HAMAP-Rule:MF_01589}; DE Short=Cx-SAM synthase {ECO:0000255|HAMAP-Rule:MF_01589}; DE EC=2.1.3.- {ECO:0000255|HAMAP-Rule:MF_01589}; GN Name=cmoA {ECO:0000255|HAMAP-Rule:MF_01589}; GN OrderedLocusNames=HI_0319; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-HOMOSELENOCYSTEINE, AND SUBUNIT. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11746687; DOI=10.1002/prot.10004; RA Lim K., Zhang H., Tempczyk A., Bonander N., Toedt J., Howard A., RA Eisenstein E., Herzberg O.; RT "Crystal structure of YecO from Haemophilus influenzae (HI0319) RT reveals a methyltransferase fold and a bound S-adenosylhomocysteine."; RL Proteins 45:397-407(2001). CC -!- FUNCTION: Catalyzes the conversion of S-adenosyl-L-methionine CC (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). CC {ECO:0000255|HAMAP-Rule:MF_01589}. CC -!- CATALYTIC ACTIVITY: Prephenate + S-adenosyl-L-methionine = CC phenylpyruvate + carboxy-S-adenosyl-L-methionine + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01589}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01589, CC ECO:0000269|PubMed:11746687}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. Cx-SAM synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01589}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21983.1; -; Genomic_DNA. DR PIR; C64006; C64006. DR RefSeq; NP_438485.1; NC_000907.1. DR RefSeq; WP_005694346.1; NC_000907.1. DR PDB; 1IM8; X-ray; 2.20 A; A/B=1-241. DR PDBsum; 1IM8; -. DR ProteinModelPortal; P43985; -. DR SMR; P43985; 17-241. DR STRING; 71421.HI0319; -. DR EnsemblBacteria; AAC21983; AAC21983; HI_0319. DR GeneID; 949432; -. DR KEGG; hin:HI0319; -. DR PATRIC; 20189181; VBIHaeInf48452_0337. DR eggNOG; ENOG4105DA6; Bacteria. DR eggNOG; COG0500; LUCA. DR KO; K15256; -. DR OMA; MIELYYL; -. DR OrthoDB; EOG628F44; -. DR PhylomeDB; P43985; -. DR EvolutionaryTrace; P43985; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01589; Cx_SAM_synthase; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR005271; tRNA_cmo5U34_MeTrfase. DR PIRSF; PIRSF006325; MeTrfase_bac; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00740; TIGR00740; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 241 Carboxy-S-adenosyl-L-methionine synthase. FT /FTId=PRO_0000169084. FT REGION 63 65 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01589, FT ECO:0000305|PubMed:11746687}. FT REGION 88 89 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01589, FT ECO:0000305|PubMed:11746687}. FT REGION 116 117 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01589, FT ECO:0000305|PubMed:11746687}. FT BINDING 38 38 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01589, FT ECO:0000305|PubMed:11746687}. FT BINDING 131 131 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01589, FT ECO:0000305|PubMed:11746687}. FT BINDING 198 198 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01589}. FT HELIX 21 34 {ECO:0000244|PDB:1IM8}. FT HELIX 38 52 {ECO:0000244|PDB:1IM8}. FT STRAND 58 63 {ECO:0000244|PDB:1IM8}. FT HELIX 68 75 {ECO:0000244|PDB:1IM8}. FT STRAND 83 87 {ECO:0000244|PDB:1IM8}. FT HELIX 91 102 {ECO:0000244|PDB:1IM8}. FT STRAND 110 113 {ECO:0000244|PDB:1IM8}. FT TURN 117 119 {ECO:0000244|PDB:1IM8}. FT STRAND 124 132 {ECO:0000244|PDB:1IM8}. FT HELIX 134 136 {ECO:0000244|PDB:1IM8}. FT HELIX 139 141 {ECO:0000244|PDB:1IM8}. FT HELIX 142 152 {ECO:0000244|PDB:1IM8}. FT STRAND 153 164 {ECO:0000244|PDB:1IM8}. FT HELIX 170 186 {ECO:0000244|PDB:1IM8}. FT HELIX 189 191 {ECO:0000244|PDB:1IM8}. FT HELIX 195 204 {ECO:0000244|PDB:1IM8}. FT HELIX 210 220 {ECO:0000244|PDB:1IM8}. FT STRAND 223 231 {ECO:0000244|PDB:1IM8}. FT STRAND 234 240 {ECO:0000244|PDB:1IM8}. SQ SEQUENCE 241 AA; 27372 MW; 08743633A3E853F8 CRC64; MVKDTLFSTP IAKLGDFIFD ENVAEVFPDM IQRSVPGYSN IITAIGMLAE RFVTADSNVY DLGCSRGAAT LSARRNINQP NVKIIGIDNS QPMVERCRQH IAAYHSEIPV EILCNDIRHV EIKNASMVIL NFTLQFLPPE DRIALLTKIY EGLNPNGVLV LSEKFRFEDT KINHLLIDLH HQFKRANGYS ELEVSQKRTA LENVMRTDSI ETHKVRLKNV GFSQVELWFQ CFNFGSMIAV K // ID CLPX_HAEIN Reviewed; 411 AA. AC P44838; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; GN OrderedLocusNames=HI_0715; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. CC It directs the protease to specific substrates. Can perform CC chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP- CC Rule:MF_00175}. CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric CC ring that, in the presence of ATP, binds to fourteen ClpP subunits CC assembled into a disk-like structure with a central cavity, CC resembling the structure of eukaryotic proteasomes. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. CC {ECO:0000255|HAMAP-Rule:MF_00175}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22372.1; -; Genomic_DNA. DR PIR; E64088; E64088. DR RefSeq; NP_438873.1; NC_000907.1. DR RefSeq; WP_005661954.1; NC_000907.1. DR ProteinModelPortal; P44838; -. DR SMR; P44838; 8-43. DR STRING; 71421.HI0715; -. DR PRIDE; P44838; -. DR EnsemblBacteria; AAC22372; AAC22372; HI_0715. DR GeneID; 949862; -. DR KEGG; hin:HI0715; -. DR PATRIC; 20190053; VBIHaeInf48452_0747. DR eggNOG; ENOG4105CHN; Bacteria. DR eggNOG; COG1219; LUCA. DR KO; K03544; -. DR OMA; HYKRVQA; -. DR OrthoDB; EOG625JZK; -. DR PhylomeDB; P44838; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00175; ClpX; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010603; Znf_CppX_C4. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR Pfam; PF06689; zf-C4_ClpX; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SMART; SM00994; zf-C4_ClpX; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00382; clpX; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 411 ATP-dependent Clp protease ATP-binding FT subunit ClpX. FT /FTId=PRO_0000160363. FT ZN_FING 10 35 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00175}. FT NP_BIND 118 125 ATP. {ECO:0000255|HAMAP-Rule:MF_00175}. SQ SEQUENCE 411 AA; 45733 MW; 6C8F4ACEA154FA2C CRC64; MTDKDKDLHC SFCGKEKGEV DRLIAGTDGY ICNECIELCH SMLEESHDKN LEESAVENEE KLPTPHEIRA HLDDYVIGQD YAKKVLSVAV YNHYKRLRTN YESNDVELGK SNILLIGPTG SGKTLLAQTL ARRLNVPFAM ADATTLTEAG YVGEDVENVL QKLLQNCEYD TEKAEKGIIY IDEIDKISRK SEGASITRDV SGEGVQQALL KLIEGTIASI PPQGGRKHPQ QEMVKLDTSK ILFICGGAFA GLDKIIDKRT QTSTSIGFNA KVEKDEKQQS LSELFRQVEP DDLMKFGLIP EFIGRLPMIA PLSELDEDAL IQILTKPKNA LIKQYQALFG LEKVELDFTP EALKAMAKKA LERKTGARGL RSIVEAVLLD TMYDLPSLEN LQKVIVDEST IVDNLAPKLE Y // ID COAA_HAEIN Reviewed; 311 AA. AC P44793; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Pantothenate kinase; DE EC=2.7.1.33; DE AltName: Full=Pantothenic acid kinase; GN Name=coaA; OrderedLocusNames=HI_0631; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 1/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22291.1; -; Genomic_DNA. DR PIR; I64082; I64082. DR RefSeq; NP_438791.1; NC_000907.1. DR RefSeq; WP_005667563.1; NC_000907.1. DR ProteinModelPortal; P44793; -. DR SMR; P44793; 5-311. DR STRING; 71421.HI0631; -. DR EnsemblBacteria; AAC22291; AAC22291; HI_0631. DR GeneID; 949538; -. DR KEGG; hin:HI0631; -. DR PATRIC; 20189857; VBIHaeInf48452_0657. DR eggNOG; ENOG4105CS9; Bacteria. DR eggNOG; COG1072; LUCA. DR KO; K00867; -. DR OMA; LMQRKGF; -. DR OrthoDB; EOG62C9GX; -. DR PhylomeDB; P44793; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00215; Pantothen_kinase_1; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004566; PanK_bact. DR InterPro; IPR006083; PRK/URK. DR PANTHER; PTHR10285:SF7; PTHR10285:SF7; 2. DR Pfam; PF00485; PRK; 1. DR PIRSF; PIRSF000545; Pantothenate_kin; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00554; panK_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 311 Pantothenate kinase. FT /FTId=PRO_0000194431. FT NP_BIND 93 100 ATP. {ECO:0000255}. SQ SEQUENCE 311 AA; 35907 MW; E81F8BBC21EB1D4E CRC64; MEFSTQQTPF LSFNREQWAE LRKSVPLKLT EQDLKPLLGF NEDLSLDEVS TIYLPLTRLI NYYIDENLHR QTVLHRFLGR NNAKTPYIIS IAGSVAVGKS TSARILQSLL SHWPTERKVD LITTDGFLYP LNKLKQDNLL QKKGFPVSYD TPKLIRFLAD VKSGKSNVTA PIYSHLTYDI IPDKFDVVDK PDILILEGLN VLQTGNNKTD QTFVSDFVDF SIYVDAEEKL LKEWYIKRFL KFRESAFNDP NSYFKHYASL SKEEAIATAS KIWDEINGLN LNQNILPTRE RANLILKKGH NHQVELIKLR K // ID COAE_HAEIN Reviewed; 206 AA. AC P44920; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 17-FEB-2016, entry version 119. DE RecName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; GN Name=coaE; OrderedLocusNames=HI_0890; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC22550.1; 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; L42023; AAC22550.1; ALT_INIT; Genomic_DNA. DR PIR; A64161; A64161. DR RefSeq; NP_439051.1; NC_000907.1. DR RefSeq; WP_010869082.1; NC_000907.1. DR PDB; 1JJV; X-ray; 2.00 A; A=1-206. DR PDBsum; 1JJV; -. DR ProteinModelPortal; P44920; -. DR SMR; P44920; 1-205. DR STRING; 71421.HI0890m; -. DR EnsemblBacteria; AAC22550; AAC22550; HI_0890. DR GeneID; 950766; -. DR KEGG; hin:HI0890m; -. DR PATRIC; 20190437; VBIHaeInf48452_0932. DR eggNOG; ENOG4108ZQD; Bacteria. DR eggNOG; COG0237; LUCA. DR KO; K00859; -. DR OMA; GGKKRYP; -. DR OrthoDB; EOG6HTP3H; -. DR PhylomeDB; P44920; -. DR BRENDA; 2.7.1.24; 2529. DR UniPathway; UPA00241; UER00356. DR EvolutionaryTrace; P44920; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1. DR InterPro; IPR001977; Depp_CoAkinase. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01121; CoaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00152; TIGR00152; 1. DR PROSITE; PS51219; DPCK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 206 Dephospho-CoA kinase. FT /FTId=PRO_0000172947. FT DOMAIN 4 204 DPCK. FT NP_BIND 9 16 ATP. {ECO:0000255}. FT STRAND 3 8 {ECO:0000244|PDB:1JJV}. FT HELIX 15 23 {ECO:0000244|PDB:1JJV}. FT TURN 24 26 {ECO:0000244|PDB:1JJV}. FT STRAND 29 31 {ECO:0000244|PDB:1JJV}. FT HELIX 32 38 {ECO:0000244|PDB:1JJV}. FT HELIX 45 54 {ECO:0000244|PDB:1JJV}. FT HELIX 67 75 {ECO:0000244|PDB:1JJV}. FT HELIX 78 101 {ECO:0000244|PDB:1JJV}. FT STRAND 105 111 {ECO:0000244|PDB:1JJV}. FT TURN 113 119 {ECO:0000244|PDB:1JJV}. FT HELIX 121 123 {ECO:0000244|PDB:1JJV}. FT STRAND 125 131 {ECO:0000244|PDB:1JJV}. FT HELIX 134 141 {ECO:0000244|PDB:1JJV}. FT HELIX 149 158 {ECO:0000244|PDB:1JJV}. FT HELIX 162 168 {ECO:0000244|PDB:1JJV}. FT STRAND 170 174 {ECO:0000244|PDB:1JJV}. FT HELIX 179 203 {ECO:0000244|PDB:1JJV}. SQ SEQUENCE 206 AA; 23287 MW; DF85B65D50131C01 CRC64; MTYIVGLTGG IGSGKTTIAN LFTDLGVPLV DADVVAREVV AKDSPLLSKI VEHFGAQILT EQGELNRAAL RERVFNHDED KLWLNNLLHP AIRERMKQKL AEQTAPYTLF VVPLLIENKL TALCDRILVV DVSPQTQLAR SAQRDNNNFE QIQRIMNSQV SQQERLKWAD DVINNDAELA QNLPHLQQKV LELHQFYLQQ AENKNA // ID CLPB_HAEIN Reviewed; 856 AA. AC P44403; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 110. DE RecName: Full=Chaperone protein ClpB; GN Name=clpB; OrderedLocusNames=HI_0859; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22518.1; -; Genomic_DNA. DR PIR; F64098; F64098. DR RefSeq; NP_439019.1; NC_000907.1. DR RefSeq; WP_010869072.1; NC_000907.1. DR ProteinModelPortal; P44403; -. DR SMR; P44403; 4-141, 159-351. DR STRING; 71421.HI0859; -. DR PRIDE; P44403; -. DR EnsemblBacteria; AAC22518; AAC22518; HI_0859. DR GeneID; 949871; -. DR KEGG; hin:HI0859; -. DR PATRIC; 20190373; VBIHaeInf48452_0900. DR eggNOG; ENOG4105C2Z; Bacteria. DR eggNOG; COG0542; LUCA. DR KO; K03695; -. DR OMA; PVERILM; -. DR OrthoDB; EOG65F8SM; -. DR PhylomeDB; P44403; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016485; P:protein processing; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR Gene3D; 1.10.1780.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR017730; Chaperonin_ClpB. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004176; Clp_N. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR018368; ClpA/B_CS1. DR InterPro; IPR028299; ClpA/B_CS2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF02861; Clp_N; 2. DR Pfam; PF10431; ClpB_D2-small; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 2. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF81923; SSF81923; 1. DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1. 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 1 856 Chaperone protein ClpB. FT /FTId=PRO_0000191127. FT NP_BIND 206 213 ATP 1. {ECO:0000250}. FT NP_BIND 605 612 ATP 2. {ECO:0000250}. FT REGION 1 143 N-terminal. {ECO:0000250}. FT REGION 159 340 NBD1. {ECO:0000250}. FT REGION 341 545 Linker. {ECO:0000250}. FT REGION 555 764 NBD2. {ECO:0000250}. FT REGION 765 856 C-terminal. {ECO:0000250}. FT COILED 391 523 {ECO:0000250}. SQ SEQUENCE 856 AA; 95837 MW; B8958ED9BD03EA3B CRC64; MNIEKFTTKF QEALSERQSL AIGKDNQFIE PVHLLTALLN QQGGSIAPIL TASGVNVALL RNELKTELNK LPQVIGNGGD VQLSRQLINL LNLCDKFAQQ NQDKFISSEL FLFAALEERG TISDILKKCG AKKEQISQAI QHIRGGQNVN DQNAEESRQA LEKYTIDLTA RAESGKLDPV IGRDEEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNKRVLSL DMGALIAGAK YRGEFEERLK AVLNELSKEE GRVILFIDEI HTMVGAGKTD GAMDAGNLLK PSLARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVDE PSVEDTIAIL RGLKERYEIH HHVDITDPAI VAAATLSHRY ISDRQLPDKA IDLIDEAASS IRMEIDSKPE PLDRLERRII QLKLEQQALQ KEEDEASRKR LEMLEKELAE KEREYAELEE VWKSEKATLS GSQHIKQELD TAKTELEQAR RAGDLAKMSE LQYGRIPDLE KQLEQAETSE GKEMTLLRYR VTDEEIAEVL SKATGIPVSK MMEGEKEKLL RMEDELHKRV IGQEEAVDAV ANAIRRSRAG LSDPNRPIGS FLFLGPTGVG KTELCKTLAK FLFDSEDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG YLTEAVRRRP YSVILLDEVE KAHADVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL GSDLIQGNKD ESYSEMKALV MSVVSQHFRP EFINRIDETV VFHPLGKENI RAIASIQLER LAKRMETRGY ELVFTDALLD FIGEVGYDPI YGARPLKRAI QQEIENSLAQ QILSGALLPG KVVTIDYANA EVQARQ // ID COMC_HAEIN Reviewed; 173 AA. AC P31770; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Competence protein C; DE AltName: Full=DNA transformation protein ComC; GN Name=comC; OrderedLocusNames=HI_0437; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25010.1; -; Genomic_DNA. DR EMBL; L42023; AAC22096.1; -; Genomic_DNA. DR PIR; A64068; JH0432. DR RefSeq; NP_438598.1; NC_000907.1. DR RefSeq; WP_005693726.1; NC_000907.1. DR STRING; 71421.HI0437; -. DR EnsemblBacteria; AAC22096; AAC22096; HI_0437. DR GeneID; 950528; -. DR KEGG; hin:HI0437; -. DR PATRIC; 20189427; VBIHaeInf48452_0457. DR OMA; DSPLQTE; -. DR OrthoDB; EOG65QWJ6; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. PE 4: Predicted; KW Competence; Complete proteome; Reference proteome. FT CHAIN 1 173 Competence protein C. FT /FTId=PRO_0000090006. SQ SEQUENCE 173 AA; 19941 MW; 8E056A7B58EF6FA7 CRC64; MKAFFNDPFT PFGKWLSQPF YVHGLTFLLL LSAVIFRPVL DYIEGSSRFH EIENELAVKR SELLHQQKIL TSLQQQSESR KLSPELAAQI IPLNKQIQRL AARNGLSQHL RWEMGQKPIL HLQLTGHFEK TKTFLSALLA NSSQLSVSRL QFMKPEDGPL QTEIIFQLDK ETK // ID COMD_HAEIN Reviewed; 137 AA. AC P31771; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 01-APR-2015, entry version 67. DE RecName: Full=Competence protein D; DE AltName: Full=DNA transformation protein ComD; GN Name=comD; OrderedLocusNames=HI_0436; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25011.1; -; Genomic_DNA. DR EMBL; L42023; AAC22095.1; -; Genomic_DNA. DR PIR; I64067; JH0433. DR RefSeq; NP_438597.1; NC_000907.1. DR RefSeq; WP_005693727.1; NC_000907.1. DR STRING; 71421.HI0436; -. DR EnsemblBacteria; AAC22095; AAC22095; HI_0436. DR GeneID; 950663; -. DR KEGG; hin:HI0436; -. DR PATRIC; 20189425; VBIHaeInf48452_0456. DR OMA; ISEDKAF; -. DR OrthoDB; EOG64XXNS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR InterPro; IPR016506; ComD_Pasteurellaceae. DR InterPro; IPR007446; Pilus_assembly_PilP. DR Pfam; PF04351; PilP; 1. DR PIRSF; PIRSF007059; ComD; 1. PE 4: Predicted; KW Competence; Complete proteome; Reference proteome. FT CHAIN 1 137 Competence protein D. FT /FTId=PRO_0000090007. SQ SEQUENCE 137 AA; 15682 MW; 60AC1B9C0DC1A1A1 CRC64; MKHWFFLIIL FFMNCSWGQD PFDKTQRNRS QFDNAQTVME QTEIISSDVP NNLCGADENR QAAEIPLNAL KLVGVVISKD KAFALLQDQG LQVYSVLEGV DVAQEGYIVE KINQNNVQFM RKLGEQCDSS EWKKLSF // ID CORA_HAEIN Reviewed; 315 AA. AC P44998; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Magnesium transport protein CorA; GN Name=corA; OrderedLocusNames=HI_1035; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Mediates influx of magnesium ions. Can also mediate CC cobalt and manganese uptake (By similarity). Alternates between CC open and closed states. Activated by low cytoplasmic Mg(2+) CC levels. Inactive when cytoplasmic Mg(2+) levels are high (By CC similarity). {ECO:0000250|UniProtKB:P0ABI4, CC ECO:0000250|UniProtKB:Q9WZ31}. CC -!- SUBUNIT: Homopentamer. In the absence of Mg(2+), interactions CC between subunits are weakened, and dimers, trimers and tetramers CC can be observed in vitro (By similarity). CC {ECO:0000250|UniProtKB:Q9WZ31}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0ABI4}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9WZ31}. CC -!- DOMAIN: The central ion permeation pathway is formed by the first CC transmembrane domain from each of the five subunits. Mg(2+) CC binding strengthens interactions between subunits and leads to the CC formation of a symmetrical homopentamer surrounding a closed ion CC permeation pathway. Co(2+) binding also induces a conformation CC change. Low Mg(2+) concentrations trigger both a conformation CC change within each subunit and a loosening of the interactions CC between subunits. This results in an open ion conduction pathway. CC In addition, this results in a less symmetrical shape of the whole CC complex. {ECO:0000250|UniProtKB:Q9WZ31}. CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) CC (TC 1.A.35) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22695.1; -; Genomic_DNA. DR PIR; A64109; A64109. DR RefSeq; NP_439195.1; NC_000907.1. DR RefSeq; WP_005651675.1; NC_000907.1. DR ProteinModelPortal; P44998; -. DR STRING; 71421.HI1035; -. DR EnsemblBacteria; AAC22695; AAC22695; HI_1035. DR GeneID; 950726; -. DR KEGG; hin:HI1035; -. DR PATRIC; 20190733; VBIHaeInf48452_1079. DR eggNOG; ENOG4107QUT; Bacteria. DR eggNOG; COG0598; LUCA. DR KO; K03284; -. DR OMA; RRAVSFM; -. DR OrthoDB; EOG6MD91T; -. DR PhylomeDB; P44998; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006824; P:cobalt ion transport; IBA:GO_Central. DR GO; GO:1903830; P:magnesium ion transmembrane transport; IBA:GOC. DR GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central. DR GO; GO:0035444; P:nickel cation transmembrane transport; IBA:GO_Central. DR InterPro; IPR004488; Mg/Co-transport_prot_CorA. DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB. DR Pfam; PF01544; CorA; 1. DR TIGRFAMs; TIGR00383; corA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Magnesium; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 315 Magnesium transport protein CorA. FT /FTId=PRO_0000201530. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT MOTIF 276 278 Probable selectivity filter. FT {ECO:0000250|UniProtKB:Q9WZ31}. FT SITE 252 252 Essential for ion permeation. FT {ECO:0000250|UniProtKB:Q9WZ31}. SQ SEQUENCE 315 AA; 36594 MW; DA4EDA284CC68DCC CRC64; MINAFAINDS RLVRIDEDQT DLNTAIWLDL LEPTGEEREM LQEGLGQSLA SFLELEDIEA SARFFEDEDG LHLHSFFYCE DEDNYADLAS VAFTIRDGRL FTLRDRELPA FRLYRMRSRS QRLLECNSYE VLLDLFETKI EQLADVIENI YADLEELSRV ILNGKQDEAF DEALNTLTEQ EDTSSKVRLC LMDTQRALGF LVRKTRLPTN QLEQAREILR DIESLQPHNE SLFQKVNFLM QAAMGYINIE QNKIMKFFSV VSVMFLPATL VASTYGMNFD FMPELHFKYG YPMAIGLMIA AALTPYIYFR RKGWL // ID CITXG_HAEIN Reviewed; 465 AA. AC P44458; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-MAY-2016, entry version 104. DE RecName: Full=Protein CitXG; DE Includes: DE RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase; DE EC=2.7.7.61; DE AltName: Full=Apo-ACP nucleodityltransferase; DE AltName: Full=Holo-ACP synthase; DE AltName: Full=Holo-citrate lyase synthase; DE Includes: DE RecName: Full=2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase; DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase; DE EC=2.4.2.52; GN Name=citXG; Synonyms=citG; OrderedLocusNames=HI_0021; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Bifunctional enzyme that catalyzes formation of 2-(5''- CC triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer CC of this prosthetic group precursor to the apo-acyl carrier protein CC (gamma chain) of the citrate lyase to yield the holo-acyl carrier CC protein. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + CC citrate lyase apo-[acyl-carrier protein] = citrate lyase holo- CC [acyl-carrier protein] + diphosphate. CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = 2'-(5-triphospho- CC alpha-D-ribosyl)-3'-dephospho-CoA + adenine. CC -!- SIMILARITY: In the N-terminal section; belongs to the CitX family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CitG/MdcB CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21699.1; 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; L42023; AAC21699.1; ALT_INIT; Genomic_DNA. DR PIR; E64140; E64140. DR RefSeq; NP_438194.1; NC_000907.1. DR RefSeq; WP_010868918.1; NC_000907.1. DR STRING; 71421.HI0021; -. DR EnsemblBacteria; AAC21699; AAC21699; HI_0021. DR GeneID; 950919; -. DR KEGG; hin:HI0021; -. DR PATRIC; 20188493; VBIHaeInf48452_0021. DR eggNOG; ENOG4108K6F; Bacteria. DR eggNOG; COG1767; LUCA. DR eggNOG; COG3697; LUCA. DR KO; K13927; -. DR OMA; QSLAQNH; -. DR OrthoDB; EOG6WHNRS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:InterPro. DR GO; GO:0051191; P:prosthetic group biosynthetic process; IBA:GO_Central. DR HAMAP; MF_00397; CitG; 1. DR HAMAP; MF_00398; CitX; 1. DR InterPro; IPR002736; CitG. DR InterPro; IPR005551; CitX. DR InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG. DR Pfam; PF01874; CitG; 1. DR Pfam; PF03802; CitX; 1. DR TIGRFAMs; TIGR03125; citrate_citG; 1. DR TIGRFAMs; TIGR03124; citrate_citX; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Multifunctional enzyme; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 465 Protein CitXG. FT /FTId=PRO_0000214682. FT REGION 1 182 Apo-citrate lyase phosphoribosyl- FT dephospho-CoA transferase. FT REGION 183 465 2-(5''-triphosphoribosyl)-3'- FT dephosphocoenzyme-A synthase. SQ SEQUENCE 465 AA; 51835 MW; 4467221C3DB58A96 CRC64; MQHFFTTFST EGSKISLEAL LNAREERAIL QQQLITQYGQ TLLCITLTAM GGVKKNALLD YVFTKALENL TALFTQLNIT AVKEIIRPLE TGHEAYFVLP IDARTLKVLM IELEESIPLA RLWDLDVFNA KGNLLSRTDF DLSPRTCLVC GENAKICART HKHEIDEIVD KIQSLAQNHD FAEHIGEQVY LALIQEARLS PKPGLVDAIN NGSHKDMNLH TFEQSAISLK PFFTQFVLKG MMTAHLSENQ ILSEIRPLGL LAEKAMFKVT DGVNTHKGAI FSFGLVCTAI GRLLAQKSLV QSAVDFDVKL ICSLVAQFTQ GLTDELKNYP EHLPSTAGVR LFQKYGLTGV RGEAENGFNL IQTLLPQFDE YHQLEWEHRL LILLLNLMAI NSDTNVVHRG GLAGLYFIQQ TAQDLLTDQH LVTDKTALTQ ALMKFDTACI ERNLSSGGSA DLLALTIFFL SFRGN // ID CMOB_HAEIN Reviewed; 321 AA. AC P44167; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=tRNA U34 carboxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_01590}; DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01590}; GN Name=cmoB {ECO:0000255|HAMAP-Rule:MF_01590}; GN OrderedLocusNames=HI_1351; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S- CC adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form CC 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_01590}. CC -!- CATALYTIC ACTIVITY: 5-hydroxyuridine(34) in tRNA + carboxy-S- CC adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + S- CC adenosyl-L-homocysteine. {ECO:0000255|HAMAP-Rule:MF_01590}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01590}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. CmoB family. {ECO:0000255|HAMAP- CC Rule:MF_01590}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22998.1; -; Genomic_DNA. DR PIR; E64026; E64026. DR RefSeq; NP_439502.1; NC_000907.1. DR RefSeq; WP_005694009.1; NC_000907.1. DR ProteinModelPortal; P44167; -. DR STRING; 71421.HI1351; -. DR EnsemblBacteria; AAC22998; AAC22998; HI_1351. DR GeneID; 950443; -. DR KEGG; hin:HI1351; -. DR PATRIC; 20191387; VBIHaeInf48452_1404. DR eggNOG; ENOG4105PFA; Bacteria. DR eggNOG; COG0500; LUCA. DR KO; K15257; -. DR OMA; CEWRSDF; -. DR OrthoDB; EOG6PZX8S; -. DR PhylomeDB; P44167; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01590; tRNA_carboxymethyltr_CmoB; 1. DR InterPro; IPR027555; mo5U34_MeTrfas-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR010017; tRNA_mo5U34_MeTrfase. DR Pfam; PF08003; Methyltransf_9; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00452; TIGR00452; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Transferase; tRNA processing. FT CHAIN 1 321 tRNA U34 carboxymethyltransferase. FT /FTId=PRO_0000169086. FT REGION 151 153 Carboxy-S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT REGION 180 181 Carboxy-S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT BINDING 90 90 Carboxy-S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT BINDING 104 104 Carboxy-S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT BINDING 109 109 Carboxy-S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT BINDING 129 129 Carboxy-S-adenosyl-L-methionine; via FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01590}. FT BINDING 195 195 Carboxy-S-adenosyl-L-methionine; via FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01590}. FT BINDING 199 199 Carboxy-S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01590}. FT BINDING 314 314 Carboxy-S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01590}. SQ SEQUENCE 321 AA; 36854 MW; 6CC25B67E4F5995A CRC64; MIDFRPFYQQ IATTNLSDWL ETLPCQLKEW ETQTHGDYAK WSKIVDFLPN LHADEIDLKS AVKSDRTSPL SEGEKQRIIH HLKQLMPWRK GPYHLFGIHV DCEWRSDFKW DRVLPHLSPL QGRTILDVGC GSGYHMWRMV GEGAKMVVGI DPTELFLCQF EAVRKLLNND RRANLIPLGI EQMQPLAAFD TVFSMGVLYH RKSPLDHLSQ LKNQLVKGGE LVLETLVVDG DINTVLVPAD RYAKMKNVYF IPSVATLINW LEKVGFTNVR CVDVATTTLE EQRKTDWLEN ESLIDFLDPN DHSKTIEGYQ APKRAVILAN K // ID COABC_HAEIN Reviewed; 400 AA. AC P44953; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC; DE AltName: Full=DNA/pantothenate metabolism flavoprotein; DE Includes: DE RecName: Full=Phosphopantothenoylcysteine decarboxylase; DE Short=PPCDC; DE EC=4.1.1.36; DE AltName: Full=CoaC; DE Includes: DE RecName: Full=Phosphopantothenate--cysteine ligase; DE EC=6.3.2.5; DE AltName: Full=CoaB; DE AltName: Full=PPC synthetase; DE Short=PPCS; DE AltName: Full=Phosphopantothenoylcysteine synthase; GN Name=coaBC; Synonyms=dfp; OrderedLocusNames=HI_0953; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. CC In the first step cysteine is conjugated to 4'-phosphopantothenate CC to form 4-phosphopantothenoylcysteine, in the latter compound is CC decarboxylated to form 4'-phosphopantotheine (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine = CC pantotheine 4'-phosphate + CO(2). CC -!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 2/5. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 3/5. CC -!- SUBUNIT: Homododecamer, the CoaB domains form homodimers. CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo- CC oligomeric flavin containing Cys decarboxylase) superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC CC 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; L42023; AAC22614.1; -; Genomic_DNA. DR PIR; G64104; G64104. DR RefSeq; NP_439114.1; NC_000907.1. DR RefSeq; WP_005693302.1; NC_000907.1. DR ProteinModelPortal; P44953; -. DR SMR; P44953; 185-398. DR STRING; 71421.HI0953; -. DR EnsemblBacteria; AAC22614; AAC22614; HI_0953. DR GeneID; 949948; -. DR KEGG; hin:HI0953; -. DR PATRIC; 20190565; VBIHaeInf48452_0995. DR eggNOG; ENOG4105CJS; Bacteria. DR eggNOG; COG0452; LUCA. DR KO; K13038; -. DR OMA; VRFIGNH; -. DR OrthoDB; EOG6FFSBB; -. DR PhylomeDB; P44953; -. DR UniPathway; UPA00241; UER00353. DR UniPathway; UPA00241; UER00354. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 1. DR InterPro; IPR005252; CoaBC. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Flavoprotein; FMN; Ligase; Lyase; KW Reference proteome. FT CHAIN 1 400 Coenzyme A biosynthesis bifunctional FT protein CoaBC. FT /FTId=PRO_0000232693. FT REGION 1 188 Phosphopantothenoylcysteine FT decarboxylase. FT REGION 189 400 Phosphopantothenate--cysteine ligase. FT ACT_SITE 158 158 Proton donor. {ECO:0000250}. FT BINDING 125 125 Substrate. {ECO:0000250}. FT BINDING 279 279 CTP. {ECO:0000250}. FT BINDING 289 289 CTP. {ECO:0000250}. FT BINDING 338 338 CTP. {ECO:0000250}. FT BINDING 342 342 CTP. {ECO:0000250}. SQ SEQUENCE 400 AA; 43401 MW; 1D6FEAE20C26B913 CRC64; MKLNGKHIVV GITGGIAAYK TIELIRLLRK AEAEVRVVLT PAAAEFVTPL TLQAISGNAV SQSLLDPQAE LAMGHIELAK WADAIIIAPA SADFIARLTI GMANDLLSTI CLATNAPIFL APAMNQQMYH QSITQQNLTT LQTRGIELIG PNSGFQACGD MGKGRMSEPE EIFTALSDFF SQKQDLQGLN VSITAGPTRE AIDPVRYISN HSSGKMGFAI AEAFAKRGAN VTLIAGPVNL TTPKNVNRIN VISAQEMWQA SLESAVKNQI FIGCAAVADY RVTEVAEQKI KKSGDEISIK LIKNPDIISD VGHLKTHRPF TVGFAAETQN VDDYAKDKLE RKNLDMICAN DVSGGQVFNA DENALQLFWK NGHKKLSLKS KVELAADLVN EIIERYQKTL // ID COMM_HAEIN Reviewed; 509 AA. AC P45049; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 106. DE RecName: Full=Competence protein ComM; GN Name=comM; OrderedLocusNames=HI_1117; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9457884; RA Gwinn M.L., Ramanathan R., Smith H.O., Tomb J.-F.; RT "A new transformation-deficient mutant of Haemophilus influenzae Rd RT with normal DNA uptake."; RL J. Bacteriol. 180:746-748(1998). CC -!- FUNCTION: Induced during competence development. Not needed for CC DNA uptake. May be involved in a recombination step. CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM 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; L42023; AAC22771.1; -; Genomic_DNA. DR PIR; I64183; I64183. DR RefSeq; NP_439274.1; NC_000907.1. DR RefSeq; WP_010869133.1; NC_000907.1. DR ProteinModelPortal; P45049; -. DR STRING; 71421.HI1117; -. DR EnsemblBacteria; AAC22771; AAC22771; HI_1117. DR GeneID; 950645; -. DR KEGG; hin:HI1117; -. DR PATRIC; 20190907; VBIHaeInf48452_1166. DR eggNOG; ENOG4105C0P; Bacteria. DR eggNOG; COG0606; LUCA. DR KO; K07391; -. DR OMA; CRCTPDQ; -. DR OrthoDB; EOG6ZWJFW; -. DR PhylomeDB; P45049; -. DR BioCyc; RETL1328306-WGS:GSTH-327-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR004482; Mg_chelat-rel. DR InterPro; IPR025158; Mg_chelat-rel_C. DR InterPro; IPR000523; Mg_chelatse_chII_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR32039:SF7; PTHR32039:SF7; 1. DR Pfam; PF01078; Mg_chelatase; 1. DR Pfam; PF13335; Mg_chelatase_C; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00368; TIGR00368; 1. PE 1: Evidence at protein level; KW ATP-binding; Competence; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 509 Competence protein ComM. FT /FTId=PRO_0000206876. FT NP_BIND 222 229 ATP. {ECO:0000255}. SQ SEQUENCE 509 AA; 55915 MW; 9CA5F217CD64305A CRC64; MSLAIVYSRA SMGVQAPLVT IEVHLSNGKP GFTLVGLPEK TVKEAQDRVR SALMNAQFKY PAKRITVNLA PADLPKEGGR FDLPIAIGIL AASDQLDASH LKQFEFVAEL ALTGQLRGVH GVIPAILAAQ KSKRELIIAK QNANEASLVS DQNTYFAQTL LDVVQFLNGQ EKLPLATEIV KESAVNFSGK NTLDLTDIIG QQHAKRALTI AAAGQHNLLF LGPPGTGKTM LASRLTGLLP EMTDLEAIET ASVTSLVQNE LNFHNWKQRP FRAPHHSASM PALVGGGTIP KPGEISLATN GVLFLDELPE FERKVLDALR QPLESGEIII SRANAKIQFP ARFQLVAAMN PSPTGHYTGT HNRTSPQQIM RYLNRLSGPF LDRFDLSIEV PLLPQGSLQN TGDRGETSAQ VREKVLKVRE IQMERAGKIN AYLNSKEIER DCKLNDKDAF FLEKALNKLG LSVRAYHRIL KVSRTIADLQ GEQQIFQPHL AEALGYRAMV RLLQKLSNM // ID CPDB_HAEIN Reviewed; 657 AA. AC P44764; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 119. DE RecName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; DE EC=3.1.3.6; DE EC=3.1.4.16; DE Flags: Precursor; GN Name=cpdB; OrderedLocusNames=HI_0583; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This bifunctional enzyme catalyzes two consecutive CC reactions during ribonucleic acid degradation. Converts a 2',3'- CC cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to CC the corresponding nucleoside and phosphate (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside 2',3'-cyclic phosphate + H(2)O = CC nucleoside 3'-phosphate. CC -!- CATALYTIC ACTIVITY: A 3'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase 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; L42023; AAC22242.1; -; Genomic_DNA. DR PIR; A64079; A64079. DR RefSeq; NP_438741.1; NC_000907.1. DR RefSeq; WP_005694555.1; NC_000907.1. DR ProteinModelPortal; P44764; -. DR STRING; 71421.HI0583; -. DR DNASU; 949588; -. DR EnsemblBacteria; AAC22242; AAC22242; HI_0583. DR GeneID; 949588; -. DR KEGG; hin:HI0583; -. DR PATRIC; 20189723; VBIHaeInf48452_0604. DR eggNOG; ENOG4107RNS; Bacteria. DR eggNOG; COG0737; LUCA. DR KO; K01119; -. DR OMA; MVWDKAN; -. DR OrthoDB; EOG696BW0; -. DR PhylomeDB; P44764; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0008254; F:3'-nucleotidase 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:0009166; P:nucleotide catabolic process; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.90.780.10; -; 1. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR006146; 5'-Nucleotdase_CS. DR InterPro; IPR006179; 5_nucleotidase/apyrase. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR006294; Cyc_nuc_PDE_nucleotidase. DR InterPro; IPR029052; Metallo-depent_PP-like. DR PANTHER; PTHR11575; PTHR11575; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR SUPFAM; SSF55816; SSF55816; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR01390; CycNucDiestase; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Periplasm; Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 657 2',3'-cyclic-nucleotide 2'- FT phosphodiesterase/3'-nucleotidase. FT /FTId=PRO_0000000037. FT REGION 554 559 Substrate binding. {ECO:0000250}. FT METAL 41 41 Divalent metal cation 1. {ECO:0000250}. FT METAL 43 43 Divalent metal cation 1. {ECO:0000250}. FT METAL 86 86 Divalent metal cation 1. {ECO:0000250}. FT METAL 86 86 Divalent metal cation 2. {ECO:0000250}. FT METAL 126 126 Divalent metal cation 2. {ECO:0000250}. FT METAL 235 235 Divalent metal cation 2. {ECO:0000250}. FT METAL 267 267 Divalent metal cation 2. {ECO:0000250}. FT METAL 269 269 Divalent metal cation 1. {ECO:0000250}. FT BINDING 450 450 Substrate. {ECO:0000250}. SQ SEQUENCE 657 AA; 72763 MW; 201CAAB415014499 CRC64; MMNRRHFIQI SATSILALSA NRFAMAKGKS DVDLRIVATT DVHSFLTDFD YYKDAPTDKF GFTRAASLIR QARAEVKNSV LVDNGDLIQG NPIADYQAAQ GYKEGKSNPA IDCLNAMNYE VGTLGNHEFN YGLNYLADAI KQAKFPIVNS NVVKAGTEEP YFTPYVIQEK SVVDNQGKTH KLKIGYIGFV PPQIMVWDKA NLQGKVETRD IVKTAQKYVP EMKKKGADIV VALAHTGPSD EPYQEGAENS AFYLADVPHI DAVIFGHSHR LFPNKEFAKS PNADIVNGTV KGIPESMAGY WANNISVVDL GLTEHKGKWI VTSGKAVLRP IYDIETKKAL AKNDPEITAL LKPVHEATRK YVSQPIGKAT DNMYSYLALL QDDPTIQIVN QAQKAYVEKV APSIAAMAGL PILSAGAPFK AGGRKNDPTG YTEVNKGKLT FRNAADLYLY PNTLVVVKAT GEQLKEWLEC SAGMFKQIDP TSDKPQSLID WEGFRTYNFD VIDGVNYEYD LTKPARYDGE CKLINPESHR VVNLTYQGKP VDPKAEFLIA TNNYRAYGNK FPGTGDKHIV YASPDESRQI LADYIKATSE KEGSVNPNAD KNWRFVPITG NDKLDVRFET SPSEQAAKFI AEKAQYPMKQ VGTDEIGFAV YQIDLSK // ID COMA_HAEIN Reviewed; 265 AA. AC P31768; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Competence protein A; DE AltName: Full=DNA transformation protein ComA; GN Name=comA; OrderedLocusNames=HI_0439; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25008.1; -; Genomic_DNA. DR EMBL; L42023; AAC22098.1; -; Genomic_DNA. DR PIR; C64068; JH0430. DR RefSeq; NP_438600.1; NC_000907.1. DR RefSeq; WP_005693722.1; NC_000907.1. DR STRING; 71421.HI0439; -. DR EnsemblBacteria; AAC22098; AAC22098; HI_0439. DR GeneID; 949534; -. DR KEGG; hin:HI0439; -. DR PATRIC; 20189431; VBIHaeInf48452_0459. DR OMA; FQPFKIN; -. DR OrthoDB; EOG6RRKM5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. PE 4: Predicted; KW Competence; Complete proteome; Reference proteome. FT CHAIN 1 265 Competence protein A. FT /FTId=PRO_0000090003. SQ SEQUENCE 265 AA; 31542 MW; EC1E167D659A8759 CRC64; MQFSLKNYRT LQIGIHRKQS YFDFVWFDDL EQPQSYQIFV NDRYFKNRFL QQLKTQYQGK TFPLQFVASI PAHLTWSKVL MLPQVLNAQE CHQQCKFVIE KELPIFLEEL WFDYRSTPLK QGFRLEVTAI RKSSAQTYLQ DFQPFNINIL DVASNAVLRA FQYLLNEQVR SENTLFLFQE DDYCLAICER SQQSQILQSH ENLTALYEQF TERFEGQLEQ VFVYQIPSSH TPLPENWQRV ETELPFIALG NALWQKDLHQ QKVGG // ID COAD_HAEIN Reviewed; 156 AA. AC P44805; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151}; DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; Synonyms=kdtB; GN OrderedLocusNames=HI_0651; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC {ECO:0000255|HAMAP-Rule:MF_00151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22310.1; -; Genomic_DNA. DR PIR; E64084; E64084. DR RefSeq; NP_438811.1; NC_000907.1. DR RefSeq; WP_005694492.1; NC_000907.1. DR ProteinModelPortal; P44805; -. DR SMR; P44805; 3-156. DR STRING; 71421.HI0651; -. DR EnsemblBacteria; AAC22310; AAC22310; HI_0651. DR GeneID; 949693; -. DR KEGG; hin:HI0651; -. DR PATRIC; 20189917; VBIHaeInf48452_0680. DR eggNOG; ENOG4108ZEF; Bacteria. DR eggNOG; COG0669; LUCA. DR KO; K00954; -. DR OMA; YELQIAH; -. DR OrthoDB; EOG6MH5J7; -. DR PhylomeDB; P44805; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 156 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_0000156215. SQ SEQUENCE 156 AA; 17316 MW; 1E3F6BC291617C51 CRC64; MTSVIYPGTF DPITNGHLDI IERSAVIFPR VLVAVANSPS KKPLFSLEER VELVRQSVVH LSNVEVFGFS DLLANVIKQH NISAIIRGVR TTTDFEYELQ LAALNRLLTK GVDSLFFPPA EKWAFVSSTI VREIYLHGGD VAELVPVPVF NALKAR // ID COME_HAEIN Reviewed; 445 AA. AC P31772; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 115. DE RecName: Full=Competence protein E; DE AltName: Full=DNA transformation protein ComE; DE Flags: Precursor; GN Name=comE; OrderedLocusNames=HI_0435; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-445. RX PubMed=1856167; RA Larson T.G., Goodgal S.H.; RT "Sequence and transcriptional regulation of com101A, a locus required RT for genetic transformation in Haemophilus influenzae."; RL J. Bacteriol. 173:4683-4691(1991). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GSP D 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; M62809; AAA25012.1; -; Genomic_DNA. DR EMBL; L42023; AAC22094.1; -; Genomic_DNA. DR EMBL; M59751; AAA24947.1; -; Genomic_DNA. DR PIR; H64067; H64067. DR RefSeq; NP_438596.1; NC_000907.1. DR RefSeq; WP_005693728.1; NC_000907.1. DR STRING; 71421.HI0435; -. DR TCDB; 1.B.22.4.1; the outer bacterial membrane secretin (secretin) family. DR EnsemblBacteria; AAC22094; AAC22094; HI_0435. DR GeneID; 950687; -. DR KEGG; hin:HI0435; -. DR PATRIC; 20189423; VBIHaeInf48452_0455. DR eggNOG; ENOG4105E4G; Bacteria. DR eggNOG; COG4796; LUCA. DR KO; K02507; -. DR OMA; TDNERFF; -. DR OrthoDB; EOG6423BN; -. DR PhylomeDB; P31772; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0009297; P:pilus assembly; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR001775; GspD/PilQ. DR InterPro; IPR005644; NolW-like. DR InterPro; IPR013355; Pilus_4_PilQ. DR InterPro; IPR004846; T2SS/T3SS. DR InterPro; IPR004845; T2SS_GspD_CS. DR Pfam; PF00263; Secretin; 1. DR Pfam; PF03958; Secretin_N; 1. DR PRINTS; PR00811; BCTERIALGSPD. DR TIGRFAMs; TIGR02515; IV_pilus_PilQ; 1. DR PROSITE; PS00875; T2SP_D; 1. PE 3: Inferred from homology; KW Cell outer membrane; Competence; Complete proteome; Membrane; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 445 Competence protein E. FT /FTId=PRO_0000013121. FT CONFLICT 433 443 TLEALKQKSEG -> NVRGVET (in Ref. 1; FT AAA25012). {ECO:0000305}. SQ SEQUENCE 445 AA; 49208 MW; 0901DA0D3D42D0E2 CRC64; MKKYFLKCGY FLVCFCLPLI VFANPKTDNE RFFIRLSQAP LAQTLEQLAF QQDVNLVIGD ILENKISLKL NNIDMPRLLQ IIAKSKHLTL NKDDGIYYLN GSQSGKGQVA GNLTTNEPHL VSHTVKLHFA KASELMKSLT TGSGSLLSPA GSITFDDRSN LLVIQDEPRS VQNIKKLIAE MDKPIEQIAI EARIVTITDE SLKELGVRWG IFNPTENARR VAGSLTGNSF ENIADNLNVN FATTTTPAGS IALQVAKING RLLDLELSAL ERENNVEIIA SPRLLTTNKK SASIKQGTEI PYIVSNTRND TQSVEFREAV LGLEVTPHIS KDNNILLDLL VSQNSPGSRV AYGQNEVVSI DKQEINTQVF AKDGETIVLG GVFHDTITKS EDKVPLLGDI PVIKRLFSKE SERHQKRELV IFVTPHILKA GETLEALKQK SEGKK // ID CRP_HAEIN Reviewed; 224 AA. AC P29281; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-DEC-2015, entry version 114. DE RecName: Full=cAMP-activated global transcriptional regulator CRP; DE AltName: Full=Catabolite activator protein; DE Short=CAP; DE AltName: Full=cAMP receptor protein; DE Short=CRP; DE AltName: Full=cAMP regulatory protein; GN Name=crp; Synonyms=cap; OrderedLocusNames=HI_0957; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PROBABLE AUTOREGULATION, RP AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1542653; DOI=10.1073/pnas.89.5.1626; RA Chandler M.S.; RT "The gene encoding cAMP receptor protein is required for competence RT development in Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1626-1630(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8226661; RA Dorocicz I.R., Williams P.M., Redfield R.J.; RT "The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, RT and essential role in competence."; RL J. Bacteriol. 175:7142-7149(1993). RN [4] RP FUNCTION, REGULON, AND INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15769466; DOI=10.1016/j.jmb.2005.01.012; RA Redfield R.J., Cameron A.D., Qian Q., Hinds J., Ali T.R., Kroll J.S., RA Langford P.R.; RT "A novel CRP-dependent regulon controls expression of competence genes RT in Haemophilus influenzae."; RL J. Mol. Biol. 347:735-747(2005). RN [5] RP DNA-BINDING. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=18761017; DOI=10.1016/j.jmb.2008.08.027; RA Cameron A.D., Redfield R.J.; RT "CRP binding and transcription activation at CRP-S sites."; RL J. Mol. Biol. 383:313-323(2008). CC -!- FUNCTION: A global transcription regulator required for bacterial CC competence. Complexes with cyclic AMP (cAMP) which allosterically CC activates DNA binding (to consensus sequence 5'- CC AAATGTGATCTAGATCACATTT-3') to regulate transcription at 54 CC promoters (PubMed:15769466). There are 2 consensus subclasses; CC CRP-N (above) and CRP-S (T6 changed to C and A17 changed to G) CC which obligatorily also requires Sxy for expression. CRP-S sites CC bind DNA but do not activate transcription in the absence of Sxy. CC Probably induces a severe bend in DNA. Probably acts as a negative CC regulator of its own synthesis as well as for adenylate cyclase CC (cyaA), which generates cAMP. {ECO:0000269|PubMed:1542653, CC ECO:0000269|PubMed:15769466}. CC -!- SUBUNIT: Homodimer, which upon binding cAMP is able to bind DNA CC (Probable). Binds RNA polymerase subunit RpoA (By similarity). CC {ECO:0000250, ECO:0000305}. CC -!- INDUCTION: Constitutively expressed; slightly induced on shifting CC to starvation media. {ECO:0000269|PubMed:15769466}. CC -!- DOMAIN: The N-terminal domain binds cAMP and is responsible for CC homodimerization, while the C-terminal domain binds DNA when cAMP CC is bound. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Loss of competence, the ability to bind, CC take-up and integrate exogenous DNA. Loss of the ability to CC ferment ribose or xylose. {ECO:0000269|PubMed:1542653, CC ECO:0000269|PubMed:8226661}. CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00060}. CC -!- SIMILARITY: Contains 1 HTH crp-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00387}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77207; AAA24952.1; -; Genomic_DNA. DR EMBL; L42023; AAC22618.1; -; Genomic_DNA. DR PIR; B38225; B38225. DR RefSeq; NP_439118.1; NC_000907.1. DR RefSeq; WP_005647998.1; NC_000907.1. DR ProteinModelPortal; P29281; -. DR SMR; P29281; 21-222. DR STRING; 71421.HI0957; -. DR EnsemblBacteria; AAC22618; AAC22618; HI_0957. DR GeneID; 949963; -. DR KEGG; hin:HI0957; -. DR PATRIC; 20190573; VBIHaeInf48452_0999. DR eggNOG; ENOG4107RYR; Bacteria. DR eggNOG; COG0664; LUCA. DR KO; K10914; -. DR OMA; IMARRLR; -. DR OrthoDB; EOG69GZGV; -. DR PhylomeDB; P29281; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF00325; Crp; 1. DR PRINTS; PR00034; HTHCRP. DR SMART; SM00100; cNMP; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51206; SSF51206; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS00042; HTH_CRP_1; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; cAMP; cAMP-binding; Competence; KW Complete proteome; DNA-binding; Nucleotide-binding; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 224 cAMP-activated global transcriptional FT regulator CRP. FT /FTId=PRO_0000100147. FT DOMAIN 152 224 HTH crp-type. {ECO:0000255|PROSITE- FT ProRule:PRU00387}. FT NP_BIND 71 77 cAMP 1. {ECO:0000250}. FT NP_BIND 86 88 cAMP 1. {ECO:0000250}. FT NP_BIND 97 98 cAMP 1. {ECO:0000250}. FT NP_BIND 142 143 cAMP 1. {ECO:0000250}. FT NP_BIND 150 151 cAMP 2. {ECO:0000250}. FT NP_BIND 185 195 cAMP 2. {ECO:0000250}. FT DNA_BIND 194 200 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00387}. FT REGION 34 36 Activating region 2 (AR2); probably FT contacts the N-terminus of RpoA. FT {ECO:0000250}. FT REGION 67 73 Activating region 3 (AR3); probably FT contacts sigma-70 (RpoD). {ECO:0000250}. FT REGION 168 177 Activating region 1 (AR1); probably FT contacts the C-terminus of RpoA. FT {ECO:0000250}. FT SITE 111 111 Activating region 2 (AR2); probably FT contacts the N-terminus of RpoA. FT {ECO:0000250}. FT SITE 116 116 Activating region 2 (AR2); probably FT contacts the N-terminus of RpoA. FT {ECO:0000250}. FT MOD_RES 115 115 N6-acetyllysine. {ECO:0000250}. SQ SEQUENCE 224 AA; 25152 MW; 421B7790A48FF50C CRC64; MSNELTEIDE VVTSSQEEAT QRDPVLDWFL THCHLHKYPA KSTLIHAGED ATTLYYVIKG SVMVSSKDDE GKEMILTYLG AGQFFGEAGL FDEGSKRSAW VKTKTTCEIA EISYKKYRQL IQANPEILMF LTAQLARRLQ NTSRQVTNLA FLDVAGRIAQ TLMNLAKQPE AMTHPDGMQI KITRQEIGQM VGCSRETVGR IIKMLEDQNL IHAHGKTIVV YGAR // ID CSD_HAEIN Reviewed; 437 AA. AC Q57476; O05054; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Probable cysteine desulfurase; DE EC=2.8.1.7; GN Name=csd; OrderedLocusNames=HI_1295; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22941.1; -; Genomic_DNA. DR PIR; I64114; I64114. DR RefSeq; NP_439446.2; NC_000907.1. DR ProteinModelPortal; Q57476; -. DR STRING; 71421.HI1295; -. DR EnsemblBacteria; AAC22941; AAC22941; HI_1295. DR GeneID; 950232; -. DR KEGG; hin:HI1295; -. DR PATRIC; 20191271; VBIHaeInf48452_1346. DR eggNOG; ENOG4105C9B; Bacteria. DR eggNOG; COG0520; LUCA. DR KO; K01766; -. DR OMA; HGRHDVQ; -. DR OrthoDB; EOG68DD0M; -. DR Proteomes; UP000000579; 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; IPR016454; Cysteine_dSase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF005572; NifS; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 437 Probable cysteine desulfurase. FT /FTId=PRO_0000150298. FT MOD_RES 258 258 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 437 AA; 49048 MW; 1126FEC23DE8BB9B CRC64; MIRFIFKHKK MHKPKELVFG QTIIQLNQVN GADKRKLIWL LIIKRSRQAF PYFQREDAVI YLDNAATTLK PQVLIDRTAE FYASAGSVHR SQYDAAQTVQ YEQARTQVKE WVHAEDKHAV IWTSGTTHAI NLVANGLMPQ LNAEDEILIS QADHHANFVT WHETAKKCGA KIQVLPILDN WLIDENALIS ALSEKTKLVA LNFVSNVTGT EQPIKRLIQL IRKHSNALVL VDAAQAISHI KIDLQDLDAD FLAFSAHKIY GPNGLGVLTG KLTALSQLQP LFFGGKMVDR VSNDRITFAE LPYRLEAGTP NIAGVIGFNA VLDWLQKWDF TAAEQYAISL AESVKVRLKS YENCRLFNSP QASTVVCFVF DGIDCSDLST LLSEQNIALR VGEHCAQPYL ARLGERTTLR LSFAPYNTQE DVEAFFTALD KALDLLQ // ID COMB_HAEIN Reviewed; 168 AA. AC P31769; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Competence protein B; DE AltName: Full=DNA transformation protein ComB; GN Name=comB; OrderedLocusNames=HI_0438; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25009.1; -; Genomic_DNA. DR EMBL; L42023; AAC22097.1; -; Genomic_DNA. DR PIR; B64068; JH0431. DR RefSeq; NP_438599.1; NC_000907.1. DR RefSeq; WP_005693724.1; NC_000907.1. DR STRING; 71421.HI0438; -. DR DNASU; 949525; -. DR EnsemblBacteria; AAC22097; AAC22097; HI_0438. DR GeneID; 949525; -. DR KEGG; hin:HI0438; -. DR PATRIC; 20189429; VBIHaeInf48452_0458. DR OMA; FILYLTQ; -. DR OrthoDB; EOG6BCSSZ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR InterPro; IPR016778; Competence_ComB. DR PIRSF; PIRSF020785; Competence_ComB; 1. PE 4: Predicted; KW Competence; Complete proteome; Reference proteome. FT CHAIN 1 168 Competence protein B. FT /FTId=PRO_0000090005. SQ SEQUENCE 168 AA; 19751 MW; 2B62CBE837D2EC74 CRC64; MSMNLLPWRT YQHQKRLRRL AFYIALFILL AINLMLAFSN LIEQQKQNLQ AQQKSFEQLN QQLHKTTMQI DQLRIAVKVG EVLTSIPNEQ VKKSLQQLSE LPFQQGELNK FKQDANNLSL EGNAQDQTEF ELIHQFLKKH FPNVKLSQVQ PEQDTLFFHF DVEQGAEK // ID CORC_HAEIN Reviewed; 299 AA. AC Q57368; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Magnesium and cobalt efflux protein CorC; GN Name=corC; OrderedLocusNames=HI_0301; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a role in the transport of magnesium and cobalt CC ions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UPF0053 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21966.1; -; Genomic_DNA. DR PIR; G64060; G64060. DR RefSeq; NP_438468.1; NC_000907.1. DR RefSeq; WP_005694364.1; NC_000907.1. DR ProteinModelPortal; Q57368; -. DR STRING; 71421.HI0301; -. DR EnsemblBacteria; AAC21966; AAC21966; HI_0301. DR GeneID; 949422; -. DR KEGG; hin:HI0301; -. DR PATRIC; 20189143; VBIHaeInf48452_0318. DR eggNOG; ENOG4108JU5; Bacteria. DR eggNOG; COG4535; LUCA. DR KO; K06189; -. DR OMA; IPENSAQ; -. DR OrthoDB; EOG60W7V4; -. DR PhylomeDB; Q57368; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 2. DR Pfam; PF03471; CorC_HlyC; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Cobalt; Complete proteome; Magnesium; Reference proteome; KW Repeat; Transport. FT CHAIN 1 299 Magnesium and cobalt efflux protein CorC. FT /FTId=PRO_0000088348. FT DOMAIN 73 134 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 140 197 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 299 AA; 34584 MW; 181F455BF44F0213 CRC64; MNDEQQNSNQ SENTKKPFFQ SLFGRFFQGE LKNREELVEV IRDSEQNDLI DQNTREMIEG VMEIAELRVR DIMIPRSQII FIEDQQDLNT CLNTIIESAH SRFPVIADAD DRDNIVGILH AKDLLKFLRE DAEVFDLSSL LRPVVIVPES KRVDRMLKDF RSERFHMAIV VDEFGAVSGL VTIEDILEQI VGDIEDEFDE EEIADIRQLS RHTYAVRALT DIDDFNAQFN TDFDDEEVDT IGGLIMQTFG YLPKRGEEII LKNLQFKVTS ADSRRLIQLR VTVPDEHLAE MNNVDEKSE // ID COMF_HAEIN Reviewed; 229 AA. AC P31773; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Competence protein F; DE AltName: Full=DNA transformation protein ComF; DE AltName: Full=Protein COM101A; GN Name=comF; OrderedLocusNames=HI_0434; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1856167; RA Larson T.G., Goodgal S.H.; RT "Sequence and transcriptional regulation of com101A, a locus required RT for genetic transformation in Haemophilus influenzae."; RL J. Bacteriol. 173:4683-4691(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transformation (competence for DNA uptake). CC -!- SIMILARITY: Belongs to the ComF/GntX 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; M62809; AAA25014.1; -; Genomic_DNA. DR EMBL; M59751; AAA24949.1; -; Genomic_DNA. DR EMBL; L42023; AAC22093.1; -; Genomic_DNA. DR PIR; JH0435; JH0435. DR RefSeq; NP_438595.1; NC_000907.1. DR RefSeq; WP_005693729.1; NC_000907.1. DR ProteinModelPortal; P31773; -. DR STRING; 71421.HI0434; -. DR EnsemblBacteria; AAC22093; AAC22093; HI_0434. DR GeneID; 950316; -. DR KEGG; hin:HI0434; -. DR PATRIC; 20189421; VBIHaeInf48452_0454. DR eggNOG; ENOG4105MJ2; Bacteria. DR eggNOG; COG1040; LUCA. DR OMA; LARWLGC; -. DR OrthoDB; EOG6716R8; -. DR PhylomeDB; P31773; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR InterPro; IPR005222; Competence_ComF. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR00201; comF; 1. PE 3: Inferred from homology; KW Competence; Complete proteome; Reference proteome. FT CHAIN 1 229 Competence protein F. FT /FTId=PRO_0000209456. FT COMPBIAS 9 54 Cys-rich. SQ SEQUENCE 229 AA; 26791 MW; 2F5B72B6C8C79503 CRC64; MMNFFNFRCI HCRGNLHIAK NGLCSGCQKQ IKSFPYCGHC GSELQYYAQH CGNCLKQEPS WDKMVIIGHY IEPLSILIQR FKFQNQFWID RTLARLLYLA VRDAKRTHQL KLPEAIIPVP LYHFRQWRRG YNQADLLSQQ LSRWLDIPNL NNIVKRVKHT YTQRGLSAKD RRQNLKNAFS LAVSKNEFPY RRVALVDDVI TTGSTLNEIS KLLRKLGVEE IQVWGLARA // ID CVPA_HAEIN Reviewed; 163 AA. AC P45108; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Colicin V production protein homolog; GN Name=cvpA; OrderedLocusNames=HI_1206; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli CvpA. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22860.1; -; Genomic_DNA. DR PIR; H64189; H64189. DR RefSeq; NP_439362.1; NC_000907.1. DR RefSeq; WP_005694239.1; NC_000907.1. DR STRING; 71421.HI1206; -. DR EnsemblBacteria; AAC22860; AAC22860; HI_1206. DR GeneID; 950153; -. DR KEGG; hin:HI1206; -. DR PATRIC; 20191091; VBIHaeInf48452_1258. DR eggNOG; ENOG4105E96; Bacteria. DR eggNOG; COG1286; LUCA. DR KO; K03558; -. DR OMA; QWLASGI; -. DR OrthoDB; EOG6W4609; -. DR PhylomeDB; P45108; -. DR Proteomes; UP000000579; 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:0009403; P:toxin biosynthetic process; IEA:InterPro. DR InterPro; IPR003825; Colicin-V_CvpA. DR Pfam; PF02674; Colicin_V; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 163 Colicin V production protein homolog. FT /FTId=PRO_0000079582. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. SQ SEQUENCE 163 AA; 18246 MW; BD29AF54481062A3 CRC64; MIDYIIIGII AFSILVSLLR GFVREVLSLG SWIVAFIVAS QFYPYLAAYL TQIESMYIRN GTAIAILFVL TLIVGAIVNY VISQLVDKTG LSGTDRVLGA AFGLVRGALI VAALLFFMDT FTNFEQTDWW KESQLIPHFG FIIEWFFQQL QASSSFLTPT LNQ // ID CPDA_HAEIN Reviewed; 274 AA. AC P44685; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000255|HAMAP-Rule:MF_00905}; DE Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_00905}; DE Short=cAMP phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_00905}; DE EC=3.1.4.53 {ECO:0000255|HAMAP-Rule:MF_00905}; GN Name=cpdA {ECO:0000255|HAMAP-Rule:MF_00905}; Synonyms=icc; GN OrderedLocusNames=HI_0399; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9721275; RA Macfadyen L.P., Ma C., Redfield R.J.; RT "A 3',5' cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and RT optimizes competence in Haemophilus influenzae Rd."; RL J. Bacteriol. 180:4401-4405(1998). CC -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory CC role in modulating the intracellular concentration of cAMP, CC thereby influencing cAMP-dependent processes. May coordinate CC responses to nutritional stress, ensuring optimal competence CC development. {ECO:0000255|HAMAP-Rule:MF_00905, CC ECO:0000269|PubMed:9721275}. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O = CC adenosine 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00905}. CC -!- COFACTOR: CC Name=a metal cation; Xref=ChEBI:CHEBI:25213; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00905}; CC Note=Binds 2 metal cations per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00905}; CC -!- DISRUPTION PHENOTYPE: Mutants show increased levels of cellular CC cAMP. {ECO:0000269|PubMed:9721275}. CC -!- SIMILARITY: Belongs to the cAMP phosphodiesterase class-III CC family. {ECO:0000255|HAMAP-Rule:MF_00905}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22058.1; -; Genomic_DNA. DR PIR; E64065; E64065. DR RefSeq; NP_438561.1; NC_000907.1. DR RefSeq; WP_005693770.1; NC_000907.1. DR ProteinModelPortal; P44685; -. DR STRING; 71421.HI0399; -. DR DNASU; 949501; -. DR EnsemblBacteria; AAC22058; AAC22058; HI_0399. DR GeneID; 949501; -. DR KEGG; hin:HI0399; -. DR PATRIC; 20189349; VBIHaeInf48452_0418. DR eggNOG; ENOG41070EG; Bacteria. DR eggNOG; COG1409; LUCA. DR KO; K03651; -. DR OMA; DPHLFKD; -. DR OrthoDB; EOG6QG8GQ; -. DR PhylomeDB; P44685; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042545; P:cell wall modification; IBA:GO_Central. DR Gene3D; 3.60.21.10; -; 1. DR HAMAP; MF_00905; cAMP_phophodiest_CpdA; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR026575; cAMP_Pdiest_CpdA. DR InterPro; IPR013622; CpdA_C. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR ProDom; PD587589; Calcineurin-like_phos_C; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 3: Inferred from homology; KW cAMP; Complete proteome; Hydrolase; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 274 3',5'-cyclic adenosine monophosphate FT phosphodiesterase CpdA. FT /FTId=PRO_0000084148. FT NP_BIND 93 94 cAMP. {ECO:0000255|HAMAP-Rule:MF_00905}. FT METAL 21 21 Metal cation 1. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 23 23 Metal cation 1. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 63 63 Metal cation 1. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 63 63 Metal cation 2. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 93 93 Metal cation 2. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 163 163 Metal cation 2. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 202 202 Metal cation 2. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT METAL 204 204 Metal cation 1. {ECO:0000255|HAMAP- FT Rule:MF_00905}. FT BINDING 23 23 cAMP. {ECO:0000255|HAMAP-Rule:MF_00905}. FT BINDING 63 63 cAMP. {ECO:0000255|HAMAP-Rule:MF_00905}. FT BINDING 204 204 cAMP. {ECO:0000255|HAMAP-Rule:MF_00905}. SQ SEQUENCE 274 AA; 31556 MW; A810BF2072CA4957 CRC64; MKNTFVYQAE KPVIKLLQIT DPHLFKDESA ELLGVNTQAS FAQVLKEIQQ ENNEFDVILA TGDLVQDSSD EGYIRFVEMM KPFNKPVFWI PGNHDFQPKM AEFLNQPPMN AAKHLLLGEH WQALLLDSQV YGVPHGQLSQ HQLDLLKETL GKNPERYTLV VLHHHLLPTN SAWLDQHNLR NSHELAEVLA PFTNVKAILY GHIHQEVNSE WNGYQVMATP ATCIQFKPDC QYFSLDTLQP GWREIELHSD GSIRTEVKRI QQAEFFPNMQ EEGY // ID CSPD_HAEIN Reviewed; 72 AA. AC P46449; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Cold shock-like protein CspD; GN Name=cspD; OrderedLocusNames=HI_1434.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 CSD (cold-shock) domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23082.1; -; Genomic_DNA. DR RefSeq; NP_439584.1; NC_000907.1. DR RefSeq; WP_005652728.1; NC_000907.1. DR ProteinModelPortal; P46449; -. DR STRING; 71421.HI1434.1; -. DR EnsemblBacteria; AAC23082; AAC23082; HI_1434.1. DR GeneID; 949903; -. DR KEGG; hin:HI1434.1; -. DR PATRIC; 20191565; VBIHaeInf48452_1492. DR eggNOG; ENOG4105VEQ; Bacteria. DR eggNOG; COG1278; LUCA. DR KO; K03704; -. DR OMA; QFDVHEG; -. DR OrthoDB; EOG618R0J; -. DR PhylomeDB; P46449; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR019844; Cold-shock_CS. DR InterPro; IPR012156; Cold_shock_CspA. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR002059; CSP_DNA-bd. DR InterPro; IPR012751; CspD. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF00313; CSD; 1. DR PIRSF; PIRSF002599; Cold_shock_A; 1. DR PRINTS; PR00050; COLDSHOCK. DR SMART; SM00357; CSP; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR02381; cspD; 1. DR PROSITE; PS00352; COLD_SHOCK; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome. FT CHAIN 1 72 Cold shock-like protein CspD. FT /FTId=PRO_0000100252. FT DOMAIN 4 64 CSD. SQ SEQUENCE 72 AA; 7958 MW; EB5C68C8FE0DDB08 CRC64; MEIGIVKWFN NAKGFGFISA EGVDADIFAH YSVIEMDGYR SLKAGQKVQF EVLHSDKGSH ATKIIPIADT QE // ID CPXR_HAEIN Reviewed; 227 AA. AC P44895; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 108. DE RecName: Full=Transcriptional regulatory protein CpxR homolog; GN Name=cpxR; OrderedLocusNames=HI_0837; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Member of a two-component regulatory system. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- PTM: Phosphorylated. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 OmpR/PhoB-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01091}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22495.1; -; Genomic_DNA. DR PIR; C64159; C64159. DR RefSeq; NP_438997.1; NC_000907.1. DR RefSeq; WP_005693189.1; NC_000907.1. DR ProteinModelPortal; P44895; -. DR STRING; 71421.HI0837; -. DR EnsemblBacteria; AAC22495; AAC22495; HI_0837. DR GeneID; 949851; -. DR KEGG; hin:HI0837; -. DR PATRIC; 20190329; VBIHaeInf48452_0878. DR eggNOG; ENOG4105E3W; Bacteria. DR eggNOG; COG0745; LUCA. DR KO; K07662; -. DR OMA; LWDEAKH; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P44895; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Two-component regulatory system. FT CHAIN 1 227 Transcriptional regulatory protein CpxR FT homolog. FT /FTId=PRO_0000081081. FT DOMAIN 3 115 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DNA_BIND 128 227 OmpR/PhoB-type. {ECO:0000255|PROSITE- FT ProRule:PRU01091}. FT MOD_RES 51 51 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 227 AA; 25727 MW; F8A8C632170C001F CRC64; MSKLLLVDDD IELTELLSTL LELEGFDVET ANNGLEALQK LNESYKLVLL DVMMPKLNGI ETLKEIRKVS NVPVMMLTAR GEDIDRVLGL ELGADDCLPK PFNDRELIAR IKAILRRSAS PSNNISNVEI LSFDGITLHF SHGIATYNEE NLNLTDYEFK ILCLLLKSKG NVVSREELSL EVMEKPLTPF DRSLDMHISN LRRKLPKRKN KPSWFKTLRG KGYALVT // ID CRCB_HAEIN Reviewed; 160 AA. AC P46491; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN Name=crcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=HI_0597.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Important for reducing fluoride concentration in the CC cell, thus reducing its toxicity. {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SIMILARITY: Belongs to the CrcB (TC 9.B.71) family. CC {ECO:0000255|HAMAP-Rule:MF_00454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22255.1; -; Genomic_DNA. DR RefSeq; NP_438755.1; NC_000907.1. DR RefSeq; WP_010869016.1; NC_000907.1. DR STRING; 71421.HI0597.1; -. DR EnsemblBacteria; AAC22255; AAC22255; HI_0597.1. DR GeneID; 949807; -. DR KEGG; hin:HI0597.1; -. DR PATRIC; 20189753; VBIHaeInf48452_0619. DR eggNOG; ENOG4107Z6W; Bacteria. DR eggNOG; COG0239; LUCA. DR KO; K06199; -. DR OMA; IPWGTLA; -. DR OrthoDB; EOG6091KP; -. DR PhylomeDB; P46491; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00454; CrcB; 1. DR InterPro; IPR003691; CrcB. DR Pfam; PF02537; CRCB; 1. DR TIGRFAMs; TIGR00494; crcB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 160 Putative fluoride ion transporter CrcB. FT /FTId=PRO_0000110108. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 34 54 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 99 119 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. SQ SEQUENCE 160 AA; 18285 MW; D8A7EC5652C1D96A CRC64; MQALLFISYG AILGASLRWA IGLLFNPLFS SFAFGTLIAN LFGCLIIGVL LGLFWQFPQI SAEWRLFLIT GFLGSLTTFS SFSSEVVELF FNDKWLNGFC VLMMHLFGCL AMTVLGIWIY KICLNFYLNP IHFGFAQLNQ QIHRYEIRVI AYIAKFFVSF // ID CYAY_HAEIN Reviewed; 101 AA. AC P71358; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Protein CyaY; GN Name=cyaY; OrderedLocusNames=HI_0727.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the frataxin 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; L42023; AAC22386.1; -; Genomic_DNA. DR RefSeq; NP_438886.1; NC_000907.1. DR RefSeq; WP_005655473.1; NC_000907.1. DR ProteinModelPortal; P71358; -. DR STRING; 71421.HI0727.1; -. DR EnsemblBacteria; AAC22386; AAC22386; HI_0727.1. DR GeneID; 949756; -. DR KEGG; hin:HI0727.1; -. DR PATRIC; 20190091; VBIHaeInf48452_0761. DR eggNOG; ENOG4105XQ6; Bacteria. DR eggNOG; COG1965; LUCA. DR KO; K06202; -. DR OMA; VVNKQEP; -. DR OrthoDB; EOG6GXTXM; -. DR PhylomeDB; P71358; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR Gene3D; 3.30.920.10; -; 1. DR HAMAP; MF_00142; CyaY; 1. DR InterPro; IPR002908; Frataxin/CyaY. DR InterPro; IPR020895; Frataxin_CS. DR PANTHER; PTHR16821; PTHR16821; 1. DR Pfam; PF01491; Frataxin_Cyay; 1. DR SMART; SM01219; Frataxin_Cyay; 1. DR SUPFAM; SSF55387; SSF55387; 1. DR TIGRFAMs; TIGR03421; FeS_CyaY; 1. DR PROSITE; PS01344; FRATAXIN_1; 1. DR PROSITE; PS50810; FRATAXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 101 Protein CyaY. FT /FTId=PRO_0000193941. SQ SEQUENCE 101 AA; 11653 MW; 982E5615BCE7FFC0 CRC64; MNIAEFHQNI EQVWQKIEEE LENQGADVDC ETQGSVFTIT FDNRTQIVIN KQEPLLELWI ASKLGGFHFA FKNGDWVSND GQRFWDCFVE ACAAHGENVQ F // ID CYDC_HAEIN Reviewed; 576 AA. AC P45081; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=ATP-binding/permease protein CydC; GN Name=cydC; OrderedLocusNames=HI_1156; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Somehow involved in the cytochrome D branch of aerobic CC respiration. Seems to be a component of a transport system (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine CC exporter (TC 3.A.1.129.1) family. {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; L42023; AAC22811.1; -; Genomic_DNA. DR PIR; E64186; E64186. DR RefSeq; NP_439314.1; NC_000907.1. DR RefSeq; WP_005693471.1; NC_000907.1. DR ProteinModelPortal; P45081; -. DR STRING; 71421.HI1156; -. DR EnsemblBacteria; AAC22811; AAC22811; HI_1156. DR GeneID; 949498; -. DR KEGG; hin:HI1156; -. DR PATRIC; 20190989; VBIHaeInf48452_1207. DR eggNOG; ENOG4108JJ8; Bacteria. DR eggNOG; COG4987; LUCA. DR KO; K16012; -. DR OMA; FASADKI; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45081; -. DR Proteomes; UP000000579; 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; IPR014223; ABC_CydC. 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 TIGRFAMs; TIGR02868; CydC; 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 inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 576 ATP-binding/permease protein CydC. FT /FTId=PRO_0000092242. FT TRANSMEM 16 36 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 38 58 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 133 153 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 155 175 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 244 264 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 281 301 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 18 308 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 338 574 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 372 379 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 576 AA; 64832 MW; A9ACD8B9B294B1B3 CRC64; MRTLLPFIRL FKFAKFPLIL GLVLMILGLG SSMGLLTVSG WFLAATAIAG LGTLFNFFYP SASVRGLAIG RTVMRYFEKI VTHDATFRIL SKLRVQVFEK IIPLSPAVLN RYRNSDLLNR LVSDVDTLDS LYLRLLAPFF TAVFVIIAMM IGLSFINIPL ALGLGLFLLI LLMIIPTVFY RLGQQFGERL IQARATYRTQ FLEFIQAQAE LLLFNAEDKL KEKMLVTEKT WQEDQAKEAK LSGFSTALVL FLNGLLISGM LWFASNADFG TDEYHTAYIA LFTFAALAAF EIIMPLGAAF LHIGQVIAAA ERVTEIIEQK PLVEFNGNEE FETKVRLISA KNLNFSYPEQ ETLVLKNLTL DLEQGKKIAI LGKTGSGKSS LLQLLVRNYD ANQGELLLAE KPISAYSEET LRHQICFLTQ RVHVFSDTLR QNLQFASADK ISDEQMIEML HQVGLSKLLE QEGKGLNLWL GDGGRPLSGG EQRRLGLARI LLNNASILLL DEPTEGLDRE TERQILRLIL QHAENKTLII VTHRLSSIEQ FDKICVIDNG RLIEEGDYNS LITKENGFFK RLIERV // ID CSRA_HAEIN Reviewed; 63 AA. AC P44879; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Carbon storage regulator homolog; GN Name=csrA; OrderedLocusNames=HI_0813; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could accelerate the degradation of some genes CC transcripts potentially through selective RNA binding. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CsrA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22472.1; -; Genomic_DNA. DR PIR; H64095; H64095. DR RefSeq; NP_438973.1; NC_000907.1. DR RefSeq; WP_005632782.1; NC_000907.1. DR ProteinModelPortal; P44879; -. DR SMR; P44879; 1-53. DR STRING; 71421.HI0813; -. DR DNASU; 949827; -. DR EnsemblBacteria; AAC22472; AAC22472; HI_0813. DR GeneID; 949827; -. DR KEGG; hin:HI0813; -. DR PATRIC; 20190281; VBIHaeInf48452_0854. DR eggNOG; ENOG4105VM8; Bacteria. DR eggNOG; COG1551; LUCA. DR KO; K03563; -. DR OMA; IYARIQR; -. DR OrthoDB; EOG6DC6PM; -. DR PhylomeDB; P44879; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00167; CsrA; 1. DR InterPro; IPR003751; CsrA. DR Pfam; PF02599; CsrA; 1. DR ProDom; PD009007; CsrA; 1. DR TIGRFAMs; TIGR00202; csrA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 63 Carbon storage regulator homolog. FT /FTId=PRO_0000177068. SQ SEQUENCE 63 AA; 7024 MW; FF52F5A9D7684B38 CRC64; MLILTRKVGE SVLIGDDISI TVLSVRGNQV KLGVEAPKEV SVHREEIYQR IKQTKDEPYL GSS // ID CYDD_HAEIN Reviewed; 586 AA. AC P45082; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=ATP-binding/permease protein CydD; GN Name=cydD; OrderedLocusNames=HI_1157; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Somehow involved in the cytochrome D branch of aerobic CC respiration. Seems to be a component of a transport system (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine CC exporter (TC 3.A.1.129.1) family. {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; L42023; AAC22812.1; -; Genomic_DNA. DR PIR; F64186; F64186. DR RefSeq; NP_439315.1; NC_000907.1. DR RefSeq; WP_005693472.1; NC_000907.1. DR ProteinModelPortal; P45082; -. DR STRING; 71421.HI1157; -. DR PRIDE; P45082; -. DR EnsemblBacteria; AAC22812; AAC22812; HI_1157. DR GeneID; 949785; -. DR KEGG; hin:HI1157; -. DR PATRIC; 20190991; VBIHaeInf48452_1208. DR eggNOG; ENOG4108JJ9; Bacteria. DR eggNOG; COG4988; LUCA. DR KO; K16013; -. DR OMA; LGFLPYQ; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45082; -. DR Proteomes; UP000000579; 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:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0042883; P:cysteine transport; IEA:InterPro. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR014216; ABC_transptr_CydD. 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 TIGRFAMs; TIGR02857; CydD; 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 inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 586 ATP-binding/permease protein CydD. FT /FTId=PRO_0000092245. FT TRANSMEM 28 48 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 62 82 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 146 166 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 167 187 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 250 270 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 278 298 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 24 316 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 350 581 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 383 390 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 586 AA; 65645 MW; A01E8A9920BB5966 CRC64; MNKLRQKYLQ KWLRAQQEPI KKLMRANIVL ATLSSFILVA QTYFLATLLD KLIMQNVPRD ELIPYFLGLI IGFGMRAIIL WAREKIGFQS GQLLRNHIRQ KILDKIHLVG PATINQKPAG SWASIMLEQV ENLHNFYARF LPQQSLSAIV PVVIFIAVFP LNWAAGLILM ITAPLVPLFM IIVGIAAADN SQKNMDTLSR LSAQFLDRLR GLETLRLFNR TSEQTEHIEN ATEDFRETTM DVLKLAFLSS AVLEFFTSIS IALMAVYFGF SYLGQIEFGT YNAPLTLFTG FFCLILAPEF YQPLRDLGTY YHDRAAGIGA ADAIVDFLES DYLTVHQNEK TISLESAVEI SAENLVVLST QGSALTKPLN FQIPANHNVA LVGQSGAGKT SLMNVILGFL PYEGSLKING QELRESNLAD WRKHIAWVGQ NPLLLQGTIK ENLLLGDVQA NDEEINQALM RSQAKEFTDK LGLHHEIKDG GLGISVGQAQ RLAIARALLR KGDLLLLDEP TASLDAQSEN LVLQALNEAS QHQTTLMITH RIEDLKQCDQ IFVMQRGEIV QQGKFTELQH EGFFAELLAQ RQQDIQ // ID CYOA_HAEIN Reviewed; 521 AA. AC P45021; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Probable cytochrome oxidase subunit 1; DE Short=Cytochrome oxidase subunit I; DE EC=1.10.3.-; GN OrderedLocusNames=HI_1076; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable cytochrome oxidase subunit. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC Note=May bind up to 3 heme groups per complex. {ECO:0000250}; CC -!- SUBUNIT: Heterodimer of subunits I and II. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Probable ortholog of the ancestor of E.coli CC AppC/CydA. CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1 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; L42023; AAC22732.1; -; Genomic_DNA. DR PIR; E64181; E64181. DR RefSeq; NP_439232.1; NC_000907.1. DR RefSeq; WP_010869127.1; NC_000907.1. DR STRING; 71421.HI1076; -. DR EnsemblBacteria; AAC22732; AAC22732; HI_1076. DR GeneID; 950049; -. DR KEGG; hin:HI1076; -. DR PATRIC; 20190811; VBIHaeInf48452_1118. DR eggNOG; ENOG4105C4M; Bacteria. DR eggNOG; COG1271; LUCA. DR KO; K00425; -. DR OMA; GWDRFSK; -. DR OrthoDB; EOG600DNV; -. DR PhylomeDB; P45021; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central. DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central. DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1. DR Pfam; PF01654; Cyt_bd_oxida_I; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Heme; Iron; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 521 Probable cytochrome oxidase subunit 1. FT /FTId=PRO_0000183923. FT TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 23 42 Helical. {ECO:0000255}. FT TOPO_DOM 43 94 Periplasmic. {ECO:0000255}. FT TRANSMEM 95 114 Helical. {ECO:0000255}. FT TOPO_DOM 115 129 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 130 149 Helical. {ECO:0000255}. FT TOPO_DOM 150 187 Periplasmic. {ECO:0000255}. FT TRANSMEM 188 207 Helical. {ECO:0000255}. FT TOPO_DOM 208 219 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 220 239 Helical. {ECO:0000255}. FT TOPO_DOM 240 397 Periplasmic. {ECO:0000255}. FT TRANSMEM 398 417 Helical. {ECO:0000255}. FT TOPO_DOM 418 475 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 476 495 Helical. {ECO:0000255}. FT TOPO_DOM 496 521 Periplasmic. {ECO:0000255}. FT METAL 19 19 Iron (heme 1 axial ligand). FT {ECO:0000250}. FT METAL 186 186 Iron (heme 2 axial ligand). FT {ECO:0000250}. FT METAL 398 398 Iron (heme 2 axial ligand). FT {ECO:0000250}. SQ SEQUENCE 521 AA; 58137 MW; FD444C20457D2265 CRC64; MLDVVDLSRL QFALTALYHF IFVPLTLGLS FILVIMETIY VATGKEVYKD MTKFWGKLFG INFALGVTTG IIMEFQFGTN WSYYSHYVGD IFGAPLAIEA LLAFFLESTF VGLFFFGWDR LSKGKHLLAT YCVAFGSNLS AMWILVANGW MQAPTGSEFN FETVRMEMTN FLDLWLNPVA QSKFLHTLSA GYVTGAFFVL AISSYFLLKG RDFEFAKRSF SVAATFGFIA SISVLILGDE SGYDIGKAQP VKLAAMEAEF ETHPAPAPFL PVAIPNTAEM KNDFAIEIPY LGGVIATRSI DKEIIGLKDL QALNETRVRS GIRAYELFTQ LRAEKKANGQ VNEETKAQFN EVKKDLGFGL LLKRYTNNVV DATEEQIKQA ARDTIPNVGP NFWAFRAMIA AGGLIALLTF GAFVQNLRNK VTQIPLLLKV LLWGLPLPWI AIECGWFLAE YGRQPWATYE ILPVGVSASN LSTGDLWFSI GLICALYLAF IIVEMYLMFK YARLGPSALK TGKYYFEQSA K // ID CYOB_HAEIN Reviewed; 378 AA. AC P45020; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable cytochrome oxidase subunit 2; DE EC=1.10.3.-; DE AltName: Full=Cytochrome oxidase subunit II; GN OrderedLocusNames=HI_1075; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable cytochrome oxidase subunit. CC -!- SUBUNIT: Heterodimer of subunits I and II. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Probable ortholog of the ancestor of E.coli CC AppB/CydB. CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2 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; L42023; AAC22731.1; -; Genomic_DNA. DR PIR; D64181; D64181. DR RefSeq; NP_439231.1; NC_000907.1. DR RefSeq; WP_010869126.1; NC_000907.1. DR STRING; 71421.HI1075; -. DR EnsemblBacteria; AAC22731; AAC22731; HI_1075. DR GeneID; 949877; -. DR KEGG; hin:HI1075; -. DR PATRIC; 20190809; VBIHaeInf48452_1117. DR eggNOG; ENOG4105CFY; Bacteria. DR eggNOG; COG1294; LUCA. DR KO; K00426; -. DR OMA; FLWGVAF; -. DR OrthoDB; EOG6K4031; -. DR PhylomeDB; P45020; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central. DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central. DR InterPro; IPR003317; Cyt-d_oxidase_su2. DR Pfam; PF02322; Cyt_bd_oxida_II; 1. DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1. DR TIGRFAMs; TIGR00203; cydB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Heme; Iron; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 378 Probable cytochrome oxidase subunit 2. FT /FTId=PRO_0000183929. FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 9 28 Helical. {ECO:0000255}. FT TOPO_DOM 29 79 Periplasmic. {ECO:0000255}. FT TRANSMEM 80 99 Helical. {ECO:0000255}. FT TOPO_DOM 100 122 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 123 142 Helical. {ECO:0000255}. FT TOPO_DOM 143 164 Periplasmic. {ECO:0000255}. FT TRANSMEM 165 184 Helical. {ECO:0000255}. FT TOPO_DOM 185 205 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 206 224 Helical. {ECO:0000255}. FT TOPO_DOM 225 261 Periplasmic. {ECO:0000255}. FT TRANSMEM 262 281 Helical. {ECO:0000255}. FT TOPO_DOM 282 291 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 292 311 Helical. {ECO:0000255}. FT TOPO_DOM 312 335 Periplasmic. {ECO:0000255}. FT TRANSMEM 336 355 Helical. {ECO:0000255}. FT TOPO_DOM 356 378 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 378 AA; 42067 MW; 2760245B44FE3473 CRC64; MIDYEFLRFI WWVLVIVLLI GFSVTDGFDM GVTALLPVIG KKEVERRIMI NTIAPHWDGN QVWLLTAGGA IFAAWPIVYA VSFSGFYIAL VLVLAALFLR PLGFEYRAKI DNPTWRSVWD WGLFAGGFVP ALVFGVAFGN LLQGVPFHFN ELTQVTYTGS FFELLNPFAL LCGVISLSML VTHGANWLQM KTTEALRDRA RTVSQIGSIV TLIAFVLAGV WLYSKDGYVV TSTIDHFAPS SPMNKEVAVE TGAWFRNFNE MPILWIFPAL AVVAALLNAA FSKANRCGFA FFFSALTMAG VIITAAVSMF PFVMPSSSHP EQSLLMWDST SSELTLTLML IFAVVFVVIA LAYTIWSYSK MFGRLDANFI DKNKHSLY // ID CYSQ_HAEIN Reviewed; 269 AA. AC P44332; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 16-MAR-2016, entry version 99. DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase CysQ; DE EC=3.1.3.7; DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase; DE AltName: Full=3'-phosphoadenosine 5'-phosphate phosphatase; DE Short=PAP phosphatase; DE AltName: Full=DPNPase; GN Name=cysQ; OrderedLocusNames=HI_0559; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to CC AMP. May also convert adenosine 3'-phosphate 5'-phosphosulfate CC (PAPS) to adenosine 5'-phosphosulfate (APS) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O = CC adenosine 5'-phosphate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22214.1; Type=Frameshift; Positions=5; 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; L42023; AAC22214.1; ALT_FRAME; Genomic_DNA. DR PIR; F64077; F64077. DR RefSeq; NP_438716.1; NC_000907.1. DR ProteinModelPortal; P44332; -. DR STRING; 71421.HI0559; -. DR EnsemblBacteria; AAC22214; AAC22214; HI_0559. DR GeneID; 949609; -. DR KEGG; hin:HI0559; -. DR PATRIC; 20189673; VBIHaeInf48452_0579. DR eggNOG; COG1218; LUCA. DR KO; K01082; -. DR OMA; TVNIAYI; -. DR OrthoDB; EOG6QK4W4; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. DR InterPro; IPR006240; Bisphos_bac. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR TIGRFAMs; TIGR01331; bisphos_cysQ; 1. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW Hydrolase; Magnesium; Membrane; Metal-binding; Reference proteome. FT CHAIN 1 269 3'(2'),5'-bisphosphate nucleotidase CysQ. FT /FTId=PRO_0000142549. FT REGION 91 94 Substrate binding. {ECO:0000250}. FT METAL 69 69 Magnesium 1. {ECO:0000250}. FT METAL 89 89 Magnesium 1. {ECO:0000250}. FT METAL 89 89 Magnesium 2. {ECO:0000250}. FT METAL 91 91 Magnesium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 92 92 Magnesium 2. {ECO:0000250}. FT METAL 216 216 Magnesium 2. {ECO:0000250}. FT BINDING 69 69 Substrate. {ECO:0000250}. FT BINDING 216 216 Substrate. {ECO:0000250}. SQ SEQUENCE 269 AA; 30723 MW; 52DC1BB9E0FD71DC CRC64; MLTLNEHLLN QVLLIAYQSG KHLQQFYQKQ VHVELKEDNT PVTEADLFVS QFLTEKLTAL FPNVPVLSEE NCHISFEERK NWKEYWLIDP LDGTQQFINR TDQFSVLITL VRKNKPVLSV IHAPILSTTY YAMCDFGTFK KQLDQVKKLT KNTTNFDRPL RIAVGATTSQ EKVRSILPKD FPCEFVVVGS SSLKSGLVAE GAVDCYVRLG QTGEWDTAGA EVLLGETHGA IFDSHFEPLT YNQRETLINP HFVMVGDQSF DWRSIFQFN // ID CYAA_HAEIN Reviewed; 843 AA. AC P40134; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Adenylate cyclase; DE EC=4.6.1.1; DE AltName: Full=ATP pyrophosphate-lyase; DE AltName: Full=Adenylyl cyclase; GN Name=cyaA; Synonyms=cya; OrderedLocusNames=HI_0604; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8226661; RA Dorocicz I.R., Williams P.M., Redfield R.J.; RT "The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, RT and essential role in competence."; RL J. Bacteriol. 175:7142-7149(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15769466; DOI=10.1016/j.jmb.2005.01.012; RA Redfield R.J., Cameron A.D., Qian Q., Hinds J., Ali T.R., Kroll J.S., RA Langford P.R.; RT "A novel CRP-dependent regulon controls expression of competence genes RT in Haemophilus influenzae."; RL J. Mol. Biol. 347:735-747(2005). CC -!- FUNCTION: Plays an essential role in competence development. CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Expressed during exponential growth; expression CC decreases 10-fold on shifting to starvation media. CC {ECO:0000269|PubMed:15769466}. CC -!- DISRUPTION PHENOTYPE: Loss of competence, the ability to bind, CC take-up and integrate exogenous DNA. Loss of the ability to CC ferment ribose or xylose. {ECO:0000269|PubMed:8226661}. CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L23824; AAC36855.1; -; Unassigned_DNA. DR EMBL; L42023; AAC22262.1; -; Genomic_DNA. DR PIR; A49922; A49922. DR RefSeq; NP_438762.1; NC_000907.1. DR RefSeq; WP_005694539.1; NC_000907.1. DR STRING; 71421.HI0604; -. DR EnsemblBacteria; AAC22262; AAC22262; HI_0604. DR GeneID; 950010; -. DR KEGG; hin:HI0604; -. DR PATRIC; 20189787; VBIHaeInf48452_0628. DR eggNOG; ENOG4107T0K; Bacteria. DR eggNOG; COG3072; LUCA. DR KO; K05851; -. DR OMA; DYVMSLY; -. DR OrthoDB; EOG63JR9H; -. DR PhylomeDB; P40134; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR InterPro; IPR000274; Adenylate_cyclase_1. DR InterPro; IPR024686; Adenylate_cyclase_1_CS. DR InterPro; IPR024685; Adenylate_cyclase_1_N. DR Pfam; PF12633; Adenyl_cycl_N; 1. DR Pfam; PF01295; Adenylate_cycl; 1. DR PIRSF; PIRSF001444; Adenylate_cycl; 1. DR PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1. DR PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; cAMP biosynthesis; Competence; Complete proteome; KW Cytoplasm; Lyase; Nucleotide-binding; Reference proteome. FT CHAIN 1 843 Adenylate cyclase. FT /FTId=PRO_0000195676. FT REGION 1 542 Catalytic. {ECO:0000255}. FT REGION 549 843 Regulatory. {ECO:0000255}. SQ SEQUENCE 843 AA; 97927 MW; B8C7BDFDFB07EEE7 CRC64; MECNLAQAKQ WVSALDQRRF ERALQGSGDA FQHVLAIVPL LLHLNHPQLP GYVIHAPSGI ASFLASDYQK KWLTNEYGIH YADHKPSTLK SAVNFHEVFP PILGVYVMGS FGSISQTSSS DLDTWICVRD GLSLDEYTLL TQKAKRISEW AMQFNVEINF YLMDQQRFRN EHYADPLTIE NSGSAQYMLL LDEFYRSAVR LAGKPLLWLH LWVENEKDYE KEVARLITEG EIDPNDWVDF GGLGQFSANE YFGASLWHLY KGIDSPYKSV LKILLLEAYS KEYPNTCLIA RTFKRDLLAG NTNPDHHFDP YIAILAKVTQ YLTALSEFKR LDFVHRCFYV KATEDFARYQ ANNWRIRYME ILAQEWGWSA ETVKHLNKRP FWKIKAVKEN HDNIMKFLML SYRNLVEFAR KHHIHSSVVP QDINILSRKL YTAFEELPGK VSLLNTQISH NLSEAHLTFV EVRGNKHFKD GWYLINQPIH HIMFSKERVI EYGESLNKLV SWAYFNHLLT EKTELSIFSK NVTLSTLQRF VTNLRQSFPS TIAKQPKNSD LLNQCEIRSL FIAINLTTDP TSKVEEVLTG ISSRDLFSFG SLEQSLVGSI DFTYRNVWNE IRTLHFEGQN AILLALKVLS NKIYRGVNRP DSIQVYCYSE RYRQDLRQLV MGLVNRCVSI QVGDIQQPCQ TSRLRVAGKN WQLFFEDRGI SLQEIGNESV CNEAESAVDF DEVLQTPIED GETNQESRRY PPEMDAFASE GFLQFFFEDN SDHSFNVYIL DESNHLEIYR HCDGEKDEKV REINQLYQNA KQEGDKNPYN IVQHNFNYPQ FYQLQNGKNG ISIVPFKFRQ MNK // ID CYSE_HAEIN Reviewed; 267 AA. AC P43886; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 111. DE RecName: Full=Serine acetyltransferase; DE Short=SAT; DE EC=2.3.1.30; GN Name=cysE; OrderedLocusNames=HI_0606; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-serine = CoA + O-acetyl-L- CC serine. CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L- CC cysteine from L-serine: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat 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; L42023; AAC22265.1; -; Genomic_DNA. DR PIR; G64080; G64080. DR RefSeq; NP_438764.1; NC_000907.1. DR RefSeq; WP_005694542.1; NC_000907.1. DR PDB; 1S80; X-ray; 2.70 A; A/B/C/D/E/F=2-266. DR PDB; 1SSM; X-ray; 2.15 A; A/B/C/D/E/F=1-242. DR PDB; 1SSQ; X-ray; 1.85 A; A/D=1-267. DR PDB; 1SST; X-ray; 2.00 A; A/B/C=1-267. DR PDB; 1Y7L; X-ray; 1.55 A; P=258-267. DR PDBsum; 1S80; -. DR PDBsum; 1SSM; -. DR PDBsum; 1SSQ; -. DR PDBsum; 1SST; -. DR PDBsum; 1Y7L; -. DR ProteinModelPortal; P43886; -. DR SMR; P43886; 1-240. DR STRING; 71421.HI0606; -. DR DNASU; 949654; -. DR EnsemblBacteria; AAC22265; AAC22265; HI_0606. DR GeneID; 949654; -. DR KEGG; hin:HI0606; -. DR PATRIC; 20189791; VBIHaeInf48452_0630. DR eggNOG; ENOG4105D7W; Bacteria. DR eggNOG; COG1045; LUCA. DR KO; K00640; -. DR OMA; FHALQSY; -. DR OrthoDB; EOG6HMXK6; -. DR PhylomeDB; P43886; -. DR BRENDA; 2.3.1.30; 2529. DR SABIO-RK; P43886; -. DR UniPathway; UPA00136; UER00199. DR EvolutionaryTrace; P43886; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR010493; Ser_AcTrfase_N. DR InterPro; IPR005881; Ser_O-AcTrfase. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF06426; SATase_N; 1. DR SMART; SM00971; SATase_N; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01172; cysE; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; KW Complete proteome; Cysteine biosynthesis; Cytoplasm; KW Reference proteome; Repeat; Transferase. FT CHAIN 1 267 Serine acetyltransferase. FT /FTId=PRO_0000068674. FT HELIX 3 19 {ECO:0000244|PDB:1SSQ}. FT HELIX 21 30 {ECO:0000244|PDB:1SSQ}. FT TURN 31 33 {ECO:0000244|PDB:1SSQ}. FT STRAND 34 36 {ECO:0000244|PDB:1SSQ}. FT HELIX 37 49 {ECO:0000244|PDB:1SSQ}. FT STRAND 52 54 {ECO:0000244|PDB:1SST}. FT HELIX 56 69 {ECO:0000244|PDB:1SSQ}. FT HELIX 72 87 {ECO:0000244|PDB:1SSQ}. FT HELIX 95 100 {ECO:0000244|PDB:1SSQ}. FT HELIX 102 117 {ECO:0000244|PDB:1SSQ}. FT TURN 118 120 {ECO:0000244|PDB:1SSQ}. FT HELIX 122 136 {ECO:0000244|PDB:1SSQ}. FT STRAND 137 140 {ECO:0000244|PDB:1SST}. FT STRAND 151 154 {ECO:0000244|PDB:1SSQ}. FT STRAND 158 160 {ECO:0000244|PDB:1SST}. FT STRAND 171 173 {ECO:0000244|PDB:1SST}. FT STRAND 177 179 {ECO:0000244|PDB:1SSQ}. FT STRAND 182 184 {ECO:0000244|PDB:1SSQ}. FT STRAND 185 187 {ECO:0000244|PDB:1SSM}. FT STRAND 203 207 {ECO:0000244|PDB:1SSQ}. FT STRAND 231 233 {ECO:0000244|PDB:1SSQ}. FT TURN 234 237 {ECO:0000244|PDB:1SSQ}. FT STRAND 238 240 {ECO:0000244|PDB:1SST}. FT HELIX 248 251 {ECO:0000244|PDB:1SSQ}. SQ SEQUENCE 267 AA; 29166 MW; 93428DE9D504DFB4 CRC64; MTLDVWQHIR QEAKELAENE PMLASFFHST ILKHQNLGGA LSYLLANKLA NPIMPAISLR EIIEEAYQSN PSIIDCAACD IQAVRHRDPA VELWSTPLLY LKGFHAIQSY RITHYLWNQN RKSLALYLQN QISVAFDVDI HPAAKIGHGI MFDHATGIVV GETSVIENDV SILQGVTLGG TGKESGDRHP KVREGVMIGA GAKILGNIEV GKYAKIGANS VVLNPVPEYA TAAGVPARIV SQDKAAKPAF DMNQYFIGID DGMNLNI // ID DACB_HAEIN Reviewed; 479 AA. AC P45161; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacB; DE Short=DD-carboxypeptidase; DE Short=DD-peptidase; DE EC=3.4.16.4; DE AltName: Full=D-alanyl-D-alanine endopeptidase; DE Short=DD-endopeptidase; DE EC=3.4.21.-; DE AltName: Full=Penicillin-binding protein 4; DE Short=PBP-4; DE Flags: Precursor; GN Name=dacB; OrderedLocusNames=HI_1330; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Not involved in transpeptidation but exclusively CC catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|- CC D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are CC N-acyl substituents of D-alanine. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S13 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; L42023; AAC22975.1; -; Genomic_DNA. DR PIR; A64117; A64117. DR RefSeq; NP_439482.1; NC_000907.1. DR RefSeq; WP_005694445.1; NC_000907.1. DR PDB; 3A3D; X-ray; 1.60 A; A/B=28-479. DR PDB; 3A3E; X-ray; 2.40 A; A/B=28-479. DR PDB; 3A3F; X-ray; 2.10 A; A/B=28-479. DR PDB; 3A3I; X-ray; 2.00 A; A/B=28-479. DR PDBsum; 3A3D; -. DR PDBsum; 3A3E; -. DR PDBsum; 3A3F; -. DR PDBsum; 3A3I; -. DR ProteinModelPortal; P45161; -. DR STRING; 71421.HI1330; -. DR MEROPS; S13.001; -. DR EnsemblBacteria; AAC22975; AAC22975; HI_1330. DR GeneID; 950252; -. DR KEGG; hin:HI1330; -. DR PATRIC; 20191345; VBIHaeInf48452_1383. DR eggNOG; ENOG4106HRJ; Bacteria. DR eggNOG; COG2027; LUCA. DR KO; K07259; -. DR OMA; AHSKPMK; -. DR OrthoDB; EOG6NGVQ4; -. DR PhylomeDB; P45161; -. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P45161; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR000667; Peptidase_S13. DR Pfam; PF02113; Peptidase_S13; 1. DR PRINTS; PR00922; DADACBPTASE3. DR SUPFAM; SSF56601; SSF56601; 1. DR TIGRFAMs; TIGR00666; PBP4; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Hydrolase; Peptidoglycan synthesis; Periplasm; Reference proteome; KW Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 479 D-alanyl-D-alanine carboxypeptidase DacB. FT /FTId=PRO_0000027242. FT ACT_SITE 69 69 Acyl-ester intermediate. {ECO:0000250}. FT ACT_SITE 72 72 Proton acceptor. {ECO:0000250}. FT ACT_SITE 310 310 {ECO:0000250}. FT BINDING 420 420 Substrate. {ECO:0000250}. FT HELIX 30 34 {ECO:0000244|PDB:3A3D}. FT STRAND 42 49 {ECO:0000244|PDB:3A3D}. FT TURN 50 53 {ECO:0000244|PDB:3A3D}. FT STRAND 54 60 {ECO:0000244|PDB:3A3D}. FT HELIX 68 71 {ECO:0000244|PDB:3A3D}. FT HELIX 72 82 {ECO:0000244|PDB:3A3D}. FT STRAND 90 97 {ECO:0000244|PDB:3A3D}. FT STRAND 108 111 {ECO:0000244|PDB:3A3D}. FT HELIX 120 132 {ECO:0000244|PDB:3A3D}. FT STRAND 142 145 {ECO:0000244|PDB:3A3D}. FT HELIX 160 162 {ECO:0000244|PDB:3A3D}. FT HELIX 166 168 {ECO:0000244|PDB:3A3D}. FT HELIX 177 179 {ECO:0000244|PDB:3A3D}. FT STRAND 180 186 {ECO:0000244|PDB:3A3D}. FT STRAND 196 198 {ECO:0000244|PDB:3A3D}. FT STRAND 206 208 {ECO:0000244|PDB:3A3D}. FT STRAND 212 214 {ECO:0000244|PDB:3A3D}. FT TURN 216 218 {ECO:0000244|PDB:3A3D}. FT HELIX 219 221 {ECO:0000244|PDB:3A3D}. FT STRAND 224 229 {ECO:0000244|PDB:3A3D}. FT TURN 230 232 {ECO:0000244|PDB:3A3D}. FT STRAND 233 241 {ECO:0000244|PDB:3A3D}. FT STRAND 247 252 {ECO:0000244|PDB:3A3D}. FT HELIX 256 270 {ECO:0000244|PDB:3A3D}. FT STRAND 289 295 {ECO:0000244|PDB:3A3D}. FT HELIX 299 309 {ECO:0000244|PDB:3A3D}. FT HELIX 312 327 {ECO:0000244|PDB:3A3D}. FT HELIX 333 346 {ECO:0000244|PDB:3A3D}. FT STRAND 359 361 {ECO:0000244|PDB:3A3D}. FT HELIX 370 382 {ECO:0000244|PDB:3A3D}. FT HELIX 384 387 {ECO:0000244|PDB:3A3D}. FT HELIX 390 392 {ECO:0000244|PDB:3A3D}. FT TURN 396 398 {ECO:0000244|PDB:3A3D}. FT HELIX 400 402 {ECO:0000244|PDB:3A3D}. FT HELIX 406 408 {ECO:0000244|PDB:3A3D}. FT TURN 411 416 {ECO:0000244|PDB:3A3D}. FT STRAND 418 424 {ECO:0000244|PDB:3A3D}. FT STRAND 427 435 {ECO:0000244|PDB:3A3D}. FT STRAND 441 450 {ECO:0000244|PDB:3A3D}. FT HELIX 463 478 {ECO:0000244|PDB:3A3D}. SQ SEQUENCE 479 AA; 52686 MW; 632868C61206CB48 CRC64; MKKLSSISTA LGSFLLSVSF SLPTFANINV SDLTQKLPEG SNVGFIAKNI NQNQIIADYN GSTFMLSAST QKVFTAVAAK LALDDQFQFE TALLSNGKIQ NGNLDGNLIV RFTGDPDLTR GQLYSLLAEL KKQGIKKING DLVLDTSVFS SHDRGLGWIW NDLTMCFNSP PAAANIDNNC FYAELDANKN PGEIVKINVP AQFPIQVFGQ VYVADSNEAP YCQLDVVVHD NNRYQVKGCL ARQYKPFGLS FAVQNTDAYA AEIIQRQLRQ LGIEFNGKVL LPQKPQQGQL LAKHLSKPLP DLLKKMMKKS DNQIADSLFR AVAFNYYKRP ASFQLGTLAV KSILQKQGIR FGNSILADGS GLSRHNLVAP KTMLSVLEYI AKNEDKLHLM ETFPIAGVDG TISGRGGLIS PPLVKNVIAK TGSLKGVYNL AGFMTNARGE KVAFVQFING YSTGDLESKT KRAPLVQFER NLYNELYKY // ID DAPB_HAEIN Reviewed; 270 AA. AC P45153; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; GN OrderedLocusNames=HI_1308; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy- CC tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6- CC dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5- CC tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC reductase (DHDPR), catalyzing the conversion of CC dihydrodipicolinate to tetrahydrodipicolinate. However, it was CC shown in E.coli that the substrate of the enzymatic reaction is CC not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy- CC 2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by CC the DapA-catalyzed reaction. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22955.1; -; Genomic_DNA. DR PIR; G64115; G64115. DR RefSeq; NP_439459.1; NC_000907.1. DR RefSeq; WP_005694461.1; NC_000907.1. DR ProteinModelPortal; P45153; -. DR SMR; P45153; 3-270. DR STRING; 71421.HI1308; -. DR EnsemblBacteria; AAC22955; AAC22955; HI_1308. DR GeneID; 950240; -. DR KEGG; hin:HI1308; -. DR PATRIC; 20191299; VBIHaeInf48452_1360. DR eggNOG; ENOG4105DUK; Bacteria. DR eggNOG; COG0289; LUCA. DR KO; K00215; -. DR OMA; EAHHRMK; -. DR OrthoDB; EOG6SV5DS; -. DR PhylomeDB; P45153; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IBA:GO_Central. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00102; DapB; 1. DR InterPro; IPR022663; DapB_C. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR022664; DapB_N_CS. DR InterPro; IPR023940; DHDPR_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR20836; PTHR20836; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF51735; SSF51735; 2. DR TIGRFAMs; TIGR00036; dapB; 1. DR PROSITE; PS01298; DAPB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 270 4-hydroxy-tetrahydrodipicolinate FT reductase. FT /FTId=PRO_0000141443. FT NP_BIND 9 14 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 99 101 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 123 126 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT REGION 166 167 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT ACT_SITE 156 156 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00102}. FT ACT_SITE 160 160 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT BINDING 35 35 NAD. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 36 36 NADP. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 157 157 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00102}. SQ SEQUENCE 270 AA; 28869 MW; D15E4C9AACB23641 CRC64; MTLKIAIAGA GGRMGCQLIQ AVHSAEGVEL GAAFERKGSS LVGTDAGELA GIGHLGVAVS DDLESQKDKF DLLIDFTRPE GTLEHIAFCV ANNKKMVIGT TGFDENGKVA IKAASDKIAI VFASNFSVGV NLVFKLLEKA AKVMGDYCDI EVIEAHHRHK VDAPSGTALS MGEHIAKTLG RDLKTHGVFC REGITGERKR DEIGFSTIRA SDVVGEHSVW FADIGERVEI SHKASSRMTF ANGAVRAGKW LENKANGLFD MTDVLDLNNL // ID DAPE_HAEIN Reviewed; 377 AA. AC P44514; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Succinyl-diaminopimelate desuccinylase; DE Short=SDAP desuccinylase; DE EC=3.5.1.18; DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase; GN Name=dapE; OrderedLocusNames=HI_0102; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 1-10, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND ENZYME REGULATION. RX PubMed=9671518; DOI=10.1021/bi9806807; RA Born T.L., Zheng R., Blanchard J.S.; RT "Hydrolysis of N-succinyl-L,L-diaminopimelic acid by the Haemophilus RT influenzae dapE-encoded desuccinylase: metal activation, solvent RT isotope effects, and kinetic mechanism."; RL Biochemistry 37:10478-10487(1998). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE RP SPECIFICITY, AND COFACTOR. RX PubMed=12962500; DOI=10.1021/bi034845+; RA Bienvenue D.L., Gilner D.M., Davis R.S., Bennett B., Holz R.C.; RT "Substrate specificity, metal binding properties, and spectroscopic RT characterization of the DapE-encoded N-succinyl-L,L-diaminopimelic RT acid desuccinylase from Haemophilus influenzae."; RL Biochemistry 42:10756-10763(2003). RN [4] RP COFACTOR, AND ENZYME REGULATION. RX PubMed=14640610; DOI=10.1021/ja036650v; RA Cosper N.J., Bienvenue D.L., Shokes J.E., Gilner D.M., Tsukamoto T., RA Scott R.A., Holz R.C.; RT "The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase RT from Haemophilus influenzae is a dinuclear metallohydrolase."; RL J. Am. Chem. Soc. 125:14654-14655(2003). RN [5] RP FUNCTION, MUTAGENESIS OF GLU-134, BIOPHYSICOCHEMICAL PROPERTIES, AND RP REACTION MECHANISM. RX PubMed=16421726; DOI=10.1007/s00775-005-0071-8; RA Davis R., Bienvenue D., Swierczek S.I., Gilner D.M., Rajagopal L., RA Bennett B., Holz R.C.; RT "Kinetic and spectroscopic characterization of the E134A- and E134D- RT altered dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase RT from Haemophilus influenzae."; RL J. Biol. Inorg. Chem. 11:206-216(2006). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-67 AND HIS-349, AND RP COFACTOR. RX PubMed=18712420; DOI=10.1007/s00775-008-0418-z; RA Gillner D.M., Bienvenue D.L., Nocek B.P., Joachimiak A., Zachary V., RA Bennett B., Holz R.C.; RT "The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase RT from Haemophilus influenzae contains two active-site histidine RT residues."; RL J. Biol. Inorg. Chem. 14:1-10(2009). RN [7] RP ENZYME REGULATION. RX PubMed=21577314; DOI=10.1155/2011/306465; RA Uda N.R., Creus M.; RT "Selectivity of inhibition of N-succinyl-L,L-diaminopimelic acid RT desuccinylase in bacteria: The product of dapE-gene is not the target RT of L-captopril antimicrobial activity."; RL Bioinorg. Chem. Appl. 2011:306465-306465(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS, RP COFACTOR, REACTION MECHANISM, ACTIVE SITE, AND SUBUNIT. RX PubMed=20138056; DOI=10.1016/j.jmb.2010.01.062; RA Nocek B.P., Gillner D.M., Fan Y., Holz R.C., Joachimiak A.; RT "Structural basis for catalysis by the mono- and dimetalated forms of RT the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase."; RL J. Mol. Biol. 397:617-626(2010). CC -!- FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L- CC diaminopimelic acid (SDAP), forming succinate and LL-2,6- CC diaminoheptanedioate (DAP), an intermediate involved in the CC bacterial biosynthesis of lysine and meso-diaminopimelic acid, an CC essential component of bacterial cell walls. It can only hydrolyze CC L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive CC toward D,L-, L,D-, and D,D-SDAP. {ECO:0000269|PubMed:12962500, CC ECO:0000269|PubMed:16421726, ECO:0000269|PubMed:18712420}. CC -!- CATALYTIC ACTIVITY: N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O CC = succinate + LL-2,6-diaminoheptanedioate. CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:18712420}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ion per subunit.; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Note=Binds 1 Co(2+) ion per subunit.; CC -!- ENZYME REGULATION: Competitively inhibited by L,L-DAP, D,L-DAP, 2- CC carboxyethylphosphonic acid (CEPA) and 5-mercaptopentanoic acid CC (MSPA). Succinate is a poor inhibitor. CC {ECO:0000269|PubMed:14640610, ECO:0000269|PubMed:21577314, CC ECO:0000269|PubMed:9671518}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.73 mM for zinc ion (at 30 degrees Celsius and at pH 7.5) CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:16421726, CC ECO:0000269|PubMed:9671518}; CC KM=0.73 mM for L,L-SDAP (at 30 degrees Celsius and at pH 7.5) CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:16421726, CC ECO:0000269|PubMed:9671518}; CC KM=0.99 mM for cobalt ion (at 30 degrees Celsius and at pH 7.5) CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:16421726, CC ECO:0000269|PubMed:9671518}; CC KM=1.3 mM for L,L-SDAP (in the presence of Zn(2+) at 25 degrees CC Celsius and at pH 7.6) {ECO:0000269|PubMed:12962500, CC ECO:0000269|PubMed:16421726, ECO:0000269|PubMed:9671518}; CC KM=1.6 mM for L,L-SDAP (in the presence of Co(2+) at 25 degrees CC Celsius and at pH 7.6) {ECO:0000269|PubMed:12962500, CC ECO:0000269|PubMed:16421726, ECO:0000269|PubMed:9671518}; CC KM=3.2 mM for a mixture of L,L-SDAP and D,D-SDAP (in the CC presence of Zn(2+) at 25 degrees Celsius and at pH 7.6) CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:16421726, CC ECO:0000269|PubMed:9671518}; CC KM=4.7 mM for a mixture of L,L-SDAP and D,D-SDAP (in the CC presence of Co(2+) at 25 degrees Celsius and at pH 7.6) CC {ECO:0000269|PubMed:12962500, ECO:0000269|PubMed:16421726, CC ECO:0000269|PubMed:9671518}; CC pH dependence: CC Optimum pH is 7.0 in the presence of Zn(2+). The maximal CC velocities are independent of pH in the alkaline region but CC decrease below pH 7.0. {ECO:0000269|PubMed:12962500, CC ECO:0000269|PubMed:16421726, ECO:0000269|PubMed:9671518}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20138056}. CC -!- MASS SPECTROMETRY: Mass=41350; Method=Electrospray; Range=1-377; CC Evidence={ECO:0000269|PubMed:9671518}; CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE 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; L42023; AAC21776.1; -; Genomic_DNA. DR PIR; F64048; F64048. DR RefSeq; NP_438276.1; NC_000907.1. DR RefSeq; WP_005693818.1; NC_000907.1. DR PDB; 3IC1; X-ray; 2.30 A; A/B=1-377. DR PDB; 3ISZ; X-ray; 2.00 A; A/B=1-377. DR PDB; 4H2K; X-ray; 1.84 A; A/B=1-180, A/B=294-377. DR PDBsum; 3IC1; -. DR PDBsum; 3ISZ; -. DR PDBsum; 4H2K; -. DR ProteinModelPortal; P44514; -. DR SMR; P44514; 3-375. DR STRING; 71421.HI0102; -. DR BindingDB; P44514; -. DR ChEMBL; CHEMBL1075192; -. DR MEROPS; M20.010; -. DR EnsemblBacteria; AAC21776; AAC21776; HI_0102. DR GeneID; 950999; -. DR KEGG; hin:HI0102; -. DR PATRIC; 20188671; VBIHaeInf48452_0105. DR eggNOG; ENOG4105C9Y; Bacteria. DR eggNOG; COG0624; LUCA. DR KO; K01439; -. DR OMA; AGFACEH; -. DR OrthoDB; EOG60651W; -. DR PhylomeDB; P44514; -. DR BioCyc; MetaCyc:MONOMER-6421; -. DR BRENDA; 3.5.1.18; 2529. DR SABIO-RK; P44514; -. DR UniPathway; UPA00034; UER00021. DR EvolutionaryTrace; P44514; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.360; -; 1. DR HAMAP; MF_01690; DapE; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR005941; DapE_proteobac. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01246; dapE_proteo; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cobalt; Complete proteome; KW Diaminopimelate biosynthesis; Direct protein sequencing; Hydrolase; KW Lysine biosynthesis; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 377 Succinyl-diaminopimelate desuccinylase. FT /FTId=PRO_0000185262. FT ACT_SITE 69 69 {ECO:0000305|PubMed:20138056}. FT ACT_SITE 134 134 Proton acceptor. FT {ECO:0000269|PubMed:20138056}. FT METAL 67 67 Cobalt or zinc 1. FT METAL 100 100 Cobalt or zinc 1. FT METAL 100 100 Cobalt or zinc 2. FT METAL 135 135 Cobalt or zinc 2. FT METAL 163 163 Cobalt or zinc 1. FT METAL 349 349 Cobalt or zinc 2. FT MUTAGEN 67 67 H->A: Reduction of affinity for L,L-SDAP FT and of catalytic efficiency. FT {ECO:0000269|PubMed:18712420}. FT MUTAGEN 134 134 E->A: Absence of desuccinylase activity. FT {ECO:0000269|PubMed:16421726}. FT MUTAGEN 134 134 E->D: Reduction of the catalytic FT efficiency. FT {ECO:0000269|PubMed:16421726}. FT MUTAGEN 349 349 H->A: Absence of desuccinylase activity FT and of zinc ion. FT {ECO:0000269|PubMed:18712420}. FT HELIX 1 13 {ECO:0000244|PDB:4H2K}. FT HELIX 25 34 {ECO:0000244|PDB:4H2K}. FT TURN 35 37 {ECO:0000244|PDB:4H2K}. FT STRAND 39 42 {ECO:0000244|PDB:4H2K}. FT STRAND 50 55 {ECO:0000244|PDB:4H2K}. FT STRAND 57 59 {ECO:0000244|PDB:4H2K}. FT STRAND 61 67 {ECO:0000244|PDB:4H2K}. FT HELIX 76 78 {ECO:0000244|PDB:4H2K}. FT TURN 83 85 {ECO:0000244|PDB:3IC1}. FT STRAND 92 95 {ECO:0000244|PDB:4H2K}. FT TURN 96 101 {ECO:0000244|PDB:4H2K}. FT HELIX 102 118 {ECO:0000244|PDB:4H2K}. FT STRAND 123 132 {ECO:0000244|PDB:4H2K}. FT STRAND 134 136 {ECO:0000244|PDB:4H2K}. FT STRAND 139 141 {ECO:0000244|PDB:3ISZ}. FT HELIX 142 151 {ECO:0000244|PDB:4H2K}. FT STRAND 158 161 {ECO:0000244|PDB:4H2K}. FT STRAND 166 169 {ECO:0000244|PDB:4H2K}. FT STRAND 172 175 {ECO:0000244|PDB:4H2K}. FT STRAND 180 189 {ECO:0000244|PDB:3ISZ}. FT HELIX 200 202 {ECO:0000244|PDB:3ISZ}. FT HELIX 204 217 {ECO:0000244|PDB:3ISZ}. FT STRAND 225 227 {ECO:0000244|PDB:3ISZ}. FT STRAND 231 239 {ECO:0000244|PDB:3ISZ}. FT STRAND 249 259 {ECO:0000244|PDB:3ISZ}. FT HELIX 265 278 {ECO:0000244|PDB:3ISZ}. FT STRAND 283 289 {ECO:0000244|PDB:3ISZ}. FT HELIX 300 313 {ECO:0000244|PDB:4H2K}. FT STRAND 318 320 {ECO:0000244|PDB:4H2K}. FT HELIX 326 332 {ECO:0000244|PDB:4H2K}. FT TURN 333 335 {ECO:0000244|PDB:4H2K}. FT STRAND 337 340 {ECO:0000244|PDB:4H2K}. FT TURN 346 349 {ECO:0000244|PDB:4H2K}. FT STRAND 354 356 {ECO:0000244|PDB:4H2K}. FT HELIX 357 374 {ECO:0000244|PDB:4H2K}. SQ SEQUENCE 377 AA; 41353 MW; C852C7550FFD40C2 CRC64; MKEKVVSLAQ DLIRRPSISP NDEGCQQIIA ERLEKLGFQI EWMPFNDTLN LWAKHGTSEP VIAFAGHTDV VPTGDENQWS SPPFSAEIID GMLYGRGAAD MKGSLAAMIV AAEEYVKANP NHKGTIALLI TSDEEATAKD GTIHVVETLM ARDEKITYCM VGEPSSAKNL GDVVKNGRRG SITGNLYIQG IQGHVAYPHL AENPIHKAAL FLQELTTYQW DKGNEFFPPT SLQIANIHAG TGSNNVIPAE LYIQFNLRYC TEVTDEIIKQ KVAEMLEKHN LKYRIEWNLS GKPFLTKPGK LLDSITSAIE ETIGITPKAE TGGGTSDGRF IALMGAEVVE FGPLNSTIHK VNECVSVEDL GKCGEIYHKM LVNLLDS // ID DCDA_HAEIN Reviewed; 415 AA. AC P44316; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120}; DE EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120}; GN Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120}; GN OrderedLocusNames=HI_0727; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso- CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000255|HAMAP- CC Rule:MF_02120}. CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine + CC CO(2). {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02120}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22385.1; -; Genomic_DNA. DR PIR; B64089; B64089. DR RefSeq; NP_438885.1; NC_000907.1. DR RefSeq; WP_005693130.1; NC_000907.1. DR ProteinModelPortal; P44316; -. DR STRING; 71421.HI0727; -. DR EnsemblBacteria; AAC22385; AAC22385; HI_0727. DR GeneID; 949755; -. DR KEGG; hin:HI0727; -. DR PATRIC; 20190087; VBIHaeInf48452_0759. DR eggNOG; ENOG4105CU5; Bacteria. DR eggNOG; COG0019; LUCA. DR KO; K01586; -. DR OMA; LKGNKFG; -. DR OrthoDB; EOG6Z9B18; -. DR PhylomeDB; P44316; -. DR UniPathway; UPA00034; UER00027. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_02120; LysA; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR002986; DAP_deCOOHase_LysA. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01181; DAPDCRBXLASE. DR PRINTS; PR01179; ODADCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR01048; lysA; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Decarboxylase; Lyase; KW Lysine biosynthesis; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 415 Diaminopimelate decarboxylase. FT /FTId=PRO_0000149924. FT REGION 274 277 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_02120}. FT ACT_SITE 344 344 Proton donor. {ECO:0000255}. FT BINDING 239 239 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02120}. FT BINDING 277 277 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 313 313 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 317 317 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 345 345 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 372 372 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 372 372 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT MOD_RES 60 60 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_02120}. SQ SEQUENCE 415 AA; 46107 MW; 0E73AE9BA3FFE38A CRC64; MNFFQYKHNK LYAEDMPVQQ LAEQFGTPLY VYSRATLERH WHAFDSAFGN RPHLICFAVK SCSNIGVLNI MAKLGSGFDI VSQGELERVL AAGGDASKVV FSGVAKSREE IMRALEVRIR CFNVESVSEL KHINQIAGEM GKIAPISLRV NPDVDAHTHP YISTGLKENK FGVSVNEARE VYKLASTLPN IKITGMDCHI GSQLTELQPF LDATDRLIVL MEQLKEDGIT LKHLDLGGGL GVTYTDETPP HPSDYANALL EKLKNYPELE IILEPGRAIS ANAGILVAKV QYLKSNESRN FAITDTGMND MIRPALYEAY MNIVEIDRTL EREKAIYDVV GPVCETSDFL GKQRELSIAE GDYIAQCSAG AYGASMSSNY NSRARTAEVL VDGDQSYLIR RRETLQELWA LESTI // ID CYSK_HAEIN Reviewed; 316 AA. AC P45040; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 126. DE RecName: Full=Cysteine synthase; DE Short=CSase; DE EC=2.5.1.47; DE AltName: Full=O-acetylserine (thiol)-lyase; DE Short=OAS-TL; DE AltName: Full=O-acetylserine sulfhydrylase; GN Name=cysK; OrderedLocusNames=HI_1103; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SAT. RX PubMed=15838047; DOI=10.1128/JB.187.9.3201-3205.2005; RA Huang B., Vetting M.W., Roderick S.L.; RT "The active site of O-acetylserine sulfhydrylase is the anchor point RT for bienzyme complex formation with serine acetyltransferase."; RL J. Bacteriol. 187:3201-3205(2005). CC -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L- CC cysteine + acetate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L- CC cysteine from L-serine: step 2/2. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22758.1; -; Genomic_DNA. DR PIR; F64182; F64182. DR RefSeq; NP_439260.1; NC_000907.1. DR RefSeq; WP_005693427.1; NC_000907.1. DR PDB; 1Y7L; X-ray; 1.55 A; A=1-316. DR PDB; 3IQG; X-ray; 1.90 A; X=1-316. DR PDB; 3IQH; X-ray; 1.90 A; X=1-316. DR PDB; 3IQI; X-ray; 1.70 A; X=1-316. DR PDB; 4HO1; X-ray; 1.86 A; X=1-316. DR PDB; 4LI3; X-ray; 2.59 A; X=1-316. DR PDB; 4NU8; X-ray; 2.07 A; X=1-316. DR PDB; 4ORE; X-ray; 2.20 A; X=1-316. DR PDB; 4ZU1; X-ray; 2.20 A; X=1-316. DR PDB; 4ZU6; X-ray; 2.03 A; X=1-316. DR PDB; 5DBE; X-ray; 2.25 A; X=1-316. DR PDB; 5DBH; X-ray; 1.98 A; X=1-316. DR PDBsum; 1Y7L; -. DR PDBsum; 3IQG; -. DR PDBsum; 3IQH; -. DR PDBsum; 3IQI; -. DR PDBsum; 4HO1; -. DR PDBsum; 4LI3; -. DR PDBsum; 4NU8; -. DR PDBsum; 4ORE; -. DR PDBsum; 4ZU1; -. DR PDBsum; 4ZU6; -. DR PDBsum; 5DBE; -. DR PDBsum; 5DBH; -. DR ProteinModelPortal; P45040; -. DR SMR; P45040; 2-311. DR STRING; 71421.HI1103; -. DR BindingDB; P45040; -. DR ChEMBL; CHEMBL1075088; -. DR PRIDE; P45040; -. DR EnsemblBacteria; AAC22758; AAC22758; HI_1103. DR GeneID; 950077; -. DR KEGG; hin:HI1103; -. DR PATRIC; 20190873; VBIHaeInf48452_1149. DR eggNOG; ENOG4105C6T; Bacteria. DR eggNOG; COG0031; LUCA. DR KO; K01738; -. DR OMA; VKCRIGS; -. DR OrthoDB; EOG6Q2SP8; -. DR PhylomeDB; P45040; -. DR BRENDA; 2.5.1.47; 2529. DR UniPathway; UPA00136; UER00200. DR EvolutionaryTrace; P45040; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central. DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central. DR InterPro; IPR005856; Cys_synth. DR InterPro; IPR005859; CysK. DR InterPro; IPR001216; P-phosphate_BS. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01139; cysK; 1. DR TIGRFAMs; TIGR01136; cysKM; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; KW Complete proteome; Cysteine biosynthesis; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 316 Cysteine synthase. FT /FTId=PRO_0000167090. FT REGION 177 181 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 7 7 Allosteric inhibitor. {ECO:0000250}. FT BINDING 72 72 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 268 268 Allosteric inhibitor; via amide nitrogen. FT {ECO:0000250}. FT BINDING 272 272 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 42 42 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT HELIX 7 10 {ECO:0000244|PDB:1Y7L}. FT STRAND 16 18 {ECO:0000244|PDB:1Y7L}. FT STRAND 20 24 {ECO:0000244|PDB:1Y7L}. FT STRAND 28 32 {ECO:0000244|PDB:1Y7L}. FT HELIX 37 39 {ECO:0000244|PDB:1Y7L}. FT HELIX 42 55 {ECO:0000244|PDB:1Y7L}. FT STRAND 64 68 {ECO:0000244|PDB:1Y7L}. FT HELIX 72 84 {ECO:0000244|PDB:1Y7L}. FT STRAND 88 93 {ECO:0000244|PDB:1Y7L}. FT STRAND 94 97 {ECO:0000244|PDB:4ORE}. FT HELIX 98 106 {ECO:0000244|PDB:1Y7L}. FT STRAND 110 114 {ECO:0000244|PDB:1Y7L}. FT HELIX 116 118 {ECO:0000244|PDB:1Y7L}. FT HELIX 119 133 {ECO:0000244|PDB:1Y7L}. FT TURN 135 137 {ECO:0000244|PDB:1Y7L}. FT STRAND 138 140 {ECO:0000244|PDB:5DBH}. FT TURN 143 145 {ECO:0000244|PDB:1Y7L}. FT HELIX 148 155 {ECO:0000244|PDB:1Y7L}. FT HELIX 157 164 {ECO:0000244|PDB:1Y7L}. FT TURN 165 167 {ECO:0000244|PDB:1Y7L}. FT STRAND 169 175 {ECO:0000244|PDB:1Y7L}. FT STRAND 177 179 {ECO:0000244|PDB:1Y7L}. FT HELIX 180 191 {ECO:0000244|PDB:1Y7L}. FT STRAND 198 204 {ECO:0000244|PDB:1Y7L}. FT HELIX 209 215 {ECO:0000244|PDB:1Y7L}. FT HELIX 240 242 {ECO:0000244|PDB:1Y7L}. FT STRAND 245 249 {ECO:0000244|PDB:1Y7L}. FT HELIX 251 265 {ECO:0000244|PDB:1Y7L}. FT HELIX 271 284 {ECO:0000244|PDB:1Y7L}. FT HELIX 287 289 {ECO:0000244|PDB:1Y7L}. FT STRAND 293 298 {ECO:0000244|PDB:1Y7L}. FT HELIX 302 305 {ECO:0000244|PDB:3IQI}. FT TURN 308 310 {ECO:0000244|PDB:1Y7L}. SQ SEQUENCE 316 AA; 33384 MW; CA753FC79BBD05BD CRC64; MAIYADNSYS IGNTPLVRLK HFGHNGNVVV KIEGRNPSYS VKCRIGANMV WQAEKDGTLT KGKEIVDATS GNTGIALAYV AAARGYKITL TMPETMSLER KRLLCGLGVN LVLTEGAKGM KGAIAKAEEI VASDPSRYVM LKQFENPANP QIHRETTGPE IWKDTDGKVD VVVAGVGTGG SITGISRAIK LDFGKQITSV AVEPVESPVI SQTLAGEEVK PGPHKIQGIG AGFIPKNLDL SIIDRVETVD SDTALATARR LMAEEGILAG ISSGAAVAAA DRLAKLPEFA DKLIVVILPS ASERYLSTAL FEGIEG // ID CYSB_HAEIN Reviewed; 323 AA. AC P45105; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=HTH-type transcriptional regulator CysB; DE AltName: Full=Cys regulon transcriptional activator; GN Name=cysB; OrderedLocusNames=HI_1200; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is a positive regulator of gene expression CC for the cysteine regulon. The inducer for CysB is N-acetylserine CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22854.1; -; Genomic_DNA. DR PIR; E64189; E64189. DR RefSeq; NP_439356.1; NC_000907.1. DR RefSeq; WP_005667393.1; NC_000907.1. DR ProteinModelPortal; P45105; -. DR SMR; P45105; 88-323. DR STRING; 71421.HI1200; -. DR EnsemblBacteria; AAC22854; AAC22854; HI_1200. DR GeneID; 950152; -. DR KEGG; hin:HI1200; -. DR PATRIC; 20191079; VBIHaeInf48452_1252. DR eggNOG; ENOG4107R11; Bacteria. DR eggNOG; ENOG410XP61; LUCA. DR KO; K13634; -. DR OMA; QGHPLTK; -. DR OrthoDB; EOG6WQD4N; -. DR PhylomeDB; P45105; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Activator; Amino-acid biosynthesis; Complete proteome; KW Cysteine biosynthesis; Cytoplasm; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 323 HTH-type transcriptional regulator CysB. FT /FTId=PRO_0000105617. FT DOMAIN 1 60 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 19 38 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 323 AA; 36485 MW; DCFB1F1400FF9886 CRC64; MKMHQLRYIV EIVNQNLNVT EAANALYTSQ PGISKQVRLL EDELGLEIFE RHGKHIKSIT PAGKKIISIA RELLVKAQGI RAVADEYTRP NHGVLRIATT NTQARYMLPS VIERFSKKYP DVSLHIHQGS PTQIHDALMS GEVDLAITTE APYLFDDLVQ IPCYWWNRAV IVSPEHPLAK VKELTIEELG KYPLVTYTFG FTGVSDLDYA FNSAGILPNI VFTATDADVI KTYVRLGLGV GIMASMAHTA LDTDLVLIDA SHLFRPSMTN IAFKHSTFLR NYMYDFMEYF SPHLTRSVVE KAERLRDNNS VKKLFEGIEL ETK // ID DAT_HAEIN Reviewed; 454 AA. AC P44951; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase; DE EC=2.6.1.76; DE AltName: Full=Diaminobutyrate transaminase; DE AltName: Full=L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; DE Short=DABA aminotransferase; DE Short=DABA-AT; DE AltName: Full=L-diaminobutyric acid transaminase; GN Name=dat; OrderedLocusNames=HI_0949; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP CHARACTERIZATION. RX PubMed=9514614; RA Ikai H., Yamamoto S.; RT "Two genes involved in the 1,3-diaminopropane production pathway in RT Haemophilus influenzae."; RL Biol. Pharm. Bull. 21:170-173(1998). CC -!- CATALYTIC ACTIVITY: L-2,4-diaminobutanoate + 2-oxoglutarate = L- CC aspartate 4-semialdehyde + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000305}; CC -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane CC biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: CC step 1/2. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22610.1; -; Genomic_DNA. DR PIR; C64104; C64104. DR RefSeq; NP_439110.1; NC_000907.1. DR RefSeq; WP_005693298.1; NC_000907.1. DR ProteinModelPortal; P44951; -. DR STRING; 71421.HI0949; -. DR PRIDE; P44951; -. DR EnsemblBacteria; AAC22610; AAC22610; HI_0949. DR GeneID; 949951; -. DR KEGG; hin:HI0949; -. DR PATRIC; 20190557; VBIHaeInf48452_0991. DR eggNOG; ENOG4108JPW; Bacteria. DR eggNOG; COG0160; LUCA. DR KO; K00836; -. DR OMA; PRDCELA; -. DR OrthoDB; EOG6QVRHN; -. DR PhylomeDB; P44951; -. DR UniPathway; UPA00010; UER00731. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR004637; Dat. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00709; dat; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW Aminotransferase; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 454 Diaminobutyrate--2-oxoglutarate FT aminotransferase. FT /FTId=PRO_0000120515. FT MOD_RES 287 287 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255}. SQ SEQUENCE 454 AA; 49369 MW; B4B26F3AB7C55063 CRC64; MTMITPVQAI LASNQHFLDR QDVMESNVRS YPRKLPFAYA KAQGCWVTDV EGNEYLDFLA GAGTLALGHN HPILMQAIKD VLDSGLPLHT LDLTTPLKDA FSEELLSFFP KDKYILQFTG PSGADANEAA IKLAKTYTGR GNIIAFSGGF HGMTQGALAL TGNLGAKNAV ENLMPGVQFM PYPHEYRCPF GIGGEAGAKA VEQYFENFIE DVESGVVKPA AVILEAIQGE GGVVSAPISF LQKVREVTQK HGILMIVDEV QAGFCRSGRM FAFEHAGIEP DIIVMSKAVG GSLPLAVLAI RKEFDAWQPA GHTGTFRGNQ LAMATGYASL KIMRDENLAQ NAQERGEYLT NALRELSKEY PCIGNVRGRG LMMGIDIVDE RQSKDATGAY PRDCELAAAI QKACFKNKLL LERGGRGGNV VRVLCAVNIN QSECEEFIKR FKQSVVDALK VVRS // ID DACA_HAEIN Reviewed; 393 AA. AC P44466; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 122. DE RecName: Full=D-alanyl-D-alanine carboxypeptidase DacA; DE Short=DD-carboxypeptidase; DE Short=DD-peptidase; DE EC=3.4.16.4; DE AltName: Full=Penicillin-binding protein 5; DE Short=PBP-5; DE Flags: Precursor; GN Name=dacA; OrderedLocusNames=HI_0029; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide CC cell wall precursors. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|- CC D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are CC N-acyl substituents of D-alanine. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Note=N-terminal lies in CC the periplasmic space. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S11 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; L42023; AAC21707.1; -; Genomic_DNA. DR PIR; I64043; I64043. DR RefSeq; NP_438202.1; NC_000907.1. DR RefSeq; WP_005693881.1; NC_000907.1. DR PDB; 3A3J; X-ray; 2.15 A; A=30-373. DR PDBsum; 3A3J; -. DR ProteinModelPortal; P44466; -. DR SMR; P44466; 32-374. DR STRING; 71421.HI0029; -. DR EnsemblBacteria; AAC21707; AAC21707; HI_0029. DR GeneID; 950922; -. DR KEGG; hin:HI0029; -. DR PATRIC; 20188509; VBIHaeInf48452_0029. DR eggNOG; ENOG4105DZ1; Bacteria. DR eggNOG; COG1686; LUCA. DR KO; K07258; -. DR OMA; GKIHQDD; -. DR OrthoDB; EOG6RJV2H; -. DR PhylomeDB; P44466; -. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P44466; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 2.60.410.10; -; 1. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR015956; Peniciliin-bd_prot-assoc. DR InterPro; IPR018044; Peptidase_S11. DR InterPro; IPR012907; Peptidase_S11_C. DR InterPro; IPR001967; Peptidase_S11_N. DR Pfam; PF07943; PBP5_C; 1. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SMART; SM00936; PBP5_C; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR SUPFAM; SSF69189; SSF69189; 1. PE 1: Evidence at protein level; KW 3D-structure; Carboxypeptidase; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Hydrolase; Membrane; Peptidoglycan synthesis; Protease; KW Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 393 D-alanyl-D-alanine carboxypeptidase DacA. FT /FTId=PRO_0000027232. FT ACT_SITE 65 65 Acyl-ester intermediate. {ECO:0000250}. FT ACT_SITE 68 68 Proton acceptor. {ECO:0000250}. FT ACT_SITE 128 128 {ECO:0000250}. FT BINDING 231 231 Substrate. {ECO:0000250}. FT STRAND 38 45 {ECO:0000244|PDB:3A3J}. FT TURN 46 48 {ECO:0000244|PDB:3A3J}. FT STRAND 51 56 {ECO:0000244|PDB:3A3J}. FT HELIX 64 66 {ECO:0000244|PDB:3A3J}. FT HELIX 67 80 {ECO:0000244|PDB:3A3J}. FT STRAND 89 91 {ECO:0000244|PDB:3A3J}. FT TURN 94 96 {ECO:0000244|PDB:3A3J}. FT HELIX 98 100 {ECO:0000244|PDB:3A3J}. FT STRAND 114 116 {ECO:0000244|PDB:3A3J}. FT HELIX 117 127 {ECO:0000244|PDB:3A3J}. FT HELIX 130 141 {ECO:0000244|PDB:3A3J}. FT HELIX 144 157 {ECO:0000244|PDB:3A3J}. FT STRAND 166 169 {ECO:0000244|PDB:3A3J}. FT HELIX 180 193 {ECO:0000244|PDB:3A3J}. FT HELIX 195 198 {ECO:0000244|PDB:3A3J}. FT HELIX 199 202 {ECO:0000244|PDB:3A3J}. FT STRAND 205 208 {ECO:0000244|PDB:3A3J}. FT STRAND 211 214 {ECO:0000244|PDB:3A3J}. FT HELIX 218 221 {ECO:0000244|PDB:3A3J}. FT STRAND 225 235 {ECO:0000244|PDB:3A3J}. FT TURN 236 238 {ECO:0000244|PDB:3A3J}. FT STRAND 239 247 {ECO:0000244|PDB:3A3J}. FT STRAND 253 263 {ECO:0000244|PDB:3A3J}. FT HELIX 264 281 {ECO:0000244|PDB:3A3J}. FT STRAND 282 288 {ECO:0000244|PDB:3A3J}. FT STRAND 293 310 {ECO:0000244|PDB:3A3J}. FT STRAND 315 320 {ECO:0000244|PDB:3A3J}. FT TURN 324 326 {ECO:0000244|PDB:3A3J}. FT STRAND 328 340 {ECO:0000244|PDB:3A3J}. FT STRAND 347 355 {ECO:0000244|PDB:3A3J}. FT STRAND 358 367 {ECO:0000244|PDB:3A3J}. SQ SEQUENCE 393 AA; 43414 MW; 31DF0C563A833B7C CRC64; MLKRTTKIAF LSSFVALSAF SVSAEDMQFG VTPPQITAQT YVLMDYNSGA ILTALNPDQR QYPASLTKMM TSYVVGVALK QGKIHNTDMV TIGESAWGRN FPDSSKMFLD LNTQVSVADL NRGVIVVSGN DATVALAEHI SGNVPNFVET MNKYVQQFGL KNTNFTTPHG LDDPNQYSSA RDMAIIGAHI IRDLPEEYKI YSEKNFTFNK IKQANRNGLL WDKTINVDGM KTGHTSQAGY NLVASATTSN NMRLISVVMG VPTYKGREVE SKKLLQWGFA NFETFKTLEA GKEISEQRVY YGDKNSVKLG ALMDHFITIP KGKQSEVKAR YELADKNLQA PLVKGQVIGK VVYQLDGKDI ASANLQVMND VGEAGIFGKL WDWLVLTVKG LFS // ID DEOC_HAEIN Reviewed; 223 AA. AC P44430; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 118. 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=HI_1116; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22770.1; -; Genomic_DNA. DR PIR; H64183; H64183. DR RefSeq; NP_439273.1; NC_000907.1. DR RefSeq; WP_005693439.1; NC_000907.1. DR ProteinModelPortal; P44430; -. DR STRING; 71421.HI1116; -. DR EnsemblBacteria; AAC22770; AAC22770; HI_1116. DR GeneID; 950311; -. DR KEGG; hin:HI1116; -. DR PATRIC; 20190905; VBIHaeInf48452_1165. DR eggNOG; ENOG4105FCI; Bacteria. DR eggNOG; COG0274; LUCA. DR KO; K01619; -. DR OMA; FFSVCVN; -. DR OrthoDB; EOG6QZMW5; -. DR PhylomeDB; P44430; -. DR UniPathway; UPA00002; UER00468. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IBA:GO_Central. DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central. DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00114; DeoC_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase. DR InterPro; IPR028581; DeoC_typeI. DR PANTHER; PTHR10889; PTHR10889; 1. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF001357; DeoC; 1. DR SMART; SM01133; DeoC; 1. DR TIGRFAMs; TIGR00126; deoC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lyase; Reference proteome; Schiff base. FT CHAIN 1 223 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057234. FT ACT_SITE 154 154 Schiff-base intermediate with FT acetaldehyde. {ECO:0000250}. FT ACT_SITE 182 182 {ECO:0000250}. SQ SEQUENCE 223 AA; 23614 MW; F631CACB7768FE18 CRC64; MTSNQLAQYI DHTALTAEKN EQDISTLCNE AIEHGFYSVC INSAYIPLAK EKLAGSNVKI CTVVGFPLGA NLTSVKAFET QESIKAGANE IDMVINVGWI KSQKWDEVKQ DIQAVFNACN GTPLKVILET CLLTKDEIVK ACEICKEIGV AFVKTSTGFN KGGATVEDVA LMKNTVGNIG VKASGGVRDT ETALAMIKAG ATRIGASAGI AIISGTQDTQ STY // ID CYSZ_HAEIN Reviewed; 272 AA. AC P45039; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Sulfate transporter CysZ {ECO:0000255|HAMAP-Rule:MF_00468}; GN Name=cysZ {ECO:0000255|HAMAP-Rule:MF_00468}; GN OrderedLocusNames=HI_1102; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: High affinity, high specificity proton-dependent sulfate CC transporter, which mediates sulfate uptake. Provides the sulfur CC source for the cysteine synthesis pathway. {ECO:0000255|HAMAP- CC Rule:MF_00468}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00468}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00468}. CC -!- SIMILARITY: Belongs to the CysZ family. {ECO:0000255|HAMAP- CC Rule:MF_00468}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22757.1; -; Genomic_DNA. DR PIR; E64182; E64182. DR RefSeq; NP_439259.1; NC_000907.1. DR RefSeq; WP_005693426.1; NC_000907.1. DR STRING; 71421.HI1102; -. DR EnsemblBacteria; AAC22757; AAC22757; HI_1102. DR GeneID; 950075; -. DR KEGG; hin:HI1102; -. DR PATRIC; 20190871; VBIHaeInf48452_1148. DR eggNOG; ENOG4105EXN; Bacteria. DR eggNOG; COG2981; LUCA. DR KO; K06203; -. DR OMA; ATLFWVR; -. DR OrthoDB; EOG657JBT; -. DR PhylomeDB; P45039; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro. DR HAMAP; MF_00468; CysZ; 1. DR InterPro; IPR022985; Sulfate_CysZ. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cell inner membrane; Cell membrane; KW Complete proteome; Cysteine biosynthesis; Membrane; KW Reference proteome; Sulfate transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 272 Sulfate transporter CysZ. FT /FTId=PRO_0000204340. FT TRANSMEM 29 49 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00468}. FT TRANSMEM 66 86 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00468}. FT TRANSMEM 148 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00468}. FT TRANSMEM 219 239 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00468}. SQ SEQUENCE 272 AA; 31075 MW; 3CC4ECB5B5047AA3 CRC64; MLNLNELKSG FHYFVMGWHF ITQKGLRRFV IMPIVLNTVL LCGLFWLFIS QISSAIDWVM NFIPDWLSFL SVILLILSIL TILLLFYFTF TTISGFIAAP FNGLLAEKVE KMLTGENIND DGLVDIMRDV PRMLAREWQK LRYSLPKIIA LFLLSFIPLV GQTIVPVLTF LFTCWMMAIQ YCDYPFDNHK VSFDIMKNVL GNQRTQSLTF GGLVTCCTFV PVINLLIMPV AVCGATLMWV ENYRNDLGFN MNKSFSSQTG LDVRSENTGI VK // ID DAPD_HAEIN Reviewed; 275 AA. AC P45284; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE EC=2.3.1.117 {ECO:0000255|HAMAP-Rule:MF_00811}; DE AltName: Full=Tetrahydrodipicolinate N-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=THDP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=THP succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00811}; DE Short=Tetrahydropicolinate succinylase {ECO:0000255|HAMAP-Rule:MF_00811}; GN Name=dapD {ECO:0000255|HAMAP-Rule:MF_00811}; GN OrderedLocusNames=HI_1634; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine- CC 2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6- CC oxoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (succinylase route): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC {ECO:0000255|HAMAP-Rule:MF_00811}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23279.1; 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; L42023; AAC23279.1; ALT_INIT; Genomic_DNA. DR PIR; H64133; H64133. DR RefSeq; NP_439776.2; NC_000907.1. DR RefSeq; WP_005632504.1; NC_000907.1. DR ProteinModelPortal; P45284; -. DR SMR; P45284; 1-274. DR STRING; 71421.HI1634; -. DR EnsemblBacteria; AAC23279; AAC23279; HI_1634. DR GeneID; 950847; -. DR KEGG; hin:HI1634; -. DR PATRIC; 20192011; VBIHaeInf48452_1709. DR eggNOG; ENOG4105DMJ; Bacteria. DR eggNOG; COG2171; LUCA. DR KO; K00674; -. DR OMA; QVPCALI; -. DR OrthoDB; EOG68H8BV; -. DR PhylomeDB; P45284; -. DR UniPathway; UPA00034; UER00019. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008666; F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.166.10; -; 1. DR HAMAP; MF_00811; DapD; 1. DR InterPro; IPR005664; DapD_Trfase_Hexpep_rpt_fam. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR023180; THP_succinylTrfase_dom1. DR InterPro; IPR011004; Trimer_LpxA-like. DR PANTHER; PTHR19136:SF52; PTHR19136:SF52; 1. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF14602; Hexapep_2; 1. DR Pfam; PF14805; THDPS_N_2; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR00965; dapD; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Amino-acid biosynthesis; Complete proteome; KW Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; KW Reference proteome; Repeat; Transferase. FT CHAIN 1 275 2,3,4,5-tetrahydropyridine-2,6- FT dicarboxylate N-succinyltransferase. FT /FTId=PRO_0000196940. FT BINDING 104 104 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00811}. FT BINDING 141 141 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00811}. SQ SEQUENCE 275 AA; 29723 MW; 60E8BC21B4283498 CRC64; MSNLQAIIEA AFEKRAEITP KTVDAETRAA IEEVIEGLDS GKYRVAEKIA GEWVTHQWLK KAVLLSFRIN DNQIIDGAET KYYDKVALKF ADYTEERFTE EGFRVVPSAT VRKGAYISKN CVLMPSYVNI GAYVGEGTMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQANPTIIGD NCFIGARSEV VEGVIVEDGC VISMGVFIGQ STKIYDRETG EIHYGRVPAG SVVVSGSLPS KCGKYSLYCA VIVKKVDAKT LGKVGINELL RSIEE // ID DCUB_HAEIN Reviewed; 440 AA. AC P44855; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Anaerobic C4-dicarboxylate transporter DcuB; GN Name=dcuB; OrderedLocusNames=HI_0746; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for the transport of C4-dicarboxylates from CC the periplasm across the inner membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) 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; L42023; AAC22404.1; -; Genomic_DNA. DR PIR; B64090; B64090. DR RefSeq; NP_438905.1; NC_000907.1. DR RefSeq; WP_005655513.1; NC_000907.1. DR STRING; 71421.HI0746; -. DR EnsemblBacteria; AAC22404; AAC22404; HI_0746. DR GeneID; 950696; -. DR KEGG; hin:HI0746; -. DR PATRIC; 20190135; VBIHaeInf48452_0783. DR eggNOG; ENOG4105DS2; Bacteria. DR eggNOG; COG2704; LUCA. DR KO; K07792; -. DR OMA; APWTFAF; -. DR OrthoDB; EOG6FNHP5; -. DR PhylomeDB; P44855; -. DR Proteomes; UP000000579; 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:0015556; F:C4-dicarboxylate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR004668; Anaer_Dcu_memb_transpt. DR Pfam; PF03605; DcuA_DcuB; 1. DR PIRSF; PIRSF004539; C4-dicrbxl_trns; 1. DR TIGRFAMs; TIGR00770; Dcu; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 440 Anaerobic C4-dicarboxylate transporter FT DcuB. FT /FTId=PRO_0000170359. FT TRANSMEM 1 21 Helical. {ECO:0000250}. FT TOPO_DOM 22 22 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 23 41 Helical. {ECO:0000250}. FT TOPO_DOM 42 57 Periplasmic. {ECO:0000250}. FT TRANSMEM 58 75 Helical. {ECO:0000250}. FT TOPO_DOM 76 89 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 90 107 Helical. {ECO:0000250}. FT TOPO_DOM 108 136 Periplasmic. {ECO:0000250}. FT TRANSMEM 137 151 Helical. {ECO:0000250}. FT TOPO_DOM 152 236 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 237 254 Helical. {ECO:0000250}. FT TOPO_DOM 255 271 Periplasmic. {ECO:0000250}. FT TRANSMEM 272 289 Helical. {ECO:0000250}. FT TOPO_DOM 290 299 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 300 317 Helical. {ECO:0000250}. FT TOPO_DOM 318 339 Periplasmic. {ECO:0000250}. FT TRANSMEM 340 357 Helical. {ECO:0000250}. FT TOPO_DOM 358 362 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 363 380 Helical. {ECO:0000250}. FT TOPO_DOM 381 440 Periplasmic. {ECO:0000250}. SQ SEQUENCE 440 AA; 46557 MW; 84AFF11D4712F9C0 CRC64; MSAMFLLQFA IVLLCIFVGA RVGGIGLGVF GGLGLAILSF GFGLKPAGLP IDVMFMIMAV VAAAAAMQAA GGLDYMIKIA TKILRRNPKH ITFIAPAVTW LFTLLAGTGH VAYSVLPVIA EVSRQNGIRP ERPMSMAVIA SQFAIVASPI AAAVVAVVAY LEPQGIHLGD VLMVTIPSTI LGLFLACLFV NKMGKELKDD PEYQRRLNDP KYADIFASTT SVKEVEVSKT AKISVSLFLF GALLVVLMGA APSIRPVFDG KPMGMAHTIE IIMLSIGALI ILTCKPDGTA ITKGSVFHAG MRAVIAIFGI AWLGDTLMQA HITEVKEMVK GLVETAPWAF AFALFVLSVL VNSQGATVAT LFPLGIALGI PAPVLIGVFV AVNGYFFIPN YGPIIASLDF DTTGTTKIGK YILNHSFMLP GLLSMFFCLL IGLGLSHVIL // ID DDL_HAEIN Reviewed; 306 AA. AC P44405; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; Synonyms=ddlB; GN OrderedLocusNames=HI_1140; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D- CC alanyl-D-alanine. {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00047}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22795.1; -; Genomic_DNA. DR PIR; F64185; F64185. DR RefSeq; NP_439298.1; NC_000907.1. DR RefSeq; WP_005693454.1; NC_000907.1. DR ProteinModelPortal; P44405; -. DR SMR; P44405; 6-305. DR STRING; 71421.HI1140; -. DR EnsemblBacteria; AAC22795; AAC22795; HI_1140. DR GeneID; 950555; -. DR KEGG; hin:HI1140; -. DR PATRIC; 20190955; VBIHaeInf48452_1190. DR eggNOG; ENOG4105CPF; Bacteria. DR eggNOG; COG1181; LUCA. DR KO; K01921; -. DR OMA; IDRAFIV; -. DR OrthoDB; EOG6ND0KB; -. DR PhylomeDB; P44405; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 306 D-alanine--D-alanine ligase. FT /FTId=PRO_0000177827. FT DOMAIN 104 303 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00047}. FT NP_BIND 134 189 ATP. {ECO:0000255|HAMAP-Rule:MF_00047}. FT ACT_SITE 18 18 {ECO:0000250}. FT ACT_SITE 150 150 {ECO:0000250}. FT ACT_SITE 281 281 {ECO:0000250}. FT METAL 257 257 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 270 270 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 270 270 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. FT METAL 272 272 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00047}. SQ SEQUENCE 306 AA; 33491 MW; C20B30CB540E6D7A CRC64; MNLKQEKIAV LLGGTSAERE VSLNSGKAVL EALLKQGYNA HPIDPKEYNV ANLKKDGFNR AFNILHGRGG EDGTMQGLLE QIGLPYTGCG VMASALTMDK MRTKMLWKAF GLPVADMKVV TRETFSELDP QAVVAKLGLP LMVKPSLEGS SVGLTKVKAV EELKSAVEYA LKFDNTILIE EWLAGDELTV PVLDNQVLPA IRIVPEGEFY DYEAKYISDN TQYFCPAGLT PEREQALSTL VKRAYDAVGC RGWSRIDVMC DAKGNFRLVE VNTNPGMTSH SLFPKSAATV GISFEQLVVK ILELSL // ID DAPA_HAEIN Reviewed; 298 AA. AC P43797; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; GN OrderedLocusNames=HI_0255; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)- CC 4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC synthase (DHDPS), catalyzing the condensation of (S)-aspartate- CC beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate CC (DHDP). However, it was shown in E.coli that the product of the CC enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4- CC hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that CC the consecutive dehydration reaction leading to DHDP is not CC spontaneous but catalyzed by DapB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21921.1; -; Genomic_DNA. DR PIR; A64058; A64058. DR RefSeq; NP_438424.1; NC_000907.1. DR RefSeq; WP_010868967.1; NC_000907.1. DR ProteinModelPortal; P43797; -. DR SMR; P43797; 7-298. DR STRING; 71421.HI0255; -. DR EnsemblBacteria; AAC21921; AAC21921; HI_0255. DR GeneID; 949381; -. DR KEGG; hin:HI0255; -. DR PATRIC; 20189035; VBIHaeInf48452_0270. DR eggNOG; ENOG4105CDP; Bacteria. DR eggNOG; COG0329; LUCA. DR KO; K01714; -. DR OMA; GMDACVP; -. DR OrthoDB; EOG6W7235; -. DR PhylomeDB; P43797; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00418; DapA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; KW Reference proteome; Schiff base. FT CHAIN 1 298 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_0000103115. FT ACT_SITE 139 139 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT ACT_SITE 167 167 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT BINDING 51 51 Pyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00418}. FT BINDING 209 209 Pyruvate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 50 50 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 113 113 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. SQ SEQUENCE 298 AA; 32117 MW; 9BF0F9F9BDB10DCA CRC64; MSAQNSLFSG SIVALVTPMN HYGEVDFSCL EKLVEHHIEA GSNALVSVGT TGESATLSIE ENVKVIEKTV EFAKGRIPII AGAGANATSE AITMTKLLRD SGVAGCLSVV PYYNKPTQEG MYQHFKAIAE CTDLPQILYN VPSRTGSDMK PETVARLAEI ENIVGIKEAT RDVSRIVKIK QLAGKNFIVL SGDDATGLEA IKLGAEGVIS VTNNIAAKDM ADMCRYALAG DFDKAEEINA RLMRLHHDLF IESNPIPVKW AAYRLGLIKS PHLRLPLTTL SEEIQPKVGD ALKIAGLL // ID DCOR_HAEIN Reviewed; 720 AA. AC P44317; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Ornithine decarboxylase; DE EC=4.1.1.17; GN Name=speF; OrderedLocusNames=HI_0591; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I 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; L42023; AAC22248.1; -; Genomic_DNA. DR PIR; F64079; F64079. DR RefSeq; NP_438749.1; NC_000907.1. DR RefSeq; WP_010869015.1; NC_000907.1. DR ProteinModelPortal; P44317; -. DR SMR; P44317; 2-719. DR STRING; 71421.HI0591; -. DR EnsemblBacteria; AAC22248; AAC22248; HI_0591. DR GeneID; 949823; -. DR KEGG; hin:HI0591; -. DR PATRIC; 20189743; VBIHaeInf48452_0614. DR eggNOG; ENOG4105CXN; Bacteria. DR eggNOG; COG1982; LUCA. DR KO; K01581; -. DR OMA; VNHKRFN; -. DR OrthoDB; EOG696BRZ; -. DR PhylomeDB; P44317; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004586; F:ornithine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.220; -; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.100.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR027568; ODC_inducible. DR InterPro; IPR005308; OKR_de-COase_N. DR InterPro; IPR011193; Orn/lys/arg_de-COase. DR InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom. DR InterPro; IPR027464; Ornithine_deCO2ase_N. DR InterPro; IPR008286; Prn/Lys/Arg_de-COase_C. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF01276; OKR_DC_1; 1. DR Pfam; PF03711; OKR_DC_1_C; 1. DR Pfam; PF03709; OKR_DC_1_N; 1. DR PIRSF; PIRSF009393; Orn_decarb; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR SUPFAM; SSF55904; SSF55904; 1. DR TIGRFAMs; TIGR04301; ODC_inducible; 1. DR PROSITE; PS00703; OKR_DC_1; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 720 Ornithine decarboxylase. FT /FTId=PRO_0000201136. FT MOD_RES 354 354 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 720 AA; 82027 MW; 9F89EFD178752F5F CRC64; MPNLKIAYSP KVEQYFSTNR ELVEIAKTDF TDVAAIVLSS SDVGEYLDRI KATKFDVPVF IVQTDEQQVD PKFYDSIYHI QDLNGYDIKL YSRQIETAAK LYEEKMLPPF FKMLSEYVEM GNIAFDCPGH QGGQYYRKHP AGRFLYDFYG ENIFRSDICN ADVKLGDLLI HEGAACDAQK YAAQVFNADK TYFVLNGTSS SNKVALNAVL APGDLVLFDR NNHKSNHHGA LIQAGATPIY LETARNPFGF IGGIDSHCFE EDYLKSLIKE VAPEKLNQKR PFRLAVIQLG TYDGTIYNAR QVVDKIGHLC DYILFDSAWV GYEQFIPMMK DCSPLLLELN ENDPGILVTQ SVHKQQAGFS QTSQIHKKDK HIKGQDRYVN HKRFNNAFML HASTSPFYPL FATLDVNAKI QGSEAGRRLW HECVKVGIEA RKLVLNHCEL IRPFIPTTIK GKKWQDYDTE EIATNLEFFK FHPTDTWHKF EGYADEQYFV DPCKFLLTTP GISLETGEYE EFGVPATILA NYLRENGIIP EKCDLNSILF LLTPAETITK MQTLVAQIAL FEKHIKQDSL LKYVLPTVYK NNEDRYKGYT IRQLCQEMHD LYVSRNVKQL QKDLFRKATL PEYVLNPHDA NIELIRNKVE LVPLTDIVGR VAAEGALPYP PGVLCVVPGE KWSTTAHQYF LALEEGINTL PGFAPEIQGV YLQKDPDGRT RAYGYVLTDY // ID DEAD_HAEIN Reviewed; 613 AA. AC P44586; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=ATP-dependent RNA helicase DeaD {ECO:0000255|HAMAP-Rule:MF_00964}; DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00964}; DE AltName: Full=Cold-shock DEAD box protein A {ECO:0000255|HAMAP-Rule:MF_00964}; GN Name=deaD {ECO:0000255|HAMAP-Rule:MF_00964}; Synonyms=csdA; GN OrderedLocusNames=HI_0231; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DEAD-box RNA helicase involved in various cellular CC processes at low temperature, including ribosome biogenesis, mRNA CC degradation and translation initiation. {ECO:0000255|HAMAP- CC Rule:MF_00964}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00964}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00964}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DeaD CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00964}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00964}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00964}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21900.1; -; Genomic_DNA. DR PIR; F64056; F64056. DR RefSeq; NP_438403.1; NC_000907.1. DR RefSeq; WP_005694061.1; NC_000907.1. DR ProteinModelPortal; P44586; -. DR STRING; 71421.HI0231; -. DR EnsemblBacteria; AAC21900; AAC21900; HI_0231. DR GeneID; 951147; -. DR KEGG; hin:HI0231; -. DR PATRIC; 20188985; VBIHaeInf48452_0245. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR KO; K05592; -. DR OMA; LPQGMPK; -. DR OrthoDB; EOG6GBMBM; -. DR PhylomeDB; P44586; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070417; P:cellular response to cold; IEA:InterPro. DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00964; DEAD_helicase_DeaD; 1. DR InterPro; IPR005580; DbpA_RNA-bd_dom. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR028618; DEAD_helicase_DeaD. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF03880; DbpA; 1. 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; PS00039; DEAD_ATP_HELICASE; 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; Cytoplasm; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding; Stress response. FT CHAIN 1 613 ATP-dependent RNA helicase DeaD. FT /FTId=PRO_0000055104. FT DOMAIN 36 207 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00964}. FT DOMAIN 231 378 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00964}. FT NP_BIND 49 56 ATP. {ECO:0000255|HAMAP-Rule:MF_00964}. FT MOTIF 5 33 Q motif. FT MOTIF 155 158 DEAD box. SQ SEQUENCE 613 AA; 69705 MW; 1B826CBDEB1704DF CRC64; MTDKITFNDL GLPEFILKAV SDLGFETPSP IQQSCIPHLL NGNDVLGMAQ TGSGKTAAFA LPLLAQIDPS EKHPQMLVMA PTRELAIQVA DACELFVKYA QGTRIVTLYG GQRYDIQLRA LKQGAQVVVG TPGRILDHIR RGTLNLSELR FIVLDEADEM LRMGFIDDVE TVMAELPENH QTALFSATMP EPIRRITKRF MNDPQEVKIK VNNENAPDID QSCWYVHGVR KNEALLRFLE VEDFDAAIIF ARTKTGTLDI TELLEKNGFR SAALNGDMTQ QLREQTLDRL RNGSLDIVVA TDVAARGIDI ERISLVVNYD IPLDAESYVH RIGRTGRAGR SGRALLFVEP RERRLLRNIE HLMKKGINEV ELPNHLVLQE CRRKKFVAKI TKQLEHHDLE QYRSLLEDLF TADQDQENIA AAMLMLLQGK QKLILPPDPP MEKRRRERND RGDRRENPRS AERRGERKGY GNPQPMDLYR IEVGRADGVE VRHIVGAIAN EGDINSRYIG HIKLYDDYTT VELPQGMPKE LLQQFAKTRV LNKQMQMSFL GAVKSDNSRG SDDFNGKRKG RGGDFRGERG RERGNDNRGN RKFNEKSNRT FSDKPRRDRR SSF // ID DAPF_HAEIN Reviewed; 274 AA. AC P44859; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Diaminopimelate epimerase; DE Short=DAP epimerase; DE EC=5.1.1.7; DE AltName: Full=PLP-Independent Amino Acid Racemases; GN Name=dapF; OrderedLocusNames=HI_0750; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10194362; DOI=10.1021/bi982911f; RA Koo C.W., Blanchard J.S.; RT "Chemical mechanism of Haemophilus influenzae diaminopimelate RT epimerase."; RL Biochemistry 38:4416-4422(1999). RN [3] RP MUTAGENESIS OF CYS-73 AND CYS-217, ACTIVE SITE, AND ENZYME REGULATION. RX DOI=10.1021/ja001193t; RA Koo C.W., Sutherland A., Vederas J.C., Blanchard J.S.; RT "Identification of active site cysteine residues that function as RT general bases: diaminopimelate epimerase."; RL J. Am. Chem. Soc. 122:6122-6123(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS), ACTIVE SITE, DISULFIDE BOND, RP AND SUBUNIT. RX PubMed=9843410; DOI=10.1021/bi982138o; RA Cirilli M., Zheng R., Scapin G., Blanchard J.S.; RT "Structural symmetry: the three-dimensional structure of Haemophilus RT influenzae diaminopimelate epimerase."; RL Biochemistry 37:16452-16458(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND REACTION MECHANISM. RX PubMed=14747737; DOI=10.1107/S0907444903027999; RA Lloyd A.J., Huyton T., Turkenburg J., Roper D.I.; RT "Refinement of Haemophilus influenzae diaminopimelic acid epimerase RT (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol RT during catalysis."; RL Acta Crystallogr. D 60:397-400(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS, SUBSTRATE SPECIFICITY, AND ENZYME REGULATION. RX PubMed=16723397; DOI=10.1073/pnas.0602537103; RA Pillai B., Cherney M.M., Diaper C.M., Sutherland A., Blanchard J.S., RA Vederas J.C., James M.N.; RT "Structural insights into stereochemical inversion by diaminopimelate RT epimerase: an antibacterial drug target."; RL Proc. Natl. Acad. Sci. U.S.A. 103:8668-8673(2006). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT SER-73 AND SER-217 IN RP COMPLEX WITH SUBSTRATE ANALOGS, AND MUTAGENESIS OF CYS-73 AND CYS-217. RX PubMed=17889830; DOI=10.1016/j.bbrc.2007.09.012; RA Pillai B., Cherney M., Diaper C.M., Sutherland A., Blanchard J.S., RA Vederas J.C., James M.N.; RT "Dynamics of catalysis revealed from the crystal structures of mutants RT of diaminopimelate epimerase."; RL Biochem. Biophys. Res. Commun. 363:547-553(2007). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6- CC diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- CC DAP), a precursor of L-lysine and an essential component of the CC bacterial peptidoglycan. Only accepts DAP isomers with the L CC configuration. {ECO:0000269|PubMed:10194362}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000269|PubMed:10194362}. CC -!- ENZYME REGULATION: Inhibited by LL-aziridino (LL-AziDAP), DL- CC aziridino (DL-AziDAP), (2S,3R,6S)-2,6-diamino-3-fluoropimelate CC (L,L-3-fluoro-DAP) and (2R,3S,6S)-2,6-diamino-3-fluoropimelate CC (D,L-3-fluoro-DAP). {ECO:0000269|PubMed:16723397, CC ECO:0000269|Ref.3}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.7 mM for L,L-DAP (at pH 7.8) {ECO:0000269|PubMed:10194362}; CC KM=1.1 mM for D,L-DAP (at pH 7.8) {ECO:0000269|PubMed:10194362}; CC Note=Kcat is 128 and 82 (sec-1) for L,L-DAP and D,L-DAP, CC respectively.; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step CC 1/1. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16723397, CC ECO:0000269|PubMed:17889830, ECO:0000269|PubMed:9843410}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the diaminopimelate 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; L42023; AAC22409.1; -; Genomic_DNA. DR PIR; F64090; F64090. DR RefSeq; NP_438909.1; NC_000907.1. DR RefSeq; WP_005655521.1; NC_000907.1. DR PDB; 1BWZ; X-ray; 2.72 A; A=1-274. DR PDB; 1GQZ; X-ray; 1.75 A; A=1-274. DR PDB; 2GKE; X-ray; 1.35 A; A=1-274. DR PDB; 2GKJ; X-ray; 1.70 A; A=1-274. DR PDB; 2Q9H; X-ray; 2.30 A; A=1-274. DR PDB; 2Q9J; X-ray; 2.20 A; A=1-274. DR PDBsum; 1BWZ; -. DR PDBsum; 1GQZ; -. DR PDBsum; 2GKE; -. DR PDBsum; 2GKJ; -. DR PDBsum; 2Q9H; -. DR PDBsum; 2Q9J; -. DR ProteinModelPortal; P44859; -. DR SMR; P44859; 1-274. DR STRING; 71421.HI0750; -. DR EnsemblBacteria; AAC22409; AAC22409; HI_0750. DR GeneID; 949560; -. DR KEGG; hin:HI0750; -. DR PATRIC; 20190143; VBIHaeInf48452_0787. DR eggNOG; ENOG4105E4Z; Bacteria. DR eggNOG; COG0253; LUCA. DR KO; K01778; -. DR OMA; RFTKMQG; -. DR OrthoDB; EOG6ND0M5; -. DR PhylomeDB; P44859; -. DR BRENDA; 5.1.1.7; 2529. DR UniPathway; UPA00034; UER00025. DR EvolutionaryTrace; P44859; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00197; DAP_epimerase; 1. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR PANTHER; PTHR31689; PTHR31689; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR TIGRFAMs; TIGR00652; DapF; 1. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Disulfide bond; Isomerase; Lysine biosynthesis; Reference proteome. FT CHAIN 1 274 Diaminopimelate epimerase. FT /FTId=PRO_0000149842. FT REGION 8 9 Substrate. FT REGION 73 75 Substrate binding. FT REGION 208 209 Substrate binding. FT REGION 218 219 Substrate binding. FT ACT_SITE 73 73 Proton donor/acceptor. FT ACT_SITE 217 217 Proton donor/acceptor. FT BINDING 11 11 Substrate. FT BINDING 44 44 Substrate. FT BINDING 64 64 Substrate. FT BINDING 157 157 Substrate. FT BINDING 190 190 Substrate. FT SITE 159 159 Important for catalytic activity. FT {ECO:0000255}. FT SITE 208 208 Important for catalytic activity. FT {ECO:0000255}. FT DISULFID 73 217 {ECO:0000269|PubMed:9843410}. FT MUTAGEN 73 73 C->A: Inactive as epimerases, but it is FT able to rapidly catalyze the HF FT eliminatio via abstraction of the C-2 FT hydrogen of the D,L-3-fluoro-DAP analog FT and is essentially unable to catalyze the FT same elimination with the L,L-3-fluoro- FT DAP analog. {ECO:0000269|PubMed:17889830, FT ECO:0000269|Ref.3}. FT MUTAGEN 73 73 C->S: It is able to catalyze both FT epimerization of DAP and HF elimination FT of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. FT Able to slowly eliminate HF but does not FT catalyze epimerization; when associated FT with S-217. {ECO:0000269|PubMed:17889830, FT ECO:0000269|Ref.3}. FT MUTAGEN 217 217 C->A: Inactive as epimerases. It is able FT to rapidly catalyze the HF eliminatio via FT abstraction of the C-2 hydrogen of the FT L,L-3-fluoro-DAP analog and is FT essentially unable to catalyze the same FT elimination with the D,L-3-fluoro-DAP FT analog. {ECO:0000269|PubMed:17889830, FT ECO:0000269|Ref.3}. FT MUTAGEN 217 217 C->S: It is able to catalyze both FT epimerization of DAP and HF elimination FT of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. FT Able to slowly eliminate HF but does not FT catalyze epimerization; when associated FT with S-73. {ECO:0000269|PubMed:17889830, FT ECO:0000269|Ref.3}. FT STRAND 2 8 {ECO:0000244|PDB:2GKE}. FT STRAND 11 17 {ECO:0000244|PDB:2GKE}. FT STRAND 19 21 {ECO:0000244|PDB:2GKE}. FT HELIX 27 34 {ECO:0000244|PDB:2GKE}. FT TURN 36 38 {ECO:0000244|PDB:2GKE}. FT STRAND 43 49 {ECO:0000244|PDB:2GKE}. FT STRAND 56 64 {ECO:0000244|PDB:2GKE}. FT STRAND 69 71 {ECO:0000244|PDB:2GKE}. FT HELIX 74 86 {ECO:0000244|PDB:2GKE}. FT STRAND 93 98 {ECO:0000244|PDB:2GKE}. FT STRAND 103 108 {ECO:0000244|PDB:2GKE}. FT STRAND 114 117 {ECO:0000244|PDB:2GKE}. FT HELIX 125 127 {ECO:0000244|PDB:2GKE}. FT STRAND 137 142 {ECO:0000244|PDB:2GKE}. FT STRAND 147 163 {ECO:0000244|PDB:2GKE}. FT TURN 167 169 {ECO:0000244|PDB:2GKE}. FT HELIX 172 180 {ECO:0000244|PDB:2GKE}. FT STRAND 190 198 {ECO:0000244|PDB:2GKE}. FT STRAND 201 208 {ECO:0000244|PDB:2GKE}. FT TURN 209 211 {ECO:0000244|PDB:2GKE}. FT HELIX 218 230 {ECO:0000244|PDB:2GKE}. FT STRAND 236 242 {ECO:0000244|PDB:2GKE}. FT STRAND 245 251 {ECO:0000244|PDB:2GKE}. FT STRAND 258 262 {ECO:0000244|PDB:2GKE}. FT STRAND 265 271 {ECO:0000244|PDB:2GKE}. SQ SEQUENCE 274 AA; 30249 MW; 321B3CDAFFE81EDA CRC64; MQFSKMHGLG NDFVVVDGVT QNVFFTPETI RRLANRHCGI GFDQLLIVEA PYDPELDFHY RIFNADGSEV SQCGNGARCF ARFVTLKGLT NKKDISVSTQ KGNMVLTVKD DNQIRVNMGE PIWEPAKIPF TANKFEKNYI LRTDIQTVLC GAVSMGNPHC VVQVDDIQTA NVEQLGPLLE SHERFPERVN AGFMQIINKE HIKLRVYERG AGETQACGSG ACAAVAVGIM QGLLNNNVQV DLPGGSLMIE WNGVGHPLYM TGEATHIYDG FITL // ID DBH_HAEIN Reviewed; 90 AA. AC P43722; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=DNA-binding protein HU; GN Name=hup; Synonyms=hupA; OrderedLocusNames=HI_0430; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Histone-like DNA-binding protein which is capable of CC wrapping DNA to stabilize it, and thus to prevent its denaturation CC under extreme environmental conditions. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22089.1; 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; L42023; AAC22089.1; ALT_INIT; Genomic_DNA. DR PIR; E64067; E64067. DR RefSeq; NP_438591.2; NC_000907.1. DR RefSeq; WP_005630954.1; NC_000907.1. DR ProteinModelPortal; P43722; -. DR SMR; P43722; 1-90. DR STRING; 71421.HI0430; -. DR EnsemblBacteria; AAC22089; AAC22089; HI_0430. DR GeneID; 950715; -. DR KEGG; hin:HI0430; -. DR PATRIC; 20189413; VBIHaeInf48452_0450. DR eggNOG; ENOG4105K70; Bacteria. DR eggNOG; COG0776; LUCA. DR KO; K05787; -. DR OMA; MNSITYE; -. DR OrthoDB; EOG615VS6; -. DR PhylomeDB; P43722; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IBA:GO_Central. DR Gene3D; 4.10.520.10; -; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA condensation; DNA-binding; Reference proteome. FT CHAIN 1 90 DNA-binding protein HU. FT /FTId=PRO_0000104943. SQ SEQUENCE 90 AA; 9421 MW; 3815CC7DD7B7F92F CRC64; MNKTDLIDAI ANAAELNKKQ AKAALEATLD AITASLKEGE PVQLIGFGTF KVNERAARTG RNPQTGAEIQ IAASKVPAFV SGKALKDAIK // ID DDC_HAEIN Reviewed; 511 AA. AC P71362; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=L-2,4-diaminobutyrate decarboxylase; DE Short=DABA decarboxylase; DE Short=DABA-DC; DE EC=4.1.1.86; GN Name=ddc; OrderedLocusNames=HI_0946.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION. RX PubMed=9514614; RA Ikai H., Yamamoto S.; RT "Two genes involved in the 1,3-diaminopropane production pathway in RT Haemophilus influenzae."; RL Biol. Pharm. Bull. 21:170-173(1998). CC -!- CATALYTIC ACTIVITY: L-2,4-diaminobutanoate = propane-1,3-diamine + CC CO(2). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane CC biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: CC step 2/2. CC -!- SIMILARITY: Belongs to the group II decarboxylase 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; L42023; AAC22607.1; -; Genomic_DNA. DR PIR; JC5880; JC5880. DR RefSeq; NP_439107.1; NC_000907.1. DR RefSeq; WP_005693296.1; NC_000907.1. DR ProteinModelPortal; P71362; -. DR STRING; 71421.HI0946.1; -. DR EnsemblBacteria; AAC22607; AAC22607; HI_0946.1. DR GeneID; 950216; -. DR KEGG; hin:HI0946.1; -. DR PATRIC; 20190551; VBIHaeInf48452_0988. DR eggNOG; ENOG4105DY8; Bacteria. DR eggNOG; COG0076; LUCA. DR KO; K13745; -. DR OMA; KVKVICS; -. DR OrthoDB; EOG6QVRHN; -. DR PhylomeDB; P71362; -. DR UniPathway; UPA00010; UER00732. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0033983; F:diaminobutyrate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR021115; Pyridoxal-P_BS. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. PE 1: Evidence at protein level; KW Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 511 L-2,4-diaminobutyrate decarboxylase. FT /FTId=PRO_0000147004. FT MOD_RES 320 320 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 511 AA; 56638 MW; 42832FA4AC4F297A CRC64; MSNLKQHKQA LFCNDNEAIN DYETAMHNAV QAVSAWLKNE KMYTGGSIKQ MRALISGFNP TKEGMGVQKS LDHLVEIFLN PSLKVHHPHS LAHLHCPTMV TSQIAEVLIN ATNQSMDSWD QSPAGSIMEE HLINWLRQKA GYGEGTSGVF TSGGTQSNLM GVLLARDWAI ANHWKNEDGS EWSVQRDGIP AEAMQKVKVI CSENAHFSVQ KNMAMMGMGF QSVVTVPSNA NAQMDLIALK QTLAQLKADG KITACIVATA GTTDAGAIDD LKAIRKLADE YQAWLHVDAA WGGALLLSKD YRYFLDGIEL TDSITLDFHK HFFQTISCGA FLLKDPENYR FIDYKADYLN SEYDEAHGVP NLVAKSLQTT RRFDALKLWF TLEALGEDLY ASMIDHGVKL TKEVEQYIND TPDLEMLVPS QFASVLFRVV PKDYPAEFID ALNQNVADEL FARGEANIGV TKVGDKQSLK MTTLSPIATL ENVKALLTQV LTEANRIKDD IKNGTYTPPI D // ID DDH_HAEIN Reviewed; 331 AA. AC P44501; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=2-hydroxyacid dehydrogenase homolog; DE EC=1.1.1.-; GN Name=ddh; OrderedLocusNames=HI_0085; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21763.1; -; Genomic_DNA. DR PIR; F64047; F64047. DR RefSeq; NP_438258.1; NC_000907.1. DR RefSeq; WP_005693834.1; NC_000907.1. DR ProteinModelPortal; P44501; -. DR STRING; 71421.HI0085; -. DR EnsemblBacteria; AAC21763; AAC21763; HI_0085. DR GeneID; 950977; -. DR KEGG; hin:HI0085; -. DR PATRIC; 20188625; VBIHaeInf48452_0086. DR eggNOG; ENOG4105C5I; Bacteria. DR eggNOG; COG1052; LUCA. DR KO; K03778; -. DR OMA; VIVTAHQ; -. DR OrthoDB; EOG61VZ8G; -. DR PhylomeDB; P44501; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 331 2-hydroxyacid dehydrogenase homolog. FT /FTId=PRO_0000076021. FT NP_BIND 154 155 NAD. {ECO:0000250}. FT NP_BIND 232 234 NAD. {ECO:0000250}. FT NP_BIND 295 298 NAD. {ECO:0000250}. FT ACT_SITE 234 234 {ECO:0000250}. FT ACT_SITE 263 263 {ECO:0000250}. FT ACT_SITE 295 295 Proton donor. {ECO:0000250}. FT BINDING 258 258 NAD. {ECO:0000250}. SQ SEQUENCE 331 AA; 37088 MW; AB13300E94962566 CRC64; MKIAIYSTKS YDRKYIELIN AKYNFDLEFF DFMLNESTVR LAEHCEVVCI FVNDNGSRKV LEKLAALGVK IVALRCAGFN NVDLKAAQEL GIQVVRVPAY SPEAVAEHTI GLMMTLNRRI HRAYQRTREA NFSLEGLIGF NMYGRTVGVI GTGKIGIAVM RILKGFGMNI LAYDPFKNPV VEELGGQYVE LDELYAKSHV ITLHCPATPE NYHLLNCEAF AKMKDGVMIV NTSRGSLIDT QAAIDALKQR KIGALGMDVY ENERDLFFED KSNEVIQDDI FRRLSSCHNV LLTGHQAFLT EEALTNIADV TLSNIYKLKS GKVCENIVLP S // ID DEGS_HAEIN Reviewed; 340 AA. AC P44947; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 115. DE RecName: Full=Serine endoprotease DegS; DE EC=3.4.21.107; DE AltName: Full=Site-1 protease DegS; DE Short=S1P protease DegS; DE AltName: Full=Site-1-type intramembrane protease; GN Name=degS; Synonyms=hhoB, htrH; OrderedLocusNames=HI_0945; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A site-1 protease (S1P) that cleaves the peptide bond CC between 'Val-148' and 'Ser-149' in RseA. Part of a regulated CC intramembrane proteolysis (RIP) cascade. When heat shock or other CC environmental stresses disrupt protein folding in the periplasm, CC DegS senses the accumulation of unassembled outer membrane porins CC (OMP) and then initiates RseA (anti sigma-E factor) degradation by CC cleaving its periplasmic domain, making it a substrate for CC subsequent cleavage by RseP. This cascade ultimately leads to the CC sigma-E-driven expression of a variety of factors dealing with CC folding stress in the periplasm and OMP assembly. Required for CC basal and stress-induced degradation of RseA (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acts on substrates that are at least partially CC unfolded. The cleavage site P1 residue is normally between a pair CC of hydrophobic residues, such as Val-|-Val. CC -!- ENZYME REGULATION: Allosterically activated by the C-terminus of CC exposed OMP peptides (consensus Tyr-X-Phe-COOH); cleavage only CC occurs in the presence of peptides. Inhibited when RseB is bound CC to RseA. CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass membrane protein {ECO:0000305}. CC -!- DOMAIN: The PDZ domain probably binds peptides ending with C- CC terminal Tyr-X-Phe sequences, which activates proteolysis. In the CC absence of OMP peptides the PDZ domain inhibits peptidase activity CC (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs CC when an extracytoplasmic signal triggers a concerted proteolytic CC cascade to transmit information and elicit cellular responses. A CC membrane-spanning regulatory substrate protein is first cut CC extracytoplasmically (site-1 protease, S1P, this enzyme), then CC within the membrane itself (site-2 protease, S2P), while CC cytoplasmic proteases finish degrading the regulatory protein, CC liberating the effector protein (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22599.1; -; Genomic_DNA. DR PIR; I64103; I64103. DR RefSeq; NP_439105.1; NC_000907.1. DR RefSeq; WP_010869093.1; NC_000907.1. DR ProteinModelPortal; P44947; -. DR SMR; P44947; 33-339. DR STRING; 71421.HI0945; -. DR MEROPS; S01.275; -. DR EnsemblBacteria; AAC22599; AAC22599; HI_0945. DR GeneID; 949947; -. DR KEGG; hin:HI0945; -. DR PATRIC; 20190547; VBIHaeInf48452_0986. DR eggNOG; ENOG4105C0H; Bacteria. DR eggNOG; COG0265; LUCA. DR KO; K04691; -. DR OMA; VYNQAND; -. DR OrthoDB; EOG6ZPT18; -. DR PhylomeDB; P44947; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011783; Pept_S1C_DegS. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001940; Peptidase_S1C. DR Pfam; PF13180; PDZ_2; 1. DR PRINTS; PR00834; PROTEASES2C. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR TIGRFAMs; TIGR02038; protease_degS; 1. DR PROSITE; PS50106; PDZ; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Serine protease; KW Transmembrane; Transmembrane helix. FT CHAIN 1 340 Serine endoprotease DegS. FT /FTId=PRO_0000026939. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 5 24 Helical. {ECO:0000255}. FT TOPO_DOM 25 340 Periplasmic. {ECO:0000250}. FT DOMAIN 251 323 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 92 92 Charge relay system. FT {ECO:0000250|UniProtKB:P0AEE4}. FT ACT_SITE 122 122 Charge relay system. FT {ECO:0000250|UniProtKB:P0AEE4}. FT ACT_SITE 197 197 Charge relay system. FT {ECO:0000250|UniProtKB:P0AEE4}. SQ SEQUENCE 340 AA; 36039 MW; 69EA452DF5A10649 CRC64; MLKKLFHSAL WGLAAAGVIL FAVPRLNNSN IFTSDDIISF KNAVRIASPA VVNVYNRSFS SASINDNDQL QVNNLGSGVI MSKDGYILTN KHLIQNADQI VVALQNGNIF EASLVGSDDL TDLAVLKIRA DNLSTIPQNS ARQAHVGDVV LAIGNPYNLG QSVSQGIISA IGRNAVGDSV GRQNFIQTDA SINRGNSGGA LINSAGELVG ISTLSIGKTA NEIAEGLNFA IPIDIANDVL RKIMRDGRVI RGYFGVQSDI SSSSEEGIVI TDVSPNSPAA KSGIQVGDVI LKLNNQEGIS AREMMQIIAN TKPNSKVLVT ILRLGKILQI PVVIEEFPVN // ID DGAL_HAEIN Reviewed; 331 AA. AC P44883; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=D-galactose-binding periplasmic protein; DE Short=GBP; DE AltName: Full=D-galactose/ D-glucose-binding protein; DE Short=GGBP; DE Flags: Precursor; GN Name=mglB; OrderedLocusNames=HI_0822; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 25-29. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: This protein is involved in the active transport of CC galactose and glucose. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- DOMAIN: The calcium-binding site is structurally similar to that CC of EF-hand proteins, but is in two parts, with the last calcium CC ligand provided by Glu-229. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22481.1; 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; L42023; AAC22481.1; ALT_INIT; Genomic_DNA. DR PIR; G64096; G64096. DR RefSeq; NP_438982.2; NC_000907.1. DR RefSeq; WP_010869062.1; NC_000907.1. DR ProteinModelPortal; P44883; -. DR SMR; P44883; 25-331. DR STRING; 71421.HI0822; -. DR EnsemblBacteria; AAC22481; AAC22481; HI_0822. DR GeneID; 949834; -. DR KEGG; hin:HI0822; -. DR PATRIC; 20190299; VBIHaeInf48452_0863. DR eggNOG; ENOG4105EMA; Bacteria. DR eggNOG; COG1879; LUCA. DR KO; K10540; -. DR OMA; AMWDTAM; -. DR OrthoDB; EOG6G7R0P; -. DR PhylomeDB; P44883; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW Calcium; Complete proteome; Direct protein sequencing; Metal-binding; KW Periplasm; Reference proteome; Signal; Sugar transport; Transport. FT SIGNAL 1 24 {ECO:0000269|PubMed:10675023}. FT CHAIN 25 331 D-galactose-binding periplasmic protein. FT /FTId=PRO_0000031724. FT CA_BIND 158 166 First part of site. {ECO:0000250}. FT CA_BIND 228 229 Second part of site. {ECO:0000250}. SQ SEQUENCE 331 AA; 35518 MW; D4A0E639D9FD22A2 CRC64; MKKTAVLSTV AFAIALGSAS ASFAADNRIG VTIYKYDDNF MSLMRKEIDK EAKVVGGIKL LMNDSQNAQS IQNDQVDILL SKGVKALAIN LVDPAAAPTI IGKAKSDNIP VVFFNKDPGA KAIGSYEQAY YVGTDPKESG LIQGDLIAKQ WKANPALDLN KDGKIQFVLL KGEPGHPDAE VRTKYVIEEL NAKGIQTEQL FIDTGMWDAA MAKDKVDAWL SSSKANDIEV IISNNDGMAL GALEATKAHG KKLPIFGVDA LPEALQLISK GELAGTVLND SVNQGKAVVQ LSNNLAQGKS ATEGTKWELK DRVVRIPYVG VDKDNLGDFL K // ID DHE4_HAEIN Reviewed; 449 AA. AC P43793; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 98. DE RecName: Full=NADP-specific glutamate dehydrogenase; DE Short=NADP-GDH; DE EC=1.4.1.4; GN Name=gdhA; OrderedLocusNames=HI_0189; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible oxidative deamination of CC glutamate to alpha-ketoglutarate and ammonia. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate CC + NH(3) + NADPH. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21858.1; -; Genomic_DNA. DR PIR; A64053; A64053. DR RefSeq; NP_438358.1; NC_000907.1. DR RefSeq; WP_005664327.1; NC_000907.1. DR ProteinModelPortal; P43793; -. DR SMR; P43793; 6-449. DR STRING; 71421.HI0189; -. DR PRIDE; P43793; -. DR EnsemblBacteria; AAC21858; AAC21858; HI_0189. DR GeneID; 951095; -. DR KEGG; hin:HI0189; -. DR PATRIC; 20188875; VBIHaeInf48452_0194. DR eggNOG; ENOG4105D82; Bacteria. DR eggNOG; COG0334; LUCA. DR KO; K00262; -. DR OMA; VPWVDDA; -. DR OrthoDB; EOG65XN4D; -. DR PhylomeDB; P43793; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0006537; P:glutamate biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 449 NADP-specific glutamate dehydrogenase. FT /FTId=PRO_0000182770. FT ACT_SITE 128 128 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU10011}. FT BINDING 92 92 Substrate. {ECO:0000250}. FT BINDING 113 113 Substrate. {ECO:0000250}. FT BINDING 116 116 Substrate. {ECO:0000250}. FT BINDING 167 167 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 211 211 NADP. {ECO:0000250}. FT BINDING 242 242 NADP. {ECO:0000250}. FT BINDING 380 380 Substrate. {ECO:0000250}. FT SITE 168 168 Important for catalysis. {ECO:0000250}. SQ SEQUENCE 449 AA; 48660 MW; 4698E0CD6C665A34 CRC64; MSKVASLDAF LTKVAQRDGY QPEFLQAVRE VFTSIWPFLE ANPKYRSEAL LERLVEPERA FQFRVAWTDD KGQVQVNRAF RVQFNSAIGP FKGGMRFHPS VNLSILKFLG FEQIFKNALT TLPMGGAKGG SDFDPKGKSD AEVMRFCQAL MAELYRHVGA DTDVPAGDIG VGGREVGYLA GYMKKLSNQS ACVFTGRGLS FGGSLIRPEA TGYGLIYFAQ AMLAEKGDSF AGKVVSVSGS GNVAQYAIEK ALSLGAKVVT CSDSSGYVYD PNGFTTEKLA ALFDIKNTKR GRVKDYAEQF GLQYFEGKRP WEVQVDIALP CATQNELELS DAQRLIKNGV KLVAEGANMP TTIEATEALL AADVLFGPGK AANAGGVATS GLEMAQSSQR LYWTAEEVDA QLHRIMLDIH ANCKKYGTIE GQENINYVVG ANVAGFVKVA DAMLAQGVY // ID DLDH_HAEIN Reviewed; 478 AA. AC P43784; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 126. DE RecName: Full=Dihydrolipoyl dehydrogenase; DE EC=1.8.1.4; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; GN Name=lpdA; OrderedLocusNames=HI_1231; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22884.1; -; Genomic_DNA. DR PIR; H64111; H64111. DR RefSeq; NP_439387.1; NC_000907.1. DR RefSeq; WP_010869158.1; NC_000907.1. DR ProteinModelPortal; P43784; -. DR SMR; P43784; 19-470. DR STRING; 71421.HI1231; -. DR PRIDE; P43784; -. DR EnsemblBacteria; AAC22884; AAC22884; HI_1231. DR GeneID; 950173; -. DR KEGG; hin:HI1231; -. DR PATRIC; 20191141; VBIHaeInf48452_1283. DR eggNOG; ENOG4107QN2; Bacteria. DR eggNOG; COG1249; LUCA. DR KO; K00382; -. DR OMA; KRVMDST; -. DR OrthoDB; EOG6QCD6D; -. DR PhylomeDB; P43784; -. DR Proteomes; UP000000579; 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; -; 3. 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 478 Dihydrolipoyl dehydrogenase. FT /FTId=PRO_0000068030. FT NP_BIND 36 45 FAD. {ECO:0000250}. FT NP_BIND 183 187 NAD. {ECO:0000250}. FT NP_BIND 270 273 NAD. {ECO:0000250}. FT ACT_SITE 445 445 Proton acceptor. {ECO:0000250}. FT BINDING 54 54 FAD. {ECO:0000250}. FT BINDING 117 117 FAD; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 206 206 NAD. {ECO:0000250}. FT BINDING 239 239 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 313 313 FAD. {ECO:0000250}. FT BINDING 321 321 FAD; via amide nitrogen. {ECO:0000250}. FT DISULFID 45 50 Redox-active. {ECO:0000250}. SQ SEQUENCE 478 AA; 51154 MW; E2554EE977AF749C CRC64; MSKEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYST LGGVCLNVGC IPSKALLHVA KVIEEAKHAN KNGIYFSEPR IELDEVRAGK EAVVAKLTGG LAGMAKARKV TVVEGLATFT DSHTLVARDR DGNPTTVKFD NAIIAAGSRP VQLPFIPHED PRIWDSTDAL KLKEVPKKLL IMGGGIIGLE MGTVYNALGS EVEVVEMFDQ VIPAADKDVV GIYTKQVEKK FKLMLETKVT AVEAKDDGIY VSMEGKACND TKRYDAVLVA IGRVPNGKLI DAGKAGVEVD DRGFIHVDKQ MRTNVPHIYA IGDIVGQPML AHKGVHEGHV AAEVIAGQKH YFDPKVIPSI AYTEPEVAWV GKTEKECKQE GLNYEVAKFP WAASGRAIAS ECSEGMTKLI FDKDTHRVLG GAIVGSNGGE LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNAK AKEKIISI // ID DMSB_HAEIN Reviewed; 205 AA. AC P45003; Q48049; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Anaerobic dimethyl sulfoxide reductase chain B; DE AltName: Full=DMSO reductase iron-sulfur subunit; GN Name=dmsB; OrderedLocusNames=HI_1046; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B; RX PubMed=8635740; DOI=10.1016/0378-1119(95)00808-X; RA Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.; RT "Sequences of the genes encoding the A, B and C subunits of the RT Haemophilus influenzae dimethylsulfoxide reductase complex."; RL Gene 169:137-138(1996). CC -!- FUNCTION: Electron transfer subunit of the terminal reductase CC during anaerobic growth on various sulfoxide and N-oxide CC compounds. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}. CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22705.1; -; Genomic_DNA. DR EMBL; U26665; AAB06234.1; -; Genomic_DNA. DR PIR; F64109; F64109. DR RefSeq; NP_439205.1; NC_000907.1. DR RefSeq; WP_005656008.1; NC_000907.1. DR ProteinModelPortal; P45003; -. DR STRING; 71421.HI1046; -. DR EnsemblBacteria; AAC22705; AAC22705; HI_1046. DR GeneID; 950772; -. DR KEGG; hin:HI1046; -. DR PATRIC; 20190757; VBIHaeInf48452_1091. DR eggNOG; ENOG4105QAX; Bacteria. DR eggNOG; COG0437; LUCA. DR KO; K07307; -. DR OMA; VKPNKHA; -. DR OrthoDB; EOG6JTC8Q; -. DR PhylomeDB; P45003; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR014297; DMSO_DmsB. DR Pfam; PF13247; Fer4_11; 1. DR Pfam; PF12800; Fer4_4; 1. DR TIGRFAMs; TIGR02951; DMSO_dmsB; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 205 Anaerobic dimethyl sulfoxide reductase FT chain B. FT /FTId=PRO_0000159246. FT DOMAIN 4 32 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 57 89 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 90 119 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 13 13 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 16 16 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 23 23 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 67 67 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 70 70 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 75 75 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 79 79 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 99 99 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 102 102 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 105 105 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 109 109 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 126 126 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 129 129 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 141 141 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 145 145 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT VARIANT 60 60 A -> G (in strain: Eagan). SQ SEQUENCE 205 AA; 22927 MW; 006A89D0802BF685 CRC64; MEQYGFYFDS ERCTGCKTCE LACKDYKDLG TEVNFRRIYE YTGGQWNQQA DGCWHQNIFA YYMSISCNHC ADPACTKVCP TGAMHKNADG FVIVNEEICI GCRYCHMACP YDAPQYDAQK GHMTKCDGCY SRVKSGQKPI CVDACPLRAL DFAPIDELRT KYGTQASIAP LPPTDITQPN LVVKPNKYAR LSGDTSGFLG NPREV // ID DCD_HAEIN Reviewed; 195 AA. AC P44534; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Deoxycytidine triphosphate deaminase; DE Short=dCTP deaminase; DE EC=3.5.4.13; GN Name=dcd; OrderedLocusNames=HI_0133; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: dCTP + H(2)O = dUTP + NH(3). CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 1/2. CC -!- SIMILARITY: Belongs to the dCTP deaminase 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; L42023; AAC21805.1; -; Genomic_DNA. DR PIR; A64050; A64050. DR RefSeq; NP_438302.1; NC_000907.1. DR RefSeq; WP_010868941.1; NC_000907.1. DR ProteinModelPortal; P44534; -. DR STRING; 71421.HI0133; -. DR EnsemblBacteria; AAC21805; AAC21805; HI_0133. DR GeneID; 951042; -. DR KEGG; hin:HI0133; -. DR PATRIC; 20188753; VBIHaeInf48452_0135. DR eggNOG; ENOG4105DHP; Bacteria. DR eggNOG; COG0717; LUCA. DR KO; K01494; -. DR OMA; NIPCIHP; -. DR OrthoDB; EOG67DPKR; -. DR PhylomeDB; P44534; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008829; F:dCTP deaminase activity; IBA:GO_Central. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. DR InterPro; IPR011962; dCTP_deam. DR InterPro; IPR010550; dCTP_deam_bac. DR InterPro; IPR029054; dUTPase-like. DR Pfam; PF06559; DCD; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR02274; dCTP_deam; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Nucleotide metabolism; KW Reference proteome. FT CHAIN 1 195 Deoxycytidine triphosphate deaminase. FT /FTId=PRO_0000155988. SQ SEQUENCE 195 AA; 21618 MW; 39EE5C2370A6C1CB CRC64; MRLCDTDIER YLDDGIISLT PRPNNDKING ATIDVRLGNS FRVFREHSAP FIDLSGPKEE VSAQLESVMS DEIIIPEGEA FFLHPGTLAL ATTLESVKLP ANIIGWLDGR SSLARLGLMV HVTAHRIDPG WEGKIVLEFY NSGKLPLALR PNMVIGALSF EVLSGEXKRP YSSRKDAKYK NQQSAVASRI DEDKE // ID DEOD_HAEIN Reviewed; 238 AA. AC P44417; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 105. DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627}; DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627}; DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627}; GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627}; GN OrderedLocusNames=HI_0518; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 1-10. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01627}. CC -!- CATALYTIC ACTIVITY: Purine deoxynucleoside + phosphate = purine + CC 2'-deoxy-alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01627}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01627}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. CC {ECO:0000255|HAMAP-Rule:MF_01627}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22176.1; -; Genomic_DNA. DR PIR; B64074; B64074. DR RefSeq; NP_438676.1; NC_000907.1. DR RefSeq; WP_005694122.1; NC_000907.1. DR ProteinModelPortal; P44417; -. DR SMR; P44417; 2-236. DR STRING; 71421.HI0518; -. DR EnsemblBacteria; AAC22176; AAC22176; HI_0518. DR GeneID; 949650; -. DR KEGG; hin:HI0518; -. DR PATRIC; 20189589; VBIHaeInf48452_0537. DR eggNOG; ENOG4105D3A; Bacteria. DR eggNOG; COG0813; LUCA. DR KO; K03784; -. DR OMA; PQCLLCG; -. DR OrthoDB; EOG6BKJC5; -. DR PhylomeDB; P44417; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-HAMAP. 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 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 238 Purine nucleoside phosphorylase DeoD- FT type. FT /FTId=PRO_0000063135. FT REGION 87 90 Phosphate binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 179 181 Purine nucleoside binding. FT {ECO:0000250|UniProtKB:P50389}. FT REGION 203 204 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; 25885 MW; 0C49C06495AFA706 CRC64; MTPHINAPEG AFADVVLMPG DPLRAKYIAE TFLQDVVEVT NVRNMLGFTG TYKGRKISIM GHGMGIPSCS IYAKELITEY GVKKIIRVGS CGTVRMDVKV RDVIIGLGAC TDSKVNRIRF KDNDFAAIAD FDMAQAAVQA AKAKGKVVRV GNLFSADLFY TPDVEMFDVM EKYGILGVEM EAAGIYGVAA EYGAKALTIC TVSDHIRTHE QTTAEERQLT FNDMIEIALD SVLIGDAL // ID DNAA_HAEIN Reviewed; 454 AA. AC P43742; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Chromosomal replication initiator protein DnaA; GN Name=dnaA; OrderedLocusNames=HI_0993; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22655.1; -; Genomic_DNA. DR PIR; B64107; B64107. DR RefSeq; NP_439156.1; NC_000907.1. DR RefSeq; WP_005693336.1; NC_000907.1. DR ProteinModelPortal; P43742; -. DR SMR; P43742; 362-454. DR STRING; 71421.HI0993; -. DR EnsemblBacteria; AAC22655; AAC22655; HI_0993. DR GeneID; 950755; -. DR KEGG; hin:HI0993; -. DR PATRIC; 20190647; VBIHaeInf48452_1036. DR eggNOG; ENOG4105CI4; Bacteria. DR eggNOG; COG0593; LUCA. DR KO; K02313; -. DR OMA; QSKTRKR; -. DR OrthoDB; EOG689HR1; -. DR PhylomeDB; P43742; -. DR Proteomes; UP000000579; 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; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006275; P:regulation of DNA replication; IBA:GO_Central. DR Gene3D; 1.10.1750.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00377; DnaA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001957; Chromosome_initiator_DnaA. DR InterPro; IPR020591; Chromosome_initiator_DnaA-like. DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS. DR InterPro; IPR013317; DnaA. DR InterPro; IPR013159; DnaA_C. DR InterPro; IPR024633; DnaA_N_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR Pfam; PF00308; Bac_DnaA; 1. DR Pfam; PF08299; Bac_DnaA_C; 1. DR Pfam; PF11638; DnaA_N; 1. DR PRINTS; PR00051; DNAA. DR SMART; SM00382; AAA; 1. DR SMART; SM00760; Bac_DnaA_C; 1. DR SUPFAM; SSF48295; SSF48295; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00362; DnaA; 1. DR PROSITE; PS01008; DNAA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 454 Chromosomal replication initiator protein FT DnaA. FT /FTId=PRO_0000114186. FT NP_BIND 160 167 ATP. {ECO:0000255}. SQ SEQUENCE 454 AA; 51724 MW; B7ED007B48433A65 CRC64; MNLSNLWQSC LLQLQDQVSA SDLSTWLRPL QADVVADNHI VLYASNMFVK GWVETHYLAQ IQQICQTLAQ NPELRISLKE GVKPAPKIVE STPNTSLRSE SAVDFQAESS ASVKFESHLN TKHLFDNFVE GKSNQLARAV GQKLAQAPGE PSANPFFLYG GTGLGKTHLL HAIGNGILAD KPNARVLYIH ANNFMQHMVK AVRDNKMDQF KKFYRSLDAL LVDDIQFFAE KEKTQEEFFH IFNSLFETGR QIILTSDRYP KEIEKIEERL KSRFGWGLTT AIEPPDLETR VAILLKKAEE HNMNLPEEVA FFIAQRLRTN VRELEGALNR VKAMQDFKGG DIDIDFVRDT LKDILALQER LVTIENIQKV VAEYYRIKVS DLKSKSRARS VTRPRQIAMA LAKELTNRSL PEIGRAFDRD HTTVLNACRE VPKFREQDNS IQEDWANLIR TLSA // ID DER_HAEIN Reviewed; 504 AA. AC P44536; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 109. 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=HI_0136; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21807.1; -; Genomic_DNA. DR PIR; F64143; F64143. DR RefSeq; NP_438305.1; NC_000907.1. DR RefSeq; WP_005694423.1; NC_000907.1. DR ProteinModelPortal; P44536; -. DR STRING; 71421.HI0136; -. DR EnsemblBacteria; AAC21807; AAC21807; HI_0136. DR GeneID; 951041; -. DR KEGG; hin:HI0136; -. DR PATRIC; 20188759; VBIHaeInf48452_0138. DR eggNOG; ENOG4105DKZ; Bacteria. DR eggNOG; COG1160; LUCA. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR PhylomeDB; P44536; -. DR Proteomes; UP000000579; 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; IPR003593; AAA+_ATPase. DR InterPro; IPR031166; G_ENGA. DR InterPro; IPR016484; GTP-bd_EngA. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR032859; KH_dom-like. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11649:SF5; PTHR11649:SF5; 1. DR Pfam; PF14714; KH_dom-like; 1. DR Pfam; PF01926; MMR_HSR1; 2. DR PIRSF; PIRSF006485; GTP-binding_EngA; 1. DR PRINTS; PR00326; GTP1OBG. DR SMART; SM00382; AAA; 2. 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 1 504 GTPase Der. FT /FTId=PRO_0000178998. FT DOMAIN 4 168 EngA-type G 1. FT DOMAIN 216 389 EngA-type G 2. FT DOMAIN 390 474 KH-like. {ECO:0000255|HAMAP- FT Rule:MF_00195}. FT NP_BIND 10 17 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 57 61 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 120 123 GTP 1. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 222 229 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 269 273 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. FT NP_BIND 334 337 GTP 2. {ECO:0000255|HAMAP-Rule:MF_00195}. SQ SEQUENCE 504 AA; 56437 MW; 6A36C7F9CCB8261C CRC64; MATPVVALVG RPNVGKSTLF NRLTRTRDAL VADFPGLTRD RKYGHAHIAG YDFIVIDTGG IDGTEEGVEE KMAEQSLLAI DEADIVLFLV DARAGLTAAD IGIANYLRQR QNKITVVVAN KTDGIDADSH CAEFYQLGLG EIEQIAASQG RGVTQLMEQV LAPFAEKMEN ADENDRTSEE EQDEWEQEFD FDSEEDTALI DDALDEELEE EQDKNIKIAI VGRPNVGKST LTNRILGEDR VVVFDMPGTT RDSIYIPMER DGQQYTLIDT AGVRKRGKVH LAVEKFSVIK TLQAIQDANV VLLTIDAREN ISDQDLSLLG FILNAGRSLV IVVNKWDGLD QDVKDRVKSE LDRRLDFIDF ARVHFISALH GSGVGNLFDS IKEAYACATQ KMTTSLLTRI LQMATDEHQP PMIGGRRIKL KYAHPGGYNP PIIVVHGNQM DKLPDSYKRY LSNYYRKSLK IIGSPIRLLF QEGSNPFAGR KNKLTPNQLR KRKRLMKFIK KAKR // ID DHAS_HAEIN Reviewed; 371 AA. AC P44801; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 122. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000269|PubMed:12071715, ECO:0000269|PubMed:15272161}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=HI_0646; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=12071715; DOI=10.1006/prep.2002.1626; RA Moore R.A., Bocik W.E., Viola R.E.; RT "Expression and purification of aspartate beta-semialdehyde RT dehydrogenase from infectious microorganisms."; RL Protein Expr. Purif. 25:189-194(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH RP L-ASPARTATE-SEMIALDEHYDE AND PHOSPHATE, SUBUNIT, DOMAIN, AND CATALYTIC RP MECHANISM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=14559965; DOI=10.1073/pnas.1634958100; RA Blanco J., Moore R.A., Viola R.E.; RT "Capture of an intermediate in the catalytic cycle of L-aspartate- RT beta-semialdehyde dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12613-12617(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF MUTANTS LEU-103; LYS-103; RP SER-136; ASP-243; ARG-246; LYS-270 AND ASN-277 IN COMPLEX WITH NADP, RP CATALYTIC ACTIVITY, KINETIC STUDIES, AND MUTAGENESIS OF ARG-103; RP GLU-243; LYS-246 AND ARG-270. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15272161; DOI=10.1107/S0907444904012971; RA Blanco J., Moore R.A., Faehnle C.R., Coe D.M., Viola R.E.; RT "The role of substrate-binding groups in the mechanism of aspartate- RT beta-semialdehyde dehydrogenase."; RL Acta Crystallogr. D 60:1388-1395(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH ARSENATE AND RP PERIODATE IONS. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15583380; DOI=10.1107/S0907444904026411; RA Faehnle C.R., Blanco J., Viola R.E.; RT "Structural basis for discrimination between oxyanion substrates or RT inhibitors in aspartate-beta-semialdehyde dehydrogenase."; RL Acta Crystallogr. D 60:2320-2324(2004). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. {ECO:0000269|PubMed:12071715}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. CC {ECO:0000269|PubMed:12071715, ECO:0000269|PubMed:15272161}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.24 mM for L-aspartate 4-semialdehyde CC {ECO:0000269|PubMed:12071715}; CC KM=0.15 mM for NADP(+) {ECO:0000269|PubMed:12071715}; CC KM=1.6 mM for phosphate {ECO:0000269|PubMed:12071715}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14559965, CC ECO:0000269|PubMed:15272161}. CC -!- DOMAIN: Consists of two domains, an N-terminal nucleotide-binding CC domain and a C-terminal dimerization domain. CC {ECO:0000269|PubMed:14559965}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_02121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22306.1; -; Genomic_DNA. DR PIR; B64084; B64084. DR RefSeq; NP_438806.1; NC_000907.1. DR RefSeq; WP_005694497.1; NC_000907.1. DR PDB; 1NWC; X-ray; 2.04 A; A/B=1-371. DR PDB; 1NWH; X-ray; 2.00 A; A/B=1-371. DR PDB; 1NX6; X-ray; 2.15 A; A=1-371. DR PDB; 1OZA; X-ray; 2.06 A; A=1-371. DR PDB; 1PQP; X-ray; 2.06 A; A=1-371. DR PDB; 1PQU; X-ray; 1.92 A; A/B/C/D=1-371. DR PDB; 1PR3; X-ray; 2.15 A; A=1-371. DR PDB; 1PS8; X-ray; 2.40 A; A=1-371. DR PDB; 1PU2; X-ray; 2.06 A; A=1-371. DR PDB; 1Q2X; X-ray; 2.05 A; A/B=1-371. DR PDB; 1TA4; X-ray; 2.28 A; A=1-371. DR PDB; 1TB4; X-ray; 2.15 A; A=1-371. DR PDBsum; 1NWC; -. DR PDBsum; 1NWH; -. DR PDBsum; 1NX6; -. DR PDBsum; 1OZA; -. DR PDBsum; 1PQP; -. DR PDBsum; 1PQU; -. DR PDBsum; 1PR3; -. DR PDBsum; 1PS8; -. DR PDBsum; 1PU2; -. DR PDBsum; 1Q2X; -. DR PDBsum; 1TA4; -. DR PDBsum; 1TB4; -. DR ProteinModelPortal; P44801; -. DR SMR; P44801; 1-371. DR STRING; 71421.HI0646; -. DR PRIDE; P44801; -. DR EnsemblBacteria; AAC22306; AAC22306; HI_0646. DR GeneID; 949960; -. DR KEGG; hin:HI0646; -. DR PATRIC; 20189907; VBIHaeInf48452_0675. DR eggNOG; ENOG4105CM3; Bacteria. DR eggNOG; COG0136; LUCA. DR KO; K00133; -. DR OMA; SCQGGDY; -. DR OrthoDB; EOG67X1PS; -. DR PhylomeDB; P44801; -. DR BRENDA; 1.2.1.11; 2529. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR EvolutionaryTrace; P44801; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR011534; Asp_ADH_gamma-type. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01745; asd_gamma; 1. DR PROSITE; PS01103; ASD; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome; KW Threonine biosynthesis. FT CHAIN 1 371 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141375. FT NP_BIND 10 13 NADP. {ECO:0000269|PubMed:15272161}. FT NP_BIND 37 38 NADP. {ECO:0000269|PubMed:15272161}. FT ACT_SITE 136 136 Acyl-thioester intermediate. FT {ECO:0000269|PubMed:14559965, FT ECO:0000269|PubMed:15272161}. FT ACT_SITE 277 277 Proton acceptor. FT {ECO:0000269|PubMed:14559965}. FT BINDING 74 74 NADP. {ECO:0000269|PubMed:15272161}. FT BINDING 103 103 Phosphate. {ECO:0000269|PubMed:14559965}. FT BINDING 163 163 Substrate. {ECO:0000305|PubMed:15272161}. FT BINDING 166 166 NADP; via carbonyl oxygen. FT {ECO:0000269|PubMed:15272161}. FT BINDING 243 243 Substrate. {ECO:0000305|PubMed:15272161}. FT BINDING 246 246 Phosphate. {ECO:0000269|PubMed:14559965}. FT BINDING 270 270 Substrate. {ECO:0000305|PubMed:15272161}. FT BINDING 353 353 NADP. {ECO:0000269|PubMed:15272161}. FT MUTAGEN 103 103 R->K: 2-fold increase in affinity for FT ASA, 23-fold decrease in affinity for FT phosphate, and 275-fold decrease in FT activity. {ECO:0000269|PubMed:15272161}. FT MUTAGEN 103 103 R->L: 7-fold increase in affinity for FT ASA, 150-fold decrease in affinity for FT phosphate, and 1400-fold decrease in FT activity. {ECO:0000269|PubMed:15272161}. FT MUTAGEN 243 243 E->D: No change in affinity for ASA and FT 82-fold decrease in activity. FT {ECO:0000269|PubMed:15272161}. FT MUTAGEN 246 246 K->R: 2-fold increase in affinity for FT ASA, nearly no change in affinity for FT phosphate, and 30-fold decrease in FT activity. {ECO:0000269|PubMed:15272161}. FT MUTAGEN 270 270 R->K: 2-fold decrease in affinity for ASA FT and 825-fold decrease in activity. FT {ECO:0000269|PubMed:15272161}. FT STRAND 2 8 {ECO:0000244|PDB:1PQU}. FT HELIX 12 24 {ECO:0000244|PDB:1PQU}. FT TURN 25 29 {ECO:0000244|PDB:1PQU}. FT STRAND 30 38 {ECO:0000244|PDB:1PQU}. FT HELIX 47 49 {ECO:0000244|PDB:1PQU}. FT HELIX 61 64 {ECO:0000244|PDB:1PQU}. FT STRAND 68 72 {ECO:0000244|PDB:1PQU}. FT HELIX 76 88 {ECO:0000244|PDB:1PQU}. FT STRAND 93 100 {ECO:0000244|PDB:1PQU}. FT TURN 101 104 {ECO:0000244|PDB:1PQU}. FT STRAND 108 111 {ECO:0000244|PDB:1PQU}. FT HELIX 113 126 {ECO:0000244|PDB:1PQU}. FT STRAND 130 133 {ECO:0000244|PDB:1PQU}. FT HELIX 136 150 {ECO:0000244|PDB:1PQU}. FT STRAND 154 163 {ECO:0000244|PDB:1PQU}. FT HELIX 165 167 {ECO:0000244|PDB:1PQU}. FT HELIX 170 185 {ECO:0000244|PDB:1PQU}. FT HELIX 188 191 {ECO:0000244|PDB:1PQU}. FT HELIX 198 209 {ECO:0000244|PDB:1PQU}. FT TURN 217 219 {ECO:0000244|PDB:1PQU}. FT STRAND 225 228 {ECO:0000244|PDB:1PQU}. FT TURN 236 238 {ECO:0000244|PDB:1PQU}. FT HELIX 242 255 {ECO:0000244|PDB:1PQU}. FT STRAND 258 260 {ECO:0000244|PDB:1Q2X}. FT STRAND 264 267 {ECO:0000244|PDB:1PQU}. FT STRAND 270 287 {ECO:0000244|PDB:1PQU}. FT HELIX 291 300 {ECO:0000244|PDB:1PQU}. FT STRAND 303 307 {ECO:0000244|PDB:1PQU}. FT HELIX 312 318 {ECO:0000244|PDB:1PQU}. FT HELIX 321 324 {ECO:0000244|PDB:1PQU}. FT STRAND 330 338 {ECO:0000244|PDB:1PQU}. FT STRAND 341 352 {ECO:0000244|PDB:1PQU}. FT TURN 353 358 {ECO:0000244|PDB:1PQU}. FT HELIX 359 370 {ECO:0000244|PDB:1PQU}. SQ SEQUENCE 371 AA; 40539 MW; E44CE5B90F2AF041 CRC64; MKNVGFIGWR GMVGSVLMDR MSQENDFENL NPVFFTTSQA GQKAPVFGGK DAGDLKSAFD IEELKKLDII VTCQGGDYTN EVYPKLKATG WDGYWVDAAS ALRMKDDAII VLDPVNQHVI SEGLKKGIKT FVGGNCTVSL MLMAIGGLFE KDLVEWISVA TYQAASGAGA KNMRELLSQM GLLEQAVSSE LKDPASSILD IERKVTAKMR ADNFPTDNFG AALGGSLIPW IDKLLPETGQ TKEEWKGYAE TNKILGLSDN PIPVDGLCVR IGALRCHSQA FTIKLKKDLP LEEIEQIIAS HNEWVKVIPN DKEITLRELT PAKVTGTLSV PVGRLRKLAM GPEYLAAFTV GDQLLWGAAE PVRRILKQLV A // ID DHPS_HAEIN Reviewed; 275 AA. AC P43776; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 108. DE RecName: Full=Dihydropteroate synthase; DE Short=DHPS; DE EC=2.5.1.15; DE AltName: Full=Dihydropteroate pyrophosphorylase; GN Name=folP-A; OrderedLocusNames=HI_1336; GN and GN Name=folP-B; OrderedLocusNames=HI_1464; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) CC with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to CC form 7,8-dihydropteroate (H2Pte), the immediate precursor of CC folate derivatives. {ECO:0000250|UniProtKB:P0AC13}. CC -!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate CC + 4-aminobenzoate = diphosphate + dihydropteroate. CC {ECO:0000250|UniProtKB:P0AC13}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0AC13}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8- CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22983.1; -; Genomic_DNA. DR EMBL; L42023; AAC23111.1; -; Genomic_DNA. DR PIR; E64117; E64117. DR RefSeq; NP_439487.1; NC_000907.1. DR RefSeq; NP_439615.1; NC_000907.1. DR RefSeq; WP_005694653.1; NC_000907.1. DR ProteinModelPortal; P43776; -. DR SMR; P43776; 1-274. DR STRING; 71421.HI1464; -. DR EnsemblBacteria; AAC22983; AAC22983; HI_1336. DR EnsemblBacteria; AAC23111; AAC23111; HI_1464. DR GeneID; 950351; -. DR GeneID; 950701; -. DR KEGG; hin:HI1336; -. DR KEGG; hin:HI1464; -. DR PATRIC; 20191355; VBIHaeInf48452_1388. DR eggNOG; ENOG4105EEI; Bacteria. DR eggNOG; COG0294; LUCA. DR KO; K00796; -. DR OMA; SIDTYHA; -. DR OrthoDB; EOG67T5P5; -. DR PhylomeDB; P43776; -. DR UniPathway; UPA00077; UER00156. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.20; -; 1. DR InterPro; IPR006390; DHP_synth. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR01496; DHPS; 1. DR PROSITE; PS00792; DHPS_1; 1. DR PROSITE; PS00793; DHPS_2; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome; Folate biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1 275 Dihydropteroate synthase. FT /FTId=PRO_0000168210. FT DOMAIN 15 267 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. FT REGION 255 257 6-hydroxymethyl-7,8-dihydropterin FT diphosphate binding. FT {ECO:0000250|UniProtKB:P0AC13}. FT METAL 22 22 Magnesium. FT {ECO:0000250|UniProtKB:P9WND1}. FT BINDING 62 62 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 96 96 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 115 115 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 185 185 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. FT BINDING 221 221 6-hydroxymethyl-7,8-dihydropterin FT diphosphate. FT {ECO:0000250|UniProtKB:P0AC13}. SQ SEQUENCE 275 AA; 30330 MW; 8164FD3FBB7B9A30 CRC64; MKLYANNKCL DLSVPQIMGI LNFTPDSFSD SGQFFSLDKA LFQVEKMLEE GATIIDIGGE STRPNADEVS EQEELHRVVP VVEAVRNRFD CWISVDSSKA VVMREAANVG MDLINDIRAL QEPNALETAV KLALPVCIMH MQGQPRTMQA NPYYENVVQD VLAFLQKRTN ECLSAGIKKE NLIWDMGFGF GKSVQHNYQL LQNLNEFCQI GYPVLAGLSR KSMIGAVLDK PVDQRIIGSA AGALIAVQKG AKILRVHDVA ATSDMLKVWQ ATANA // ID DMA_HAEIN Reviewed; 286 AA. AC P44431; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=DNA adenine methylase; DE EC=2.1.1.72; DE AltName: Full=DNA adenine methyltransferase; DE AltName: Full=Deoxyadenosyl-methyltransferase; DE AltName: Full=M.HindIV; GN Name=dam; Synonyms=hindIVM; OrderedLocusNames=HI_0209; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Methylates DNA within the sequence GATC. Directly CC involved in methyl-directed DNA mismatch repair (By similarity). CC {ECO:0000250}. 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; L42023; AAC21877.1; -; Genomic_DNA. DR PIR; H64054; H64054. DR RefSeq; NP_438378.1; NC_000907.1. DR RefSeq; WP_010868957.1; NC_000907.1. DR STRING; 71421.HI0209; -. DR REBASE; 1152; M.HindDam. DR EnsemblBacteria; AAC21877; AAC21877; HI_0209. DR GeneID; 951117; -. DR KEGG; hin:HI0209; -. DR PATRIC; 20188915; VBIHaeInf48452_0214. DR eggNOG; ENOG4105DFE; Bacteria. DR eggNOG; COG0338; LUCA. DR KO; K06223; -. DR OMA; MNRHGFN; -. DR OrthoDB; EOG6CS08V; -. DR PhylomeDB; P44431; -. DR Proteomes; UP000000579; 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 GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 1.10.1020.10; -; 1. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR023095; Ade_MeTrfase_dom_2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR012263; M_m6A_EcoRV. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00571; dam; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 286 DNA adenine methylase. FT /FTId=PRO_0000087996. FT BINDING 21 21 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 25 25 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. FT BINDING 66 66 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 194 194 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 286 AA; 33219 MW; BE39C5725AE35DEE CRC64; MLRPKKQSLK PKLKHRPFLK WAGGKFRLTD EINKAFPNKK NCLIEPFVGA GAVFLNSNFE RYILADINPD LINLFNIVKX NVDGYIEDCK PIFFADDANT PDYYYAKRRQ FNASTEPFER SIIFLYLNRF GFNGLCRYNS KNEFNVPFGA YKTHYFPEDE LRYFAHKAQS AVFLCCDFQK TFEFADKDSV IYCDPPYAPL QQETNFTGYA GNEFGLAQQR ALADLAKSIQ KEKQISILIS NHDTKFTREI YNGAKFKRVK VQRSISQNPE KRVKVKELIA IFGARK // ID DMSC_HAEIN Reviewed; 279 AA. AC P45002; Q48050; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Anaerobic dimethyl sulfoxide reductase chain C; DE AltName: Full=DMSO reductase anchor subunit; GN Name=dmsC; OrderedLocusNames=HI_1045; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B; RX PubMed=8635740; DOI=10.1016/0378-1119(95)00808-X; RA Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.; RT "Sequences of the genes encoding the A, B and C subunits of the RT Haemophilus influenzae dimethylsulfoxide reductase complex."; RL Gene 169:137-138(1996). CC -!- FUNCTION: Terminal reductase during anaerobic growth on various CC sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to CC the membrane and stabilizes it (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {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; L42023; AAC22704.1; -; Genomic_DNA. DR EMBL; U26665; AAB06235.1; -; Genomic_DNA. DR PIR; E64109; E64109. DR RefSeq; NP_439204.1; NC_000907.1. DR RefSeq; WP_005693381.1; NC_000907.1. DR STRING; 71421.HI1045; -. DR EnsemblBacteria; AAC22704; AAC22704; HI_1045. DR GeneID; 950571; -. DR KEGG; hin:HI1045; -. DR PATRIC; 20190755; VBIHaeInf48452_1090. DR eggNOG; ENOG4107KGK; Bacteria. DR eggNOG; COG3302; LUCA. DR KO; K07308; -. DR OMA; MTRVYQI; -. DR OrthoDB; EOG60GRV1; -. DR PhylomeDB; P45002; -. DR Proteomes; UP000000579; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0019645; P:anaerobic electron transport chain; IEA:InterPro. DR InterPro; IPR007059; DmsC. DR Pfam; PF04976; DmsC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 279 Anaerobic dimethyl sulfoxide reductase FT chain C. FT /FTId=PRO_0000079948. FT TOPO_DOM 1 9 Periplasmic. {ECO:0000255}. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TOPO_DOM 31 45 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TOPO_DOM 67 86 Periplasmic. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TOPO_DOM 108 118 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TOPO_DOM 140 150 Periplasmic. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TOPO_DOM 172 181 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TOPO_DOM 203 219 Periplasmic. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TOPO_DOM 241 244 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TOPO_DOM 266 279 Periplasmic. {ECO:0000255}. FT VARIANT 21 21 V -> A (in strain: Eagan). FT VARIANT 276 276 T -> A (in strain: Eagan). SQ SEQUENCE 279 AA; 30756 MW; 892D1AFBC08867BF CRC64; MNTGLYELPL VFFTVLAQSA VGAWLVFTFV LLNEKNTKSR TYIHKVMFVI LALLGIGFIA SIMHLGLPIR AFNSLNRVGS SMMSNEIAAG AIFFTLAGFY WLIAILGKMP VSLGNVWRIV TALIGILFMY VMNQVYHITS IPTWNNALTS WSFYLTVVLG GLTLSYALLI PNKQREYQLQ HLPSLFAIGV SLVAIVAIYQ GFNLHNIHSA IQNAADLVPN YAIMTVTRLC LLSIVAFLLF RVKNIGLLGI SVLLTLVAEG IGRVLFYGLH MTYGMTIGG // ID DNAG_HAEIN Reviewed; 593 AA. AC Q08346; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974}; GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; GN OrderedLocusNames=HI_0532; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate 1775; RX PubMed=8294018; DOI=10.1016/0378-1119(93)90480-Q; RA Versalovic J., Lupski J.R.; RT "The Haemophilus influenzae dnaG sequence and conserved bacterial RT primase motifs."; RL Gene 136:281-286(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. RC STRAIN=Isolate 1775; RX PubMed=8316085; DOI=10.1111/j.1365-2958.1993.tb01578.x; RA Versalovic J., Lupski J.R.; RT "Conservation and evolution of the rpsU-dnaG-rpoD macromolecular RT synthesis operon in bacteria."; RL Mol. Microbiol. 8:343-355(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; L11044; -; NOT_ANNOTATED_CDS; Unassigned_DNA. DR EMBL; L42023; AAC22189.1; -; Genomic_DNA. DR EMBL; L01756; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A64075; A64075. DR RefSeq; NP_438690.1; NC_000907.1. DR RefSeq; WP_010868999.1; NC_000907.1. DR ProteinModelPortal; Q08346; -. DR SMR; Q08346; 119-429. DR STRING; 71421.HI0532; -. DR EnsemblBacteria; AAC22189; AAC22189; HI_0532. DR GeneID; 949627; -. DR KEGG; hin:HI0532; -. DR PATRIC; 20189617; VBIHaeInf48452_0551. DR eggNOG; ENOG4105C9G; Bacteria. DR eggNOG; COG0358; LUCA. DR KO; K02316; -. DR OMA; FPIRNTK; -. DR OrthoDB; EOG6XDGTR; -. DR PhylomeDB; Q08346; -. DR Proteomes; UP000000579; 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; 1.10.860.10; -; 1. DR Gene3D; 3.90.580.10; -; 1. DR Gene3D; 3.90.980.10; -; 1. DR HAMAP; MF_00974; DNA_primase_DnaG; 1. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR InterPro; IPR013264; DNA_primase_core_N. DR InterPro; IPR019475; DNA_primase_DnaB-bd. DR InterPro; IPR006295; DNA_primase_DnaG. DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom. DR InterPro; IPR030846; DnaG_bac. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR002694; Znf_CHC2. DR Pfam; PF10410; DnaB_bind; 1. DR Pfam; PF08278; DnaG_DnaB_bind; 1. DR Pfam; PF08275; Toprim_N; 1. DR Pfam; PF01807; zf-CHC2; 1. DR PIRSF; PIRSF002811; DnaG; 1. DR SMART; SM00766; DnaG_DnaB_bind; 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 1 593 DNA primase. FT /FTId=PRO_0000180494. FT DOMAIN 260 342 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT ZN_FING 40 64 CHC2-type. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 266 266 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 310 310 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00974}. FT METAL 310 310 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT METAL 312 312 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00974}. FT CONFLICT 83 83 I -> V (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 103 103 V -> A (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 138 138 T -> S (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 299 299 L -> F (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 346 346 E -> D (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 435 435 K -> Q (in Ref. 1; L01756). FT {ECO:0000305}. FT CONFLICT 463 463 M -> L (in Ref. 1; L01756). FT {ECO:0000305}. SQ SEQUENCE 593 AA; 68001 MW; F573AED631B27095 CRC64; MKGSIPRPFI DDLLTKSDIV DVINTRVKLK KAGRDYQACC PFHHEKTPSF TVSQKKQFYH CFGCGAHGNA ISFLMDYDKL EFIEAIEELA AMAGLEIPYE KRVNHSGKPQ ANYQTKRNLY ELMQEIATFY QNQLPLNTQA QEYLQQRGLS PEIIERFQIG FVPNAMDTVL RKFGVNREEQ QKLIELGMLS RNDRGNIYDK FRNRIMFPIR DKRGRTVAFG GRVLTDEKPK YLNSPETITY HKGKELYGLY EALQTNDEPK QLLVVEGYMD VVALAQFGVD YAVASLGTST TSEQIQLILR STEQVVCCYD GDRAGRDAAW RALENALPYL EDGRQLKFIF LPDGEEPDTY IRQYGKEKFE EYIESAQSLS EFMFAHLSPQ VDFSTKEGRG KLVALAAPLI HQIPGEMLRL SLRNMLAQKL GIFDQTQLEN LIPKKLEQAN TQQKVTHNKI KKTPMRMVIS LLMQNPELVK RMSESGVQAL RAEAGFEILE KLTALCRQRE GITTGQILEY FRNTSYSNPL EILATWDHLL DESDIINAFS QNYRRLNIQA IERDIEMLIA KERTEGLTNE EKTVLVHLLA GKEQQKKQLV NPL // ID DNLJ_HAEIN Reviewed; 670 AA. AC P43813; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 16-MAR-2016, entry version 116. 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, ligN; GN OrderedLocusNames=HI_1100; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC22753.1; 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; L42023; AAC22753.1; ALT_INIT; Genomic_DNA. DR PIR; D64182; D64182. DR RefSeq; NP_439257.2; NC_000907.1. DR RefSeq; WP_005665886.1; NC_000907.1. DR PDB; 3BAC; X-ray; 3.00 A; A=64-327. DR PDB; 3PN1; X-ray; 2.00 A; A=1-318. DR PDB; 3UQ8; X-ray; 1.70 A; A=3-324. DR PDB; 4UCO; X-ray; 2.50 A; A=1-324. DR PDB; 4UCR; X-ray; 2.15 A; A=1-324. DR PDB; 4UCS; X-ray; 1.90 A; A=1-324. DR PDB; 4UCT; X-ray; 2.10 A; A=1-324. DR PDB; 4UCU; X-ray; 2.10 A; A=1-324. DR PDB; 4UCV; X-ray; 2.60 A; A=1-324. DR PDB; 4UFZ; X-ray; 2.33 A; A=1-324. DR PDBsum; 3BAC; -. DR PDBsum; 3PN1; -. DR PDBsum; 3UQ8; -. DR PDBsum; 4UCO; -. DR PDBsum; 4UCR; -. DR PDBsum; 4UCS; -. DR PDBsum; 4UCT; -. DR PDBsum; 4UCU; -. DR PDBsum; 4UCV; -. DR PDBsum; 4UFZ; -. DR ProteinModelPortal; P43813; -. DR SMR; P43813; 1-584. DR STRING; 71421.HI1100; -. DR EnsemblBacteria; AAC22753; AAC22753; HI_1100. DR GeneID; 950070; -. DR KEGG; hin:HI1100; -. DR PATRIC; 20190867; VBIHaeInf48452_1146. DR eggNOG; ENOG4105C77; Bacteria. DR eggNOG; COG0272; LUCA. DR KO; K01972; -. DR OMA; FTAKSPR; -. DR OrthoDB; EOG6TTVM9; -. DR PhylomeDB; P43813; -. DR EvolutionaryTrace; P43813; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006288; P:base-excision repair, DNA ligation; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR033136; DNA_ligase_CS. DR InterPro; IPR001679; DNAligase. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004150; NAD_DNA_ligase_OB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR004149; Znf_DNAligase_C4. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 1. DR Pfam; PF03119; DNA_ligase_ZBD; 1. DR PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00278; HhH1; 4. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS01055; DNA_LIGASE_N1; 1. DR PROSITE; PS01056; DNA_LIGASE_N2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; KW DNA replication; Ligase; Magnesium; Manganese; Metal-binding; NAD; KW Reference proteome; Zinc. FT CHAIN 1 670 DNA ligase. FT /FTId=PRO_0000161746. FT DOMAIN 592 670 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 116 116 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 409 409 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 412 412 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 427 427 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 433 433 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 114 114 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 137 137 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 174 174 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 291 291 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 315 315 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT HELIX 4 23 {ECO:0000244|PDB:3UQ8}. FT HELIX 32 48 {ECO:0000244|PDB:3UQ8}. FT HELIX 50 52 {ECO:0000244|PDB:3UQ8}. FT HELIX 58 60 {ECO:0000244|PDB:3UQ8}. FT STRAND 72 74 {ECO:0000244|PDB:3UQ8}. FT HELIX 88 101 {ECO:0000244|PDB:3UQ8}. FT STRAND 102 104 {ECO:0000244|PDB:4UCS}. FT STRAND 110 127 {ECO:0000244|PDB:3UQ8}. FT STRAND 130 136 {ECO:0000244|PDB:3UQ8}. FT STRAND 140 145 {ECO:0000244|PDB:3UQ8}. FT HELIX 147 151 {ECO:0000244|PDB:3UQ8}. FT STRAND 161 164 {ECO:0000244|PDB:4UCS}. FT STRAND 167 176 {ECO:0000244|PDB:3UQ8}. FT HELIX 179 191 {ECO:0000244|PDB:3UQ8}. FT HELIX 200 208 {ECO:0000244|PDB:3UQ8}. FT HELIX 213 216 {ECO:0000244|PDB:3UQ8}. FT STRAND 222 233 {ECO:0000244|PDB:3UQ8}. FT HELIX 240 249 {ECO:0000244|PDB:3UQ8}. FT STRAND 259 263 {ECO:0000244|PDB:3UQ8}. FT HELIX 264 276 {ECO:0000244|PDB:3UQ8}. FT TURN 277 281 {ECO:0000244|PDB:3UQ8}. FT STRAND 285 294 {ECO:0000244|PDB:3UQ8}. FT HELIX 295 301 {ECO:0000244|PDB:3UQ8}. FT STRAND 311 315 {ECO:0000244|PDB:3UQ8}. FT HELIX 319 321 {ECO:0000244|PDB:3UQ8}. SQ SEQUENCE 670 AA; 74043 MW; A4110EE380A76C9C CRC64; MTNIQTQLDN LRKTLRQYEY EYHVLDNPSV PDSEYDRLFH QLKALELEHP EFLTSDSPTQ RVGAKPLSGF SQIRHEIPML SLDNAFSDAE FNAFVKRIED RLILLPKPLT FCCEPKLDGL AVSILYVNGE LTQAATRGDG TTGEDITANI RTIRNVPLQL LTDNPPARLE VRGEVFMPHA GFERLNKYAL EHNEKTFANP RNAAAGSLRQ LDPNITSKRP LVLNAYGIGI AEGVDLPTTH YARLQWLKSI GIPVNPEIRL CNGADEVLGF YRDIQNKRSS LGYDIDGTVL KINDIALQNE LGFISKAPRW AIAYKFPAQE ELTLLNDVEF QVGRTGAITP VAKLEPVFVA GVTVSNATLH NGDEIERLNI AIGDTVVIRR AGDVIPQIIG VLHERRPDNA KPIIFPTNCP VCDSQIIRIE GEAVARCTGG LFCAAQRKEA LKHFVSRKAM DIDGVGGKLI EQLVDRELIH TPADLFKLDL TTLTRLERMG AKSAENALNS LENAKSTTLA RFIFALGIRE VGEATALNLA NHFKTLDALK DANLEELQQV PDVGEVVANR IFIFWREAHN VAVVEDLIAQ GVHWETVEVK EASENLFKDK TVVLTGTLTQ MGRNEAKALL QQLGAKVSGS VSSKTDFVIA GDAAGSKLAK AQELNITVLT EEEFLAQITR // ID DEF_HAEIN Reviewed; 169 AA. AC P44786; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Peptide deformylase; DE Short=PDF; DE EC=3.5.1.88; DE AltName: Full=Polypeptide deformylase; GN Name=def; OrderedLocusNames=HI_0622; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22282.1; -; Genomic_DNA. DR PIR; D64082; D64082. DR RefSeq; NP_438782.1; NC_000907.1. DR RefSeq; WP_005694639.1; NC_000907.1. DR ProteinModelPortal; P44786; -. DR SMR; P44786; 2-169. DR STRING; 71421.HI0622; -. DR BindingDB; P44786; -. DR EnsemblBacteria; AAC22282; AAC22282; HI_0622. DR GeneID; 949678; -. DR KEGG; hin:HI0622; -. DR PATRIC; 20189839; VBIHaeInf48452_0648. DR eggNOG; ENOG4108Z02; Bacteria. DR eggNOG; COG0242; LUCA. DR KO; K01462; -. DR OMA; FDTMYEE; -. DR OrthoDB; EOG664CMF; -. DR PhylomeDB; P44786; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0042586; F:peptide deformylase activity; IBA:GO_Central. DR GO; GO:0043686; P:co-translational protein modification; IBA:GO_Central. DR GO; GO:0031365; P:N-terminal protein amino acid modification; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.45.10; -; 1. DR HAMAP; MF_00163; Pep_deformylase; 1. DR InterPro; IPR000181; Fmet_deformylase. DR InterPro; IPR023635; Peptide_deformylase. DR PANTHER; PTHR10458; PTHR10458; 1. DR Pfam; PF01327; Pep_deformylase; 1. DR PIRSF; PIRSF004749; Pep_def; 1. DR PRINTS; PR01576; PDEFORMYLASE. DR SUPFAM; SSF56420; SSF56420; 1. DR TIGRFAMs; TIGR00079; pept_deformyl; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Iron; Metal-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 169 Peptide deformylase. FT /FTId=PRO_0000082788. FT ACT_SITE 134 134 {ECO:0000250}. FT METAL 91 91 Iron. {ECO:0000250}. FT METAL 133 133 Iron. {ECO:0000250}. FT METAL 137 137 Iron. {ECO:0000250}. SQ SEQUENCE 169 AA; 19057 MW; 7EA00AB510F798CD CRC64; MTALNVLIYP DDHLKVVCEP VTKVNDAIRK IVDDMFDTMY QEKGIGLAAP QVDILQRIIT IDVEGDKQNQ FVLINPEILA SEGETGIEEG CLSIPGFRAL VPRKEKVTVR ALDRDGKEFT LDADGLLAIC IQHEIDHLNG ILFVDYLSPL KRQRIKEKLI KYKKQIAKS // ID DLGD_HAEIN Reviewed; 332 AA. AC P44995; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=2,3-diketo-L-gulonate reductase {ECO:0000255|HAMAP-Rule:MF_00820}; DE Short=2,3-DKG reductase {ECO:0000255|HAMAP-Rule:MF_00820}; DE EC=1.1.1.130 {ECO:0000255|HAMAP-Rule:MF_00820}; DE AltName: Full=3-dehydro-L-gulonate 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00820}; GN Name=dlgD {ECO:0000255|HAMAP-Rule:MF_00820}; GN OrderedLocusNames=HI_1031; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reduction of 2,3-diketo-L-gulonate in the CC presence of NADH, to form 3-keto-L-gulonate. {ECO:0000255|HAMAP- CC Rule:MF_00820}. CC -!- CATALYTIC ACTIVITY: 3-dehydro-L-gulonate + NAD(P)(+) = (4R,5S)- CC 4,5,6-trihydroxy-2,3-dioxohexanoate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00820}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00820}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00820}. CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. DlgD CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00820}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22691.1; -; Genomic_DNA. DR PIR; C64165; C64165. DR RefSeq; NP_439191.1; NC_000907.1. DR RefSeq; WP_005693365.1; NC_000907.1. DR ProteinModelPortal; P44995; -. DR SMR; P44995; 1-332. DR STRING; 71421.HI1031; -. DR DNASU; 950015; -. DR EnsemblBacteria; AAC22691; AAC22691; HI_1031. DR GeneID; 950015; -. DR KEGG; hin:HI1031; -. DR PATRIC; 20190725; VBIHaeInf48452_1075. DR eggNOG; ENOG4105DG4; Bacteria. DR eggNOG; COG2055; LUCA. DR KO; K08092; -. DR OMA; GHEFTTI; -. DR OrthoDB; EOG6QK4PJ; -. DR PhylomeDB; P44995; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047559; F:3-dehydro-L-gulonate 2-dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR HAMAP; MF_00820; Diketo_gul_reduc; 1. DR InterPro; IPR023689; Diketo_gul_Rdtase. DR InterPro; IPR003767; Malate/L-lactate_DH. DR PANTHER; PTHR11091; PTHR11091; 1. DR Pfam; PF02615; Ldh_2; 1. DR SUPFAM; SSF89733; SSF89733; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 332 2,3-diketo-L-gulonate reductase. FT /FTId=PRO_0000083832. FT NP_BIND 168 174 NAD. {ECO:0000255|HAMAP-Rule:MF_00820}. FT NP_BIND 224 225 NAD. {ECO:0000255|HAMAP-Rule:MF_00820}. FT NP_BIND 304 306 NAD. {ECO:0000255|HAMAP-Rule:MF_00820}. FT ACT_SITE 44 44 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00820}. SQ SEQUENCE 332 AA; 36970 MW; FCFABC662F495FBF CRC64; MRVSYDELKN EFKRVLLDRQ LTEELAEECA TAFTDTTQAG AYSHGINRFP RFIQQLEQGD IVPNAIPTKV LSLGSIEQWD AHQAIGNLTA KKMMDRAIEL ASQHGVGVIA LRNANHWMRG GSYGWQAAEK GYIGICWTNA LAVMPPWGAK ECRIGTNPLI IAVPTTPITM VDMSCSMYSY GMLEVHRLAG RQTFVDAGFD DEGNLTRDPS IVEKNRRLLP MGFWKGSGLS IVLDMIATLL SNGESTVAVT EDKNDEYCVS QVFIAIEVDR LIDGKSKDEK LNRIMDYVKT AERSDPTQAV RLPGHEFTTI LSDNQTNGIP VDERVWAKLK TL // ID DMSD_HAEIN Reviewed; 203 AA. AC P44102; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 79. DE RecName: Full=Probable Tat proofreading chaperone DmsD {ECO:0000255|HAMAP-Rule:MF_00940}; DE AltName: Full=DMSO reductase maturation protein {ECO:0000255|HAMAP-Rule:MF_00940}; DE AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000255|HAMAP-Rule:MF_00940}; GN Name=dmsD {ECO:0000255|HAMAP-Rule:MF_00940}; GN OrderedLocusNames=HI_1044; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for biogenesis/assembly of DMSO reductase, but CC not for the interaction of the DmsA signal peptide with the Tat CC system. May be part of a chaperone cascade complex that CC facilitates a folding-maturation pathway for the substrate CC protein. {ECO:0000255|HAMAP-Rule:MF_00940}. CC -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00940}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22703.1; -; Genomic_DNA. DR PIR; C64019; C64019. DR RefSeq; NP_439203.1; NC_000907.1. DR RefSeq; WP_005693380.1; NC_000907.1. DR ProteinModelPortal; P44102; -. DR STRING; 71421.HI1044; -. DR EnsemblBacteria; AAC22703; AAC22703; HI_1044. DR GeneID; 950592; -. DR KEGG; hin:HI1044; -. DR PATRIC; 20190753; VBIHaeInf48452_1089. DR eggNOG; ENOG4108NEM; Bacteria. DR eggNOG; COG3381; LUCA. DR OMA; AWHLLPW; -. DR OrthoDB; EOG6FZ4BH; -. DR PhylomeDB; P44102; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005048; F:signal sequence binding; IEA:InterPro. DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3480.10; -; 1. DR HAMAP; MF_00940; DmsD_chaperone; 1. DR InterPro; IPR026269; DmsD-type. DR InterPro; IPR028611; DmsD_chaperone. DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone. DR Pfam; PF02613; Nitrate_red_del; 1. DR PIRSF; PIRSF004690; DmsD; 1. DR SUPFAM; SSF89155; SSF89155; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 203 Probable Tat proofreading chaperone DmsD. FT /FTId=PRO_0000211656. SQ SEQUENCE 203 AA; 24082 MW; D1DB97790FEAA681 CRC64; MQNTLQQISI YGRLLGAVFY YEPNDARLTD ILTFFRQPNW MQEWEISFDV KTHKKITALI EKGLQQNITE QYQYLFIGPN ELPTPPWGSV YLDPECVIFG NSLLALRDFL QQHQIAFQTQ QDEPEDHIGL MLMLAAYLAE NRPHLLTKFL REHFLTWAYH FLEQLSKIEN SDFYQALALL TIKTLQQWQV DLHINVPTVR FYR // ID DNAB_HAEIN Reviewed; 468 AA. AC P45256; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 2. DT 11-MAY-2016, entry version 103. DE RecName: Full=Replicative DNA helicase; DE EC=3.6.4.12; GN Name=dnaB; OrderedLocusNames=HI_1574; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Participates in initiation and elongation during CC chromosome replication; it exhibits DNA-dependent ATPase activity CC and contains distinct active sites for ATP binding, DNA binding, CC and interaction with DnaC protein, primase, and other prepriming CC proteins. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. 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=AAC23217.1; 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; L42023; AAC23217.1; ALT_INIT; Genomic_DNA. DR PIR; D64130; D64130. DR RefSeq; NP_439720.1; NC_000907.1. DR ProteinModelPortal; P45256; -. DR SMR; P45256; 17-130. DR STRING; 71421.HI1574; -. DR EnsemblBacteria; AAC23217; AAC23217; HI_1574. DR GeneID; 950434; -. DR KEGG; hin:HI1574; -. DR PATRIC; 20191879; VBIHaeInf48452_1647. DR eggNOG; ENOG4105CDU; Bacteria. DR eggNOG; COG0305; LUCA. DR KO; K02314; -. DR OMA; FQIAEAR; -. DR OrthoDB; EOG6T4RW5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007692; DNA_helicase_DnaB. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR016136; DNA_helicase_N/primase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00772; DnaB; 1. DR Pfam; PF03796; DnaB_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48024; SSF48024; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00665; DnaB; 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_0000102022. FT DOMAIN 194 462 SF4 helicase. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. FT NP_BIND 225 232 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00596}. SQ SEQUENCE 468 AA; 52362 MW; 09A13F77D53E17EF CRC64; MASQPQIKSS DKKTAQVSIP PHSTEAEQAV LGGIMLSNQH WDGIAERVIA DDFYTFQHRL IFTEMEHLMR NQSPIDLITL DQALRSRGVS DEVGGFAYLA ELSNNTPNAI NILAYADIVR EKAILRELIS VGNRIAENSY SPKGQDIKLI LDEAEREVFA IAEKRTTSSE GPQNVINVLE STIEKIDILS KLENHSGVTG VTTGFTDLDK KTAGLQPSDL IIVAARPSMG KTTFAMNLCE NAAMASEKPV LVFSLEMPAE QIMMRMIASL ARVDQTKIRT GQNLDEIEWN KIASVVGMFK QKNNLFIDDS SGLTPTDVRS RARRVYRENG GLSMIMVDYL QLMRAPAFSD NRTLEIAEIS RSLKALAKEL QVPVVALSQL NRTLEQRGDK RPVNSDLRES GSIEQDADLI MFIYRDEVYN DNSEDKGVAE IIIGKQRNGP IGRVRLKFNG QFSRFDNLAE QREYRDDY // ID DPO3B_HAEIN Reviewed; 366 AA. AC P43744; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=DNA polymerase III subunit beta; DE EC=2.7.7.7; GN Name=dnaN; OrderedLocusNames=HI_0992; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 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; L42023; AAC22654.1; -; Genomic_DNA. DR PIR; A64107; A64107. DR RefSeq; NP_439155.1; NC_000907.1. DR RefSeq; WP_005693335.1; NC_000907.1. DR ProteinModelPortal; P43744; -. DR SMR; P43744; 1-366. DR STRING; 71421.HI0992; -. DR EnsemblBacteria; AAC22654; AAC22654; HI_0992. DR GeneID; 949992; -. DR KEGG; hin:HI0992; -. DR PATRIC; 20190645; VBIHaeInf48452_1035. DR eggNOG; ENOG4105CZ8; Bacteria. DR eggNOG; COG0592; LUCA. DR KO; K02338; -. DR OMA; THQIRLK; -. DR OrthoDB; EOG65J53F; -. DR PhylomeDB; P43744; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR001001; DNA_polIII_beta. DR InterPro; IPR022635; DNA_polIII_beta_C. DR InterPro; IPR022637; DNA_polIII_beta_cen. DR InterPro; IPR022634; DNA_polIII_beta_N. DR Pfam; PF00712; DNA_pol3_beta; 1. DR Pfam; PF02767; DNA_pol3_beta_2; 1. DR Pfam; PF02768; DNA_pol3_beta_3; 1. DR PIRSF; PIRSF000804; DNA_pol_III_b; 1. DR SMART; SM00480; POL3Bc; 1. DR TIGRFAMs; TIGR00663; dnan; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication; KW DNA-directed DNA polymerase; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 366 DNA polymerase III subunit beta. FT /FTId=PRO_0000105437. SQ SEQUENCE 366 AA; 41631 MW; 004ED9647762960D CRC64; MQFSISRENL LKPLQQVCGV LSNRPNIPVL NNVLLQIEDY RLTITGTDLE VELSSQTQLS SSSENGTFTI PAKKFLDICR TLSDDSEITV TFEQDRALVQ SGRSRFTLAT QPAEEYPNLT DWQSEVDFEL PQNTLRRLIE ATQFSMANQD ARYFLNGMKF ETEGNLLRTV ATDGHRLAVC TISLEQELQN HSVILPRKGV LELVRLLETN DEPARLQIGT NNLRVHLKNT VFTSKLIDGR FPDYRRVLPR NATKIVEGNW EMLKQAFARA SILSNERARS VRLSLKENQL KITASNTEHE EAEEIVDVNY NGEELEVGFN VTYILDVLNA LKCNQVRMCL TDAFSSCLIE NCEDSSCEYV IMPMRL // ID DHNA_HAEIN Reviewed; 444 AA. AC P44856; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=NADH dehydrogenase; DE EC=1.6.99.3; GN Name=ndh; OrderedLocusNames=HI_0747; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfer of electrons from NADH to the respiratory CC chain. The immediate electron acceptor for the enzyme is believed CC to be ubiquinone. Does not couple the redox reaction to proton CC translocation (By similarity). {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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22405.1; -; Genomic_DNA. DR PIR; C64090; C64090. DR RefSeq; NP_438906.1; NC_000907.1. DR RefSeq; WP_005693148.1; NC_000907.1. DR ProteinModelPortal; P44856; -. DR STRING; 71421.HI0747; -. DR EnsemblBacteria; AAC22405; AAC22405; HI_0747. DR GeneID; 949772; -. DR KEGG; hin:HI0747; -. DR PATRIC; 20190137; VBIHaeInf48452_0784. DR eggNOG; ENOG4105CEP; Bacteria. DR eggNOG; COG1252; LUCA. DR KO; K03885; -. DR OMA; IFLHINF; -. DR OrthoDB; EOG6QZMR6; -. DR PhylomeDB; P44856; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF07992; Pyr_redox_2; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Electron transport; FAD; KW Flavoprotein; Membrane; NAD; Oxidoreductase; Reference proteome; KW Transport; Ubiquinone. FT CHAIN 1 444 NADH dehydrogenase. FT /FTId=PRO_0000079891. FT NP_BIND 3 38 FAD. {ECO:0000250}. FT NP_BIND 181 218 NAD. {ECO:0000250}. SQ SEQUENCE 444 AA; 48778 MW; B0EFE3613FE6B78B CRC64; MKNVVIVGGG AGGIELATFL GNKLGRQKQA KVTLVDRNAT HLWKPLLHEI ATGVMDDGVD SLSYRAHGKN HFFSFEQGSI IRINREQKYV ELAPVYGQEG DMLVIARRIP YDYLVIAIGS KSNDFNTKGV ADNCIFLDSS KQALRFQHKL LELFLKFSEN RALDDIGEEE FKQKLVDENK VNIAIVGGGA TGVELTAELY HAAEDLSSYG YGKIDSSCLQ VTLVEAGTRL LPALPENLSA AVLDELKEMG TNVQLNTMIT EAQPNTLITK DGGEIKADLI VWAAGVRAST VTQQFDGLEI NRINQLVVKD TLQTTVDDSI FAIGDCAALI QSNGKLVPPR AQAAHQMAKA CAKNIFALFE NKPLKSFKYN DKGTLVSLSN FTALGSLTNK FGKNPLTVQG KFAQFAYVSL YRMHQHALHG CIKIGLIILV DKLNRYLKPR LKLH // ID DMSA_HAEIN Reviewed; 806 AA. AC P45004; Q48048; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 124. DE RecName: Full=Dimethyl sulfoxide reductase DmsA; DE Short=DMSO reductase; DE Short=DMSOR; DE Short=Me2SO reductase; DE EC=1.8.5.3; DE Flags: Precursor; GN Name=dmsA; OrderedLocusNames=HI_1047; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B; RX PubMed=8635740; DOI=10.1016/0378-1119(95)00808-X; RA Loosmore S.M., Shortreed J.M., Coleman D.C., England D.M., Klein M.H.; RT "Sequences of the genes encoding the A, B and C subunits of the RT Haemophilus influenzae dimethylsulfoxide reductase complex."; RL Gene 169:137-138(1996). CC -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to CC dimethyl sulfide (DMS). The terminal DMSO reductase can also use CC various sulfoxides and N-oxide compounds as terminal electron CC acceptor in addition to DMSO (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Dimethylsulfide + menaquinone + H(2)O = CC dimethylsulfoxide + menaquinol. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer CC (DmsAB) and a membrane anchor protein (DmsC). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- MISCELLANEOUS: The Tat signal sequence is essential for the CC expression of dmsA, the stability of the dmsAB dimer and membrane CC targeting. Despite the presence of a signal sequence, dmsA is not CC exported to the periplasm (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22706.1; -; Genomic_DNA. DR EMBL; U26665; AAB06233.1; -; Genomic_DNA. DR PIR; G64109; G64109. DR RefSeq; NP_439206.1; NC_000907.1. DR RefSeq; WP_005693382.1; NC_000907.1. DR ProteinModelPortal; P45004; -. DR STRING; 71421.HI1047; -. DR EnsemblBacteria; AAC22706; AAC22706; HI_1047. DR GeneID; 950024; -. DR KEGG; hin:HI1047; -. DR PATRIC; 20190759; VBIHaeInf48452_1092. DR eggNOG; ENOG4107QY8; Bacteria. DR eggNOG; COG0243; LUCA. DR KO; K07306; -. DR OMA; FRQQGIF; -. DR OrthoDB; EOG6GFGF8; -. DR PhylomeDB; P45004; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR InterPro; IPR011888; Anaer_DMSO_reductase. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR019546; TAT_signal_bac_arc. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR02166; dmsA_ynfE; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane; KW Metal-binding; Molybdenum; Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1 35 Tat-type signal. {ECO:0000255|PROSITE- FT ProRule:PRU00648}. FT CHAIN 36 806 Dimethyl sulfoxide reductase DmsA. FT /FTId=PRO_0000019144. FT DOMAIN 47 109 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT REGION 163 167 MGD 1 binding. {ECO:0000250}. FT REGION 236 237 MGD 2 binding. {ECO:0000250}. FT REGION 262 263 MGD 2 binding. {ECO:0000250}. FT REGION 283 285 MGD 2 binding. {ECO:0000250}. FT REGION 378 379 MGD 2 binding. {ECO:0000250}. FT REGION 504 505 MGD 1 binding. {ECO:0000250}. FT REGION 693 693 MGD 1 binding. {ECO:0000250}. FT REGION 699 701 MGD 1 binding. {ECO:0000250}. FT REGION 796 797 MGD 1 binding. {ECO:0000250}. FT METAL 54 54 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 58 58 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 62 62 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 95 95 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 196 196 Molybdenum. {ECO:0000250}. FT BINDING 382 382 Molybdopterin guanine dinucleotide 1. FT {ECO:0000250}. FT BINDING 480 480 Molybdopterin guanine dinucleotide 1. FT {ECO:0000250}. FT BINDING 780 780 Molybdopterin guanine dinucleotide 1. FT {ECO:0000250}. FT VARIANT 140 140 D -> Y (in strain: Eagan). FT VARIANT 321 321 T -> A (in strain: Eagan). FT VARIANT 431 431 V -> M (in strain: Eagan). FT VARIANT 440 440 W -> G (in strain: Eagan). FT VARIANT 465 465 S -> P (in strain: Eagan). FT VARIANT 523 523 T -> P (in strain: Eagan). FT VARIANT 724 724 E -> K (in strain: Eagan). SQ SEQUENCE 806 AA; 90427 MW; F9F90E5EB250FFBF CRC64; MSNFNQISRR DFVKASSAGA ALAVSNLTLP FNVMAKETQR LNENNQERIV WSACTVNCGS RCPLRMHVKD NRITYVETDN TGTETYNLDH QVRACLRGRS MRRRVYNPDR LKYPMKRIGK RGEGKFKRIS WDEALTEIAD ALKRNIKKYG NESIYLNYGT GTLGGTMAKS WPPASTMIAR FMNCIGGYLN HYGDYSTAQI AVGLDYTYGG GWALGNGMAD IENTKLIVLF GNNPAETRMS GGGLTYCIEQ AKARSNAKMI IIDPRYNDTG AGREDEWIPI RPGTDAALVA ALAYVMIQEN LVDQPFLDKY CVGYDEKTLP TDAPKNGHYK AYILGYGNDG IAKTPEWAAK ITGIPAERII KLAREIGSTK PAFISQGWGP QRRSNGELIS RAIAMLPILT GNVGIHGGNT GARESAYSIP FVRMPTLKNP VKASIPMFLW TDAIIRGTEM TALTDGIRGV DKLSSPIKVI WNYASNCLIN QHAQINRTHD ILQDDTQCEM IITIDNHMTS TAKYSDILLP DCTTSEQMDF ALDAFVSNMA YVIFADQVIK PSFECRPIYD MLSDLAEKMG VKEKFTEGRT QEEWLRHIYE QSREKLPELP TFEEFRQQGI FKKVDPNGFK VAYKDFRDNP EAHPLKTPSG KIEIYSSRLA EIAKTWKLAE DDVIHPLPIH AQSFEHYGDP LMEKYPLQLS GFHYKARTHS TYGNVDVLKA ANPQEVWMNP IDAEPRNIKN GDMIRIFNDR GEVHINVKIT PRIIPGVVAL SEGAWYAPDK DRIDHSGCIN VLTTQRPSPL AKGNPQHSNL VQVERL // ID DNAK_HAEIN Reviewed; 635 AA. AC P43736; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 102. 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; OrderedLocusNames=HI_1237; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22889.1; -; Genomic_DNA. DR PIR; B64112; B64112. DR RefSeq; NP_439393.1; NC_000907.1. DR RefSeq; WP_005694297.1; NC_000907.1. DR ProteinModelPortal; P43736; -. DR SMR; P43736; 3-381, 388-604. DR STRING; 71421.HI1237; -. DR PRIDE; P43736; -. DR EnsemblBacteria; AAC22889; AAC22889; HI_1237. DR GeneID; 950188; -. DR KEGG; hin:HI1237; -. DR PATRIC; 20191153; VBIHaeInf48452_1289. DR eggNOG; ENOG4105CFG; Bacteria. DR eggNOG; COG0443; LUCA. DR KO; K04043; -. DR OMA; EKMAPPQ; -. DR OrthoDB; EOG6JMMSV; -. DR PhylomeDB; P43736; -. DR Proteomes; UP000000579; 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 SUPFAM; SSF100934; SSF100934; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 635 Chaperone protein DnaK. FT /FTId=PRO_0000078468. FT MOD_RES 198 198 Phosphothreonine; by autocatalysis. FT {ECO:0000250}. SQ SEQUENCE 635 AA; 68281 MW; 58167BFA0BA661C9 CRC64; MGKIIGIDLG TTNSCVAVMD GDKARVIENA EGARTTPSII AYTDNETLVG QPAKRQAITN PKNTLFAIKR LIGRRFESEE VQRDIKIMPF EITRADNGDA WVNVKGDKLA PPQISAEVLK KMKKTAEDFL GESVTEAVIT VPAYFNDAQR QATIDAGKIA GLDVKRIINE PTAAALAFGL GSSKENQVIA VYDLGGGTFD ISIIEIDNFD GEQTFEVLAT GGNTHLGGED FDNRVIDYII DEFKKEQNID LRNDAMALQR VKEAAEKAKI ELSSAQSTEV NLPYITADAT GPKHLALNIT RAKLEALVED LVASSIESLK AVLKDADKGV SEIHDIILVG GQTRMPLVQQ KVAEFFGKEA RKDVNPDEAV AIGAAVQGGV LKGDVKDVLL LDVTPLSLGI ETMGGVMTTL IEKNTTIPTK KSQVFSTAED NQSAVTIHVL QGERKRAADN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN GVINVSAKDK NTGKEQQIRI QASSGLSDEE IQQMVRDAEA NADADRKFEE VVQARNQADG IAHATRKQIA EAGDALSVAD KEKIEAAVAE LETAAKGEDK AEIEAKIEAV IKASEPLMQA VQAKAQQAGG EQPQQSSAKD DGVVDAEFEE VKDNK // ID DSBA_HAEIN Reviewed; 205 AA. AC P31810; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Thiol:disulfide interchange protein DsbA; DE Flags: Precursor; GN Name=dsbA; Synonyms=por; OrderedLocusNames=HI_0846; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1438213; DOI=10.1073/pnas.89.21.10252; RA Tomb J.-F.; RT "A periplasmic protein disulfide oxidoreductase is required for RT transformation of Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10252-10256(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in disulfide-bond formation. Required for HI CC transformation. Acts by transferring its disulfide bond to other CC proteins. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M94205; AAA24956.1; -; Genomic_DNA. DR EMBL; L42023; AAC22503.1; -; Genomic_DNA. DR PIR; B64098; B46411. DR RefSeq; NP_439006.1; NC_000907.1. DR RefSeq; WP_005693196.1; NC_000907.1. DR ProteinModelPortal; P31810; -. DR STRING; 71421.HI0846; -. DR EnsemblBacteria; AAC22503; AAC22503; HI_0846. DR GeneID; 949506; -. DR KEGG; hin:HI0846; -. DR PATRIC; 20190347; VBIHaeInf48452_0887. DR eggNOG; ENOG4108Z33; Bacteria. DR eggNOG; COG0526; LUCA. DR KO; K03673; -. DR OMA; DKVSPLM; -. DR OrthoDB; EOG68Q0Q6; -. DR PhylomeDB; P31810; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR001853; DSBA-like_thioredoxin_dom. DR InterPro; IPR023205; DsbA/DsbL. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF01323; DSBA; 1. DR PIRSF; PIRSF001488; Tdi_protein; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Periplasm; Redox-active center; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 205 Thiol:disulfide interchange protein DsbA. FT /FTId=PRO_0000034260. FT DOMAIN 23 201 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 52 55 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 205 AA; 22964 MW; 37469B216976969C CRC64; MKKVLLALGL GVSTLMSVNS FAADLQEGKQ YVQVSQQASQ QKEVIEFFSF YCPHCYAFEM EYKIPQQVVD ALPKDVKFKQ YHVNFLGHQS ENLTRAWALA MALGAESKVK SPLFEAAQKD ALKSMDDIRA IFLSNGITAE QFDGGINSFA VNGLVNKQVN AAEQFKVRGV PDFYVNGKFR VNPEGLNYDD FVKDYVQTVK GLLQK // ID DSBD_HAEIN Reviewed; 579 AA. AC P44919; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 126. DE RecName: Full=Thiol:disulfide interchange protein DsbD; DE EC=1.8.1.8; DE AltName: Full=C-type cytochrome biogenesis protein CycZ; DE AltName: Full=Protein-disulfide reductase; DE Short=Disulfide reductase; DE Flags: Precursor; GN Name=dsbD; Synonyms=cycZ; OrderedLocusNames=HI_0885; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required to facilitate the formation of correct CC disulfide bonds in some periplasmic proteins and for the assembly CC of the periplasmic c-type cytochromes. Acts by transferring CC electrons from cytoplasmic thioredoxin to the periplasm. This CC transfer involves a cascade of disulfide bond formation and CC reduction steps (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein CC disulfide + NAD(P)H. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin 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; L42023; AAC22543.1; -; Genomic_DNA. DR PIR; A64100; A64100. DR RefSeq; NP_439046.1; NC_000907.1. DR RefSeq; WP_005693234.1; NC_000907.1. DR ProteinModelPortal; P44919; -. DR SMR; P44919; 461-579. DR STRING; 71421.HI0885; -. DR EnsemblBacteria; AAC22543; AAC22543; HI_0885. DR GeneID; 950312; -. DR KEGG; hin:HI0885; -. DR PATRIC; 20190427; VBIHaeInf48452_0927. DR eggNOG; ENOG4105CSG; Bacteria. DR eggNOG; COG4232; LUCA. DR KO; K04084; -. DR OMA; QSAVENM; -. DR OrthoDB; EOG69D3B9; -. DR PhylomeDB; P44919; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central. DR GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0022865; F:transmembrane electron transfer carrier; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0017004; P:cytochrome complex assembly; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR Gene3D; 2.60.40.1250; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00399; DbsD; 1. DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom. DR InterPro; IPR028250; DsbDN. DR InterPro; IPR022910; Thiol_diS_interchange_DbsD. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1. DR Pfam; PF11412; DsbC; 1. DR Pfam; PF02683; DsbD; 1. DR Pfam; PF13098; Thioredoxin_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF74863; SSF74863; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Disulfide bond; Electron transport; KW Membrane; NAD; Oxidoreductase; Redox-active center; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 579 Thiol:disulfide interchange protein DsbD. FT /FTId=PRO_0000007376. FT TOPO_DOM 17 177 Periplasmic. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255}. FT TOPO_DOM 199 229 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 253 Periplasmic. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT TOPO_DOM 275 295 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TOPO_DOM 317 336 Periplasmic. {ECO:0000255}. FT TRANSMEM 337 357 Helical. {ECO:0000255}. FT TOPO_DOM 358 367 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 368 388 Helical. {ECO:0000255}. FT TOPO_DOM 389 396 Periplasmic. {ECO:0000255}. FT TRANSMEM 397 417 Helical. {ECO:0000255}. FT TOPO_DOM 418 419 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 420 440 Helical. {ECO:0000255}. FT TOPO_DOM 441 579 Periplasmic. {ECO:0000255}. FT DOMAIN 449 579 Thioredoxin. FT DISULFID 124 129 Redox-active. {ECO:0000250}. FT DISULFID 193 315 Redox-active. {ECO:0000250}. FT DISULFID 495 498 Redox-active. {ECO:0000250}. SQ SEQUENCE 579 AA; 64406 MW; 2D2D1359E2246310 CRC64; MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDIADGYYL YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGAF NNADDKVEIT YQGCTEGFCY PPETKVLRIG DLVVSQKQIV EKTVEKNTAL LSEQDRLADG LFHSKWAIFG FFVLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA AIGLPFQIAL QHPYVMIGLS ILFVALALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAVTL YLLALGMGVP LMLITLFGNK ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWEPRL WAGLATVFFI WFALQMSKNG FGYAIKIISF ALAMVTVQPL QNWIWQTQTT TQSAVENMPV SQVKFKQIKN TEELDRTLAE NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVSMTKNSP ENKALMERFN VMGLPTILFF DQQNNEIKGS RVTGFMDADA FSNWIEKLL // ID DJLA_HAEIN Reviewed; 288 AA. AC P44607; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Co-chaperone protein DjlA {ECO:0000255|HAMAP-Rule:MF_01153}; GN Name=djlA {ECO:0000255|HAMAP-Rule:MF_01153}; GN OrderedLocusNames=HI_0271; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Regulatory DnaK co-chaperone. Direct interaction between CC DnaK and DjlA is needed for the induction of the wcaABCDE operon, CC involved in the synthesis of a colanic acid polysaccharide CC capsule, possibly through activation of the RcsB/RcsC CC phosphotransfer signaling pathway. The colanic acid capsule may CC help the bacterium survive conditions outside the host. CC {ECO:0000255|HAMAP-Rule:MF_01153}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01153}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01153}; Single-pass type III membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01153}. CC -!- DOMAIN: The transmembrane domain is a dimerization domain. CC {ECO:0000255|HAMAP-Rule:MF_01153}. CC -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|HAMAP- CC Rule:MF_01153}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21937.1; -; Genomic_DNA. DR PIR; G64146; G64146. DR RefSeq; NP_438440.1; NC_000907.1. DR RefSeq; WP_005694031.1; NC_000907.1. DR ProteinModelPortal; P44607; -. DR STRING; 71421.HI0271; -. DR EnsemblBacteria; AAC21937; AAC21937; HI_0271. DR GeneID; 949410; -. DR KEGG; hin:HI0271; -. DR PATRIC; 20189069; VBIHaeInf48452_0286. DR eggNOG; ENOG41066UG; Bacteria. DR eggNOG; COG1076; LUCA. DR KO; K05801; -. DR OMA; MQYWGKL; -. DR OrthoDB; EOG64BQ7P; -. DR PhylomeDB; P44607; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 1.10.3680.10; -; 2. DR HAMAP; MF_01153; DjlA; 1. DR InterPro; IPR023749; DjlA. DR InterPro; IPR007791; DjlA_N. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR029024; TerB-like. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF05099; TerB; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 288 Co-chaperone protein DjlA. FT /FTId=PRO_0000209429. FT TOPO_DOM 1 6 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01153}. FT TRANSMEM 7 30 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01153}. FT TOPO_DOM 31 288 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01153}. FT DOMAIN 222 288 J. {ECO:0000255|HAMAP-Rule:MF_01153}. SQ SEQUENCE 288 AA; 32523 MW; 6A7AA5879078DF81 CRC64; MEFIGKIIGV FLGWKVGGFF GAIAGLILGS IADKKLYELG SVSSSFFKKK TTRQDLFMQT SFAVLGHLSK SKGRVTEEDI QLANQLMIQL KLDDAGRKLA QDAFRRGKES DFPIRQVIRE FRIGCGQRAD LLRMFLQVQV QAAFADSELH ENEKEVLYVI AEELGLSRMQ FEQMIAMEMA ARAFTQGGFY QKYQQGAYQG GYQYQQQNSG GYQHASGPTL NDAYKVLGVT ESDEQSTVKR AYRRLMNEHH PDKLVAKGLP PEMMEMAKEK TQQIQAAYDL ICKAKGWK // ID DKSA_HAEIN Reviewed; 145 AA. AC P43758; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=RNA polymerase-binding transcription factor DksA {ECO:0000255|HAMAP-Rule:MF_00926}; GN Name=dksA {ECO:0000255|HAMAP-Rule:MF_00926}; Synonyms=dsh-1; GN OrderedLocusNames=HI_0062; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67. RC STRAIN=BC200; RX PubMed=8063112; DOI=10.1016/0378-1119(94)90840-0; RA Clifton S.W., McCarthy D., Roe B.A.; RT "Sequence of the rec-2 locus of Haemophilus influenzae: homologies to RT comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli."; RL Gene 146:95-100(1994). CC -!- FUNCTION: Transcription factor that acts by binding directly to CC the RNA polymerase (RNAP). Required for negative regulation of CC rRNA expression and positive regulation of several amino acid CC biosynthesis promoters. Also required for regulation of fis CC expression. {ECO:0000255|HAMAP-Rule:MF_00926}. CC -!- SUBUNIT: Interacts directly with the RNA polymerase. CC {ECO:0000255|HAMAP-Rule:MF_00926}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00926}. CC -!- SIMILARITY: Belongs to the DksA family. {ECO:0000255|HAMAP- CC Rule:MF_00926}. CC -!- SIMILARITY: Contains 1 dksA C4-type zinc finger. CC {ECO:0000255|HAMAP-Rule:MF_00926}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21740.1; -; Genomic_DNA. DR EMBL; L20805; AAC13732.1; -; Genomic_DNA. DR PIR; A64046; A64046. DR RefSeq; NP_438235.1; NC_000907.1. DR RefSeq; WP_005630220.1; NC_000907.1. DR ProteinModelPortal; P43758; -. DR SMR; P43758; 4-145. DR STRING; 71421.HI0062; -. DR PRIDE; P43758; -. DR DNASU; 950956; -. DR EnsemblBacteria; AAC21740; AAC21740; HI_0062. DR GeneID; 950956; -. DR KEGG; hin:HI0062; -. DR PATRIC; 20188577; VBIHaeInf48452_0062. DR eggNOG; ENOG4105SVQ; Bacteria. DR eggNOG; COG1734; LUCA. DR KO; K06204; -. DR OMA; AQERHEK; -. DR OrthoDB; EOG6JDWD6; -. DR PhylomeDB; P43758; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00926; DksA; 1. DR InterPro; IPR012784; DksA_RNA_pol-bd. DR InterPro; IPR000962; Znf_DskA_TraR. DR InterPro; IPR020458; Znf_DskA_TraR_CS. DR Pfam; PF01258; zf-dskA_traR; 1. DR TIGRFAMs; TIGR02420; dksA; 1. DR PROSITE; PS01102; ZF_DKSA_1; 1. DR PROSITE; PS51128; ZF_DKSA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Metal-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 145 RNA polymerase-binding transcription FT factor DksA. FT /FTId=PRO_0000187546. FT ZN_FING 108 132 dksA C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00926}. FT METAL 108 108 Zinc. {ECO:0000255|HAMAP-Rule:MF_00926}. FT METAL 111 111 Zinc. {ECO:0000255|HAMAP-Rule:MF_00926}. FT METAL 129 129 Zinc. {ECO:0000255|HAMAP-Rule:MF_00926}. FT METAL 132 132 Zinc. {ECO:0000255|HAMAP-Rule:MF_00926}. SQ SEQUENCE 145 AA; 16864 MW; ABF3EDB3CCE2733F CRC64; MSRASLSLLD LAGVKPYQMK KDEEYMNEEQ ILHFRKILNA WHEQIVEEAS RTVAHMQDEV TNFPDPADRA TQEEEFSLEL RNRDRERKLM KKIEATLKKL DTDDFGYCDC CGEEIGIRRL EARPTADLCI DCKTLAEIRE KQVAG // ID DNAJ_HAEIN Reviewed; 382 AA. AC P43735; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 113. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=HI_1238; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC22890.1; 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; L42023; AAC22890.1; ALT_INIT; Genomic_DNA. DR PIR; C64112; C64112. DR RefSeq; NP_439394.1; NC_000907.1. DR ProteinModelPortal; P43735; -. DR SMR; P43735; 2-78. DR STRING; 71421.HI1238; -. DR EnsemblBacteria; AAC22890; AAC22890; HI_1238. DR GeneID; 950178; -. DR KEGG; hin:HI1238; -. DR PATRIC; 20191155; VBIHaeInf48452_1290. DR eggNOG; ENOG4105BZ5; Bacteria. DR eggNOG; COG0484; LUCA. DR KO; K03686; -. DR OMA; IKDPCNS; -. DR OrthoDB; EOG6BPDKP; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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 1 382 Chaperone protein DnaJ. FT /FTId=PRO_0000070794. FT DOMAIN 5 70 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 147 154 CXXCXGXG motif. FT REPEAT 164 171 CXXCXGXG motif. FT REPEAT 186 193 CXXCXGXG motif. FT REPEAT 200 207 CXXCXGXG motif. FT ZN_FING 134 212 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 77 117 Gly-rich. FT METAL 147 147 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 150 150 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 164 164 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 167 167 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 186 186 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 189 189 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 200 200 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 203 203 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 382 AA; 41222 MW; 8850B88B6FB2BC2B CRC64; MAKKDYYEVL GLQKGASEDE IKRAYKRLAS KHHPDKNQGS KEAEEKFKEI NEAYEVLGDD QKRAAYDQYG HAAFEQGGGA GGFGGGFGGA DFGDMFGDIF GDIFGGGGRG RQRVVRGEDL RYDLEISLEE AVKGTTKDIQ INTLAHCDSC GGSGAEKGSK VETCPHCHGS GRIRRQQGFF VSESICPTCH GSGKKIEKPC RNCHGEGRVH KKENLSVKIP AGVDTGNQLR LAGKGAAGEN GAPAGDLYVV IHVREHNIFE RDGSNLYCEV PISFATAALG GEIEVPTLDG RVKLKIPAET QTGKLFRMRG KGVASTRSGY AGDLICRIVV ETPVNLTSEQ KELLHKLEES LQGKDLSKHA PKSSGFLDGV KKFFDNLGKS DK // ID DNLI_HAEIN Reviewed; 268 AA. AC P44121; P44122; P71371; P71372; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 07-JAN-2015, entry version 93. DE RecName: Full=DNA ligase; DE EC=6.5.1.1; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP]; GN Name=ligA; OrderedLocusNames=HI_1182/HI_1183; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP CHARACTERIZATION. RX PubMed=9060431; DOI=10.1093/nar/25.7.1369; RA Cheng C., Shuman S.; RT "Characterization of an ATP-dependent DNA ligase encoded by RT Haemophilus influenzae."; RL Nucleic Acids Res. 25:1369-1374(1997). CC -!- FUNCTION: Catalyzes efficient strand joining on a single nicked CC DNA. CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + diphosphate + CC (deoxyribonucleotide)(n+m). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000305}. CC -!- CAUTION: Was originally proposed to code for two separate adjacent CC ORFs, HI_1182 and HI_1183. {ECO:0000305|PubMed:7542800}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22836.1; Type=Frameshift; Positions=183; Evidence={ECO:0000305}; CC Sequence=AAC22846.1; Type=Frameshift; Positions=183; 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; U17295; AAA95982.1; -; Genomic_DNA. DR EMBL; L42023; AAC22836.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC22846.1; ALT_FRAME; Genomic_DNA. DR PIR; D64021; D64021. DR PIR; E64021; E64021. DR ProteinModelPortal; P44121; -. DR EnsemblBacteria; AAC22836; AAC22836; HI_1182. DR EnsemblBacteria; AAC22846; AAC22846; HI_1183. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR029319; DNA_ligase_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF14743; DNA_ligase_OB_2; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 268 DNA ligase. FT /FTId=PRO_0000059625. FT ACT_SITE 41 41 N6-AMP-lysine intermediate. FT {ECO:0000255}. FT BINDING 111 111 ATP. {ECO:0000255}. FT BINDING 181 181 ATP. {ECO:0000255}. FT BINDING 187 187 ATP. {ECO:0000255}. FT CONFLICT 93 93 T -> S (in Ref. 2; AAC22836). FT {ECO:0000305}. SQ SEQUENCE 268 AA; 30896 MW; F9EF9DD95B6B1252 CRC64; MKFYRTLLLF FASSFAFANS DLMLLHTYNN QPIEGWVMSE KLDGVRGYWN GKQLLTRQGQ RLSPPAYFIK DFPPFAIDGE LFSERNHFEE ISTITKSFKG DGWEKLKLYV FDVPDAEGNL FERLAKLKAH LLEHPTTYIE IIEQIPVKDK THLYQFLAQV ENLQGEGVVV RNPNAPYERK RSSQILKLKT ARGEECTVIA HHKGKGQFEN VMGALTCKNH RGEFKIGSGF NLNERENPPP IGSVITYKYR GITNSGKPRF ATYWREKK // ID DPO3A_HAEIN Reviewed; 1159 AA. AC P43743; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=DNA polymerase III subunit alpha; DE EC=2.7.7.7; GN Name=dnaE; OrderedLocusNames=HI_0739; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22399.1; -; Genomic_DNA. DR PIR; H64089; H64089. DR RefSeq; NP_438899.1; NC_000907.1. DR RefSeq; WP_005693144.1; NC_000907.1. DR ProteinModelPortal; P43743; -. DR SMR; P43743; 3-911. DR STRING; 71421.HI0739; -. DR EnsemblBacteria; AAC22399; AAC22399; HI_0739. DR GeneID; 949766; -. DR KEGG; hin:HI0739; -. DR PATRIC; 20190121; VBIHaeInf48452_0776. DR eggNOG; ENOG4105C0B; Bacteria. DR eggNOG; COG0587; LUCA. DR KO; K02337; -. DR OMA; DFCMDGR; -. DR OrthoDB; EOG6CZQGR; -. DR PhylomeDB; P43743; -. DR Proteomes; UP000000579; 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 Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR011708; DNA_pol3_alpha. DR InterPro; IPR029460; DNAPol_HHH. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. 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; PF14579; HHH_6; 1. DR Pfam; PF02811; PHP; 1. DR Pfam; PF01336; tRNA_anti-codon; 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 1159 DNA polymerase III subunit alpha. FT /FTId=PRO_0000103322. SQ SEQUENCE 1159 AA; 129789 MW; 21F09BE45A3DCE48 CRC64; MSSQPRFIHL RTHTDFSMID SIVKVKPLVK ACAANEMVAM GLTDFTNFCG VVSFYSEMLS SGMKPIIGAD VKVKSPLCGD EYFDLTLLAK NNEGYRNITL LLSKAYQRGY NDLPYIDQDW LIEHRDGVII LSGGTQGDVG KKLLKENVAE IESAVAFYQE FFADHFYLAL SRTGRPNEER YIQAALKLAE RCDLPLVATN DVMFLNTEDF EAHEIRVAIH DGYTLDDPKR PKCYTSQQYF RSEEDMCKLF ADIPSALENT LLIAQRCSVT LRLGQYFLPQ FPTGDLSTED FLVQKSKEGL EERLVFLFPD EKVRLEKRPK YDERLQVELD VINQMGFPGY FLIVMEFIQW SKDNDIPVGP GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMDG RDRVIEHVAE TYGRGAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPDPGMT LAKAFETEPQ LQTAYDSDEE VRALINMARK LEGVTRNAGK HAGGVVISPT LITDFAPLYC DNEGLHPVTH FDKNDVEYAG LVKFDFLGLR TLTIIKWALD IINVRMVREG KPRVDIAAIP LDDPESFELL KRSETTAVFQ LESRGMKDLI KRLQPDCFED IIALVALFRP GPLQSGMVDN FIDRKHGREE VSYPDAEYQH ASLKPILEPT YGIILYQEQV MQIAQVLAGY TLGGADLLRR AMGKKKPEEM AKQRLVFKEG AEKNGIDGEL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKTHFPA EFMAAVMTSE MDNTDKIVGL YDECLRMGLK VTPPDINIGK HHFSVNEQGE IVYGIGAIKG VGEGPIEALV AARNEGGIFK DLFDLCARVD LKKINRRTFE SLIMSGAFDK LGPHRAALSK NLEDALRASD QHAKDEAMGQ TDMFGVLTET HEDVENAYAN TPPYTEKQIL DGERETLGLY LSSHPVSRYL KELSHYTSTR LKDLAPNRRG QISTVAGLVV ASRIAMTKKG NRLGIATLDD RSGRLDLTLF GESLEQFGEK LQKDTVIVAS GQVSFDDFSG GLKMTVRELM TLDEARSRYV KSLAISLSEH QITPSFIKQF KALLEPVSGG TLPINVYYQS PKGRALLRLG VQWSIIPTDE ILTELVNLLG ESAVELEFE // ID DPO3X_HAEIN Reviewed; 688 AA. AC P43746; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=DNA polymerase III subunit tau/gamma; DE EC=2.7.7.7; GN Name=dnaX; OrderedLocusNames=HI_1229; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- 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 -!- MISCELLANEOUS: As has been shown for E.coli (strain K12) and CC suggested for Salmonella typhimurium, the gamma subunit CC (approximately resides 1-430) might be generated by ribosomal CC frameshifting, leading to 2 protein products from 1 gene. CC -!- SIMILARITY: Belongs to the DnaX/STICHEL 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; L42023; AAC22882.1; -; Genomic_DNA. DR PIR; F64111; F64111. DR RefSeq; NP_439385.1; NC_000907.1. DR RefSeq; WP_005694291.1; NC_000907.1. DR ProteinModelPortal; P43746; -. DR SMR; P43746; 3-364. DR STRING; 71421.HI1229; -. DR EnsemblBacteria; AAC22882; AAC22882; HI_1229. DR GeneID; 950174; -. DR KEGG; hin:HI1229; -. DR PATRIC; 20191137; VBIHaeInf48452_1281. DR eggNOG; ENOG4107QMP; Bacteria. DR eggNOG; COG2812; LUCA. DR KO; K02343; -. DR OMA; FFYQVIV; -. DR OrthoDB; EOG6WQD76; -. DR PhylomeDB; P43746; -. DR Proteomes; UP000000579; 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:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR022754; DNA_pol_III_gamma-3. DR InterPro; IPR012763; DNA_pol_III_sug/sutau. DR InterPro; IPR021029; DNA_pol_III_tau_dom-5. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF12169; DNA_pol3_gamma3; 1. DR Pfam; PF12170; DNA_pol3_tau_5; 1. 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 1 688 DNA polymerase III subunit tau/gamma. FT /FTId=PRO_0000105493. FT NP_BIND 45 52 ATP. {ECO:0000255}. SQ SEQUENCE 688 AA; 77042 MW; DD3401A54C6C9A6F CRC64; MSYQVLARKW RPKTFADVVG QEHIITALAN GLKDNRLHHA YLFSGTRGVG KTSIARLFAK GLNCVHGVTA TPCGECENCK AIEQGNFIDL IEIDAASRTK VEDTRELLDN VQYKPVVGRF KVYLIDEVHM LSRHSFNALL KTLEEPPEYV KFLLATTDPQ KLPVTILSRC LQFHLKALDE TQISQHLAHI LTQENIPFED PALVKLAKAA QGSIRDSLSL TDQAIAMGDR QVTNNVVSNM LGLLDDNYSV DILYALHQGN GELLMRTLQR VADAAGDWDK LLGECAEKLH QIALMQLLPQ KSSDNNEHFS FLAKHISPEN VQFFYQVIVS GRKDLSNAPN RRIGAEMTLL RALAFHPKFL TAVPKANTTI TPPPSTPSAV ENTGNYVDVP VLSQSIKSAY SQAKPNKTSI PNLASLSALD ALEHLTQLEN QERQEHKAES LAVVSETLHH IQELDEEKSH KKMTALPVRE MTEPKPKHIE KPTLPSNAAQ APQKNSTEEN SSDDNVEIAQ DEQEILSADT YRWEWSNPEL AKADTGVCPS DIKQAILKDI TPELRLKIIT QTQQQDQWAD IVERSGLTGF SKELALNCFL QSKTDDEINL GLHSEKSHLR QDRSIKNLAE ALSKLQGKDI RLTINLDDSN VTTPIEYRRN IYQALREKAQ NELQKDSKLQ ILLNEFDAKL DVESIRPV // ID DTD_HAEIN Reviewed; 144 AA. AC P44814; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518}; DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase; GN Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518}; OrderedLocusNames=HI_0670; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS). RX PubMed=12571243; DOI=10.1074/jbc.M213150200; RA Lim K., Tempczyk A., Bonander N., Toedt J., Howard A., Eisenstein E., RA Herzberg O.; RT "A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the RT crystal structure of Hemophilus influenzae HI0670."; RL J. Biol. Chem. 278:13496-13502(2003). CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate CC specificity. By recycling D-aminoacyl-tRNA to D-amino acids and CC free tRNA molecules, this enzyme counteracts the toxicity CC associated with the formation of D-aminoacyl-tRNA entities in CC vivo. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid + CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00518}. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518, CC ECO:0000305}. CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP- CC Rule:MF_00518, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22330.1; -; Genomic_DNA. DR PIR; E64156; E64156. DR RefSeq; NP_438830.1; NC_000907.1. DR RefSeq; WP_005694618.1; NC_000907.1. DR PDB; 1J7G; X-ray; 1.64 A; A=1-144. DR PDBsum; 1J7G; -. DR ProteinModelPortal; P44814; -. DR SMR; P44814; 1-144. DR STRING; 71421.HI0670; -. DR EnsemblBacteria; AAC22330; AAC22330; HI_0670. DR GeneID; 949713; -. DR KEGG; hin:HI0670; -. DR PATRIC; 20189957; VBIHaeInf48452_0700. DR eggNOG; ENOG4108YYA; Bacteria. DR eggNOG; COG1490; LUCA. DR KO; K07560; -. DR OMA; VFGADMK; -. DR OrthoDB; EOG6C2WM2; -. DR PhylomeDB; P44814; -. DR BRENDA; 3.1.1.96; 2529. DR EvolutionaryTrace; P44814; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IBA:GO_Central. DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GOC. DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central. DR Gene3D; 3.50.80.10; -; 1. DR HAMAP; MF_00518; Deacylase_Dtd; 1. DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD. DR InterPro; IPR023509; DTD-like_dom. DR PANTHER; PTHR10472; PTHR10472; 1. DR Pfam; PF02580; Tyr_Deacylase; 1. DR SUPFAM; SSF69500; SSF69500; 1. DR TIGRFAMs; TIGR00256; TIGR00256; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; KW Reference proteome. FT CHAIN 1 144 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_0000164546. FT ACT_SITE 80 80 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00518}. FT STRAND 2 15 {ECO:0000244|PDB:1J7G}. FT STRAND 18 32 {ECO:0000244|PDB:1J7G}. FT HELIX 39 51 {ECO:0000244|PDB:1J7G}. FT STRAND 62 64 {ECO:0000244|PDB:1J7G}. FT TURN 66 70 {ECO:0000244|PDB:1J7G}. FT STRAND 72 77 {ECO:0000244|PDB:1J7G}. FT HELIX 79 82 {ECO:0000244|PDB:1J7G}. FT HELIX 99 114 {ECO:0000244|PDB:1J7G}. FT STRAND 119 121 {ECO:0000244|PDB:1J7G}. FT STRAND 129 143 {ECO:0000244|PDB:1J7G}. SQ SEQUENCE 144 AA; 15862 MW; D8F84702EF5A3CBB CRC64; MIALIQRVSQ AKVDVKGETI GKIGKGLLVL LGVEKEDNRE KADKLAEKVL NYRIFSDEND KMNLNVQQAQ GELLIVSQFT LAADTQKGLR PSFSKGASPA LANELYEYFI QKCAEKLPVS TGQFAADMQV SLTNDGPVTF WLNV // ID DPO3E_HAEIN Reviewed; 256 AA. AC P43745; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=DNA polymerase III subunit epsilon; DE EC=2.7.7.7; GN Name=dnaQ; OrderedLocusNames=HI_0137; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme CC responsible for most of the replicative synthesis in bacteria. The CC epsilon subunit contain the editing function and is a proofreading CC 3'-5' exonuclease (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations. Magnesium or manganese. CC {ECO:0000250}; 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21808.1; -; Genomic_DNA. DR PIR; B64050; B64050. DR RefSeq; NP_438306.1; NC_000907.1. DR RefSeq; WP_010868942.1; NC_000907.1. DR ProteinModelPortal; P43745; -. DR STRING; 71421.HI0137; -. DR EnsemblBacteria; AAC21808; AAC21808; HI_0137. DR GeneID; 951047; -. DR KEGG; hin:HI0137; -. DR PATRIC; 20188765; VBIHaeInf48452_0139. DR eggNOG; ENOG4107RZZ; Bacteria. DR eggNOG; COG0847; LUCA. DR KO; K02342; -. DR OMA; FHVYLNP; -. DR OrthoDB; EOG696BTR; -. DR PhylomeDB; P43745; -. DR Proteomes; UP000000579; Chromosome. 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:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR006054; DnaQ. DR InterPro; IPR006309; DnaQ_proteo. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00573; dnaq; 1. DR TIGRFAMs; TIGR01406; dnaQ_proteo; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed DNA polymerase; KW Exonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 256 DNA polymerase III subunit epsilon. FT /FTId=PRO_0000105486. FT ACT_SITE 160 160 Proton acceptor. {ECO:0000250}. FT METAL 11 11 Divalent metal cation 1; catalytic. FT {ECO:0000250}. FT METAL 11 11 Divalent metal cation 2; catalytic. FT {ECO:0000250}. FT METAL 13 13 Divalent metal cation 1; catalytic. FT {ECO:0000250}. FT METAL 165 165 Divalent metal cation 1; catalytic. FT {ECO:0000250}. FT BINDING 11 11 Substrate. {ECO:0000250}. FT BINDING 13 13 Substrate. {ECO:0000250}. FT BINDING 60 60 Substrate. {ECO:0000250}. FT BINDING 65 65 Substrate. {ECO:0000250}. FT BINDING 165 165 Substrate. {ECO:0000250}. SQ SEQUENCE 256 AA; 29133 MW; 694C9273AD4438D1 CRC64; MINPNRQIVL DTETTGMNQL GAHYEGHCII EIGAVELINR RYTGNNXHIY IKPDRPXDPD AIKVHGITDE MLADKPEFKE VAQDFLDYIN GAELLIHNAP FDVGFMDYEF RKLNLNVKTD DICLVTDTLQ MARQMYPGKR NNLDALCDRL GIDNSKRTLH GALLDAEILA DVYLMMTGGQ TNLFDEEESV ESGVIRVMQE KTAEEIKSAV DFSHNLKLLQ PTNDELQAHL EFLKMMNKKS GNNCLWDKRF GNNNVH // ID DPPD_HAEIN Reviewed; 330 AA. AC P45095; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Dipeptide transport ATP-binding protein DppD; GN Name=dppD; OrderedLocusNames=HI_1185; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for dipeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22838.1; -; Genomic_DNA. DR EMBL; U17295; AAA95974.1; -; Genomic_DNA. DR PIR; F64188; F64188. DR RefSeq; NP_439341.1; NC_000907.1. DR RefSeq; WP_005694258.1; NC_000907.1. DR ProteinModelPortal; P45095; -. DR STRING; 71421.HI1185; -. DR TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22838; AAC22838; HI_1185. DR GeneID; 950137; -. DR KEGG; hin:HI1185; -. DR PATRIC; 20191047; VBIHaeInf48452_1236. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K12371; -. DR OMA; FPGRVMA; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45095; -. DR Proteomes; UP000000579; 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; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 330 Dipeptide transport ATP-binding protein FT DppD. FT /FTId=PRO_0000092315. FT DOMAIN 6 254 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 330 AA; 36328 MW; 964801E58D5656DE CRC64; MALLDVKELS VHFGDKKTPF KAVDRISYQV AQGEVLGIVG ESGSGKSVSS LAIMGLIDHP GRVSAESLQF ENTDLLTLES KAKRQLIGAD VAMIFQDPMT SLNPAYTVGF QIMEALKTHE GGTKKARKDR TLELLKLVGI PDPESRIDVY PHQLSGGMSQ RVMIAMAIAC RPKLLIADEP TTALDVTIQA QIMELLLELQ KKECMSLILI THDLALVAEA AERIIVMYAG QIVEEGTAKD IFREPKHPYT QALLRSLPEF AEGKSRLESL QGVVPGKYDR PTGCLLNPRC PYATEYCRQV EPQLHHIGSR KVKCHTPLNE QGNPVEYQGA // ID DSBB_HAEIN Reviewed; 177 AA. AC P44707; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Disulfide bond formation protein B {ECO:0000255|HAMAP-Rule:MF_00286}; DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00286}; GN Name=dsbB {ECO:0000255|HAMAP-Rule:MF_00286}; GN OrderedLocusNames=HI_0428; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for disulfide bond formation in some CC periplasmic proteins. Acts by oxidizing the DsbA protein. CC {ECO:0000255|HAMAP-Rule:MF_00286}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00286}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00286}. CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000255|HAMAP- CC Rule:MF_00286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22087.1; -; Genomic_DNA. DR PIR; C64067; C64067. DR RefSeq; NP_438589.1; NC_000907.1. DR RefSeq; WP_005693737.1; NC_000907.1. DR ProteinModelPortal; P44707; -. DR STRING; 71421.HI0428; -. DR PRIDE; P44707; -. DR EnsemblBacteria; AAC22087; AAC22087; HI_0428. DR GeneID; 950809; -. DR KEGG; hin:HI0428; -. DR PATRIC; 20189409; VBIHaeInf48452_0448. DR eggNOG; ENOG410635M; Bacteria. DR eggNOG; COG1495; LUCA. DR KO; K03611; -. DR OMA; RYLNQCS; -. DR OrthoDB; EOG6CCH7H; -. DR PhylomeDB; P44707; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1550.10; -; 1. DR HAMAP; MF_00286; DsbB; 1. DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC. DR InterPro; IPR022920; Disulphide_bond_form_DsbB. DR InterPro; IPR023380; DsbB-like_dom. DR Pfam; PF02600; DsbB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Disulfide bond; Electron transport; Membrane; Oxidoreductase; KW Redox-active center; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 177 Disulfide bond formation protein B. FT /FTId=PRO_0000059346. FT TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 15 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 32 49 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 50 65 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 66 72 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 73 90 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 91 145 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TRANSMEM 146 164 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT TOPO_DOM 165 177 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT DISULFID 41 44 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00286}. FT DISULFID 105 131 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00286}. SQ SEQUENCE 177 AA; 20443 MW; 84A83AFA2335EA3C CRC64; MLALLKQFSE KRFVWFLLAF SSLALESTAL YFQYGMGLQP CVLCVYERLA MIGLFVAGTI ALLQPRVFIL RLIALALGLF SSIKGLLISF RHLDLQMNPA PWKQCEFIPN FPETLPFHQW FPFIFNPTGS CNESQWSLFG LTMVQWLVVI FSLYVVILTL LLIAQVIKTR KQRRLFN // ID DUT_HAEIN Reviewed; 151 AA. AC P43792; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_00116}; DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00116}; DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00116}; DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00116}; GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00116}; OrderedLocusNames=HI_0954; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it CC produces dUMP, the immediate precursor of thymidine nucleotides CC and it decreases the intracellular concentration of dUTP so that CC uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP- CC Rule:MF_00116}. CC -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00116}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00116}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00116}. CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00116}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22615.1; -; Genomic_DNA. DR PIR; H64104; H64104. DR RefSeq; NP_439115.1; NC_000907.1. DR RefSeq; WP_005631431.1; NC_000907.1. DR ProteinModelPortal; P43792; -. DR SMR; P43792; 1-138. DR STRING; 71421.HI0954; -. DR EnsemblBacteria; AAC22615; AAC22615; HI_0954. DR GeneID; 949940; -. DR KEGG; hin:HI0954; -. DR PATRIC; 20190567; VBIHaeInf48452_0996. DR eggNOG; ENOG4108Z1K; Bacteria. DR eggNOG; COG0756; LUCA. DR KO; K01520; -. DR OMA; MVSAWNR; -. DR OrthoDB; EOG689HXK; -. DR PhylomeDB; P43792; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00116; dUTPase_bact; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR008180; dUTPase/dCTP_deaminase. DR InterPro; IPR008181; dUTPase_1. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR00576; dut; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Nucleotide metabolism; Reference proteome. FT CHAIN 1 151 Deoxyuridine 5'-triphosphate FT nucleotidohydrolase. FT /FTId=PRO_0000182867. FT REGION 70 72 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT REGION 87 89 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT BINDING 83 83 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00116}. FT BINDING 97 97 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00116}. SQ SEQUENCE 151 AA; 16445 MW; 78A45C50518FCDE2 CRC64; MKKIDVKILD SRIGNEFPLP TYATEGSAGL DLRALIDESF EIQPGETKLI PTGLSIYIAD PNLAAVILPR SGLGHKHGIV LGNLVGLIDS DYQGPLMVSM WNRGNEPFKI EVGDRIAQLV FVPVVQAEFN IVEDFQQTER GEGGFGHSGK Q // ID DUSB_HAEIN Reviewed; 330 AA. AC P44965; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000255|HAMAP-Rule:MF_02042}; DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02042}; GN Name=dusB {ECO:0000255|HAMAP-Rule:MF_02042}; GN OrderedLocusNames=HI_0979; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. {ECO:0000255|HAMAP- CC Rule:MF_02042}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil in tRNA + NAD(P)(+) = uracil CC in tRNA + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_02042}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02042}; CC -!- SIMILARITY: Belongs to the Dus family. DusB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02042}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22639.1; -; Genomic_DNA. DR PIR; C64163; C64163. DR RefSeq; NP_439142.1; NC_000907.1. DR RefSeq; WP_010869101.1; NC_000907.1. DR ProteinModelPortal; P44965; -. DR STRING; 71421.HI0979; -. DR EnsemblBacteria; AAC22639; AAC22639; HI_0979. DR GeneID; 949982; -. DR KEGG; hin:HI0979; -. DR PATRIC; 20190619; VBIHaeInf48452_1022. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR KO; K05540; -. DR OMA; WLFREIE; -. DR OrthoDB; EOG6VHZFQ; -. DR PhylomeDB; P44965; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central. DR Gene3D; 1.10.1200.80; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02042; DusB_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR032887; DusB. DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C. DR InterPro; IPR004652; tRNA_dU_NifR3. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00737; nifR3_yhdG; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase; KW Reference proteome; RNA-binding; tRNA processing; tRNA-binding. FT CHAIN 1 330 tRNA-dihydrouridine synthase B. FT /FTId=PRO_0000162089. FT NP_BIND 16 18 FMN. {ECO:0000255|HAMAP-Rule:MF_02042}. FT NP_BIND 200 202 FMN. {ECO:0000255|HAMAP-Rule:MF_02042}. FT NP_BIND 224 225 FMN. {ECO:0000255|HAMAP-Rule:MF_02042}. FT ACT_SITE 100 100 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02042}. FT BINDING 70 70 FMN. {ECO:0000255|HAMAP-Rule:MF_02042}. FT BINDING 139 139 FMN. {ECO:0000255|HAMAP-Rule:MF_02042}. SQ SEQUENCE 330 AA; 36765 MW; FB4B7265BD70E60B CRC64; MRIGSYQLRN RVLLAPMAGI TDQPFRRLCA YYGAGLTFSE MMSTNPQVWH TEKSKLRLAH SEDLGLNAVQ IAGSDPLEMA QAAAINVEYG AQIIDINMGC PAKKVNRKLA GSALLQFPDL VEKILREVVS AVNVPVTLKI RTGWDKSNRN CVQIGKIAEQ CGIQALTVHG RTRACLFEGE AEYDNIKAVK QAIAIPVIAN GDIDSARKAK FVLNYTGADA IMIGRAALGN PWLFQAVENL IEHNSISQMP SLKEKCGQIL RHIQELHQFY GEQKGYRIAR KHVAWYLQGI QPDSVFKQTF NAISDPKEQL IVLEDFFNLI LDKKNVRTTT // ID DUSC_HAEIN Reviewed; 310 AA. AC P44606; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000255|HAMAP-Rule:MF_02043}; DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02043}; DE AltName: Full=U16-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02043}; DE Short=U16-specific Dus {ECO:0000255|HAMAP-Rule:MF_02043}; DE AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000255|HAMAP-Rule:MF_02043}; GN Name=dusC {ECO:0000255|HAMAP-Rule:MF_02043}; GN OrderedLocusNames=HI_0270; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. Specifically modifies CC U16 in tRNAs. {ECO:0000255|HAMAP-Rule:MF_02043}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(16) in tRNA + NAD(P)(+) = CC uracil(16) in tRNA + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_02043}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02043}; CC -!- SIMILARITY: Belongs to the Dus family. DusC subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21936.1; -; Genomic_DNA. DR PIR; F64146; F64146. DR RefSeq; NP_438439.1; NC_000907.1. DR RefSeq; WP_005694032.1; NC_000907.1. DR ProteinModelPortal; P44606; -. DR STRING; 71421.HI0270; -. DR EnsemblBacteria; AAC21936; AAC21936; HI_0270. DR GeneID; 950625; -. DR KEGG; hin:HI0270; -. DR PATRIC; 20189067; VBIHaeInf48452_0285. DR eggNOG; ENOG4105FBT; Bacteria. DR eggNOG; COG0042; LUCA. DR KO; K05541; -. DR OMA; GYKPPAH; -. DR OrthoDB; EOG6VHZFQ; -. DR PhylomeDB; P44606; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02043; DusC_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR032886; DusC. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase; KW Reference proteome; RNA-binding; tRNA processing; tRNA-binding. FT CHAIN 1 310 tRNA-dihydrouridine(16) synthase. FT /FTId=PRO_0000162113. FT NP_BIND 7 9 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT NP_BIND 200 202 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT NP_BIND 224 225 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT ACT_SITE 98 98 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT BINDING 68 68 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT BINDING 139 139 FMN. {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 35 35 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 95 95 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT SITE 176 176 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT SITE 272 272 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 274 274 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02043}. FT SITE 279 279 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. FT SITE 295 295 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02043}. SQ SEQUENCE 310 AA; 35057 MW; 8393D56E26EB6409 CRC64; MRVILAPMQG VLDPFVRELL TEVNDYDLCI TEFVRVVDQL LPEKVFYRLC PELKNQGFTS SGTPVRVQLL GQHPKCLAEN AIRAIDLGSH GIDLNCGCPS KTVNGSNGGA ALLKQPELIY RATQALRRAV PSEFPVSVKV RLGWDDISQA FEIADAVEQG GATEITVHGR TKADGYRADR INWKKISEVR ERLSIPVIAN GEIWHWQDGQ DCLSQTGCQD LMVGRGALNI PNLSHVLKSN AEKMPWYEIQ KILQKYANVE NEYDSGFYHV ARIKQWLRYL NKEYNEANQV FDKIKTCQTA EDLKLRLNEK // ID DPPC_HAEIN Reviewed; 295 AA. AC P51000; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Dipeptide transport system permease protein DppC; GN Name=dppC; OrderedLocusNames=HI_1186; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for dipeptides; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22839.1; -; Genomic_DNA. DR EMBL; U17295; AAA95973.1; -; Genomic_DNA. DR RefSeq; NP_439342.1; NC_000907.1. DR RefSeq; WP_005653671.1; NC_000907.1. DR ProteinModelPortal; P51000; -. DR STRING; 71421.HI1186; -. DR TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22839; AAC22839; HI_1186. DR GeneID; 950114; -. DR KEGG; hin:HI1186; -. DR PATRIC; 20191049; VBIHaeInf48452_1237. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K12370; -. DR OMA; HNPAEQF; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P51000; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0042936; F:dipeptide transporter activity; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042938; P:dipeptide transport; IBA:GOC. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 295 Dipeptide transport system permease FT protein DppC. FT /FTId=PRO_0000060012. FT TRANSMEM 27 47 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 97 117 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 132 152 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 156 178 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 202 222 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 226 246 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 262 282 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 93 282 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 295 AA; 31840 MW; F0CBB8C8A7E4F2C0 CRC64; MSDTPLTFAP KTPLQEFWFY FKQNRGALIG LIFILIVALI SILAPYIAPF DPTEQNRTAL LLPPAWYEGG NPAYLLGTDD IGRDILSRII YGTRISVFAG FIIVLLSCAF GTSLGLISGY YGGVLDTIII RLIDIMLAIP NLLLTIVVVS ILEPSLANAT LAIAVVSIPS YVRLTRAAMM NEKNRDYVTS SKVAGAGILR LMFIVILPNC LAPLIVQMTM GISNAILELA TLGFLGIGAK PPTPELGTML SEARGFMQAA NWLVTIPGLV ILSLVLAFNL MGDGLRDALD PKLKQ // ID DSBC_HAEIN Reviewed; 229 AA. AC P45111; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Thiol:disulfide interchange protein DsbC; DE Flags: Precursor; GN Name=dsbC; Synonyms=xprA; OrderedLocusNames=HI_1213; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-229, SUBUNIT, AND RP DISULFIDE BOND. RX PubMed=15333920; DOI=10.1107/S0907444904014593; RA Zhang M., Monzingo A.F., Segatori L., Georgiou G., Robertus J.D.; RT "Structure of DsbC from Haemophilus influenzae."; RL Acta Crystallogr. D 60:1512-1518(2004). CC -!- FUNCTION: Required for disulfide bond formation in some CC periplasmic proteins. Acts by transferring its disulfide bond to CC other proteins and is reduced in the process. DsbC is reoxidized CC by a yet uncharacterized protein. Also acts as a disulfide CC isomerase (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15333920}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC 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; L42023; AAC22866.1; -; Genomic_DNA. DR PIR; E64110; E64110. DR RefSeq; NP_439369.1; NC_000907.1. DR RefSeq; WP_005647404.1; NC_000907.1. DR PDB; 1T3B; X-ray; 2.50 A; A=19-229. DR PDBsum; 1T3B; -. DR ProteinModelPortal; P45111; -. DR SMR; P45111; 20-228. DR STRING; 71421.HI1213; -. DR EnsemblBacteria; AAC22866; AAC22866; HI_1213. DR GeneID; 950655; -. DR KEGG; hin:HI1213; -. DR PATRIC; 20191105; VBIHaeInf48452_1265. DR eggNOG; ENOG4105T95; Bacteria. DR eggNOG; COG1651; LUCA. DR KO; K03981; -. DR OMA; KNEMIVY; -. DR OrthoDB; EOG632D3W; -. DR PhylomeDB; P45111; -. DR EvolutionaryTrace; P45111; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR Gene3D; 3.10.450.70; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N. DR InterPro; IPR009094; DiS-bond_isomerase_DsbC_N. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10411; DsbC_N; 1. DR Pfam; PF13098; Thioredoxin_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR SUPFAM; SSF54423; SSF54423; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Periplasm; KW Redox-active center; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000250}. FT CHAIN 19 229 Thiol:disulfide interchange protein DsbC. FT /FTId=PRO_0000034276. FT DISULFID 116 119 Redox-active. FT {ECO:0000269|PubMed:15333920}. FT TURN 21 23 {ECO:0000244|PDB:1T3B}. FT HELIX 24 28 {ECO:0000244|PDB:1T3B}. FT TURN 29 31 {ECO:0000244|PDB:1T3B}. FT STRAND 56 62 {ECO:0000244|PDB:1T3B}. FT TURN 73 75 {ECO:0000244|PDB:1T3B}. FT HELIX 81 90 {ECO:0000244|PDB:1T3B}. FT HELIX 91 95 {ECO:0000244|PDB:1T3B}. FT STRAND 96 99 {ECO:0000244|PDB:1T3B}. FT STRAND 105 112 {ECO:0000244|PDB:1T3B}. FT HELIX 117 123 {ECO:0000244|PDB:1T3B}. FT HELIX 126 131 {ECO:0000244|PDB:1T3B}. FT STRAND 134 140 {ECO:0000244|PDB:1T3B}. FT HELIX 149 159 {ECO:0000244|PDB:1T3B}. FT STRAND 160 162 {ECO:0000244|PDB:1T3B}. FT HELIX 163 171 {ECO:0000244|PDB:1T3B}. FT HELIX 184 195 {ECO:0000244|PDB:1T3B}. FT STRAND 202 204 {ECO:0000244|PDB:1T3B}. FT HELIX 217 226 {ECO:0000244|PDB:1T3B}. SQ SEQUENCE 229 AA; 25351 MW; AF0F08AFC0FD08E6 CRC64; MKKIFTALLC VAAANAMADD AAIKRKLQSF NISNIVIKSS PISGIKTAVT DQGILYVSED GKYLFEGKLY ELTNNGPVDV AGKILVDKLN SYKDEMIVYP AKNEKHVVTV FMDITCHYCH LLHQQLKEYN DLGITVRYLA FPRAGMNNQT AKQMEAIWTA KDPVFALNEA EKGNLPKEVK TPNIVKKHYE LGIQFGVRGT PSIVTSTGEL IGGYLKPADL LRALEETAQ // ID DPO1_HAEIN Reviewed; 930 AA. AC P43741; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=DNA polymerase I; DE Short=POL I; DE EC=2.7.7.7; GN Name=polA; OrderedLocusNames=HI_0856; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase CC exhibits 3' to 5' and 5' to 3' exonuclease activity. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: Single-chain monomer with multiple functions. CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 3'-5' exonuclease domain. {ECO:0000305}. 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; L42023; AAC22515.1; -; Genomic_DNA. DR PIR; E64098; E64098. DR RefSeq; NP_439016.1; NC_000907.1. DR RefSeq; WP_005693204.1; NC_000907.1. DR ProteinModelPortal; P43741; -. DR SMR; P43741; 329-930. DR STRING; 71421.HI0856; -. DR EnsemblBacteria; AAC22515; AAC22515; HI_0856. DR GeneID; 950729; -. DR KEGG; hin:HI0856; -. DR PATRIC; 20190367; VBIHaeInf48452_0897. DR eggNOG; ENOG4105C2M; Bacteria. DR eggNOG; COG0258; LUCA. DR eggNOG; COG0749; LUCA. DR KO; K02335; -. DR OMA; CFDTETT; -. DR OrthoDB; EOG6SJJH7; -. DR PhylomeDB; P43741; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central. DR GO; GO:0071897; P:DNA biosynthetic process; IBA:GOC. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR002562; 3'-5'_exonuclease_dom. DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N. DR InterPro; IPR020045; 5-3_exonuclease_C. DR InterPro; IPR002421; 5-3_exonuclease_N. DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS. DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom. DR InterPro; IPR018320; DNA_polymerase_1. DR InterPro; IPR002298; DNA_polymerase_A. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR Pfam; PF00476; DNA_pol_A; 1. DR Pfam; PF01612; DNA_pol_A_exo1; 1. DR PRINTS; PR00868; DNAPOLI. DR SMART; SM00474; 35EXOc; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SMART; SM00482; POLAc; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR TIGRFAMs; TIGR00593; pola; 1. DR PROSITE; PS00447; DNA_POLYMERASE_A; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA replication; KW DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; KW Nuclease; Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 930 DNA polymerase I. FT /FTId=PRO_0000101240. FT DOMAIN 1 327 5'-3' exonuclease. FT DOMAIN 328 520 3'-5' exonuclease. FT REGION 524 930 Polymerase. SQ SEQUENCE 930 AA; 103741 MW; 226654BB7CFF730B CRC64; MAQIATNPLV LVDGSSYLYR AFHAFPSLTN AAGEPTSAMY GVLNMLKSLI SQVQPTHIAV VFDAKGKTFR DEMFEQYKSH RPPMPDDLRK QIQPLHDMIR ALGIPLLVVE GIEADDVIGT LALQASSLGK KVLISTGDKD MAQLVDDNIM LINTMNNSLL DRKGVIEKYG IPPELIIDYL ALMGDSADNI PGVAGVGEKT ALGLLQGIGS MAEIYANLEK VAELPIRGAK KLGEKLLAEK NNADLSYTLA TIKTDVELNV TTDQLLLGES QKDQLIEYFA RYEFKRWLNE VMNGADSITQ TTEQPVKMNQ YKATSQDQSA VENTPKIQID RTKYETLLTQ ADLTRWIEKL NAAKLIAVDT ETDSLDYMSA NLVGISFALE NGEAAYLPLQ LDYLDAPKTL EKSTALAAIK PILENPNIHK IGQNIKFDES IFARHGIELQ GVEFDTMLLS YTLNSTGRHN MDDLAKRYLG HETIAFESLA GKGKSQLTFN QIPLEQATEY AAEDADVTMK LQQALWLKLQ EEPTLVELYK TMELPLLHVL SRMERTGVLI DSDALFMQSN EIASRLTALE KQAYALAGQP FNLASTKQLQ EILFDKLELP VLQKTPKGAP STNEEVLEEL SYSHELPKIL VKHRGLSKLK STYTDKLPQM VNSQTGRVHT SYHQAVTATG RLSSSDPNLQ NIPIRNEEGR HIRQAFIARE GYSIVAADYS QIELRIMAHL SGDQGLINAF SQGKDIHRST AAEIFGVSLD EVTSEQRRNA KAINFGLIYG MSAFGLSRQL GISRADAQKY MDLYFQRYPS VQQFMTDIRE KAKAQGYVET LFGRRLYLPD INSSNAMRRK GAERVAINAP MQGTAADIIK RAMIKLDEVI RHDPDIEMIM QVHDELVFEV RSEKVAFFRE QIKQHMEAAA ELVVPLIVEV GVGQNWDEAH // ID DXR_HAEIN Reviewed; 397 AA. AC P44055; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183}; GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=HI_0807; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction CC of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol CC 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00183}. CC -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) CC = 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22466.1; -; Genomic_DNA. DR PIR; A64014; A64014. DR RefSeq; NP_438967.1; NC_000907.1. DR RefSeq; WP_005693175.1; NC_000907.1. DR ProteinModelPortal; P44055; -. DR SMR; P44055; 4-392. DR STRING; 71421.HI0807; -. DR EnsemblBacteria; AAC22466; AAC22466; HI_0807. DR GeneID; 949821; -. DR KEGG; hin:HI0807; -. DR PATRIC; 20190269; VBIHaeInf48452_0848. DR eggNOG; ENOG4105CEA; Bacteria. DR eggNOG; COG0743; LUCA. DR KO; K00099; -. DR OMA; GFCPLSE; -. DR OrthoDB; EOG6R2H04; -. DR PhylomeDB; P44055; -. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central. DR GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00183; DXP_reductoisom; 1. DR InterPro; IPR003821; DXP_reductoisomerase. DR InterPro; IPR013644; DXP_reductoisomerase_C. DR InterPro; IPR013512; DXP_reductoisomerase_N. DR InterPro; IPR026877; DXPR_C. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR30525; PTHR30525; 1. DR Pfam; PF08436; DXP_redisom_C; 1. DR Pfam; PF02670; DXP_reductoisom; 1. DR Pfam; PF13288; DXPR_C; 1. DR PIRSF; PIRSF006205; Dxp_reductismrs; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69055; SSF69055; 1. DR TIGRFAMs; TIGR00243; Dxr; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Metal-binding; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 397 1-deoxy-D-xylulose 5-phosphate FT reductoisomerase. FT /FTId=PRO_0000163660. FT NP_BIND 9 38 NADP. {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 152 152 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 154 154 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT METAL 233 233 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00183}. FT BINDING 127 127 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 154 154 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 188 188 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 211 211 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. FT BINDING 233 233 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00183}. SQ SEQUENCE 397 AA; 43667 MW; A6E9B24CC6A1CEAA CRC64; MQKQNIVILG STGSIGKSTL SVIENNPQKY HAFALVGGKN VEAMFEQCIK FRPHFAALDD VNAAKILREK LIAHHIPTEV LAGRRAICEL AAHPDADQIM ASIVGAAGLL PTLSAVKAGK RVLLANKESL VTCGQLFIDA VKNYGSKLLP VDSEHNAIFQ SLPPEAQEKI GFCPLSELGV SKIILTGSGG PFRYTPLEQF TNITPEQAVA HPNWSMGKKI SVDSATMMNK GLEYIEARWL FNASAEEMEV IIHPQSIIHS MVRYVDGSVI TQMGNPDMRT PIAETMAYPH RTFAGVEPLD FFKIKELTFI EPDFNRYPNL KLAIDAFAAG QYATTAMNAA NEIAVQAFLD RQIGFMDIAK INSKTIERIS PYTIQNIDDV LEIDAQAREI AKTLLRE // ID DPPB_HAEIN Reviewed; 333 AA. AC P45096; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Dipeptide transport system permease protein DppB; GN Name=dppB; OrderedLocusNames=HI_1187; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for dipeptides; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22840.1; -; Genomic_DNA. DR EMBL; U17295; AAA95972.1; -; Genomic_DNA. DR PIR; G64188; G64188. DR RefSeq; NP_439343.2; NC_000907.1. DR ProteinModelPortal; P45096; -. DR STRING; 71421.HI1187; -. DR TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22840; AAC22840; HI_1187. DR GeneID; 950100; -. DR KEGG; hin:HI1187; -. DR PATRIC; 20191051; VBIHaeInf48452_1238. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K12369; -. DR OMA; LMLWTIV; -. DR OrthoDB; EOG66F098; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0042936; F:dipeptide transporter activity; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042938; P:dipeptide transport; IBA:GOC. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 333 Dipeptide transport system permease FT protein DppB. FT /FTId=PRO_0000060008. FT TRANSMEM 9 29 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 103 123 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 197 217 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 256 276 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 306 326 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 96 328 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 333 AA; 36788 MW; 57B3A0006CA6B3A7 CRC64; MFKFVFKRIL MVIPTFIAIT LITFALVHFI PGDPVEIMMG ERGLTAEVHQ QMMHQLGLDL PLYQQYFHYI GNVIQGDFGA SFRTQQPVLT EFFTLFPATA ELAFFALFWS LLGGIILGTI AAVKKDSWIS HTVTAASLTG YSMPIFWWGL ILILYVSPQL GLPQGGRLDN EFWIDTPTGF MLIDSWLSGV SGAFENAVKS LILPAIVLGT VPLAIITRMT RSAMLEVLGE DYIRTAKAKG LSYTRIVIVH ALRNALIPVV TVVGLIVAQL LSGAVLTETI FSWPGIGKWI IDAIQARDYP VLQGSVLIIA TIIIVVNLTV DLLYGVVNPR IRH // ID DPPF_HAEIN Reviewed; 327 AA. AC P45094; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Dipeptide transport ATP-binding protein DppF; GN Name=dppF; OrderedLocusNames=HI_1184; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for dipeptides. Probably responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22837.1; -; Genomic_DNA. DR EMBL; U17295; AAA95975.1; -; Genomic_DNA. DR PIR; E64188; E64188. DR RefSeq; NP_439340.1; NC_000907.1. DR RefSeq; WP_005691143.1; NC_000907.1. DR ProteinModelPortal; P45094; -. DR STRING; 71421.HI1184; -. DR TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22837; AAC22837; HI_1184. DR GeneID; 950622; -. DR KEGG; hin:HI1184; -. DR PATRIC; 20191045; VBIHaeInf48452_1235. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K12372; -. DR OMA; IACFMVE; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45094; -. DR Proteomes; UP000000579; 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; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 327 Dipeptide transport ATP-binding protein FT DppF. FT /FTId=PRO_0000092318. FT DOMAIN 12 261 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 54 61 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 327 AA; 36917 MW; 0BB0BBDE197DA9BE CRC64; MTNEVKENTP LLNAIGLKKY YPVKKGLFAK PQQVKALDGV SFQLERGKTL AVVGESGCGK STLGRLLTMI EEPTKGELYY KGHNFLENDS ETKALRRKKI QIVFQNPYAS LNPRKKIGSI LEEPLIINTK LSAKERREKV LSMMEKVGLR AEFYDRYPHM FSGGQRQRIA IARGLMLDPD VVVADEPVSA LDVSVRAQVL NLMMDLQDEL GLSYVFISHD LSVVEHIADE VMVMYLGRCI EKGTTEQIFS NPQHPYTKAL LSATPRLSPN LRRERIKLTG ELPSPINPPK GCAFNPRCWK ATEKCRENQP HLEQHTDGKL IACFHID // ID DSBE_HAEIN Reviewed; 181 AA. AC P45038; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Thiol:disulfide interchange protein DsbE; DE AltName: Full=Cytochrome c biogenesis protein CcmG; GN Name=dsbE; Synonyms=ccmG; OrderedLocusNames=HI_1095; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in disulfide bond formation. Catalyzes a late, CC reductive step in the assembly of periplasmic c-type cytochromes, CC probably the reduction of disulfide bonds of the apocytochrome c CC to allow covalent linkage with the heme. Possible subunit of a CC heme lyase (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}; Periplasmic side CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22752.1; -; Genomic_DNA. DR PIR; B64167; B64167. DR RefSeq; NP_439252.1; NC_000907.1. DR RefSeq; WP_005657352.1; NC_000907.1. DR ProteinModelPortal; P45038; -. DR SMR; P45038; 54-181. DR STRING; 71421.HI1095; -. DR EnsemblBacteria; AAC22752; AAC22752; HI_1095. DR GeneID; 950067; -. DR KEGG; hin:HI1095; -. DR PATRIC; 20190855; VBIHaeInf48452_1140. DR eggNOG; ENOG4107QX9; Bacteria. DR eggNOG; COG0526; LUCA. DR KO; K02199; -. DR OMA; KWLAEFH; -. DR OrthoDB; EOG6WX4Q5; -. DR PhylomeDB; P45038; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00385; dsbE; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Disulfide bond; Membrane; KW Redox-active center; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 181 Thiol:disulfide interchange protein DsbE. FT /FTId=PRO_0000201295. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 5 23 Helical. {ECO:0000255}. FT TOPO_DOM 24 181 Periplasmic. {ECO:0000255}. FT DOMAIN 38 175 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 78 81 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 181 AA; 20535 MW; 4B334B444179EF24 CRC64; MKKKLLVPLI LFLSITIAFL VQLKRNAQGE DIKALESALV GKPVPAKNLT ELFENKTYTN ELFQQGEPVL LNVWATWCPT CYAEHQYLNK LAKEGVRIIG LDYKDESPKA MKWLKDLGNP YQVVLKDEKG SFGLDLGVYG APETFIVDGK GVIHYRYAGD VNEKVWTQTL KPIYDKLSEQ Q // ID EFP_HAEIN Reviewed; 188 AA. AC P43771; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 110. DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141}; DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141}; GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141}; OrderedLocusNames=HI_0328; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome CC stalling that occurs when 3 or more consecutive Pro residues or CC the sequence PPG is present in a protein, possibly by augmenting CC the peptidyl transferase activity of the ribosome. Modification of CC Lys-34 is required for alleviation. {ECO:0000255|HAMAP- CC Rule:MF_00141}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- PTM: Is beta-lysylated on the epsilon-amino group of Lys-34 by the CC combined action of EpmA and EpmB, and then hydroxylated on the C5 CC position of the same residue by EpmC. Lysylation is critical for CC the stimulatory effect of EF-P on peptide-bond formation. The CC lysylation moiety would extend toward the peptidyltransferase CC center and stabilize the terminal 3-CCA end of the tRNA. The CC hydroxylation of the C5 position on Lys-34 would allow additional CC potential stabilizing hydrogen-bond interactions with the P-tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21989.1; -; Genomic_DNA. DR PIR; I64061; I64061. DR RefSeq; NP_438492.3; NC_000907.1. DR RefSeq; WP_005544066.1; NC_000907.1. DR ProteinModelPortal; P43771; -. DR STRING; 71421.HI0328; -. DR EnsemblBacteria; AAC21989; AAC21989; HI_0328. DR GeneID; 949790; -. DR KEGG; hin:HI0328; -. DR PATRIC; 20189199; VBIHaeInf48452_0345. DR eggNOG; ENOG4105DRH; Bacteria. DR eggNOG; COG0231; LUCA. DR KO; K02356; -. DR OMA; DYVFMDM; -. DR OrthoDB; EOG6JQH6Q; -. DR PhylomeDB; P43771; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000000579; 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; Hydroxylation; KW Protein biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 188 Elongation factor P. FT /FTId=PRO_0000094258. FT MOD_RES 34 34 N6-(3,6-diaminohexanoyl)-5-hydroxylysine. FT {ECO:0000255|HAMAP-Rule:MF_00141}. SQ SEQUENCE 188 AA; 20612 MW; A79E202E5EA8DD35 CRC64; MATYTTSDFK PGLKFMQDGE PCVIVENEFV KPGKGQAFTR TRIRKLISGK VLDVNFKSGT SVEAADVMDL NLTYSYKDDA FWYFMHPETF EQYSADAKAV GDAEKWLLDQ ADCIVTLWNG APITVTPPNF VELEIVDTDP GLKGDTAGTG GKPATLSTGA VVKVPLFVQI GEVIRVDTRS GEYVSRVK // ID DXS_HAEIN Reviewed; 625 AA. AC P45205; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315}; DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315}; GN Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=HI_1439; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C CC atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield CC 1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1- CC deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00315}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00315}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00315}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose CC 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D- CC glyceraldehyde 3-phosphate and pyruvate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23088.1; -; Genomic_DNA. DR PIR; B64172; B64172. DR RefSeq; NP_439591.1; NC_000907.1. DR RefSeq; WP_005650455.1; NC_000907.1. DR ProteinModelPortal; P45205; -. DR SMR; P45205; 4-620. DR STRING; 71421.HI1439; -. DR EnsemblBacteria; AAC23088; AAC23088; HI_1439. DR GeneID; 950315; -. DR KEGG; hin:HI1439; -. DR PATRIC; 20191583; VBIHaeInf48452_1501. DR eggNOG; ENOG4105C2V; Bacteria. DR eggNOG; COG1154; LUCA. DR KO; K01662; -. DR OMA; YKGLCGF; -. DR OrthoDB; EOG6BKJ6P; -. DR PhylomeDB; P45205; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 3. DR HAMAP; MF_00315; DXP_synth; 1. DR InterPro; IPR005477; Dxylulose-5-P_synthase. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR020826; Transketolase_BS. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF13292; DXP_synthase_N; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 3. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00204; dxs; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate; KW Transferase. FT CHAIN 1 625 1-deoxy-D-xylulose-5-phosphate synthase. FT /FTId=PRO_0000189117. FT REGION 121 123 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT REGION 153 154 Thiamine pyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT METAL 152 152 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT METAL 181 181 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00315}. FT BINDING 80 80 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 181 181 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 290 290 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. FT BINDING 371 371 Thiamine pyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00315}. SQ SEQUENCE 625 AA; 68503 MW; ACC12E985DEC134E CRC64; MTNNMNNYPL LSLINSPEDL RLLNKDQLPQ LCQELRAYLL ESVSQTSGHL ASGLGTVELT VALHYVYKTP FDQLIWDVGH QAYPHKILTG RREQMSTIRQ KDGIHPFPWR EESEFDVLSV GHSSTSISAG LGIAVAAERE NAGRKTVCVI GDGAITAGMA FEALNHAGAL HTDMLVILND NEMSISENVG ALNNHLARIF SGSLYSTLRD GSKKILDKVP PIKNFMKKTE EHMKGVMFSP ESTLFEELGF NYIGPVDGHN IDELVATLTN MRNLKGPQFL HIKTKKGKGY APAEKDPIGF HGVPKFDPIS GELPKNNSKP TYSKIFGDWL CEMAEKDAKI IGITPAMREG SGMVEFSQRF PKQYFDVAIA EQHAVTFATG LAIGGYKPVV AIYSTFLQRA YDQLIHDVAI QNLPVLFAID RAGIVGADGA THQGAFDISF MRCIPNMIIM TPSDENECRQ MLYTGYQCGK PAAVRYPRGN AVGVKLTPLE MLPIGKSRLI RKGQKIAILN FGTLLPSALE LSEKLNATVV DMRFVKPIDI EMINVLAQTH DYLVTLEENA IQGGAGSAVA EVLNSSGKST ALLQLGLPDY FIPQATQQEA LADLGLDTKG IEEKILNFIA KQGNL // ID DUSA_HAEIN Reviewed; 327 AA. AC P44794; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000255|HAMAP-Rule:MF_02041}; DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02041}; DE EC=1.3.1.91 {ECO:0000255|HAMAP-Rule:MF_02041}; DE AltName: Full=U20-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02041}; DE Short=U20-specific Dus {ECO:0000255|HAMAP-Rule:MF_02041}; DE AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000255|HAMAP-Rule:MF_02041}; GN Name=dusA {ECO:0000255|HAMAP-Rule:MF_02041}; GN OrderedLocusNames=HI_0634; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. Specifically modifies CC U20 and U20a in tRNAs. {ECO:0000255|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20) in tRNA + NAD(P)(+) = CC uracil(20) in tRNA + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) = CC uracil(20a) in tRNA + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_02041}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041}; CC -!- SIMILARITY: Belongs to the Dus family. DusA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02041}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22293.1; -; Genomic_DNA. DR PIR; H64155; H64155. DR RefSeq; NP_438794.1; NC_000907.1. DR RefSeq; WP_005694659.1; NC_000907.1. DR ProteinModelPortal; P44794; -. DR STRING; 71421.HI0634; -. DR EnsemblBacteria; AAC22293; AAC22293; HI_0634. DR GeneID; 950134; -. DR KEGG; hin:HI0634; -. DR PATRIC; 20189873; VBIHaeInf48452_0661. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR KO; K05539; -. DR OMA; IPPLDYD; -. DR OrthoDB; EOG6C8MTR; -. DR PhylomeDB; P44794; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02041; DusA_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004653; DusA. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00742; yjbN; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NADP; Oxidoreductase; KW Reference proteome; RNA-binding; tRNA processing; tRNA-binding. FT CHAIN 1 327 tRNA-dihydrouridine(20/20a) synthase. FT /FTId=PRO_0000162067. FT NP_BIND 17 19 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT NP_BIND 210 212 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT NP_BIND 232 233 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT ACT_SITE 99 99 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02041}. FT BINDING 69 69 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT BINDING 138 138 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT BINDING 170 170 FMN. {ECO:0000255|HAMAP-Rule:MF_02041}. FT SITE 96 96 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02041}. FT SITE 182 182 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02041}. FT SITE 185 185 Interacts with tRNA. {ECO:0000255|HAMAP- FT Rule:MF_02041}. FT SITE 298 298 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02041}. FT SITE 301 301 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000255|HAMAP-Rule:MF_02041}. SQ SEQUENCE 327 AA; 37186 MW; 0D086C3385FB43E7 CRC64; MPQNLPHFYR GRFSVAPMLD WTTRHCRYFH RQFSKHALLY TEMVTAPAII HAKYDHLDFD LQENPVALQL GGSDPEQLKY CAKLAEERGY HEINLNVGCP SDRVQNGMFG ACLMAKADLV ADCVEQMQSA VKIPVTVKTR IGIDELDSYE FLCDFIEKVQ GKGCQEFIIH ARKAWLSGLS PKENREIPPL DYIRVYQLKR DFPHLTIAIN GGIKTIEEMK QHLQYVDGVM VGREAYQNPS LLGQIDQALF DPNAPIVTAH EAVESMLPYI EQQLSQGIHL NHIVRHILGA FQNCKGARQW RRYLSENAFK QGAGIEVVET ALSFVES // ID DYR_HAEIN Reviewed; 160 AA. AC P43791; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Dihydrofolate reductase; DE EC=1.5.1.3; GN Name=folA; Synonyms=folH; OrderedLocusNames=HI_0899; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate R1042, Isolate R1047, and Isolate R906; RA de Groot R.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. 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 -!- MISCELLANEOUS: Isolates R906, R1042, and R1047 are trimethoprim- CC resistant. 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; L42023; AAC22559.1; -; Genomic_DNA. DR EMBL; X84207; CAA58993.1; -; Genomic_DNA. DR EMBL; X84205; CAA58991.1; -; Genomic_DNA. DR EMBL; X84206; CAA58992.1; -; Genomic_DNA. DR PIR; C64101; C64101. DR PIR; S52336; S52336. DR PIR; S52337; S52337. DR PIR; S52338; S52338. DR RefSeq; NP_439060.1; NC_000907.1. DR RefSeq; WP_005648125.1; NC_000907.1. DR ProteinModelPortal; P43791; -. DR SMR; P43791; 3-160. DR STRING; 71421.HI0899; -. DR EnsemblBacteria; AAC22559; AAC22559; HI_0899. DR GeneID; 949905; -. DR KEGG; hin:HI0899; -. DR PATRIC; 20190455; VBIHaeInf48452_0941. DR eggNOG; ENOG4108YYV; Bacteria. DR eggNOG; COG0262; LUCA. DR KO; K00287; -. DR OMA; DTQFPDW; -. DR OrthoDB; EOG6KT2V2; -. DR PhylomeDB; P43791; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000579; 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:0046677; P:response to antibiotic; 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 PIRSF; PIRSF000194; DHFR; 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 Antibiotic resistance; Complete proteome; NADP; One-carbon metabolism; KW Oxidoreductase; Reference proteome; Trimethoprim resistance. FT CHAIN 1 160 Dihydrofolate reductase. FT /FTId=PRO_0000186391. FT DOMAIN 2 159 DHFR. {ECO:0000255|PROSITE- FT ProRule:PRU00660}. FT NP_BIND 14 20 NADP. {ECO:0000250}. FT NP_BIND 46 47 NADP. {ECO:0000250}. FT NP_BIND 64 65 NADP. {ECO:0000250}. FT NP_BIND 96 103 NADP. {ECO:0000250}. FT BINDING 6 6 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 8 8 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 28 28 Substrate. {ECO:0000250}. FT BINDING 53 53 Substrate. {ECO:0000250}. FT BINDING 58 58 Substrate. {ECO:0000250}. FT BINDING 114 114 Substrate. {ECO:0000250}. FT VARIANT 13 13 N -> S (in strain: Isolate R1042 and FT Isolate R1047). FT VARIANT 21 21 M -> I (in strain: Isolate R1047). FT VARIANT 54 54 P -> A (in strain: Isolate R1047). FT VARIANT 56 56 P -> A (in strain: Isolate R906). FT VARIANT 67 67 L -> P (in strain: Isolate R1042). FT VARIANT 69 69 E -> K (in strain: Isolate R1042). FT VARIANT 74 74 I -> V (in strain: Isolate R1042). FT VARIANT 77 77 D -> N (in strain: Isolate R1042). FT VARIANT 79 79 F -> L (in strain: Isolate R1042). FT VARIANT 95 95 I -> L (in strain: Isolate R1047). FT VARIANT 135 135 E -> K (in strain: Isolate R1042). FT VARIANT 142 142 R -> H (in strain: Isolate R1042). FT VARIANT 154 154 F -> S (in strain: Isolate R1042). SQ SEQUENCE 160 AA; 18913 MW; 384A1D64092B8C4F CRC64; MTFSLIVATT LNNVIGKDNQ MPWHLPADLA WFRQNTTGKP VIMGRKTFES IGRPLPKRTN IVLSRQLFEH EGVIWKDSFE SAVNFVRDFD EIMLIGGGEL FKQYLPKADK LYLTQIQTEL DGDTFFPQLN WEEWEIEFDE YRKADEQNRY DCRFLILTRK // ID EFTU_HAEIN Reviewed; 394 AA. AC P43926; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-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=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=HI_0578; GN and GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=HI_0632; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22236.1; -; Genomic_DNA. DR EMBL; L42023; AAC22292.1; -; Genomic_DNA. DR PIR; E64078; E64078. DR RefSeq; NP_438736.1; NC_000907.1. DR RefSeq; NP_438792.1; NC_000907.1. DR RefSeq; WP_005667564.1; NC_000907.1. DR ProteinModelPortal; P43926; -. DR SMR; P43926; 4-393. DR STRING; 71421.HI0632; -. DR PRIDE; P43926; -. DR EnsemblBacteria; AAC22236; AAC22236; HI_0578. DR EnsemblBacteria; AAC22292; AAC22292; HI_0632. DR GeneID; 949623; -. DR GeneID; 950329; -. DR KEGG; hin:HI0578; -. DR KEGG; hin:HI0632; -. DR PATRIC; 20189713; VBIHaeInf48452_0599. DR eggNOG; ENOG4105CGV; Bacteria. DR eggNOG; COG0050; LUCA. DR KO; K02358; -. DR OMA; GMVICKP; -. DR OrthoDB; EOG6R5C6X; -. DR PhylomeDB; P43926; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00485; EF-Tu; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 394 Elongation factor Tu. FT /FTId=PRO_0000091332. 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}. SQ SEQUENCE 394 AA; 43354 MW; 79AC25FAAF3CEE26 CRC64; MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKHY GGAARAFDQI DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN GVAEWEEKIL ELANHLDTYI PEPERAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG DEVEIVGIKD TAKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT PHTDFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK // ID EFG_HAEIN Reviewed; 700 AA. AC P43925; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 116. DE RecName: Full=Elongation factor G; DE Short=EF-G; GN Name=fusA; Synonyms=fus; OrderedLocusNames=HI_0579; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22237.1; -; Genomic_DNA. DR PIR; F64078; F64078. DR RefSeq; NP_438737.1; NC_000907.1. DR RefSeq; WP_010869011.1; NC_000907.1. DR ProteinModelPortal; P43925; -. DR SMR; P43925; 4-695. DR STRING; 71421.HI0579; -. DR PRIDE; P43925; -. DR EnsemblBacteria; AAC22237; AAC22237; HI_0579. DR GeneID; 950282; -. DR KEGG; hin:HI0579; -. DR PATRIC; 20189715; VBIHaeInf48452_0600. DR eggNOG; ENOG4105CEJ; Bacteria. DR eggNOG; COG0480; LUCA. DR KO; K02355; -. DR OMA; KLGVAIQ; -. DR OrthoDB; EOG6X6RBF; -. DR PhylomeDB; P43925; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004540; Transl_elong_EFG/EF2. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_II; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00484; EF-G; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 700 Elongation factor G. FT /FTId=PRO_0000091132. FT DOMAIN 8 290 tr-type G. FT NP_BIND 17 24 GTP. {ECO:0000250}. FT NP_BIND 88 92 GTP. {ECO:0000250}. FT NP_BIND 142 145 GTP. {ECO:0000250}. SQ SEQUENCE 700 AA; 77264 MW; ADF6F34159A674B0 CRC64; MARTTPIERY RNIGISAHID AGKTTTTERI LFYTGVSHKI GEVHDGAATM DWMEQEQERG ITITSAATTA FWSGMSQQFP QHRINVIDTP GHVDFTVEVE RSMRVLDGAV MVYCAVGGVQ PQSETVWRQA NKYEVPRIAF VNKMDRTGAN FLRVVEQLKT RLGANAIPLQ LPVGAEENFT GVVDLIKMKA INWNEADQGM TFTYEEVPAN MQADCEEWRQ NLVEAAAEAS EELMEKYLGG EDLTEEEIKS ALRQRVLANE IILVTCGSAF KNKGVQAMLD AVVEYLPAPT DIPAIKGINP DETEGERHAS DEEPFSSLAF KIATDPFVGN LTFFRVYSGV INSGDTVLNS VRQKRERFGR IVQMHANKRE EIKEVRAGDI AAAIGLKDVT TGDTLCAIDA PIILERMEFP EPVISVAVEP KTKADQEKMG LALGRLAQED PSFRVHTDEE SGETIISGMG ELHLDIIVDR MKREFKVEAN IGKPQVSYRE TIRTRVNDVE GKHAKQSGGR GQYGHVVIDL YPLDPEGPGY EFVNEIKGGV IPGEYIPAVD KGIQEQLKSG PLAGYPVVDL GVRLHFGSYH DVDSSELAFK LAASLAFKAA FSKANPVLLE PIMKVEVETP PEYVGDVIGD LSRRRAMVNG QEANEFVVKI YAEVPLSEMF GYATDLRSQT QGRASYSMEP LKYAEAPTSV AAAVIEARKK // ID EFTS_HAEIN Reviewed; 283 AA. AC P43894; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 113. DE RecName: Full=Elongation factor Ts; DE Short=EF-Ts; GN Name=tsf; OrderedLocusNames=HI_0914; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22572.1; -; Genomic_DNA. DR PIR; C64102; C64102. DR RefSeq; NP_439074.1; NC_000907.1. DR RefSeq; WP_005693261.1; NC_000907.1. DR ProteinModelPortal; P43894; -. DR SMR; P43894; 2-279. DR STRING; 71421.HI0914; -. DR PRIDE; P43894; -. DR EnsemblBacteria; AAC22572; AAC22572; HI_0914. DR GeneID; 949917; -. DR KEGG; hin:HI0914; -. DR PATRIC; 20190483; VBIHaeInf48452_0955. DR eggNOG; ENOG4105CU7; Bacteria. DR eggNOG; COG0264; LUCA. DR KO; K02357; -. DR OMA; FIMEPKK; -. DR OrthoDB; EOG66B42N; -. DR PhylomeDB; P43894; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central. DR Gene3D; 3.30.479.20; -; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 283 Elongation factor Ts. FT /FTId=PRO_0000161128. FT REGION 80 83 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000250}. SQ SEQUENCE 283 AA; 30188 MW; 5001460E620720E4 CRC64; MAEITASLVK ELRDRTGAGM MECKKALVEA NGDIELAIDN MRKSGQAKAA KKAGRVAAEG VILARVENGF GVLVEMNCET DFVAKDAGFL GLANEVTDFA AANKGTTIEA LQAQFEEKRA ALVAKIGENM NIRRVAYLDG QVIAQYLHGA KIGVLVAGEG SADELKKVAM HVAASKPEFV NPEDVSAEVV EHERQIQIDI AINSGKPKEI AEKMVEGRMK KFTGEVSLTG QAFVMDPSVS VGDFLKSVNT SVSNFIRLEV GEGIEKKEED FAAEVAKITG GNA // ID ERA_HAEIN Reviewed; 302 AA. AC P43728; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367}; GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=HI_0013; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00367}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Contains 1 Era-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_00367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21691.1; -; Genomic_DNA. DR PIR; F64042; F64042. DR RefSeq; NP_438186.1; NC_000907.1. DR RefSeq; WP_005657841.1; NC_000907.1. DR ProteinModelPortal; P43728; -. DR SMR; P43728; 6-298. DR STRING; 71421.HI0013; -. DR EnsemblBacteria; AAC21691; AAC21691; HI_0013. DR GeneID; 950911; -. DR KEGG; hin:HI0013; -. DR PATRIC; 20188477; VBIHaeInf48452_0013. DR eggNOG; ENOG4105CWT; Bacteria. DR eggNOG; COG1159; LUCA. DR KO; K03595; -. DR OMA; KVAKDWQ; -. DR OrthoDB; EOG68DD1Q; -. DR PhylomeDB; P43728; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00367; GTPase_Era; 1. DR InterPro; IPR030388; G_ERA_dom. DR InterPro; IPR005662; GTP-bd_Era. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF07650; KH_2; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR TIGRFAMs; TIGR00436; era; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51713; G_ERA; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW GTP-binding; Membrane; Nucleotide-binding; Reference proteome; KW Ribosome biogenesis; RNA-binding; rRNA-binding. FT CHAIN 1 302 GTPase Era. FT /FTId=PRO_0000180017. FT DOMAIN 9 177 Era-type G. FT DOMAIN 208 285 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_00367}. FT NP_BIND 17 24 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 64 68 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. FT NP_BIND 126 129 GTP. {ECO:0000255|HAMAP-Rule:MF_00367}. SQ SEQUENCE 302 AA; 34354 MW; ACD724D8A3170328 CRC64; MTEQFDKTYC GFIAIVGRPN VGKSTLLNKI LGQKISITSR KAQTTRHRIV GIKTEGAYQE IYVDTPGLHI EEKRAINRLM NRAASSAIGD VDLIIFVVDG THWNADDEMV LNKLRNAKAP VVLAINKVDN IKNKDDLLPF ITDLSSKFNF AHIVPISAQR GNNVHELEKI VRQSLREGVH HFPEDYVTDR SQRFMASEII REKLMRFTGE ELPYSVTVEI EQFKVNERGT YEINGLILVE REGQKKMVIG AGGQKIKTIG MEARADMERL FDNKVHLELW VKVKSGWADD ERALRSLGYM DE // ID ETCA_HAEIN Reviewed; 192 AA. AC P71395; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Electron transport complex subunit A {ECO:0000255|HAMAP-Rule:MF_00459}; GN OrderedLocusNames=HI_1683; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00459}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00459}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00459}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00459}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00459}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23329.1; -; Genomic_DNA. DR RefSeq; NP_439825.1; NC_000907.1. DR RefSeq; WP_005694403.1; NC_000907.1. DR STRING; 71421.HI1683; -. DR EnsemblBacteria; AAC23329; AAC23329; HI_1683. DR GeneID; 950867; -. DR KEGG; hin:HI1683; -. DR PATRIC; 20192117; VBIHaeInf48452_1762. DR eggNOG; ENOG4105DGN; Bacteria. DR eggNOG; COG4657; LUCA. DR KO; K03617; -. DR OMA; FTEMVIN; -. DR OrthoDB; EOG6GBMG7; -. DR PhylomeDB; P71395; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00459; RsxA_RnfA; 1. DR InterPro; IPR011293; Elect_transpt_RnfA/RsxA. DR InterPro; IPR003667; Rnf-Nqr. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01943; rnfA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 192 Electron transport complex subunit A. FT /FTId=PRO_0000214293. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 63 83 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 102 122 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 134 154 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. FT TRANSMEM 171 191 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00459}. SQ SEQUENCE 192 AA; 20590 MW; 2AB1D907D202223A CRC64; MTHYILLIIG TALINNFVLV KFLGLCPFMG VSKKIETAVG MGLATMFVLT VASLCAYLVD HYILIPLNAT FLRTLVFILV IAVVVQFTEM AINKTSPTLY RLLGIFLPLI TTNCAVLGVA LLNVNLAHNL TESVVYGFGA SLGFSLVLVL FAALRERLVA ADIPATFRGS SIALITAGLM SLAFMGFTGL VK // ID ETCC_HAEIN Reviewed; 819 AA. AC P71397; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 125. DE RecName: Full=Electron transport complex subunit C {ECO:0000255|HAMAP-Rule:MF_00461}; GN OrderedLocusNames=HI_1685; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00461}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00461}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00461}; CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00461}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00461}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00461}. CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. CC RnfC subfamily. {ECO:0000255|HAMAP-Rule:MF_00461}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|HAMAP-Rule:MF_00461}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23331.1; -; Genomic_DNA. DR PIR; E64136; E64136. DR RefSeq; NP_439827.1; NC_000907.1. DR RefSeq; WP_010869271.1; NC_000907.1. DR ProteinModelPortal; P71397; -. DR STRING; 71421.HI1685; -. DR PRIDE; P71397; -. DR EnsemblBacteria; AAC23331; AAC23331; HI_1685. DR GeneID; 950866; -. DR KEGG; hin:HI1685; -. DR PATRIC; 20192121; VBIHaeInf48452_1764. DR eggNOG; ENOG4107QTR; Bacteria. DR eggNOG; COG4656; LUCA. DR KO; K03615; -. DR OMA; QNREESQ; -. DR OrthoDB; EOG6W45RX; -. DR PhylomeDB; P71397; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central. DR HAMAP; MF_00461; RsxC_RnfC; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010208; Elect_transpt_RnfC/RsxC. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR011538; Nuo51_FMN-bd. DR InterPro; IPR026902; RnfC_N. DR InterPro; IPR019554; Soluble_ligand-bd. DR Pfam; PF01512; Complex1_51K; 1. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF13375; RnfC_N; 1. DR Pfam; PF10531; SLBB; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR01945; rnfC; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 819 Electron transport complex subunit C. FT /FTId=PRO_0000073208. FT DOMAIN 368 398 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT DOMAIN 408 437 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 378 378 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 381 381 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 384 384 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 388 388 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 417 417 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 420 420 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 423 423 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. FT METAL 427 427 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00461}. SQ SEQUENCE 819 AA; 89284 MW; 541EAA2AEC6AEA93 CRC64; MADVLSRFNS GKLWDFKGGI HPPEMKSQSN SQPLRHLPLG TDFYIPLKQH LGTTGNLLIK EGDYVLKGQA LTKGDGLRML PVHAPTSGTI KSIKPYVATH PSGLDEPTIH LQADGLDQWI ERNPIDDFST LSSEQLIHKI YQAGIAGLGG AVFPTAAKIQ SAEQKVKLLI INGAECEPYI TCDDRLMRER ADEIIKGIRI LRYILHPEKV VIAIEDNKPE AISAIRNALQ GANDISIRVI PTKYPSGATK QLIYLLTGIE VPSGERSSSI GVLMQNVGTM FAIKRAIIND EPLIERVVTL TGNKIAEKGN YWVRLGTPIS QILSDAGYQF DKHFPIFAGG PMMGLELPNL NAPVTKLVNC LLAPDYLEYA EPEAEQACIR CSSCSDACPV NLMPQQLYWF ARSEDHKKSE EYALKDCIEC GICAYVCPSH IPLIQYFRQE KAKIWQIKEK QKKSDEAKIR FEAKQARMER EEQERKARSQ RAAQARREEL AQTKGEDPVK AALERLKAKK ANETESTQIK TLTSEKGEVL PDNTDLMAQR KARRLARQQA ASQVENQEQQ TQPTNAKKAA VAAALARAKA KKLAQANSTS EAISNSQTAE NQVEKTKSAV EKTQENSTAL DPKKAAVAAA IARAKAKKLA QTNSTSEAIS NSQTAENEVE KTKSAVEKTE ENSTALDAKK AAIAAAIARA KAKKLAQANS ASEAISNSQT AENEVEKTKS AVEKTQQNST ALDPKKAAVA AAIARAKAKK LAQANSTSEA ISNSQTAENE VEKTKSAVEK TQENSTALDP KKAAVAAAIA RAKAKKLAKT QATLENNQE // ID END3_HAEIN Reviewed; 211 AA. AC P44319; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=Endonuclease III {ECO:0000255|HAMAP-Rule:MF_00942}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00942}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00942}; GN Name=nth {ECO:0000255|HAMAP-Rule:MF_00942}; OrderedLocusNames=HI_1689; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. The DNA N-glycosylase activity CC releases various damaged pyrimidines from DNA by cleaving the N- CC glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The CC AP-lyase activity cleaves the phosphodiester bond 3' to the AP CC site by a beta-elimination, leaving a 3'-terminal unsaturated CC sugar and a product with a terminal 5'-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00942}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00942}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC -!- SIMILARITY: Contains 1 HhH domain. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23335.1; -; Genomic_DNA. DR PIR; G64136; G64136. DR RefSeq; NP_439831.1; NC_000907.1. DR RefSeq; WP_005654382.1; NC_000907.1. DR ProteinModelPortal; P44319; -. DR SMR; P44319; 1-210. DR STRING; 71421.HI1689; -. DR EnsemblBacteria; AAC23335; AAC23335; HI_1689. DR GeneID; 950507; -. DR KEGG; hin:HI1689; -. DR PATRIC; 20192129; VBIHaeInf48452_1768. DR eggNOG; ENOG4105CSM; Bacteria. DR eggNOG; COG0177; LUCA. DR KO; K10773; -. DR OMA; HHALILF; -. DR OrthoDB; EOG6H4KC5; -. DR PhylomeDB; P44319; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF10576; EndIII_4Fe-2S; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR TIGRFAMs; TIGR01083; nth; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 211 Endonuclease III. FT /FTId=PRO_0000102212. FT DOMAIN 108 127 HhH. {ECO:0000255|HAMAP-Rule:MF_00942}. FT METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 197 197 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 203 203 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. SQ SEQUENCE 211 AA; 23715 MW; 9A46D42F296A2E3D CRC64; MNKTKRIEIL TRLREQNPHP TTELQYNSPF ELLIAVILSA QATDKGVNKA TEKLFPVANT PQAILDLGLD GLKSYIKTIG LFNSKAENII KTCRDLIEKH NGEVPENREA LEALAGVGRK TANVVLNTAF GHPTIAVDTH IFRVCNRTNF AAGKDVVKVE EKLLKVVPNE FKVDVHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEKVE F // ID ENGB_HAEIN Reviewed; 205 AA. AC P46453; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; GN OrderedLocusNames=HI_1118; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22772.1; -; Genomic_DNA. DR RefSeq; NP_439275.1; NC_000907.1. DR RefSeq; WP_005651790.1; NC_000907.1. DR ProteinModelPortal; P46453; -. DR SMR; P46453; 13-200. DR STRING; 71421.HI1118; -. DR EnsemblBacteria; AAC22772; AAC22772; HI_1118. DR GeneID; 950084; -. DR KEGG; hin:HI1118; -. DR PATRIC; 20190909; VBIHaeInf48452_1167. DR eggNOG; ENOG4105WHM; Bacteria. DR eggNOG; COG0218; LUCA. DR KO; K03978; -. DR OMA; NKHESMV; -. DR OrthoDB; EOG6ND0NG; -. DR PhylomeDB; P46453; -. DR Proteomes; UP000000579; 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 Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03598; GTPase_YsxC; 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 1 205 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157752. FT DOMAIN 27 201 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT NP_BIND 35 42 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 62 66 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 80 83 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 147 150 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 180 182 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT METAL 42 42 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 64 64 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. SQ SEQUENCE 205 AA; 22939 MW; 62DA2AD22B13675D CRC64; MSEIKLNYHK THFLTSAPNI RSIPEDTGIE IAFAGRSNAG KSTALNALTN QKNLARTSKT PGRTQLINLF EVEPNCKLVD LPGYGYAAVP EQMKIQWQKS LGEYLQKREC LAGLVVLMDI RHPLKDLDQQ MIEWAVSANL PVLLLLTKAD KLSQSARSKQ VKMVREAILP FQGDIQVEAF SAQNKIGIDK LAVKLDFWFS PLFAE // ID EPMC_HAEIN Reviewed; 178 AA. AC P44255; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Elongation factor P hydroxylase; DE Short=EF-P hydroxylase; DE EC=1.14.-.-; DE AltName: Full=EF-P post-translational modification enzyme C; GN Name=epmC; OrderedLocusNames=HI_1563; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Is involved in the final hydroxylation step of the post- CC translational modification of translation elongation factor P (EF- CC P) on 'Lys-34'. Acts after beta-lysylation of 'Lys-34' by EpmA and CC EpmB. EpmC adds an oxygen atom to the C5 position of 'Lys-34' and CC does not modify the added beta-lysine (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the EpmC 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; L42023; AAC23212.1; -; Genomic_DNA. DR PIR; D64036; D64036. DR RefSeq; NP_439712.1; NC_000907.1. DR RefSeq; WP_005688501.1; NC_000907.1. DR STRING; 71421.HI1563; -. DR EnsemblBacteria; AAC23212; AAC23212; HI_1563. DR GeneID; 950423; -. DR KEGG; hin:HI1563; -. DR PATRIC; 20191851; VBIHaeInf48452_1634. DR eggNOG; ENOG4108BPE; Bacteria. DR eggNOG; COG3101; LUCA. DR KO; K09906; -. DR OMA; SGLHEIA; -. DR OrthoDB; EOG6091BQ; -. DR PhylomeDB; P44255; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR InterPro; IPR007411; EpmC. DR Pfam; PF04315; EpmC; 1. PE 3: Inferred from homology; KW Complete proteome; Monooxygenase; Oxidoreductase; Reference proteome. FT CHAIN 1 178 Elongation factor P hydroxylase. FT /FTId=PRO_0000169197. SQ SEQUENCE 178 AA; 20604 MW; BD3BF8F231D2B638 CRC64; MEHKLEDIIA IFNQCFEEEY NTRLVKGGDE PIYLPANDEV PYNAIYFARG FYSSALHEIA HWLVAGKERR KLEDFGYWYE PDGRSEERQR DFEKVEVKPQ ALEWILATAA GFRYFASADN LNGNPGDTQP FKQAVYEQVK IYAEKGLPKR AETLRKALVA FYSTEDDINL AKFDVTCI // ID EMRA_HAEIN Reviewed; 390 AA. AC P44928; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Multidrug export protein EmrA; GN Name=emrA; OrderedLocusNames=HI_0898; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Confers resistance to antibiotics. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}; Periplasmic side CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) CC (TC 8.A.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22558.1; -; Genomic_DNA. DR PIR; B64101; B64101. DR RefSeq; NP_439059.1; NC_000907.1. DR RefSeq; WP_005693250.1; NC_000907.1. DR ProteinModelPortal; P44928; -. DR STRING; 71421.HI0898; -. DR EnsemblBacteria; AAC22558; AAC22558; HI_0898. DR GeneID; 949904; -. DR KEGG; hin:HI0898; -. DR PATRIC; 20190453; VBIHaeInf48452_0940. DR eggNOG; ENOG4105CW7; Bacteria. DR eggNOG; COG1566; LUCA. DR KO; K03543; -. DR OMA; MWIEANF; -. DR OrthoDB; EOG6C014B; -. DR PhylomeDB; P44928; -. DR Proteomes; UP000000579; 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:0015238; F:drug transmembrane transporter activity; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR InterPro; IPR005694; Emr. DR InterPro; IPR032317; HlyD_D23. DR InterPro; IPR006143; RND_pump_MFP. DR Pfam; PF00529; HlyD; 1. DR Pfam; PF16576; HlyD_D23; 1. DR TIGRFAMs; TIGR00998; 8a0101; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; KW Coiled coil; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 390 Multidrug export protein EmrA. FT /FTId=PRO_0000201870. FT TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TOPO_DOM 47 390 Periplasmic. {ECO:0000255}. FT COILED 160 190 {ECO:0000255}. SQ SEQUENCE 390 AA; 43062 MW; 42CF0AFA588BAFD8 CRC64; MTQIATENPS TKSVSNKTDR KKGLSIFILL LLIIGIACAL YWFFFLKDFE ETEDAYVGGN QVMVSSQVAG NVAKINADNM DKVHAGDILV ELDDTNAKLS FEQAKSNLAN AVRQVEQLGF TVQQLQSAVH ANEISLAQAQ GNLARRVQLE KMGAIDKESF QHAKEAVELA KANLNASKNQ LAANQALLRN VPLREQPQIQ NAINSLKQAW LNLQRTKIRS PIDGYVARRN VQVGQAVSVG GALMAVVSNE QMWLEANFKE TQLTNMRIGQ PVKIHFDLYG KNKEFDGVIN GIEMGTGNAF SLLPSQNATG NWIKVVQRVP VRIKLDPQQF TETPLRIGLS ATAKVRISDS SGAMLREKTE PKTLFSTDTL KYDESAVENL IESIIQQNSH // ID EMRB_HAEIN Reviewed; 510 AA. AC P44927; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Multidrug export protein EmrB; GN Name=emrB; OrderedLocusNames=HI_0897; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Confers resistance to antibiotics. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB 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; L42023; AAC22557.1; -; Genomic_DNA. DR PIR; A64101; A64101. DR RefSeq; NP_439058.1; NC_000907.1. DR RefSeq; WP_005693249.1; NC_000907.1. DR ProteinModelPortal; P44927; -. DR STRING; 71421.HI0897; -. DR EnsemblBacteria; AAC22557; AAC22557; HI_0897. DR GeneID; 949901; -. DR KEGG; hin:HI0897; -. DR PATRIC; 20190451; VBIHaeInf48452_0939. DR eggNOG; ENOG4105C0R; Bacteria. DR eggNOG; ENOG410XNN3; LUCA. DR KO; K03446; -. DR OMA; LAWMTIA; -. DR OrthoDB; EOG6ZH2DN; -. DR PhylomeDB; P44927; -. DR Proteomes; UP000000579; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004638; Drug-R_transpt_efflux_EmrB. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 3. DR TIGRFAMs; TIGR00711; efflux_EmrB; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 510 Multidrug export protein EmrB. FT /FTId=PRO_0000173324. FT TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TOPO_DOM 29 31 Periplasmic. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TOPO_DOM 53 56 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TOPO_DOM 78 91 Periplasmic. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TOPO_DOM 113 113 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. FT TOPO_DOM 135 144 Periplasmic. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TOPO_DOM 166 168 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TOPO_DOM 190 203 Periplasmic. {ECO:0000255}. FT TRANSMEM 204 224 Helical. {ECO:0000255}. FT TOPO_DOM 225 237 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT TOPO_DOM 259 278 Periplasmic. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255}. FT TOPO_DOM 300 308 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 309 329 Helical. {ECO:0000255}. FT TOPO_DOM 330 338 Periplasmic. {ECO:0000255}. FT TRANSMEM 339 359 Helical. {ECO:0000255}. FT TOPO_DOM 360 375 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 376 396 Helical. {ECO:0000255}. FT TOPO_DOM 397 483 Periplasmic. {ECO:0000255}. FT TRANSMEM 484 504 Helical. {ECO:0000255}. FT TOPO_DOM 505 510 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 510 AA; 55827 MW; DC2D452221A85F29 CRC64; MGNSAKKFPP IQGGALILLT LALSLATFMQ VLDSTIANVA IPTIAGDLGA SFSQGTWVIT SFGVANAISI PITGWLAKRF GEVRLFLVST FLFVVSSWLC GIADSLEALI IFRVIQGAVA GPVIPLSQSL LLNNYPPEKR GMALAFWSMT IVVAPIFGPI LGGWISDNIH WGWIFFINVP IGLSVVLISW KILGSRESEI VHQPIDKVGL VLLVLGVGCL QLMLDQGREQ DWFNSNEIII LAVVAVVCLI ALVIWELTDD NPVVDISLFH SRNFSVGCLC TSLAFLIYLG SVVLIPLLLQ QVFHYTATWA GLAASPVGLF PILLSPIIGR FGYKIDMRIL VTISFIVYAI TFYWRAVTFE PSMTFVDVAL PQLVQGLAVS CFFMPLTTIT LSGLPAHKMA SASSLFNFLR TLAGSVGTSL TTFMWYNREA VHHTQLTEHI NPYNPISQSF YHQMNQFGLS DTQTSAYLAQ QITSQGFIIG ANEIFWLSAM GFLGLLIVIW FAKPPFGTQH // ID FABH_HAEIN Reviewed; 316 AA. AC P43711; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 114. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815}; DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815}; GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; GN OrderedLocusNames=HI_0157; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP INHIBITION BY ANTIBIOTICS. RX PubMed=11375394; DOI=10.1074/jbc.M101769200; RA Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., RA Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., RA Brandt M., Daines R.A., Lonsdale J.T.; RT "Identification, substrate specificity, and inhibition of the RT Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase RT III (FabH)."; RL J. Biol. Chem. 276:30024-30030(2001). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. Catalyzes the first condensation reaction which CC initiates fatty acid synthesis and may therefore play a role in CC governing the total rate of fatty acid production. Possesses both CC acetoacetyl-ACP synthase and acetyl transacylase activities. Its CC substrate specificity determines the biosynthesis of branched- CC chain and/or straight-chain of fatty acids. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + malonyl-[acyl-carrier-protein] = CC acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential CC for the weak association between ACP/AcpP and FabH. CC {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- MISCELLANEOUS: Inhibited by the SB418011 antibiotic. Not inhibited CC by cerulenin, and weakly inhibited by thiolactomycin. CC -!- SIMILARITY: Belongs to the FabH family. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21826.1; -; Genomic_DNA. DR PIR; F64051; F64051. DR RefSeq; NP_438327.1; NC_000907.1. DR RefSeq; WP_005691510.1; NC_000907.1. DR PDB; 3IL3; X-ray; 2.70 A; A=1-316. DR PDBsum; 3IL3; -. DR ProteinModelPortal; P43711; -. DR SMR; P43711; 1-316. DR STRING; 71421.HI0157; -. DR BindingDB; P43711; -. DR ChEMBL; CHEMBL3822; -. DR PRIDE; P43711; -. DR EnsemblBacteria; AAC21826; AAC21826; HI_0157. DR GeneID; 951067; -. DR KEGG; hin:HI0157; -. DR PATRIC; 20188811; VBIHaeInf48452_0162. DR eggNOG; ENOG4105CCZ; Bacteria. DR eggNOG; COG0332; LUCA. DR KO; K00648; -. DR OMA; ESGMYEN; -. DR OrthoDB; EOG6J74XN; -. DR PhylomeDB; P43711; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P43711; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.47.10; -; 2. DR HAMAP; MF_01815; FabH; 1. DR InterPro; IPR013751; ACP_syn_III. DR InterPro; IPR013747; ACP_syn_III_C. DR InterPro; IPR004655; FabH_synth. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF08545; ACP_syn_III; 1. DR Pfam; PF08541; ACP_syn_III_C; 1. DR SUPFAM; SSF53901; SSF53901; 1. DR TIGRFAMs; TIGR00747; fabH; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Multifunctional enzyme; Reference proteome; KW Transferase. FT CHAIN 1 316 3-oxoacyl-[acyl-carrier-protein] synthase FT 3. FT /FTId=PRO_0000110432. FT REGION 244 248 ACP-binding. {ECO:0000255|HAMAP- FT Rule:MF_01815}. FT ACT_SITE 112 112 {ECO:0000255|HAMAP-Rule:MF_01815}. FT ACT_SITE 243 243 {ECO:0000255|HAMAP-Rule:MF_01815}. FT ACT_SITE 273 273 {ECO:0000255|HAMAP-Rule:MF_01815}. FT STRAND 7 11 {ECO:0000244|PDB:3IL3}. FT STRAND 16 18 {ECO:0000244|PDB:3IL3}. FT HELIX 19 23 {ECO:0000244|PDB:3IL3}. FT HELIX 30 36 {ECO:0000244|PDB:3IL3}. FT STRAND 41 43 {ECO:0000244|PDB:3IL3}. FT HELIX 51 66 {ECO:0000244|PDB:3IL3}. FT HELIX 70 72 {ECO:0000244|PDB:3IL3}. FT STRAND 75 79 {ECO:0000244|PDB:3IL3}. FT STRAND 86 88 {ECO:0000244|PDB:3IL3}. FT HELIX 90 97 {ECO:0000244|PDB:3IL3}. FT STRAND 104 108 {ECO:0000244|PDB:3IL3}. FT HELIX 111 113 {ECO:0000244|PDB:3IL3}. FT HELIX 114 127 {ECO:0000244|PDB:3IL3}. FT STRAND 132 141 {ECO:0000244|PDB:3IL3}. FT HELIX 142 144 {ECO:0000244|PDB:3IL3}. FT TURN 151 156 {ECO:0000244|PDB:3IL3}. FT STRAND 159 171 {ECO:0000244|PDB:3IL3}. FT STRAND 174 181 {ECO:0000244|PDB:3IL3}. FT STRAND 188 190 {ECO:0000244|PDB:3IL3}. FT HELIX 208 228 {ECO:0000244|PDB:3IL3}. FT TURN 229 231 {ECO:0000244|PDB:3IL3}. FT TURN 234 236 {ECO:0000244|PDB:3IL3}. FT STRAND 239 242 {ECO:0000244|PDB:3IL3}. FT HELIX 247 256 {ECO:0000244|PDB:3IL3}. FT HELIX 261 263 {ECO:0000244|PDB:3IL3}. FT HELIX 268 271 {ECO:0000244|PDB:3IL3}. FT HELIX 275 277 {ECO:0000244|PDB:3IL3}. FT HELIX 278 288 {ECO:0000244|PDB:3IL3}. FT STRAND 297 304 {ECO:0000244|PDB:3IL3}. FT TURN 305 307 {ECO:0000244|PDB:3IL3}. FT STRAND 308 315 {ECO:0000244|PDB:3IL3}. SQ SEQUENCE 316 AA; 34280 MW; 2D00ADD61DCB6A66 CRC64; MNSRILSTGS YLPSHIRTNA DLEKMVDTSD EWIVTRSGIR ERRIAAEDET VATMGFEAAK NAIEAAQINP QDIELIIVAT TSHSHAYPSA ACQVQGLLNI DDAISFDLAA ACTGFVYALS VADQFIRAGK VKKALVIGSD LNSRKLDETD RSTVVLFGDG AGAVILEASE QEGIISTHLH ASADKNNALV LAQPERGIEK SGYIEMQGNE TFKLAVRELS NVVEETLLAN NLDKKDLDWL VPHQANLRII TATAKKLEMD MSQVVVTLDK YANNSAATVP VALDEAIRDG RIQRGQLLLL EAFGGGWTWG SALVRF // ID ENO_HAEIN Reviewed; 436 AA. AC P43806; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 117. 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=HI_0932; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. CC {ECO:0000255|HAMAP-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; L42023; AAC22590.1; -; Genomic_DNA. DR PIR; E64103; E64103. DR RefSeq; NP_439092.1; NC_000907.1. DR RefSeq; WP_010869090.1; NC_000907.1. DR ProteinModelPortal; P43806; -. DR STRING; 71421.HI0932; -. DR EnsemblBacteria; AAC22590; AAC22590; HI_0932. DR GeneID; 949935; -. DR KEGG; hin:HI0932; -. DR PATRIC; 20190521; VBIHaeInf48452_0973. DR eggNOG; ENOG4105C70; Bacteria. DR eggNOG; COG0148; LUCA. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR PhylomeDB; P43806; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR InterPro; IPR029017; Enolase_N-like. DR PANTHER; PTHR11902; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; KW Metal-binding; Reference proteome; Secreted. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 436 Enolase. FT /FTId=PRO_0000133895. FT REGION 370 373 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 209 209 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 343 343 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 246 246 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 291 291 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 318 318 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 159 159 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 168 168 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 291 291 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 318 318 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 343 343 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 394 394 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. SQ SEQUENCE 436 AA; 46115 MW; 3FB36CF50CDEF0F7 CRC64; MAKIVKVIGR EIIDSRGNPT VEAEVHLXGG FVGLAAAPSG ASTGSREALE LRDGDKSRFL GKGVLKAVAA VNNEIAQAIV GKDATNQAEI DQIMIDLDGT ENKSNFGANA ILAVSLANAK AAAASKGLPL YAYIAELNGT AGVYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLR EALRIGAEVF HNLAKVLKAK GMSTAVGDEG GFAPNLASNA DALACIKEAV EKAGYVLGKD VTLAMDCASS EFYNKENGMY EMKGEGKSFT SQEFTHYLEE LCKEYPIVSI EDGQDESDWE GFAYQTKVLG DRVQLVGDDL FVTNTKILKE GIEKGIANSI LIKFNQIGSL TETLAAIKMA KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRIAKYNQL IRIEEALERA GTPAAFPGLK AVKGQA // ID EPMA_HAEIN Reviewed; 323 AA. AC P43826; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Elongation factor P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174}; DE Short=EF-P--(R)-beta-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00174}; DE EC=6.3.1.- {ECO:0000255|HAMAP-Rule:MF_00174}; DE AltName: Full=EF-P post-translational modification enzyme A {ECO:0000255|HAMAP-Rule:MF_00174}; DE AltName: Full=EF-P-lysine lysyltransferase {ECO:0000255|HAMAP-Rule:MF_00174}; GN Name=epmA {ECO:0000255|HAMAP-Rule:MF_00174}; Synonyms=genX, yjeA; GN OrderedLocusNames=HI_0836; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: With EpmB is involved in the beta-lysylation step of the CC post-translational modification of translation elongation factor P CC (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine CC produced by EpmB, forming a lysyl-adenylate, from which the beta- CC lysyl moiety is then transferred to the epsilon-amino group of a CC conserved specific lysine residue in EF-P. {ECO:0000255|HAMAP- CC Rule:MF_00174}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00174}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. EpmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00174}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22494.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22494.1; ALT_INIT; Genomic_DNA. DR PIR; I64097; I64097. DR RefSeq; NP_438996.2; NC_000907.1. DR RefSeq; WP_010869065.1; NC_000907.1. DR ProteinModelPortal; P43826; -. DR STRING; 71421.HI0836; -. DR EnsemblBacteria; AAC22494; AAC22494; HI_0836. DR GeneID; 949850; -. DR KEGG; hin:HI0836; -. DR PATRIC; 20190327; VBIHaeInf48452_0877. DR eggNOG; ENOG4105CAP; Bacteria. DR eggNOG; COG2269; LUCA. DR KO; K04568; -. DR OMA; EEAGRHH; -. DR OrthoDB; EOG69PQ2M; -. DR PhylomeDB; P43826; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0071915; P:protein-lysine lysylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00174; EF_P_modif_A; 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; IPR004525; EpmA. DR InterPro; IPR018149; Lys-tRNA-synth_II_C. DR PANTHER; PTHR22594; PTHR22594; 1. DR PANTHER; PTHR22594:SF7; PTHR22594:SF7; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR PRINTS; PR00982; TRNASYNTHLYS. DR TIGRFAMs; TIGR00462; genX; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 323 Elongation factor P--(R)-beta-lysine FT ligase. FT /FTId=PRO_0000152724. FT NP_BIND 100 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00174}. FT NP_BIND 242 243 ATP. {ECO:0000255|HAMAP-Rule:MF_00174}. FT REGION 76 78 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00174}. FT BINDING 109 109 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00174}. FT BINDING 118 118 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00174}. FT BINDING 249 249 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00174}. FT BINDING 298 298 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00174}. SQ SEQUENCE 323 AA; 37156 MW; 33EF1920BD808D21 CRC64; MTALNHWQPS ADIKNHLKRA KIIAKIRQFF TERGLLEVET PVLSEFGVTD LHLSTFSTEF LAPFGEQSKT LWLSTSPEYH MKRLLAAGSG PIFQISKVFR NEEAGNRHNP EFTMLEWYRP HFHMHRLINE VDDLLQQILD CPPAESLSYQ FVFQEYVGLD PLSAERSELI EAARKHNFMA EDNEDRDTLL QFLFSEVVEP QIGKERPIAV YHFPSTQAAL AQVSPEDQRV AERFEFYYKG LELANGFHEL ADAQEQRHRF ELDNQQRQKC ELPTREIDER FLAALEAGMP DASGVALGID RLMMIALDCE KINDVISFAV DNA // ID EPMB_HAEIN Reviewed; 338 AA. AC P44641; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 91. DE RecName: Full=L-lysine 2,3-aminomutase; DE Short=LAM; DE EC=5.4.3.-; DE AltName: Full=EF-P post-translational modification enzyme B; GN Name=epmB; OrderedLocusNames=HI_0329; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: With EpmA is involved in the beta-lysylation step of the CC post-translational modification of translation elongation factor P CC (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays CC lysine 2,3-aminomutase activity, producing (R)-beta-lysine from CC (S)-alpha-lysine (L-lysine) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-lysine = (3R)-3,6-diaminohexanoate. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA 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; L42023; AAC21990.1; -; Genomic_DNA. DR PIR; B64148; B64148. DR RefSeq; NP_438493.1; NC_000907.1. DR RefSeq; WP_005691796.1; NC_000907.1. DR ProteinModelPortal; P44641; -. DR STRING; 71421.HI0329; -. DR EnsemblBacteria; AAC21990; AAC21990; HI_0329. DR GeneID; 949459; -. DR KEGG; hin:HI0329; -. DR PATRIC; 20189201; VBIHaeInf48452_0346. DR eggNOG; ENOG4105CK3; Bacteria. DR eggNOG; COG1509; LUCA. DR KO; K19810; -. DR OMA; HFPYADN; -. DR OrthoDB; EOG6742RJ; -. DR PhylomeDB; P44641; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022462; EpmB. DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004911; DUF160; 1. DR TIGRFAMs; TIGR03821; EFP_modif_epmB; 1. DR TIGRFAMs; TIGR00238; TIGR00238; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isomerase; KW Metal-binding; Pyridoxal phosphate; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 338 L-lysine 2,3-aminomutase. FT /FTId=PRO_0000172289. FT METAL 121 121 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 125 125 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 128 128 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT MOD_RES 333 333 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 338 AA; 38676 MW; 6C0079D809CE1898 CRC64; MRILPQEPVI REEQNWLTIL KNAISDPKLL LKALNLPEDD FEQSIAARKL FSLRVPQPFI DKIEKGNPQD PLFLQVMCSD LEFVQAEGFS TDPLEEKNAN AVPNILHKYR NRLLFMAKGG CAVNCRYCFR RHFPYDENPG NKKSWQLALD YIAAHSEIEE VIFSGGDPLM AKDHELAWLI KHLENIPHLQ RLRIHTRLPV VIPQRITDEF CTLLAETRLQ TVMVTHINHP NEIDQIFAHA MQKLNAVNVT LLNQSVLLKG VNDDAQILKI LSDKLFQTGI LPYYLHLLDK VQGASHFLIS DIEAMQIYKT LQSLTSGYLV PKLAREIAGE PNKTLYAE // ID ERPA_HAEIN Reviewed; 114 AA. AC P45344; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Iron-sulfur cluster insertion protein ErpA {ECO:0000255|HAMAP-Rule:MF_01380}; GN Name=erpA {ECO:0000255|HAMAP-Rule:MF_01380}; GN OrderedLocusNames=HI_1723; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP STRUCTURE BY NMR. RX PubMed=15014238; DOI=10.1023/B:JNMR.0000019242.88149.c5; RA Yeh D.C., Liu F., Bonander N., Eisenstein E., Orban J.; RT "NMR assignment of HI1723 from Haemophilus influenzae -- a sequence RT homologue from the iron sulfur cluster assembly (IscA) family."; RL J. Biomol. NMR 29:213-214(2004). RN [4] RP STRUCTURE BY NMR. RG Structure 2 function project (S2F); RT "Solution NMR structure of HI1723 from Haemophilus influenzae."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Required for insertion of 4Fe-4S clusters for at least CC IspG. {ECO:0000255|HAMAP-Rule:MF_01380}. CC -!- COFACTOR: CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01380}; CC Note=Binds 1 iron-sulfur cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01380}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01380}. CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000255|HAMAP- CC Rule:MF_01380}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23369.1; -; Genomic_DNA. DR PIR; F64176; F64176. DR RefSeq; NP_439864.1; NC_000907.1. DR RefSeq; WP_005649956.1; NC_000907.1. DR PDB; 2APN; NMR; -; A=1-114. DR PDBsum; 2APN; -. DR ProteinModelPortal; P45344; -. DR SMR; P45344; 1-114. DR STRING; 71421.HI1723; -. DR EnsemblBacteria; AAC23369; AAC23369; HI_1723. DR GeneID; 950536; -. DR KEGG; hin:HI1723; -. DR PATRIC; 20192199; VBIHaeInf48452_1802. DR eggNOG; ENOG4108YX9; Bacteria. DR eggNOG; COG0316; LUCA. DR KO; K15724; -. DR OMA; FDENVND; -. DR OrthoDB; EOG6VXF8J; -. DR PhylomeDB; P45344; -. DR EvolutionaryTrace; P45344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central. DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central. DR Gene3D; 2.60.300.12; -; 1. DR HAMAP; MF_01380; Fe_S_insert_ErpA; 1. DR InterPro; IPR000361; FeS_biogenesis. DR InterPro; IPR016092; FeS_cluster_insertion. DR InterPro; IPR017870; FeS_cluster_insertion_CS. DR InterPro; IPR023063; FeS_cluster_insertion_RrpA. DR Pfam; PF01521; Fe-S_biosyn; 1. DR SUPFAM; SSF89360; SSF89360; 1. DR TIGRFAMs; TIGR00049; TIGR00049; 1. DR PROSITE; PS01152; HESB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 114 Iron-sulfur cluster insertion protein FT ErpA. FT /FTId=PRO_0000076994. FT METAL 42 42 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. FT METAL 106 106 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. FT METAL 108 108 Iron-sulfur. {ECO:0000255|HAMAP- FT Rule:MF_01380}. FT STRAND 3 5 {ECO:0000244|PDB:2APN}. FT HELIX 14 23 {ECO:0000244|PDB:2APN}. FT TURN 24 27 {ECO:0000244|PDB:2APN}. FT STRAND 32 35 {ECO:0000244|PDB:2APN}. FT STRAND 40 43 {ECO:0000244|PDB:2APN}. FT STRAND 49 51 {ECO:0000244|PDB:2APN}. FT STRAND 60 63 {ECO:0000244|PDB:2APN}. FT STRAND 65 71 {ECO:0000244|PDB:2APN}. FT HELIX 73 79 {ECO:0000244|PDB:2APN}. FT STRAND 83 87 {ECO:0000244|PDB:2APN}. FT STRAND 89 91 {ECO:0000244|PDB:2APN}. FT STRAND 94 98 {ECO:0000244|PDB:2APN}. FT HELIX 100 103 {ECO:0000244|PDB:2APN}. SQ SEQUENCE 114 AA; 12194 MW; D57FB8986191BED0 CRC64; MIDDMAVPLT FTDAAANKVK SLISEEENTD LKLRVYITGG GCSGFQYGFT FDEKVNDGDL TIEKSGVQLV IDPMSLQYLI GGTVDYTEGL EGSRFTVNNP NATSTCGCGS SFSI // ID ETCG_HAEIN Reviewed; 207 AA. AC P44291; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Electron transport complex subunit G {ECO:0000255|HAMAP-Rule:MF_00479}; GN OrderedLocusNames=HI_1687; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00479}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00479}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00479}. CC -!- SIMILARITY: Belongs to the RnfG family. {ECO:0000255|HAMAP- CC Rule:MF_00479}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23333.1; -; Genomic_DNA. DR PIR; D64040; D64040. DR RefSeq; NP_439829.1; NC_000907.1. DR RefSeq; WP_005694178.1; NC_000907.1. DR STRING; 71421.HI1687; -. DR EnsemblBacteria; AAC23333; AAC23333; HI_1687. DR GeneID; 950514; -. DR KEGG; hin:HI1687; -. DR PATRIC; 20192125; VBIHaeInf48452_1766. DR eggNOG; ENOG4108UQQ; Bacteria. DR eggNOG; COG4659; LUCA. DR KO; K03612; -. DR OMA; AYAYETT; -. DR OrthoDB; EOG6KQ6NH; -. DR PhylomeDB; P44291; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00479; RsxG_RnfG; 1. DR InterPro; IPR010209; Elect_transpt_RnfG/RsxG. DR InterPro; IPR007329; FMN-bd. DR Pfam; PF04205; FMN_bind; 1. DR PIRSF; PIRSF006091; E_trnsport_RnfG; 1. DR SMART; SM00900; FMN_bind; 1. DR TIGRFAMs; TIGR01947; rnfG; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 207 Electron transport complex subunit G. FT /FTId=PRO_0000214635. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00479}. SQ SEQUENCE 207 AA; 22908 MW; 52A19BB21FFC273D CRC64; MGTVKITSRY GILLGFIALL CTIISAGIFF LTKDKIDAVI AAQQRELLLQ VIPQDYFNNN LLESAVIPQD KNFVGIQKIY FAKKDGNVSA YAYETTAPDG YSGDIRLLVG LDPKGEVLGV RVIEHHETPG LGDKIERRIS NWILGFTNQS INEHNLSEWA VKKDGGKFDQ FSGATITPRA VVNQTKRSAL IMLNNQALLQ QLSTQVK // ID EXBB_HAEIN Reviewed; 150 AA. AC P43008; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Biopolymer transport protein ExbB; GN Name=exbB; OrderedLocusNames=HI_0253; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=7828935; DOI=10.1016/0378-1119(94)00675-I; RA Jarosik G.P., Hansen E.J.; RT "Cloning and sequencing of the Haemophilus influenzae exbB and exbD RT genes."; RL Gene 152:89-92(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the TonB-dependent energy-dependent CC transport of various receptor-bound substrates. Protects ExbD from CC proteolytic degradation and functionally stabilizes TonB (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a CC complex with TonB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the ExbB/TolQ 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; U08209; AAA81948.1; -; Genomic_DNA. DR EMBL; L42023; AAC21919.1; -; Genomic_DNA. DR PIR; H64057; H64057. DR RefSeq; NP_438422.1; NC_000907.1. DR RefSeq; WP_005648856.1; NC_000907.1. DR STRING; 71421.HI0253; -. DR EnsemblBacteria; AAC21919; AAC21919; HI_0253. DR GeneID; 949376; -. DR KEGG; hin:HI0253; -. DR PATRIC; 20189031; VBIHaeInf48452_0268. DR eggNOG; ENOG4105M8K; Bacteria. DR eggNOG; COG0811; LUCA. DR KO; K03561; -. DR OMA; SIGANAP; -. DR OrthoDB; EOG6JDWB5; -. DR Proteomes; UP000000579; 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:0008565; F:protein transporter activity; IEA:InterPro. DR InterPro; IPR002898; MotA_ExbB_proton_chnl. DR InterPro; IPR014172; TonB_ExbB_2. DR Pfam; PF01618; MotA_ExbB; 1. DR TIGRFAMs; TIGR02805; exbB2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 150 Biopolymer transport protein ExbB. FT /FTId=PRO_0000145802. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT VARIANT 2 2 V -> L (in strain: TN106). FT VARIANT 25 25 I -> V (in strain: TN106). FT VARIANT 42 42 S -> N (in strain: TN106). FT VARIANT 58 58 R -> S (in strain: TN106). FT VARIANT 100 100 V -> E (in strain: TN106). FT VARIANT 144 144 S -> N (in strain: TN106). SQ SEQUENCE 150 AA; 16729 MW; 4FD9DD61C6CEC44A CRC64; MVQLFDFLQQ YSDYFIIGLL LLMSIIMLAM VIERYLFLRK VSVAHYSTIH ALDIDLNRNM TVISTIGANA PYVGLLGTVI GILLTFYQIG HGGGDIDPSV IMLHLSLALK ATALGILVAI PSMVFYNGLG RKVEVNRLKW KVLSEQKDKE // ID FABG_HAEIN Reviewed; 242 AA. AC P43713; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG; DE EC=1.1.1.100; DE AltName: Full=3-ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase; DE AltName: Full=Beta-ketoacyl-ACP reductase; GN Name=fabG; OrderedLocusNames=HI_0155; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta- CC ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the CC first reductive step in the elongation cycle of fatty acid CC biosynthesis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + CC NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21824.1; -; Genomic_DNA. DR PIR; D64051; D64051. DR RefSeq; NP_438325.1; NC_000907.1. DR RefSeq; WP_005694436.1; NC_000907.1. DR ProteinModelPortal; P43713; -. DR SMR; P43713; 2-241. DR STRING; 71421.HI0155; -. DR EnsemblBacteria; AAC21824; AAC21824; HI_0155. DR GeneID; 951066; -. DR KEGG; hin:HI0155; -. DR PATRIC; 20188805; VBIHaeInf48452_0159. DR eggNOG; ENOG4105CHR; Bacteria. DR eggNOG; ENOG410XNW1; LUCA. DR KO; K00059; -. DR OMA; GMMKRRW; -. DR OrthoDB; EOG6N3CR8; -. DR PhylomeDB; P43713; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR011284; 3oxo_ACP_reduc. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 242 3-oxoacyl-[acyl-carrier-protein] FT reductase FabG. FT /FTId=PRO_0000054673. FT NP_BIND 10 13 NADP. {ECO:0000250}. FT NP_BIND 57 58 NADP. {ECO:0000250}. FT NP_BIND 149 153 NADP. {ECO:0000250}. FT ACT_SITE 149 149 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 35 35 NADP. {ECO:0000250}. FT BINDING 84 84 NADP; via carbonyl oxygen. {ECO:0000250}. FT BINDING 136 136 Substrate. {ECO:0000250}. FT BINDING 182 182 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. SQ SEQUENCE 242 AA; 25507 MW; B3DE2E2C020D2F71 CRC64; MQGKIALVTG STRGIGRAIA EELSSKGAFV IGTATSEKGA EAISAYLGDK GKGLVLNVTD KESIETLLEQ IKNDFGDIDI LVNNAGITRD NLLMRMKDEE WFDIMQTNLT SVYHLSKAML RSMMKKRFGR IINIGSVVGS TGNPGQTNYC AAKAGVVGFS KSLAKEVAAR GITVNVVAPG FIATDMTEVL TDEQKAGILS NVPAGRLGEA KDIAKAVAFL ASDDAGYITG TTLHVNGGLY LS // ID ETTA_HAEIN Reviewed; 556 AA. AC P45127; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Energy-dependent translational throttle protein EttA; DE AltName: Full=Translational regulatory factor EttA; GN Name=ettA; OrderedLocusNames=HI_1252; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: A translation factor that gates the progression of the CC 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the CC P site) into the translation elongation cycle by using a mechanism CC sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E site CC where it modulates the state of the translating ribosome during CC subunit translocation (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Monomer. Probably contacts ribosomal proteins L1, L5, L33 CC and S7, the 16S and 23S rRNA and the P site containing tRNA(fMet) CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates CC with ribosomes and polysomes. {ECO:0000250}. CC -!- DOMAIN: The arm domain (residues 95-139) is inserted in the first CC ABC transporter domain. Probably contacts ribosomal protein L1 (By CC similarity). {ECO:0000250}. CC -!- DOMAIN: The P-site tRNA interaction motif (PtIM domain, residues CC 242-322) interacts with the P site tRNA(fMet) as well as the 23S CC rRNA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF CC family. Translational throttle EttA subfamily. {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; L42023; AAC22902.1; -; Genomic_DNA. DR PIR; G64169; G64169. DR RefSeq; NP_439408.1; NC_000907.1. DR RefSeq; WP_005650218.1; NC_000907.1. DR ProteinModelPortal; P45127; -. DR STRING; 71421.HI1252; -. DR PRIDE; P45127; -. DR EnsemblBacteria; AAC22902; AAC22902; HI_1252. DR GeneID; 950263; -. DR KEGG; hin:HI1252; -. DR PATRIC; 20191185; VBIHaeInf48452_1304. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR OMA; LEIAMDA; -. DR OrthoDB; EOG6F297F; -. DR PhylomeDB; P45127; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; 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:0019843; F:rRNA binding; IEA:UniProtKB-KW. 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-KW. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR022374; ABC_ATP-bd_ChvD. DR InterPro; IPR032781; ABC_tran_Xtn. 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 Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03719; ABC_ABC_ChvD; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding; KW rRNA-binding; Translation regulation; tRNA-binding. FT CHAIN 1 556 Energy-dependent translational throttle FT protein EttA. FT /FTId=PRO_0000093194. FT DOMAIN 7 261 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 325 551 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 357 364 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT REGION 96 140 Arm. {ECO:0000250}. FT REGION 243 323 PtIM. {ECO:0000250}. SQ SEQUENCE 556 AA; 62565 MW; FCCE80E23457A493 CRC64; MSSQFVYTMH RVGKVVPPKR HILKDISLSF FPGAKIGVLG LNGAGKSTLL RIMAGVDKEF EGEARPQPGI KIGYLPQEPK LEPQQTVREA VEEAVSEVKN ALTRLDEVYA LYADPDADFD KLAAEQANLE AIIQAHDGHN LDNQLERAAD ALRLPDWDAK IEHLSGGERR RVALCRLLLE KPDMLLLDEP TNHLDAESVA WLERFLHDYE GTVVAITHDR YFLDNVAGWI LELDRGEGIP WEGNYSSWLE QKEKRLEQEQ ATENARQKSI AKELEWVRQN PKGRQAKSKA RMARFDELNS GEYQKRNETN ELFIPPGPRL GDKVIEVQNL TKSYGDRTLI DDLSFSIPKG AIVGIIGANG AGKSTLFRML SGQEQPDSGS VTMGETVVLA SVDQFRDSMD DKKTVWEEVS NGQDILTIGN FEIPSRAYVG RFNFKGVDQQ KRVGELSGGE RGRLHLAKLL QRGGNVLLLD EPTNDLDVET LRALENAILE FPGCAMVISH DRWFLDRIAT HILDYGDEGK VTFYEGNFSD YEEWKKKTLG DAATQPHRIK YKRIAK // ID EX1_HAEIN Reviewed; 473 AA. AC P45188; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Exodeoxyribonuclease I; DE Short=ExoI; DE Short=Exonuclease I; DE EC=3.1.11.1 {ECO:0000250|UniProtKB:P04995}; DE AltName: Full=DNA deoxyribophosphodiesterase; DE Short=dRPase; GN Name=sbcB; OrderedLocusNames=HI_1377; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly CC processive manner. Also functions as a DNA CC deoxyribophosphodiesterase that releases deoxyribose-phosphate CC moieties following the cleavage of DNA at an apurinic/apyrimidinic CC (AP) site by either an AP endonuclease or AP lyase. CC {ECO:0000250|UniProtKB:P04995}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. CC {ECO:0000250|UniProtKB:P04995}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P04995}; CC Note=Binds 2 Mg(2+) ions per monomer. CC {ECO:0000250|UniProtKB:P04995}; CC -!- SUBUNIT: Monomer. Interacts with ssb (via C-terminus); this CC interaction stimulates the exonuclease activity by recruiting the CC enzyme to its substrate. {ECO:0000250|UniProtKB:P04995}. CC -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C- CC terminal domain form a central positively charged groove which CC binds the DNA. {ECO:0000250|UniProtKB:P04995}. CC -!- SIMILARITY: Contains 1 ExoI C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU01121}. CC -!- SIMILARITY: Contains 1 ExoI SH3-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU01120}. CC -!- SIMILARITY: Contains 1 exonuclease domain. {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23023.1; -; Genomic_DNA. DR PIR; E64120; E64120. DR RefSeq; NP_439529.1; NC_000907.1. DR RefSeq; WP_010869196.1; NC_000907.1. DR ProteinModelPortal; P45188; -. DR STRING; 71421.HI1377; -. DR EnsemblBacteria; AAC23023; AAC23023; HI_1377. DR GeneID; 950828; -. DR KEGG; hin:HI1377; -. DR PATRIC; 20191443; VBIHaeInf48452_1432. DR eggNOG; ENOG4105CJB; Bacteria. DR eggNOG; COG2925; LUCA. DR KO; K01141; -. DR OMA; RDRPAQF; -. DR OrthoDB; EOG6MWN7F; -. DR PhylomeDB; P45188; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central. DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB. DR GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB. DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central. DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR023607; Exodeoxyribonuclease_I. DR InterPro; IPR013620; Exonuc_X-T_C. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR012337; RNaseH-like_dom. DR PANTHER; PTHR11046:SF2; PTHR11046:SF2; 1. DR Pfam; PF08411; Exonuc_X-T_C; 1. DR Pfam; PF00929; RNase_T; 1. DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS51785; EXOI_C; 1. DR PROSITE; PS51784; EXOI_SH3; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA-binding; Exonuclease; KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 473 Exodeoxyribonuclease I. FT /FTId=PRO_0000087111. FT DOMAIN 9 188 Exonuclease. {ECO:0000255}. FT DOMAIN 198 353 ExoI SH3-like. {ECO:0000255|PROSITE- FT ProRule:PRU01120}. FT DOMAIN 356 472 ExoI C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU01121}. FT METAL 11 11 Magnesium 1. FT {ECO:0000250|UniProtKB:P04995}. FT METAL 13 13 Magnesium 2. FT {ECO:0000250|UniProtKB:P04995}. FT METAL 182 182 Magnesium 2. FT {ECO:0000250|UniProtKB:P04995}. FT BINDING 13 13 Substrate. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 109 109 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 120 120 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 124 124 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 138 138 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 144 144 Important for interaction with ssb. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 177 177 Important for activity. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 210 210 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 253 253 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 302 302 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 366 366 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. FT SITE 369 369 Interaction with single-stranded DNA. FT {ECO:0000250|UniProtKB:P04995}. SQ SEQUENCE 473 AA; 54388 MW; 734EA59A4F583965 CRC64; MVKDFSFFIY DYESFGVNPA TDRPAQFAGI RTDADFNIIG EPIMFYCKQT NDYLPAPEAV MVTGITPQEC NEKGLSEPEF AANILAEFSQ PNTCVMGYNN IRYDDEMTRY TFYRNFIEPY EYSWKNGNSR WDLLDLVRAC YALRPEGINW AYDDDGMPSF RLEKLTKANS IEHENAHDAM ADVYATIAMA KLIKEKQPKL FQYFFENRGK KEIEKLVDTG AMTPLVHVSG MLGNYRGNCT WVAPLAWHPT NQNALIVCDL TGDIDNLLAK SADELRADLY TKKLELEERG VSSVPLKLVH INKCPILAPA KTLLPETANR LGIDRQLCLD NLAKLRASFD IREKVADIFN EERQFASNDN VETELYNGFF SNADKNNMAI LRSLPAEKLS EHGLAFEDKR ILELLFHYRA RHFYKTLTRA EQIKWKKYRQ NKLEKSAVEF EASLQRLVEX HSDNSEKLSL LQQVYEYGIK LLG // ID F16PA_HAEIN Reviewed; 333 AA. AC P45292; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 115. DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855}; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855}; GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=HI_1645; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01855}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01855}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}. CC -!- SIMILARITY: Belongs to the FBPase class 1 family. CC {ECO:0000255|HAMAP-Rule:MF_01855}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23292.1; -; Genomic_DNA. DR PIR; G64134; G64134. DR RefSeq; NP_439787.1; NC_000907.1. DR RefSeq; WP_005693654.1; NC_000907.1. DR ProteinModelPortal; P45292; -. DR SMR; P45292; 1-333. DR STRING; 71421.HI1645; -. DR EnsemblBacteria; AAC23292; AAC23292; HI_1645. DR GeneID; 950852; -. DR KEGG; hin:HI1645; -. DR PATRIC; 20192035; VBIHaeInf48452_1721. DR eggNOG; ENOG4105CZI; Bacteria. DR eggNOG; COG0158; LUCA. DR KO; K03841; -. DR OMA; YTTRYIG; -. DR OrthoDB; EOG6X10TR; -. DR PhylomeDB; P45292; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01855; FBPase_class1; 1. DR InterPro; IPR000146; FBPase_class-1. DR InterPro; IPR033391; FBPase_N. DR InterPro; IPR028343; FBPtase. DR InterPro; IPR020548; Fructose_bisphosphatase_AS. DR PANTHER; PTHR11556; PTHR11556; 1. DR Pfam; PF00316; FBPase; 1. DR PIRSF; PIRSF500210; FBPtase; 1. DR PIRSF; PIRSF000904; FBPtase_SBPase; 1. DR PRINTS; PR00115; F16BPHPHTASE. DR PROSITE; PS00124; FBPASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 333 Fructose-1,6-bisphosphatase class 1. FT /FTId=PRO_0000200494. FT REGION 115 118 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 89 89 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 112 112 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 112 112 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 114 114 Magnesium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01855}. FT METAL 115 115 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT METAL 277 277 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT BINDING 208 208 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT BINDING 241 241 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01855}. FT BINDING 271 271 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01855}. SQ SEQUENCE 333 AA; 37077 MW; A129DA77F7895FD2 CRC64; MKTLSEFIVE RQAEYPNAKG ELSGILSSIR LLAKIIHRDI NKAGLTNILG QSGIENVQGE SQMKLDLFAH NTMKAALMAR EEVAGFASEE EESFIAFDTE RGRNAKYIIL TDPLDGSSNI DVNVSVGTIF SIYRRVSPIG SPVTLEDFMQ PGNKQVAAGY IVYGSSTMLV YTTGNGVNGF TYDPSIGTFC LSHENMQMPK EGKIYSINEG QYLKFPQGVK KYIKYCQEED KATHRPYVSR YIGSLVADFH RNLLKGGIYI YPSATNYPNG KLRLLYEGNP IAFLAEQAGG VATDGYRRIL DIEPTALHER VPLFVGSEDM VKKAQEMMEE FKE // ID FABA_HAEIN Reviewed; 177 AA. AC P45159; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase; DE EC=4.2.1.59; DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA; DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase; DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase; DE EC=5.3.3.14; GN Name=fabA; OrderedLocusNames=HI_1325; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Necessary for the introduction of cis unsaturation into CC fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl- CC ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)- CC decenoyl-ACP. Can catalyze the dehydratase reaction for beta- CC hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being CC most active on intermediate chain length (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] CC = trans-dec-2-enoyl-[acyl-carrier-protein] + H(2)O. CC -!- CATALYTIC ACTIVITY: Trans-dec-2-enoyl-[acyl-carrier-protein] = CC cis-dec-3-enoyl-[acyl-carrier-protein]. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA 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; L42023; AAC22972.1; -; Genomic_DNA. DR PIR; G64116; G64116. DR RefSeq; NP_439476.1; NC_000907.1. DR RefSeq; WP_005650386.1; NC_000907.1. DR ProteinModelPortal; P45159; -. DR SMR; P45159; 7-177. DR STRING; 71421.HI1325; -. DR EnsemblBacteria; AAC22972; AAC22972; HI_1325. DR GeneID; 950257; -. DR KEGG; hin:HI1325; -. DR PATRIC; 20191333; VBIHaeInf48452_1377. DR eggNOG; ENOG4108RKI; Bacteria. DR eggNOG; COG0764; LUCA. DR KO; K01716; -. DR OMA; FFDCHFK; -. DR OrthoDB; EOG6VB6SH; -. DR PhylomeDB; P45159; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.129.10; -; 1. DR HAMAP; MF_00405; FabA; 1. DR InterPro; IPR010083; FabA. DR InterPro; IPR013114; FabA_FabZ. DR InterPro; IPR029069; HotDog_dom. DR Pfam; PF07977; FabA; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR01749; fabA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Isomerase; Lipid biosynthesis; KW Lipid metabolism; Lyase; Reference proteome. FT CHAIN 1 177 3-hydroxydecanoyl-[acyl-carrier-protein] FT dehydratase. FT /FTId=PRO_0000091599. FT ACT_SITE 76 76 {ECO:0000250}. SQ SEQUENCE 177 AA; 19465 MW; 17E272B39A11552D CRC64; MQNACTLNKK SSYSYDDLLA SGRGELFGKE GPQLPAPTML MMDRIIEMNE ETGAFGKGYI EAELDIKPEL PFFGCHFIGD PVMPGCLGLD AMWQLVGFYL GWIGGKGKGR ALGVGEVKFT GQILPTAKKV VYRIHMKRVI NRKLVMGMAD GEVEVDGRVI YTATDLKVGL FQDTSTF // ID FABD_HAEIN Reviewed; 312 AA. AC P43712; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase; DE Short=MCT; DE EC=2.3.1.39; GN Name=fabD; OrderedLocusNames=HI_0156; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA CC + a malonyl-[acyl-carrier-protein]. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SIMILARITY: Belongs to the FabD 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; L42023; AAC21825.1; -; Genomic_DNA. DR PIR; E64051; E64051. DR RefSeq; NP_438326.1; NC_000907.1. DR RefSeq; WP_005694437.1; NC_000907.1. DR ProteinModelPortal; P43712; -. DR SMR; P43712; 3-310. DR STRING; 71421.HI0156; -. DR EnsemblBacteria; AAC21825; AAC21825; HI_0156. DR GeneID; 951062; -. DR KEGG; hin:HI0156; -. DR PATRIC; 20188807; VBIHaeInf48452_0160. DR eggNOG; ENOG4105CJF; Bacteria. DR eggNOG; COG0331; LUCA. DR KO; K00645; -. DR OMA; FHCALMQ; -. DR OrthoDB; EOG6W19KW; -. DR PhylomeDB; P43712; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.366.10; -; 2. DR InterPro; IPR001227; Ac_transferase_dom. DR InterPro; IPR014043; Acyl_transferase. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc. DR InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. DR InterPro; IPR020801; PKS_acyl_transferase. DR Pfam; PF00698; Acyl_transf_1; 1. DR PIRSF; PIRSF000446; Mct; 1. DR SMART; SM00827; PKS_AT; 1. DR SUPFAM; SSF52151; SSF52151; 2. DR SUPFAM; SSF55048; SSF55048; 1. DR TIGRFAMs; TIGR00128; fabD; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 312 Malonyl CoA-acyl carrier protein FT transacylase. FT /FTId=PRO_0000194216. FT ACT_SITE 93 93 {ECO:0000250}. FT ACT_SITE 202 202 {ECO:0000250}. SQ SEQUENCE 312 AA; 33425 MW; 6261622B834AE878 CRC64; MKKFAMVFPG QGSQTVGMLA DLATEYPIVI ETFKQASDAL GYDLWYLVQQ GPAEELNKTW QTQPALLAAS VAIYRVWKEK FPQLKPEVMA GHSLGEYSAL VCAGVLDFQD AIKLVELRGK LMQQAVPEGT GAMYAIIGLD NEAIINACKQ AEEGEVVSAV NFNSPGQVVI AGAKAAVERA AALCKEAGAK RALPLAVSVP SHCALMKPAA EQLAVTLENI QINTPTISVL NNVDVKAETE GTEIRTALVR QLYSPVRWTE TVEKMAQDGV LVLAEVGPGK VLNGLTKRIV GDLQAISVND VASFNAVEEF LV // ID ETCB_HAEIN Reviewed; 193 AA. AC P71396; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 113. DE RecName: Full=Electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463}; GN OrderedLocusNames=HI_1684; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00463}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00463}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00463}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00463}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000255|HAMAP-Rule:MF_00463}; CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00463}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00463}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00463}. CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. CC RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}. CC -!- SIMILARITY: Contains 1 4Fe-4S domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|HAMAP-Rule:MF_00463}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23330.1; -; Genomic_DNA. DR PIR; H64174; H64174. DR RefSeq; NP_439826.1; NC_000907.1. DR RefSeq; WP_005650033.1; NC_000907.1. DR ProteinModelPortal; P71396; -. DR STRING; 71421.HI1684; -. DR EnsemblBacteria; AAC23330; AAC23330; HI_1684. DR GeneID; 950511; -. DR KEGG; hin:HI1684; -. DR PATRIC; 20192119; VBIHaeInf48452_1763. DR eggNOG; ENOG4108R3D; Bacteria. DR eggNOG; COG2878; LUCA. DR KO; K03616; -. DR OMA; CIDMLPV; -. DR OrthoDB; EOG60SCM3; -. DR PhylomeDB; P71396; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00463; RsxB_RnfB; 1. DR InterPro; IPR007202; 4Fe-4S_dom. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB. DR InterPro; IPR016463; RnfB/RsxB_Proteobac. DR Pfam; PF04060; FeS; 1. DR PIRSF; PIRSF005784; Elect_transpt_RnfB; 1. DR TIGRFAMs; TIGR01944; rnfB; 1. DR PROSITE; PS51656; 4FE4S; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 193 Electron transport complex subunit B. FT /FTId=PRO_0000216274. FT DOMAIN 29 87 4Fe-4S. FT DOMAIN 101 130 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT DOMAIN 131 160 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT REGION 1 23 Hydrophobic. FT METAL 46 46 Iron-sulfur 1 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 49 49 Iron-sulfur 1 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 54 54 Iron-sulfur 1 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 70 70 Iron-sulfur 1 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 110 110 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 113 113 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 116 116 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 120 120 Iron-sulfur 3 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 140 140 Iron-sulfur 3 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 143 143 Iron-sulfur 3 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 146 146 Iron-sulfur 3 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. FT METAL 150 150 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00463}. SQ SEQUENCE 193 AA; 20762 MW; 6FAA3AF75C5C2385 CRC64; MTFLFIVITL LALIFGAILG FASIKLKVEA DPVVEKIDAI LPQSQCGQCG YPGCKPYAEA ICNGDEITKC IPGGQTTIVK IAEILGVDVP TMEGIEEPIE KVAFIDENMC IGCTKCIQAC PVDAIIGTNK AMHTIIPDLC TGCELCVAPC PTDCILMIPV KKNIDNWDWK FDAKLVIPVM NVDGSEKKLV VGE // ID ETCE_HAEIN Reviewed; 235 AA. AC Q57020; P96346; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Electron transport complex subunit E {ECO:0000255|HAMAP-Rule:MF_00478}; GN OrderedLocusNames=HI_1688; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00478}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00478}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00478}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00478}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00478}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23334.1; -; Genomic_DNA. DR PIR; I64174; I64174. DR RefSeq; NP_439830.1; NC_000907.1. DR RefSeq; WP_005658208.1; NC_000907.1. DR STRING; 71421.HI1688; -. DR EnsemblBacteria; AAC23334; AAC23334; HI_1688. DR GeneID; 950516; -. DR KEGG; hin:HI1688; -. DR PATRIC; 20192127; VBIHaeInf48452_1767. DR eggNOG; ENOG4105DZB; Bacteria. DR eggNOG; COG4660; LUCA. DR KO; K03613; -. DR OMA; FDGFAMG; -. DR OrthoDB; EOG6GBMG7; -. DR PhylomeDB; Q57020; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR HAMAP; MF_00478; RsxE_RnfE; 1. DR InterPro; IPR003667; Rnf-Nqr. DR InterPro; IPR010968; RsxE. DR PANTHER; PTHR30586:SF0; PTHR30586:SF0; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01948; rnfE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 235 Electron transport complex subunit E. FT /FTId=PRO_0000214273. FT TRANSMEM 63 83 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 93 113 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 117 137 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 152 172 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00478}. FT TRANSMEM 206 226 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00478}. SQ SEQUENCE 235 AA; 25845 MW; C054FE596647837A CRC64; MTDLTEKNTA LEEEKIESAV ENQQKSIWKE IFAQGIWKNN PAVVQLLGLC PLLAVSSTAT NALGLGLATM LVLTCTNTVI SLFRQYIPKE IRIPIYVMII ATTVTAVQLL MNAYTYTLYQ SLGIFIPLIV TNCIIIGRAE AFASKNSLLH SIWDGFSMGL GMALSLTILG ALREIIGQGT IFEGIENLFG EQAKFLTHHI YHTDSSFLLF ILPPGAFIGL GLLLAIKNRI DNIKK // ID FBPB1_HAEIN Reviewed; 632 AA. AC Q57341; O05010; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1999, sequence version 2. DT 17-FEB-2016, entry version 102. DE RecName: Full=Putative ferric transport system permease protein FbpB 1; GN Name=fbpB1; Synonyms=afuB; OrderedLocusNames=HI_0129; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Part of the ABC transporter complex FbpABC CC (TC 3.A.1.10.1) involved in Fe(3+) ions import. Probably CC responsible for the translocation of the substrate across the CC membrane (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FbpB 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; L42023; AAC21802.1; -; Genomic_DNA. DR PIR; H64049; H64049. DR RefSeq; NP_438299.1; NC_000907.1. DR RefSeq; WP_010868940.1; NC_000907.1. DR ProteinModelPortal; Q57341; -. DR STRING; 71421.HI0129; -. DR EnsemblBacteria; AAC21802; AAC21802; HI_0129. DR GeneID; 951037; -. DR KEGG; hin:HI0129; -. DR PATRIC; 20188747; VBIHaeInf48452_0132. DR eggNOG; ENOG4107RCV; Bacteria. DR eggNOG; COG1178; LUCA. DR KO; K02011; -. DR OMA; LIVIVQS; -. DR OrthoDB; EOG6P06TJ; -. DR PhylomeDB; Q57341; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Iron; Iron transport; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 632 Putative ferric transport system permease FT protein FbpB 1. FT /FTId=PRO_0000060017. FT TRANSMEM 5 25 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 37 57 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 58 78 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 93 113 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 144 164 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 178 198 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 223 243 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 270 290 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 299 319 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 330 350 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 377 397 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 436 456 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 469 489 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 490 510 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 547 567 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 140 345 ABC transmembrane type-1 1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 431 632 ABC transmembrane type-1 2. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 632 AA; 70263 MW; 5EF460BEBCC14BC0 CRC64; MGWASFNLTW AWFLPVIVYG ALPLLRLPQQ TQAKTELFLT ALSVLFMFIS ATVYKISMGY SVIVLLVGYT ALATLSLAKL KVMQGDKFII ASLLCIILLI FFFIVYPTLA IFVSMFYDGD TFAPQQVMRI LTQSYIVRVI TNSLFLSGFV GIVSTVFGLA FALYTTRIAR RTAFIGKIFS ILPIVTPPFV VGLGVTLMLG RSGYVTEFLS TNFGFSSHNW LYGFNGIAIA QILAFAPISF MILDGALKSV HPSIEEASYT LRANRYQTFY QIIFPLLRPA LANSFLIVFI QSLADFSNPL VLGGSFDVIA TQIYFYIAGS QLDYASASTL GSMLLIFSLA IFIIQYIWIG NRSYVTVSGK SYRGDVQELP NGLKYTIIGM LGFWVIFNMA LYGSIFYGSF TVNWGVNYTL TLKNYAMLFG QGLSDGAWPS LINTLIYAGI AAPLTAFFGL LIAYIVVRKD FQGKKSLEFL TMLCFAVPGT VAGVSYILAF NNAPLYITGT GIIVIISMVM RDLPIGMRAA IAGLGQLDKS LDEASLSLKG SSWKTLCFIV LPLLKPALLS ALVTSFVRAM TTVSAIIFLV TADTRVYRIY FKSCGRRRIR HCDCIRFYFN CCDDGNYFVF RLDCRRYAYF PF // ID FBPC2_HAEIN Reviewed; 356 AA. AC P44513; Q53441; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 126. DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC 2 {ECO:0000255|HAMAP-Rule:MF_01706}; DE EC=3.6.3.30 {ECO:0000255|HAMAP-Rule:MF_01706}; GN Name=fbpC2 {ECO:0000255|HAMAP-Rule:MF_01706}; Synonyms=hitC; GN OrderedLocusNames=HI_0099; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=7927717; RA Sanders J.D., Cope L.D., Hansen E.J.; RT "Identification of a locus involved in the utilization of iron by RT Haemophilus influenzae."; RL Infect. Immun. 62:4515-4525(1994). RN [3] RP CHARACTERIZATION. RC STRAIN=DL63 / Serotype B; RX PubMed=7559648; DOI=10.1074/jbc.270.42.25142; RA Adhikari P., Kirby S.D., Nowalk A.J., Veraldi K.L., Schryvers A.B., RA Mietzner T.A.; RT "Biochemical characterization of a Haemophilus influenzae periplasmic RT iron transport operon."; RL J. Biol. Chem. 270:25142-25149(1995). CC -!- FUNCTION: Part of the ABC transporter complex FbpABC involved in CC Fe(3+) ions import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + Fe(3+)(Out) = ADP + phosphate + CC Fe(3+)(In). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01706}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion CC importer (TC 3.A.1.10) family. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21775.1; -; Genomic_DNA. DR EMBL; S72674; AAB32112.1; -; Genomic_DNA. DR PIR; E64048; E64048. DR PIR; T10888; T10888. DR RefSeq; NP_438273.1; NC_000907.1. DR ProteinModelPortal; P44513; -. DR STRING; 71421.HI0099; -. DR TCDB; 3.A.1.10.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC21775; AAC21775; HI_0099. DR GeneID; 951003; -. DR KEGG; hin:HI0099; -. DR PATRIC; 20188665; VBIHaeInf48452_0102. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR KO; K02010; -. DR OMA; AINICID; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000000579; 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:0015408; F:ferric-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055072; P:iron ion homeostasis; 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; IPR015853; ABC_transpr_FbpC. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51242; FBPC; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Ion transport; Iron; Iron transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 356 Fe(3+) ions import ATP-binding protein FT FbpC 2. FT /FTId=PRO_0000092353. FT DOMAIN 12 246 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01706}. FT NP_BIND 44 51 ATP. {ECO:0000255|HAMAP-Rule:MF_01706}. FT VARIANT 45 45 S -> A (in strain: NTHi TN106). FT VARIANT 97 97 V -> I (in strain: NTHi TN106). FT VARIANT 209 209 S -> A (in strain: NTHi TN106). FT VARIANT 350 350 R -> K (in strain: NTHi TN106). FT VARIANT 356 356 S -> A (in strain: NTHi TN106). SQ SEQUENCE 356 AA; 40360 MW; 78F862F359760813 CRC64; MRLNKMINNP LLTVKNLNKF FNEQQVLHDI SFSLQRGEIL FLLGSSGCGK TTLLRAIAGF EQPSNGEIWL KERLIFGENF NLPTQQRHLG YVVQEGVLFP HLNVYRNIAY GLGNGKGKNS EEKTRIEQIM QLTGIFELAD RFPHQLSGGQ QQRVALARAL APNPELILLD EPFSALDEHL RQQIRQEMLQ ALRQSGASAI FVTHDRDESL RYADKIAIIQ QGKILQIDTP RTLYWSPNHL ETAKFMGESI VLPANLLDEN TAQCQLGNIP IKNKSISQNQ GRILLRPEQF SLFKTSENPT ALFNGQIKQI EFKGKITSIQ IEINGYAIWI ENVISPDLSI GDNLPVYLHR KGLFYS // ID ETCD_HAEIN Reviewed; 358 AA. AC Q57288; O05080; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462}; GN OrderedLocusNames=HI_1686; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a membrane complex involved in electron CC transport. {ECO:0000255|HAMAP-Rule:MF_00462}. CC -!- SUBUNIT: Composed of six subunits. {ECO:0000255|HAMAP- CC Rule:MF_00462}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00462}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00462}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP- CC Rule:MF_00462}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23332.1; -; Genomic_DNA. DR PIR; F64136; F64136. DR RefSeq; NP_439828.1; NC_000907.1. DR RefSeq; WP_005694177.1; NC_000907.1. DR STRING; 71421.HI1686; -. DR EnsemblBacteria; AAC23332; AAC23332; HI_1686. DR GeneID; 950513; -. DR KEGG; hin:HI1686; -. DR PATRIC; 20192123; VBIHaeInf48452_1765. DR eggNOG; ENOG4105D6A; Bacteria. DR eggNOG; COG4658; LUCA. DR KO; K03614; -. DR OMA; YLIRTWG; -. DR OrthoDB; EOG65BDMX; -. DR PhylomeDB; Q57288; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR HAMAP; MF_00462; RsxD_RnfD; 1. DR InterPro; IPR011303; Elect_transpt_RnfD/RsxD. DR InterPro; IPR004338; NADH_Q_Rdtase_NQR2_RnfD. DR PANTHER; PTHR30578:SF0; PTHR30578:SF0; 1. DR Pfam; PF03116; NQR2_RnfD_RnfE; 1. DR TIGRFAMs; TIGR01946; rnfD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 358 Electron transport complex subunit D. FT /FTId=PRO_0000074456. FT TRANSMEM 15 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 39 61 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 79 99 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 125 145 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 220 240 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 248 268 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 271 291 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 297 317 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. FT TRANSMEM 321 341 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00462}. SQ SEQUENCE 358 AA; 39358 MW; 485A7F7C462517EF CRC64; MFKMVSSPHT HSGKLTAHIM LWAILAMMPA FFTQIYYFGF GVVLQSALAI GTAIIAEFIA IKLRGKKPLN YLSDFSVALT ALILAMAIPP YAPYWIIIIG TLCAVLLGKQ VYGGLGQNPF NPAMIGYVIL LISFPLQMTT WMPPINLLQE PPTFSDAFSL IFSGLTTDGF TLSQLTHNID GITQATPLDS AKIFYKSHTQ LNDFYELIKL PIFMGNGTDF AQGWWQINVA FLAGGIFLIL KRVIHWQIPV AMLVTFFCLA TATAFTGFTH LSAISQLVSG AMMFGAFFIA TDPVTASITP RGKIIFGALV GLFVYLIRYH GNYPDGVAFA ILLSNICVPL IDHYTRPRVS GYPTKGRK // ID EX7L_HAEIN Reviewed; 439 AA. AC P43913; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378}; DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378}; GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; GN OrderedLocusNames=HI_0397; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}. CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP- CC Rule:MF_00378}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22056.1; -; Genomic_DNA. DR PIR; D64065; D64065. DR RefSeq; NP_438559.1; NC_000907.1. DR RefSeq; WP_005693773.1; NC_000907.1. DR STRING; 71421.HI0397; -. DR EnsemblBacteria; AAC22056; AAC22056; HI_0397. DR GeneID; 949494; -. DR KEGG; hin:HI0397; -. DR PATRIC; 20189345; VBIHaeInf48452_0416. DR eggNOG; ENOG4105DVS; Bacteria. DR eggNOG; COG1570; LUCA. DR KO; K03601; -. DR OMA; ENAQVRC; -. DR OrthoDB; EOG64R65J; -. DR PhylomeDB; P43913; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00378; Exonuc_7_L; 1. DR InterPro; IPR003753; Exonuc_VII_L. DR InterPro; IPR020579; Exonuc_VII_lsu_C. DR InterPro; IPR025824; OB-fold_nuc-bd_dom. DR Pfam; PF02601; Exonuc_VII_L; 1. DR Pfam; PF13742; tRNA_anti_2; 1. DR TIGRFAMs; TIGR00237; xseA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 439 Exodeoxyribonuclease 7 large subunit. FT /FTId=PRO_0000197849. SQ SEQUENCE 439 AA; 49433 MW; 0638F8C6807F17FA CRC64; MSDNIYSVSQ LNSAARQMLE GNFCQIWLTG EISNFTQPVS GHWYLTLKDE NAQVRCAMFR MKNLRVAFRP QNGMQVLVRA NVSLYEPRGD YQLIIDSMHP AGEGLLQQQF EALKMKLAAE GLFAQNLKKT LPHFSKAVGI ITSSTGAALQ DILHILARRD PSLKVVIYPT AVQGKEATAE IVQMIELANA RQEVDVLIVG RGGGSLEDLW CFNEEEVARA IFRSTLPIIS AVGHETDVTI ADFVADLRAP TPSAAAELVS RNQDELLQQL RHQQQRLDMA FDRLFTRKSQ RLKQLALRLQ NQHPQNQLRA QQAKNEQLTH RLQLAILRQF ENTQQKFTAL SVRLKQNPLP YRIQRYQQGL EQLKVRLNFC VNRQVTERQN KLATLCGKLD GLSPLKVLAR GYSIAENPQG KAIVSVKDVN QGDFITTQVA DGKIVSKVL // ID FABB_HAEIN Reviewed; 406 AA. AC P43710; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1; DE EC=2.3.1.41; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I; DE AltName: Full=Beta-ketoacyl-ACP synthase I; DE Short=KAS I; GN Name=fabB; OrderedLocusNames=HI_1533; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 CC and C-18 fatty acids (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl- CC carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + CC [acyl-carrier-protein]. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases 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; L42023; AAC23183.1; -; Genomic_DNA. DR PIR; A64128; A64128. DR RefSeq; NP_439682.1; NC_000907.1. DR RefSeq; WP_005693560.1; NC_000907.1. DR ProteinModelPortal; P43710; -. DR SMR; P43710; 1-403. DR STRING; 71421.HI1533; -. DR EnsemblBacteria; AAC23183; AAC23183; HI_1533. DR GeneID; 950395; -. DR KEGG; hin:HI1533; -. DR PATRIC; 20191791; VBIHaeInf48452_1604. DR eggNOG; ENOG4105C0Q; Bacteria. DR eggNOG; COG0304; LUCA. DR KO; K00647; -. DR OMA; NHVAMDQ; -. DR OrthoDB; EOG6DG2SR; -. DR PhylomeDB; P43710; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1 406 3-oxoacyl-[acyl-carrier-protein] synthase FT 1. FT /FTId=PRO_0000180313. FT ACT_SITE 162 162 {ECO:0000255|PROSITE-ProRule:PRU10022}. SQ SEQUENCE 406 AA; 42649 MW; A17B8673156FDDAF CRC64; MRRTVITGFG IISSIGNNKE EVLASLKAGK SGIEVVPEFV EMNMRSHVAG TIKLNPSEHI DRKVFRFMGD AAAYAYLSMR EAIEDAGLTE DQVSNDRTGL VIGAGTGSAH NQLVACDAVR GPRGVKAIGP YAVTKTMASS VSACLATPYK IRGVNYSMSS ACATSAHCIG HAVELIQLGK QDVVFAGGAE ELSWECATEF DAMGAVSTKY NETPEKASRA YDANRDGFVI AGGGAVVVVE ELEHALARGA KIYAEIVGYG ATSDGYDMVA PSGEGAERCM KQAMATVDTP IDYINVHGTS TPVGDVKELG AIKNVFGDKI PAISSTKSMT GHSLGAAGAH EAIYTLLMLD NDFIAPSINI ETLDEAAEGC NIVTETKENA GLQTVMSNSF GFGGTNATLI FKRYNG // ID FABZ_HAEIN Reviewed; 148 AA. AC P45012; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406}; DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406}; DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406}; GN Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; GN OrderedLocusNames=HI_1062; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-148. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8917090; DOI=10.1016/0378-1119(96)00139-4; RA Servos S., Khan S., Maskell D.; RT "Cloning and expression of genes encoding lipid A biosynthesis from RT Haemophilus influenzae type b."; RL Gene 175:137-141(1996). CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. CC Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and CC long chain saturated and unsaturated beta-hydroxyacyl-ACPs. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] = CC a trans-2-enoyl-[acyl-carrier protein] + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}. CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22717.1; -; Genomic_DNA. DR EMBL; X87416; CAA60864.1; -; Genomic_DNA. DR PIR; G64180; G64180. DR RefSeq; NP_439220.1; NC_000907.1. DR RefSeq; WP_005651704.1; NC_000907.1. DR ProteinModelPortal; P45012; -. DR STRING; 71421.HI1062; -. DR EnsemblBacteria; AAC22717; AAC22717; HI_1062. DR GeneID; 950037; -. DR KEGG; hin:HI1062; -. DR PATRIC; 20190787; VBIHaeInf48452_1106. DR eggNOG; ENOG4108YXN; Bacteria. DR eggNOG; COG0764; LUCA. DR KO; K02372; -. DR OMA; NGHFPHH; -. DR OrthoDB; EOG6JTCGM; -. DR PhylomeDB; P45012; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.129.10; -; 1. DR HAMAP; MF_00406; FabZ; 1. DR InterPro; IPR013114; FabA_FabZ. DR InterPro; IPR010084; FabZ. DR InterPro; IPR029069; HotDog_dom. DR Pfam; PF07977; FabA; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR01750; fabZ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Lyase; Reference proteome. FT CHAIN 1 148 3-hydroxyacyl-[acyl-carrier-protein] FT dehydratase FabZ. FT /FTId=PRO_0000091686. FT ACT_SITE 55 55 {ECO:0000255|HAMAP-Rule:MF_00406}. SQ SEQUENCE 148 AA; 16583 MW; 804B7B1FD7819A1C CRC64; MSEQQPKVIE SKEIMTLLPH RYPFLLVDRV LDFKEGEWLK AIKNISVNEP CFTGHFPGEP ILPGVLILEA LAQAMGILAF KTHELKGGEL FYFAGIDEAR FKRPVLPGDQ MELNVQVIKK RRGITAFTGV ATVNGEIACE AKLMCARR // ID EX3_HAEIN Reviewed; 267 AA. AC P44318; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Exodeoxyribonuclease III; DE Short=EXO III; DE Short=Exonuclease III; DE EC=3.1.11.2; GN Name=xthA; OrderedLocusNames=HI_0041; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Major apurinic-apyrimidinic endonuclease of E.coli. It CC removes the damaged DNA at cytosines and guanines by cleaving on CC the 3'-side of the AP site by a beta-elimination reaction (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA 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; L42023; AAC21719.1; -; Genomic_DNA. DR PIR; H64044; H64044. DR RefSeq; NP_438214.1; NC_000907.1. DR RefSeq; WP_005663264.1; NC_000907.1. DR ProteinModelPortal; P44318; -. DR SMR; P44318; 1-267. DR STRING; 71421.HI0041; -. DR EnsemblBacteria; AAC21719; AAC21719; HI_0041. DR GeneID; 950938; -. DR KEGG; hin:HI0041; -. DR PATRIC; 20188533; VBIHaeInf48452_0041. DR eggNOG; ENOG4105CGK; Bacteria. DR eggNOG; COG0708; LUCA. DR KO; K01142; -. DR OMA; YTPNSQQ; -. DR OrthoDB; EOG60SCPF; -. DR PhylomeDB; P44318; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.60.10.10; -; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. DR InterPro; IPR020848; AP_endonuclease_F1_CS. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR PANTHER; PTHR22748; PTHR22748; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; SSF56219; 1. DR TIGRFAMs; TIGR00633; xth; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1. DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 267 Exodeoxyribonuclease III. FT /FTId=PRO_0000200022. FT ACT_SITE 109 109 {ECO:0000250}. FT ACT_SITE 151 151 Proton donor/acceptor. {ECO:0000250}. FT METAL 34 34 Magnesium 1. {ECO:0000250}. FT METAL 151 151 Magnesium 2. {ECO:0000250}. FT METAL 153 153 Magnesium 2. {ECO:0000250}. FT METAL 258 258 Magnesium 1. {ECO:0000250}. FT SITE 153 153 Transition state stabilizer. FT {ECO:0000250}. FT SITE 229 229 Important for catalytic activity. FT {ECO:0000250}. FT SITE 259 259 Interaction with DNA substrate. FT {ECO:0000250}. SQ SEQUENCE 267 AA; 31025 MW; 6B3ADE465A1E347C CRC64; MKFISFNING LRARPHQLEA IIEKYQPDVI GLQEIKVADE AFPYEITENL GYHVFHHGQK GHYGVALLTK QEPKVIRRGF PTDNEDAQKR IIMADLETEF GLLTVINGYF PQGESRAHET KFPAKEKFYA DLQQYLEKEH DKSNPILIMG DMNISPSDLD IGIGDENRKR WLRTGKCSFL PEERAWYQRL YDYGLEDSFR KLNPTANDKF SWFDYRSKGF DDNRGLRIDH ILVSQKLAER CVDVGIALDI RAMEKPSDHA PIWAEFK // ID EX7S_HAEIN Reviewed; 84 AA. AC P43914; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 101. DE RecName: Full=Exodeoxyribonuclease 7 small subunit; DE EC=3.1.11.6; DE AltName: Full=Exodeoxyribonuclease VII small subunit; DE Short=Exonuclease VII small subunit; GN Name=xseB; OrderedLocusNames=HI_1437; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large CC acid-insoluble oligonucleotides, which are then degraded further CC into small acid-soluble oligonucleotides. It can also degrade 3' CC or 5' ss regions extending from the termini of duplex DNA CC molecules and displaced ss regions (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in either 5'- to 3'- CC or 3'- to 5'-direction to yield nucleoside 5'-phosphates. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23086.1; -; Genomic_DNA. DR PIR; A64172; A64172. DR RefSeq; NP_439589.1; NC_000907.1. DR RefSeq; WP_005693923.1; NC_000907.1. DR ProteinModelPortal; P43914; -. DR STRING; 71421.HI1437; -. DR EnsemblBacteria; AAC23086; AAC23086; HI_1437. DR GeneID; 950341; -. DR KEGG; hin:HI1437; -. DR PATRIC; 20191579; VBIHaeInf48452_1499. DR eggNOG; ENOG41067QG; Bacteria. DR eggNOG; COG1722; LUCA. DR KO; K03602; -. DR OMA; APLNDYK; -. DR OrthoDB; EOG69KV31; -. DR PhylomeDB; P43914; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro. DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.1040; -; 1. DR HAMAP; MF_00337; Exonuc_7_S; 1. DR InterPro; IPR003761; Exonuc_VII_S. DR Pfam; PF02609; Exonuc_VII_S; 1. DR ProDom; PD028235; Exonuc_VII_S; 1. DR TIGRFAMs; TIGR01280; xseB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 84 Exodeoxyribonuclease 7 small subunit. FT /FTId=PRO_0000206953. SQ SEQUENCE 84 AA; 9512 MW; 4A3CF6FF855BA72E CRC64; MARKPASSQD FETTLVQLEN IVTHLENGDL PLEEALKEFE QGVQLAKLGQ ERLQQAEQRI QILLQKTEDA PLNDYKGNDY EGNA // ID EXBD_HAEIN Reviewed; 147 AA. AC P43009; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Biopolymer transport protein ExbD; GN Name=exbD; OrderedLocusNames=HI_0252; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=7828935; DOI=10.1016/0378-1119(94)00675-I; RA Jarosik G.P., Hansen E.J.; RT "Cloning and sequencing of the Haemophilus influenzae exbB and exbD RT genes."; RL Gene 152:89-92(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the TonB-dependent energy-dependent CC transport of various receptor-bound substrates. {ECO:0000250}. CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a CC complex with TonB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II CC membrane protein. CC -!- SIMILARITY: Belongs to the ExbD/TolR 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; U08209; AAA81949.1; -; Genomic_DNA. DR EMBL; L42023; AAC21918.1; -; Genomic_DNA. DR PIR; G64057; G64057. DR RefSeq; NP_438421.1; NC_000907.1. DR RefSeq; WP_005694050.1; NC_000907.1. DR ProteinModelPortal; P43009; -. DR STRING; 71421.HI0252; -. DR EnsemblBacteria; AAC21918; AAC21918; HI_0252. DR GeneID; 949375; -. DR KEGG; hin:HI0252; -. DR PATRIC; 20189029; VBIHaeInf48452_0267. DR eggNOG; ENOG4105M15; Bacteria. DR eggNOG; COG0848; LUCA. DR KO; K03559; -. DR OMA; WDKEQKV; -. DR OrthoDB; EOG6P5ZH2; -. DR PhylomeDB; P43009; -. DR Proteomes; UP000000579; 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:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003400; ExbD. DR InterPro; IPR014171; TonB_ExbD_2. DR Pfam; PF02472; ExbD; 1. DR TIGRFAMs; TIGR02804; ExbD_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 147 Biopolymer transport protein ExbD. FT /FTId=PRO_0000129120. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TOPO_DOM 31 147 Periplasmic. {ECO:0000255}. FT VARIANT 70 70 K -> R (in strain: TN106). FT VARIANT 73 73 S -> T (in strain: TN106). SQ SEQUENCE 147 AA; 16178 MW; 0219279A468C62DA CRC64; MKKFDEINII PFIDIMLVLL TVVLITASFI SQGKIQVNVP KASTAVAFKS DELAKLLTVT ADKQLYFNDK PISQEALEAE IAQWNKDQKV TLKIDAEASF QDFVTITDML SKNEIKNVAI VSMKDKGKSA GKNSQESTPS QSVPTTP // ID FBPC1_HAEIN Reviewed; 328 AA. AC P44531; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Fe(3+) ions import ATP-binding protein FbpC 1 {ECO:0000255|HAMAP-Rule:MF_01706}; DE EC=3.6.3.30 {ECO:0000255|HAMAP-Rule:MF_01706}; GN Name=fbpC1 {ECO:0000255|HAMAP-Rule:MF_01706}; Synonyms=afuC; GN OrderedLocusNames=HI_0126; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex FbpABC involved in CC Fe(3+) ions import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + Fe(3+)(Out) = ADP + phosphate + CC Fe(3+)(In). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01706}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Fe(3+) ion CC importer (TC 3.A.1.10) family. {ECO:0000255|HAMAP-Rule:MF_01706}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21800.1; -; Genomic_DNA. DR PIR; D64143; D64143. DR RefSeq; NP_438298.1; NC_000907.1. DR RefSeq; WP_010868939.1; NC_000907.1. DR ProteinModelPortal; P44531; -. DR STRING; 71421.HI0126; -. DR EnsemblBacteria; AAC21800; AAC21800; HI_0126. DR GeneID; 951036; -. DR KEGG; hin:HI0126; -. DR PATRIC; 20188745; VBIHaeInf48452_0131. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR KO; K02010; -. DR OMA; DAQRCEI; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P44531; -. DR Proteomes; UP000000579; 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:0015408; F:ferric-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055072; P:iron ion homeostasis; 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; IPR015853; ABC_transpr_FbpC. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51242; FBPC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Ion transport; Iron; Iron transport; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 328 Fe(3+) ions import ATP-binding protein FT FbpC 1. FT /FTId=PRO_0000092352. FT DOMAIN 7 237 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01706}. FT NP_BIND 39 46 ATP. {ECO:0000255|HAMAP-Rule:MF_01706}. SQ SEQUENCE 328 AA; 36047 MW; 59B5298825D3597E CRC64; MSNNDFLVLK NITKAFGKAV VIDNLDLTIK RGTMVTLLGP SGCGKTTVLR LVAGLENPTS GQIFIDGEDV TKSSIQNRDI CIVFQSYALF PHMSIGDNVG YGLKMQGIGK EERAQRVKEA LELVDLAGFE DRFVDQISGG QQQRVALARA LVLKPKVLLF DEPLSNLDAN LRRSMREKIR ELQQRLGITS LYVTHDQTEA FAVSDEVIVM NKGKIMQKAP AKELYLRPNS LFLANFMGES SIFDGKLENG VADINGYSVP LKDAAQFNLP DGECLVGIRP EAIYLAAEGS DAQRCEIKSA VYMGQPLGKW LQTGRGKDLL VNCKPEGF // ID FDHE_HAEIN Reviewed; 302 AA. AC P44452; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Protein FdhE homolog; GN Name=fdhE; OrderedLocusNames=HI_0009; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Necessary for formate dehydrogenase activity. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FdhE 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; L42023; AAC21687.1; -; Genomic_DNA. DR PIR; C64042; C64042. DR RefSeq; NP_438182.1; NC_000907.1. DR RefSeq; WP_005693890.1; NC_000907.1. DR ProteinModelPortal; P44452; -. DR STRING; 71421.HI0009; -. DR PRIDE; P44452; -. DR EnsemblBacteria; AAC21687; AAC21687; HI_0009. DR GeneID; 950905; -. DR KEGG; hin:HI0009; -. DR PATRIC; 20188469; VBIHaeInf48452_0009. DR eggNOG; ENOG4105F46; Bacteria. DR eggNOG; COG3058; LUCA. DR KO; K02380; -. DR OMA; LDQPGLC; -. DR OrthoDB; EOG6JMMTF; -. DR PhylomeDB; P44452; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR Gene3D; 3.90.1670.10; -; 1. DR HAMAP; MF_00611; FdeH; 1. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR006452; Formate_DH_accessory. DR Pfam; PF04216; FdhE; 1. DR PIRSF; PIRSF018296; Format_dh_formtn; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR TIGRFAMs; TIGR01562; FdhE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 302 Protein FdhE homolog. FT /FTId=PRO_0000189642. SQ SEQUENCE 302 AA; 34224 MW; 376F3A031710CBA7 CRC64; MSIKILSESE IKQVANSYQA PAVLFANPKN LYQRRAKRLR DLAQNHPLSD YLLFAADIVE SQLSTLEKNP LPPQQLEQLN TIEPLNAKTF KRNSIWREYL TEILDEIKPK ANEQIAATIE FLEKASSAEL EEMANKLLAQ EFNLVSSDKA VFIWAALSLY WLQAAQQIPH NSQVENAENL HHCPVCGSLP VASMVQIGTS QGLRYLHCNL CESEWNLVRA QCTNCNSHDK LEMWSLNEEL ALVRAETCGS CESYLKMMFQ EKDPYVEPVA DDLASIFLDI EMEEKGFARS GLNPFIFPAE EA // ID FDXH_HAEIN Reviewed; 312 AA. AC P44450; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=Formate dehydrogenase iron-sulfur subunit; DE AltName: Full=Formate dehydrogenase subunit beta; DE Short=FDH subunit beta; GN Name=fdxH; OrderedLocusNames=HI_0007; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Allows to use formate as major electron donor during CC aerobic respiration. The beta chain is an electron transfer unit CC containing 4 cysteine clusters involved in the formation of iron- CC sulfur centers. Electrons are transferred from the gamma chain to CC the molybdenum cofactor of the alpha subunit (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed CC by subunits alpha, beta and gamma. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21685.1; -; Genomic_DNA. DR PIR; A64042; A64042. DR RefSeq; NP_438180.1; NC_000907.1. DR RefSeq; WP_005693893.1; NC_000907.1. DR ProteinModelPortal; P44450; -. DR SMR; P44450; 7-292. DR STRING; 71421.HI0007; -. DR EnsemblBacteria; AAC21685; AAC21685; HI_0007. DR GeneID; 950904; -. DR KEGG; hin:HI0007; -. DR PATRIC; 20188465; VBIHaeInf48452_0007. DR eggNOG; ENOG4105QA4; Bacteria. DR eggNOG; COG0437; LUCA. DR KO; K00124; -. DR OMA; QQDNCIG; -. DR OrthoDB; EOG6XSZQF; -. DR PhylomeDB; P44450; -. DR Proteomes; UP000000579; 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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0045333; P:cellular respiration; IEA:InterPro. DR GO; GO:0015944; P:formate oxidation; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR006470; Formate_DH_bsu_Proteobacteria. DR InterPro; IPR014603; Formate_DH_Fe-S_su. DR InterPro; IPR015246; Formate_DH_TM. DR Pfam; PF13247; Fer4_11; 1. DR Pfam; PF09163; Form-deh_trans; 1. DR PIRSF; PIRSF036298; FDH_4Fe4S; 1. DR TIGRFAMs; TIGR01582; FDH-beta; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat; KW Transmembrane; Transport. FT CHAIN 1 312 Formate dehydrogenase iron-sulfur FT subunit. FT /FTId=PRO_0000159252. FT DOMAIN 35 65 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 97 129 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 130 159 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 164 195 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 44 44 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 47 47 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 50 50 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 106 106 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 109 109 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 114 114 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 118 118 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 139 139 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 142 142 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 145 145 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 149 149 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 166 166 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 169 169 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 181 181 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 185 185 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 312 AA; 34069 MW; AA49DD3C17064866 CRC64; MAGTAQGVQT QDVIKISATS GLTPAPQARD HKVEIAKLID VSTCIGCKAC QVGCSEWNDI RSDINAQCVG VYDNPVDLDA KAWTVMRFNE VEENDRLEWL IRKDGCMHCT EPGCLKACPA PGAIIQYANG IVDFQSDKCI GCGYCIAGCP FNIPRMNPED NRVYKCTLCV DRVSVGQEPA CVKTCPTGAI RFGSKEEMKI YAEQRVADLK SRGYENAGLY DPPGVGGTHV MYVLHHADKP ELYNGLPKDP QIDLSVTLWK DVLKPVAAVA MGGLALAEVA HYLTVGPNVE EDVEDHHHEF EENKPSKGEN NE // ID FBPA_HAEIN Reviewed; 332 AA. AC P35755; Q53439; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 11-NOV-2015, entry version 129. DE RecName: Full=Iron-utilization periplasmic protein; DE AltName: Full=Fe(3+)-binding protein; DE AltName: Full=Iron-regulated 40 kDa protein; DE AltName: Full=Major ferric iron-binding protein; DE Short=MIRP; DE Flags: Precursor; GN Name=fbpA; Synonyms=fbp, hitA; OrderedLocusNames=HI_0097; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=NTHi TN106; RX PubMed=7927717; RA Sanders J.D., Cope L.D., Hansen E.J.; RT "Identification of a locus involved in the utilization of iron by RT Haemophilus influenzae."; RL Infect. Immun. 62:4515-4525(1994). RN [3] RP PROTEIN SEQUENCE OF 24-45. RC STRAIN=Eagan / 8358; RX PubMed=1556062; RA Harkness R.E., Chong P., Klein M.H.; RT "Identification of two iron-repressed periplasmic proteins in RT Haemophilus influenzae."; RL J. Bacteriol. 174:2425-2430(1992). RN [4] RP PROTEIN SEQUENCE OF 24-31. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 24-332. RX PubMed=9360608; DOI=10.1038/nsb1197-919; RA Bruns C.M., Nowalk A.J., Arvai A.S., McTigue M.A., Vaughan K.G., RA Mietzner T.A., McRee D.E.; RT "Structure of Haemophilus influenzae Fe(+3)-binding protein reveals RT convergent evolution within a superfamily."; RL Nat. Struct. Biol. 4:919-924(1997). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 24-332. RX PubMed=11747438; DOI=10.1021/bi0156759; RA Bruns C.M., Anderson D.S., Vaughan K.G., Williams P.A., Nowalk A.J., RA McRee D.E., Mietzner T.A.; RT "Crystallographic and biochemical analyses of the metal-free RT Haemophilus influenzae Fe(3+)-binding protein."; RL Biochemistry 40:15631-15637(2001). CC -!- FUNCTION: Part of the ABC transporter complex FbpABC CC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein CC specifically binds Fe(3+) and is involved in its transmembrane CC transport (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- INDUCTION: By iron deprivation. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21773.1; Type=Frameshift; Positions=14; 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; L42023; AAC21773.1; ALT_FRAME; Genomic_DNA. DR EMBL; S72674; AAB32110.1; -; Genomic_DNA. DR PIR; A41833; A41833. DR PIR; C64048; C64048. DR PIR; T10886; T10886. DR RefSeq; NP_438271.2; NC_000907.1. DR PDB; 1D9V; X-ray; 1.75 A; A=24-332. DR PDB; 1MRP; X-ray; 1.60 A; A=24-332. DR PDB; 1NNF; X-ray; 1.10 A; A=24-332. DR PDB; 1QVS; X-ray; 2.10 A; A=24-332. DR PDB; 1QW0; X-ray; 1.90 A; A=24-332. DR PDB; 2O68; X-ray; 1.70 A; A=24-332. DR PDB; 2O69; X-ray; 2.00 A; A=24-332. DR PDB; 2O6A; X-ray; 1.80 A; A=24-332. DR PDB; 3KN7; X-ray; 1.71 A; A=24-332. DR PDB; 3KN8; X-ray; 1.89 A; A=24-332. DR PDB; 3OD7; X-ray; 1.80 A; A=24-332. DR PDB; 3ODB; X-ray; 1.62 A; A=24-332. DR PDBsum; 1D9V; -. DR PDBsum; 1MRP; -. DR PDBsum; 1NNF; -. DR PDBsum; 1QVS; -. DR PDBsum; 1QW0; -. DR PDBsum; 2O68; -. DR PDBsum; 2O69; -. DR PDBsum; 2O6A; -. DR PDBsum; 3KN7; -. DR PDBsum; 3KN8; -. DR PDBsum; 3OD7; -. DR PDBsum; 3ODB; -. DR ProteinModelPortal; P35755; -. DR SMR; P35755; 24-332. DR STRING; 71421.HI0097; -. DR TCDB; 3.A.1.10.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC21773; AAC21773; HI_0097. DR GeneID; 950998; -. DR KEGG; hin:HI0097; -. DR PATRIC; 20188661; VBIHaeInf48452_0100. DR eggNOG; ENOG4107QKW; Bacteria. DR eggNOG; COG1840; LUCA. DR KO; K02012; -. DR OMA; NGQHKEV; -. DR OrthoDB; EOG625JVF; -. DR EvolutionaryTrace; P35755; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR InterPro; IPR026045; Ferric-bd. DR InterPro; IPR006061; SBP_1_CS. DR InterPro; IPR006059; SBP_1_dom. DR Pfam; PF01547; SBP_bac_1; 1. DR PIRSF; PIRSF002825; CfbpA; 1. DR PROSITE; PS01037; SBP_BACTERIAL_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Ion transport; Iron; Iron transport; Metal-binding; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000269|PubMed:10675023, FT ECO:0000269|PubMed:1556062}. FT CHAIN 24 332 Iron-utilization periplasmic protein. FT /FTId=PRO_0000031703. FT METAL 32 32 Iron. FT METAL 80 80 Iron. FT METAL 218 218 Iron. FT METAL 219 219 Iron. FT VARIANT 24 24 D -> A (in strain: PAK12085 and SB33). FT VARIANT 37 37 T -> A (in strain: TN106). FT VARIANT 37 37 T -> V (in strain: PAK12085 and SB33). FT VARIANT 59 59 E -> A (in strain: TN106). FT VARIANT 103 103 Q -> K (in strain: TN106). FT VARIANT 119 119 I -> V (in strain: TN106). FT VARIANT 284 284 A -> V (in strain: TN106). FT VARIANT 323 323 I -> T (in strain: TN106). FT STRAND 25 29 {ECO:0000244|PDB:1NNF}. FT HELIX 33 46 {ECO:0000244|PDB:1NNF}. FT STRAND 51 55 {ECO:0000244|PDB:1NNF}. FT HELIX 58 68 {ECO:0000244|PDB:1NNF}. FT HELIX 69 71 {ECO:0000244|PDB:1NNF}. FT STRAND 75 80 {ECO:0000244|PDB:1NNF}. FT HELIX 82 84 {ECO:0000244|PDB:1NNF}. FT HELIX 85 90 {ECO:0000244|PDB:1NNF}. FT HELIX 99 103 {ECO:0000244|PDB:1NNF}. FT STRAND 119 131 {ECO:0000244|PDB:1NNF}. FT TURN 132 134 {ECO:0000244|PDB:1NNF}. FT HELIX 137 139 {ECO:0000244|PDB:1NNF}. FT HELIX 144 148 {ECO:0000244|PDB:1NNF}. FT HELIX 150 152 {ECO:0000244|PDB:1NNF}. FT TURN 153 155 {ECO:0000244|PDB:1NNF}. FT STRAND 156 158 {ECO:0000244|PDB:1NNF}. FT HELIX 163 176 {ECO:0000244|PDB:1NNF}. FT HELIX 178 191 {ECO:0000244|PDB:1NNF}. FT STRAND 192 194 {ECO:0000244|PDB:1NNF}. FT HELIX 198 206 {ECO:0000244|PDB:1NNF}. FT STRAND 211 216 {ECO:0000244|PDB:1NNF}. FT HELIX 217 227 {ECO:0000244|PDB:1NNF}. FT HELIX 229 231 {ECO:0000244|PDB:1NNF}. FT STRAND 233 237 {ECO:0000244|PDB:1NNF}. FT HELIX 244 246 {ECO:0000244|PDB:1NNF}. FT STRAND 248 256 {ECO:0000244|PDB:1NNF}. FT HELIX 262 273 {ECO:0000244|PDB:1NNF}. FT HELIX 275 284 {ECO:0000244|PDB:1NNF}. FT STRAND 288 291 {ECO:0000244|PDB:3ODB}. FT HELIX 303 306 {ECO:0000244|PDB:1NNF}. FT HELIX 316 327 {ECO:0000244|PDB:1NNF}. SQ SEQUENCE 332 AA; 36193 MW; 4E6549FD76262CA6 CRC64; MQFKHFKLAT LAAALAFSAN SFADITVYNG QHKEAATAVA KAFEQETGIK VTLNSGKSEQ LAGQLKEEGD KTPADVFYTE QTATFADLSE AGLLAPISEQ TIQQTAQKGV PLAPKKDWIA LSGRSRVVVY DHTKLSEKDM EKSVLDYATP KWKGKIGYVS TSGAFLEQVV ALSKMKGDKV ALNWLKGLKE NGKLYAKNSV ALQAVENGEV PAALINNYYW YNLAKEKGVE NLKSRLYFVR HQDPGALVSY SGAAVLKASK NQAEAQKFVD FLASKKGQEA LVAARAEYPL RADVVSPFNL EPYEKLEAPV VSATTAQDKE HAIKLIEEAG LK // ID FBPB2_HAEIN Reviewed; 506 AA. AC P71338; Q53440; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 100. DE RecName: Full=Fe(3+)-transport system permease protein FbpB 2; DE AltName: Full=Iron(III)-transport system permease protein FbpB 2; GN Name=fbpB2; Synonyms=hitB; OrderedLocusNames=HI_0098; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=7927717; RA Sanders J.D., Cope L.D., Hansen E.J.; RT "Identification of a locus involved in the utilization of iron by RT Haemophilus influenzae."; RL Infect. Immun. 62:4515-4525(1994). CC -!- FUNCTION: Part of the ABC transporter complex FbpABC CC (TC 3.A.1.10.1) involved in Fe(3+) ions import. Probably CC responsible for the translocation of the substrate across the CC membrane (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (FbpC), two transmembrane proteins (FbpB) and a solute-binding CC protein (FbpA). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FbpB subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21774.1; 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; L42023; AAC21774.1; ALT_INIT; Genomic_DNA. DR EMBL; S72674; AAB32111.1; -; Genomic_DNA. DR PIR; T10887; D64048. DR RefSeq; NP_438272.2; NC_000907.1. DR ProteinModelPortal; P71338; -. DR STRING; 71421.HI0098; -. DR TCDB; 3.A.1.10.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC21774; AAC21774; HI_0098. DR GeneID; 951001; -. DR KEGG; hin:HI0098; -. DR PATRIC; 20188663; VBIHaeInf48452_0101. DR eggNOG; ENOG4107QVT; Bacteria. DR eggNOG; COG1178; LUCA. DR KO; K02011; -. DR OMA; SIHYAND; -. DR OrthoDB; EOG6FFS2H; -. DR Proteomes; UP000000579; 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:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Iron; Iron transport; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 506 Fe(3+)-transport system permease protein FT FbpB 2. FT /FTId=PRO_0000060018. FT TRANSMEM 9 29 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 57 77 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 90 110 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 174 194 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 218 238 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 275 295 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 314 334 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 350 370 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 379 399 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 428 448 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 480 500 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 52 233 ABC transmembrane type-1 1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 310 500 ABC transmembrane type-1 2. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT VARIANT 72 72 F -> L (in strain: TN106). FT VARIANT 104 104 G -> C (in strain: TN106). FT VARIANT 116 116 V -> G (in strain: TN106). FT VARIANT 167 167 S -> F (in strain: TN106). FT VARIANT 252 252 T -> M (in strain: TN106). SQ SEQUENCE 506 AA; 56547 MW; ADA28861C1481A1D CRC64; MPRRPPFWLT LLIILIGLPL CLPFLYVILR ATEVGLTRSV ELLFRPRMAE LLSNTMLLMV CVTIGAISLG TFCAFLLERY RFFGKAFFEV AMTLPLCIPA FVSGFTWISL TFRVEVFWGT IGIMTLSSFP LAYLPVSAIL KRLDRSLEEV SLSLGKSPVY TFWYAISPQL KPAIGSSILL IALHMLVEFG AVSILNYQTF TTAIFQEYEM SFNNSTAALL SAVLMAICIL IVFGEIFFRG KQTLYHSGKG VTRPYLVKTL SFGKQCLTFG FFSSIFILSI GVPVIMLIYW LIVGTSLESA GDFSEFLSAF SNSFIISGLG ALLTVMCALP LVWAAVRYRS YLTIWIDRLP YLLHAVPGLV IALSLVYFSI HYANDLYQTF FVIIIAYFML YLPMAQTTLR ASLEQLSDQI EKVGQSLGRN PFYIFRTLTL PAILPGVAAA FALVFLNLMK ELTATLLLTS NDIKTLSIAV WEHTSDAQYA AATPYALMLV LFSGIPVFLL KKYAFK // ID FDHD_HAEIN Reviewed; 270 AA. AC P44449; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Sulfurtransferase FdhD {ECO:0000255|HAMAP-Rule:MF_00187}; GN Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; GN OrderedLocusNames=HI_0005; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts CC as a sulfur carrier protein that transfers sulfur from IscS to the CC molybdenum cofactor prior to its insertion into FDH. CC {ECO:0000255|HAMAP-Rule:MF_00187}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00187}. CC -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000255|HAMAP- CC Rule:MF_00187}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21684.1; -; Genomic_DNA. DR PIR; I64041; I64041. DR RefSeq; NP_438178.1; NC_000907.1. DR RefSeq; WP_005649892.1; NC_000907.1. DR ProteinModelPortal; P44449; -. DR STRING; 71421.HI0005; -. DR EnsemblBacteria; AAC21684; AAC21684; HI_0005. DR GeneID; 950902; -. DR KEGG; hin:HI0005; -. DR PATRIC; 20188461; VBIHaeInf48452_0005. DR eggNOG; ENOG4107H9G; Bacteria. DR eggNOG; COG1526; LUCA. DR KO; K02379; -. DR OMA; PFTQTFS; -. DR OrthoDB; EOG6DG2R8; -. DR PhylomeDB; P44449; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00187; FdhD; 1. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR003786; FdhD. DR Pfam; PF02634; FdhD-NarQ; 1. DR PIRSF; PIRSF015626; FdhD; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00129; fdhD_narQ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 270 Sulfurtransferase FdhD. FT /FTId=PRO_0000152904. FT REGION 253 258 Molybdenum binding. {ECO:0000255|HAMAP- FT Rule:MF_00187}. FT ACT_SITE 116 116 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00187}. FT BINDING 233 233 Molybdenum. {ECO:0000255|HAMAP- FT Rule:MF_00187}. SQ SEQUENCE 270 AA; 30044 MW; F52E9CA72E4A024D CRC64; MQCWIRQTIN FFRKTKNTEK LTALLQQKED ILAVEIPVSL VYNGISHAVM MCSPNNLEDF ALGFSLTEGI INKPEDIYGI DVVEVCNGIE VQIELSSRKF MALKEHRRNL TGRTGCGICG TEQLNQVYKT FPKLDCTFQF DLNLLDSCLI DLQKNQLLGC KTGATHACAF FDLYGSMLAI YEDVGRHVAL DKLLGWHAKS GKPRGFILAS SRASYEMVQK TVACGVEMLV TISAATDLAV TMAEKHNLTL IGFAREGKGN IYSGHLRLHN // ID FDXI_HAEIN Reviewed; 238 AA. AC P44451; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-MAY-2016, entry version 111. DE RecName: Full=Formate dehydrogenase, cytochrome b556 subunit; DE AltName: Full=Formate dehydrogenase subunit gamma; DE Short=FDH subunit gamma; GN Name=fdxI; OrderedLocusNames=HI_0008; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Allows to use formate as major electron donor during CC anaerobic respiration. Subunit gamma is probably the cytochrome CC b556(FDO) component of the formate dehydrogenase (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC Note=Binds 2 heme groups per subunit. Heme 1 is located at the CC cytoplasmic interface, heme 2 is located at the periplasmic CC interface. Electrons are transferred from the periplasmic to the CC cytoplasmic heme. {ECO:0000250}; CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed CC by subunits alpha, beta and gamma. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the formate dehydrogenase gamma subunit 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; L42023; AAC21686.1; -; Genomic_DNA. DR RefSeq; NP_438181.1; NC_000907.1. DR RefSeq; WP_005663315.1; NC_000907.1. DR ProteinModelPortal; P44451; -. DR SMR; P44451; 7-210. DR STRING; 71421.HI0008; -. DR EnsemblBacteria; AAC21686; AAC21686; HI_0008. DR GeneID; 950906; -. DR KEGG; hin:HI0008; -. DR PATRIC; 20188467; VBIHaeInf48452_0008. DR eggNOG; ENOG4108MG3; Bacteria. DR eggNOG; COG2864; LUCA. DR KO; K00127; -. DR OMA; KQDIPWL; -. DR OrthoDB; EOG6B8XH2; -. DR PhylomeDB; P44451; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009326; C:formate dehydrogenase complex; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro. DR GO; GO:0036397; F:formate dehydrogenase (quinone) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central. DR GO; GO:0015944; P:formate oxidation; IBA:GO_Central. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR InterPro; IPR011577; Cyt_b561_bac/Ni-Hgenase. DR InterPro; IPR016174; Di-haem_cyt_TM. DR InterPro; IPR006471; Formate_DH_gsu. DR Pfam; PF01292; Ni_hydr_CYTB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR TIGRFAMs; TIGR01583; formate-DH-gamm; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Electron transport; Heme; Iron; KW Membrane; Metal-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 238 Formate dehydrogenase, cytochrome b556 FT subunit. FT /FTId=PRO_0000087217. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT METAL 23 23 Iron (heme B 1 axial ligand). FT {ECO:0000250}. FT METAL 62 62 Iron (heme B 2 axial ligand). FT {ECO:0000250}. FT METAL 160 160 Iron (heme B 2 axial ligand). FT {ECO:0000250}. FT METAL 174 174 Iron (heme B 1 axial ligand). FT {ECO:0000250}. SQ SEQUENCE 238 AA; 27758 MW; 4D0744AA342066A2 CRC64; MSKIEISNDT RIIRHRTPAR ISHWMLVICF FMTMFTGVAF FFPDFAWLTE ILGTPQIARA IHPFTGILMF FAFIYLALLY WDHNIPEKND IRWAKGVIEV LKGNEHAVAD NGKYNLGQKM LFWTLNLAMV TLLVTGIIMW RQYFSHYFSI PVLRIAILLH SASAFMLFTG ILVHIYMAFW VKGSIRGIVE GWVTVRWAKK HHPRWYREEV LSKLEEDLLN EQSGKVGKTK VLFKGFGK // ID FADR_HAEIN Reviewed; 241 AA. AC P44705; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=Fatty acid metabolism regulator protein {ECO:0000255|HAMAP-Rule:MF_00696}; GN Name=fadR {ECO:0000255|HAMAP-Rule:MF_00696}; GN OrderedLocusNames=HI_0426; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Multifunctional regulator of fatty acid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00696}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00696}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00696}. CC -!- SIMILARITY: Contains 1 HTH gntR-type DNA-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00696}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22085.1; -; Genomic_DNA. DR PIR; A64067; A64067. DR RefSeq; NP_438587.1; NC_000907.1. DR RefSeq; WP_005652140.1; NC_000907.1. DR ProteinModelPortal; P44705; -. DR STRING; 71421.HI0426; -. DR EnsemblBacteria; AAC22085; AAC22085; HI_0426. DR GeneID; 949831; -. DR KEGG; hin:HI0426; -. DR PATRIC; 20189405; VBIHaeInf48452_0446. DR eggNOG; ENOG4105C05; Bacteria. DR eggNOG; COG2186; LUCA. DR KO; K03603; -. DR OMA; IWETSGL; -. DR OrthoDB; EOG6D8B86; -. DR PhylomeDB; P44705; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.20.120.530; -; 1. DR HAMAP; MF_00696; HTH_FadR; 1. DR InterPro; IPR014178; FA-response_TF_FadR. DR InterPro; IPR028374; FadR_C. DR InterPro; IPR008920; TF_FadR/GntR_C. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07840; FadR_C; 1. DR Pfam; PF00392; GntR; 1. DR PRINTS; PR00035; HTHGNTR. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48008; SSF48008; 1. DR TIGRFAMs; TIGR02812; fadR_gamma; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; KW Fatty acid metabolism; Lipid metabolism; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 241 Fatty acid metabolism regulator protein. FT /FTId=PRO_0000050629. FT DOMAIN 11 79 HTH gntR-type. {ECO:0000255|HAMAP- FT Rule:MF_00696}. FT DNA_BIND 39 58 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00696}. SQ SEQUENCE 241 AA; 27764 MW; 34B67860B86D1D36 CRC64; MQNNNDILKA QSPAALAEEY IVKSIWQDVF PAGSNLPSER DLADKIGVTR TTLREVLQRL ARDGWLTIQH GKPTKVNNIW DAAGPNIIET LIALDMQSAP LIIDNMLSLR SKMSESYIYE AVKNSPQKST ALFAELEQLQ NTAQDYTEFD YQLFRQFTVV ANKPFYRLIF NSLKGVYQRI GLLFFKEKKH RELTKQFYLE MQQICLEGNA DAVVDCIRKH NLRSSTYWKA ILERLPQNLS D // ID FDXG_HAEIN Reviewed; 1028 AA. AC P46448; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 17-FEB-2016, entry version 111. DE RecName: Full=Formate dehydrogenase major subunit; DE EC=1.2.1.2; DE AltName: Full=Formate dehydrogenase subunit alpha; DE Short=FDH subunit alpha; DE Flags: Precursor; GN Name=fdxG; OrderedLocusNames=HI_0006; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Allows to use formate as major electron donor during CC anaerobic respiration. Subunit alpha possibly forms the active CC site. CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH. CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed CC by subunits alpha, beta and gamma. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR OMA; RQLIKWN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR006443; Formate-DH-alph_fdnG. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; SSF50692; 2. DR TIGRFAMs; TIGR01553; formate-DH-alph; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Molybdenum; NAD; Oxidoreductase; Periplasm; Reference proteome; KW Selenocysteine; Signal. FT SIGNAL 1 33 Tat-type signal. {ECO:0000255|PROSITE- FT ProRule:PRU00648}. FT CHAIN 34 1028 Formate dehydrogenase major subunit. FT /FTId=PRO_0000063224. FT DOMAIN 43 114 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 50 50 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 53 53 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 57 57 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 100 100 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT NON_STD 204 204 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 1028 AA; 115451 MW; 4A2E55B78B301300 CRC64; MQVSRRKFFK ICAGGMAGTS AAMLGFAPAN VLAAPREYKL LRAFESRNTC TYCAVSCGML LYSTGKPYNS LSSHTGTNTR SKLFHIEGDP DHPVSRGALC PKGAGSLDYV NSESRSLYPQ YRAPGSDKWE RISWKDAIKR IARLMKDDRD ANFVEKDSNG KTVNRWATTG IMTASAMSNE AALLTQKWIR MLGMVPVCNQ ANTUHGPTVA SLAPSFGRGA MTNNWVDIKN ANLIIVQGGN PAEAHPVGFR WAIEAKKNGA KIIVIDPRFN RTASVADLHA PIRSGSDITF LMGVIRYLLE TNQIQHEYVK HYTNASFLID EGFKFEDGLF VGYNEEKRNY DKSKWNYQFD ENGHAKRDMT LQHPRCVINI LKEHVSRYTP EMVERITGVK QKLFLQICEE IGKTSVPNKT MTHLYALGFT EHSIGTQNIR SMAIIQLLLG NMGMPGGGIN ALRGHSNVQG TTDMGLLPMS LPGYMRLPND KDTSYDQYIN AITPKDIVPN QVNYYRHTSK FFVSMMKTFY GDNATKENGW GFDFLPKADR LYDPITHVKL MNEGKLHGWI LQGFNVLNSL PNKNKTLSGM SKLKYLVVMD PLQTESSEFW RNFGESNNVN PAEIQTEVFR LPTTCFAEEE GSIVNSGRWT QWHWKGCDQP GEALPDVDIL SMLREEMHEL YKKEGGQGIE SFEAMTWNYA QPHSPSAVEL AKELNGYALE DLYDPNGNLM YKKGQLLNGF AHLRDDGTTT SGNWLYVGQW TEKGNQTANR DNSDPSGLGC TIGWGFAWPA NRRVLYSRAS LDINGNPWDK NRQLIKWNGK NWNWFDIADY GTQPPGSDTG PFIMSAEGVG RLFAVDKIAN GPMPEHYEPV ESPIDTNPFH PNVVTDPTLR IYKEDREFIG SNKEYPFVAT TYRLTEHFHS WTAQSALNII AQPQQFVEIG EKLAAEKGIQ KGDMVKITSR RGYIKAVAVV TKRLKDLEID GRVVHHIGLP IHWNMKALNG KGNRGFSTNT LTPSWGEAIT QTPEYKTFLV NIEKVGEA // ID FETP_HAEIN Reviewed; 90 AA. AC P44048; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=Probable Fe(2+)-trafficking protein {ECO:0000255|HAMAP-Rule:MF_00686}; GN OrderedLocusNames=HI_0760; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Could be a mediator in iron transactions between iron CC acquisition and iron-requiring processes, such as synthesis and/or CC repair of Fe-S clusters in biosynthetic enzymes. CC {ECO:0000255|HAMAP-Rule:MF_00686}. CC -!- SIMILARITY: Belongs to the Fe(2+)-trafficking protein family. CC {ECO:0000255|HAMAP-Rule:MF_00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22419.1; -; Genomic_DNA. DR PIR; C64013; C64013. DR RefSeq; NP_438919.1; NC_000907.1. DR RefSeq; WP_005648477.1; NC_000907.1. DR ProteinModelPortal; P44048; -. DR SMR; P44048; 1-87. DR STRING; 71421.HI0760; -. DR PRIDE; P44048; -. DR EnsemblBacteria; AAC22419; AAC22419; HI_0760. DR GeneID; 949979; -. DR KEGG; hin:HI0760; -. DR PATRIC; 20190167; VBIHaeInf48452_0799. DR eggNOG; ENOG4105KMG; Bacteria. DR eggNOG; COG2924; LUCA. DR OMA; SKQTMLI; -. DR OrthoDB; EOG654P6H; -. DR PhylomeDB; P44048; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00686; Fe_traffic_YggX; 1. DR InterPro; IPR007457; Fe_traffick_prot_YggX. DR Pfam; PF04362; Iron_traffic; 1. DR PIRSF; PIRSF029827; Fe_traffic_YggX; 1. DR ProDom; PD029191; Fe_traffick_prot_YggX; 1. DR SUPFAM; SSF111148; SSF111148; 1. PE 1: Evidence at protein level; KW Complete proteome; Iron; Reference proteome. FT CHAIN 1 90 Probable Fe(2+)-trafficking protein. FT /FTId=PRO_0000214484. SQ SEQUENCE 90 AA; 10582 MW; EB34CEFF7737B93B CRC64; MARTVFCEYL KKEAEGLDFQ LYPGELGKRI FDSVSKQAWG EWIKKQTMLV NEKKLNMMNA EHRKLLEQEM VNFLFEGKDV HIEGYVPPSN // ID FABI_HAEIN Reviewed; 262 AA. AC P44432; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-APR-2016, entry version 117. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; DE Short=ENR; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; Synonyms=envM; OrderedLocusNames=HI_1734; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP ENZYME REGULATION. RX PubMed=12109908; DOI=10.1021/jm020050+; RA Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., RA Burgess W.J., Heerding D.A., Yuan C.C., Head M.S., Payne D.J., RA Rittenhouse S.F., Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., RA Keller P.M., Polizzi B.J., Qiu X., Janson C.A., Huffman W.F.; RT "Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP RT reductase (FabI)."; RL J. Med. Chem. 45:3246-3256(2002). RN [3] RP ENZYME REGULATION. RX PubMed=12699381; DOI=10.1021/jm0204035; RA Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., RA DeWolf W.E. Jr., Elkins P.A., Head M.S., Jakas D.R., Janson C.A., RA Keller P.M., Manley P.J., Moore T.D., Payne D.J., Pearson S., RA Polizzi B.J., Qiu X., Rittenhouse S.F., Uzinskas I.N., Wallis N.G., RA Huffman W.F.; RT "Indole naphthyridinones as inhibitors of bacterial enoyl-ACP RT reductases FabI and FabK."; RL J. Med. Chem. 46:1627-1635(2003). CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond CC in an enoyl moiety that is covalently linked to an acyl carrier CC protein (ACP). Involved in the elongation cycle of fatty acid CC which are used in the lipid metabolism (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a CC trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH. CC -!- ENZYME REGULATION: Inhibited by 1,4-benzodiazepine and CC naphthyridinone derivatives. {ECO:0000269|PubMed:12109908, CC ECO:0000269|PubMed:12699381}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. FabI 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; L42023; AAC23379.1; -; Genomic_DNA. DR PIR; B64139; B64139. DR RefSeq; NP_439876.2; NC_000907.1. DR RefSeq; WP_005649928.1; NC_000907.1. DR ProteinModelPortal; P44432; -. DR SMR; P44432; 2-259. DR STRING; 71421.HI1734; -. DR BindingDB; P44432; -. DR EnsemblBacteria; AAC23379; AAC23379; HI_1734. DR GeneID; 950535; -. DR KEGG; hin:HI1734; -. DR PATRIC; 20192225; VBIHaeInf48452_1815. DR eggNOG; ENOG4105CSJ; Bacteria. DR eggNOG; COG0623; LUCA. DR KO; K00208; -. DR OMA; EEEMVEC; -. DR OrthoDB; EOG6HF644; -. DR PhylomeDB; P44432; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR PANTHER; PTHR24322:SF317; PTHR24322:SF317; 2. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 262 Enoyl-[acyl-carrier-protein] reductase FT [NADH] FabI. FT /FTId=PRO_0000054901. FT NP_BIND 19 20 NAD. {ECO:0000250}. FT NP_BIND 64 65 NAD. {ECO:0000250}. FT NP_BIND 192 196 NAD. {ECO:0000250}. FT ACT_SITE 146 146 Proton acceptor. {ECO:0000250}. FT ACT_SITE 156 156 Proton acceptor. {ECO:0000250}. FT BINDING 13 13 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 92 92 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 95 95 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000250}. FT BINDING 163 163 NAD. {ECO:0000250}. FT SITE 201 201 Involved in acyl-ACP binding. FT {ECO:0000250}. FT SITE 204 204 Involved in acyl-ACP binding. FT {ECO:0000250}. FT SITE 205 205 Involved in acyl-ACP binding. FT {ECO:0000250}. SQ SEQUENCE 262 AA; 28119 MW; 71CEF6189795388E CRC64; MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE FAKEFGSDIV LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL DGDYVNAATR EGYRIAHDIS AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE RAIPNYNVMC LAKASLEAAT RVMAADLGKE GIRVNAISAG PIRTLAASGI KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI TGEIVHVDAG FSITAMGELG EE // ID FER_HAEIN Reviewed; 113 AA. AC P44428; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 107. DE RecName: Full=2Fe-2S ferredoxin; GN Name=fdx; OrderedLocusNames=HI_0372; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Ferredoxin are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22030.1; -; Genomic_DNA. DR PIR; A64064; A64064. DR RefSeq; NP_438533.1; NC_000907.1. DR RefSeq; WP_005656373.1; NC_000907.1. DR ProteinModelPortal; P44428; -. DR SMR; P44428; 2-110. DR STRING; 71421.HI0372; -. DR EnsemblBacteria; AAC22030; AAC22030; HI_0372. DR GeneID; 949473; -. DR KEGG; hin:HI0372; -. DR PATRIC; 20189289; VBIHaeInf48452_0390. DR eggNOG; ENOG4108ZIT; Bacteria. DR eggNOG; COG0633; LUCA. DR KO; K04755; -. DR OMA; SACGGVC; -. DR OrthoDB; EOG6KMB9X; -. DR PhylomeDB; P44428; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR001055; Adrenodoxin. DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR011536; Fdx_isc. DR Pfam; PF00111; Fer2; 1. DR PRINTS; PR00355; ADRENODOXIN. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR02007; fdx_isc; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00814; ADX; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 113 2Fe-2S ferredoxin. FT /FTId=PRO_0000201171. FT DOMAIN 2 104 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 42 42 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 48 48 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 51 51 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 87 87 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. SQ SEQUENCE 113 AA; 12345 MW; C6FCD4429ABF0F29 CRC64; MPKVIFLPNE DFCPEGMVVD AATGDNLLEV AHNAGVEIHH ACDGSCACTT CHVIVREGFD SLNETSDQEE DMLDKAWGLE MDSRLSCQCV VGNEDLVVEI PKYNLNHANE AAH // ID FLAV_HAEIN Reviewed; 174 AA. AC P44562; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-JAN-2016, entry version 101. DE RecName: Full=Flavodoxin; GN Name=fldA; OrderedLocusNames=HI_0191; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. {ECO:0000250}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21860.1; -; Genomic_DNA. DR PIR; C64053; C64053. DR RefSeq; NP_438360.1; NC_000907.1. DR RefSeq; WP_005648709.1; NC_000907.1. DR ProteinModelPortal; P44562; -. DR SMR; P44562; 2-173. DR STRING; 71421.HI0191; -. DR EnsemblBacteria; AAC21860; AAC21860; HI_0191. DR GeneID; 951101; -. DR KEGG; hin:HI0191; -. DR PATRIC; 20188879; VBIHaeInf48452_0196. DR eggNOG; ENOG4105MHQ; Bacteria. DR eggNOG; COG0716; LUCA. DR KO; K03839; -. DR OMA; ASKGMAD; -. DR OrthoDB; EOG6C5RTW; -. DR PhylomeDB; P44562; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001226; Flavodoxin_CS. DR InterPro; IPR010086; Flavodoxin_lc. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF00258; Flavodoxin_1; 1. DR PIRSF; PIRSF038996; FldA; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Flavoprotein; FMN; KW Reference proteome; Transport. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 174 Flavodoxin. FT /FTId=PRO_0000171633. FT DOMAIN 4 165 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. SQ SEQUENCE 174 AA; 19627 MW; 5E95E895F04BF3F8 CRC64; MAIVGLFYGS DTGNTENIAK QIQKQLGSDL IDIRDIAKSS KEDIEAYDFL LFGIPTWYYG EAQADWDDFF PTLEEIDFTD KLVGIFGCGD QEDYADYFCD AIGTVRDIIE PHGAIVVGNW PTEGYNFEAS KALLEDGTFI GLCIDEDRQP ELTAERVEKW CKQIYDEMCL AELA // ID FOCA_HAEIN Reviewed; 284 AA. AC P43756; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable formate transporter; DE AltName: Full=Formate channel; GN Name=focA; OrderedLocusNames=HI_0181; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the bidirectional transport of formate. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FNT transporter (TC 2.A.44) 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; L42023; AAC21850.1; -; Genomic_DNA. DR PIR; G64052; G64052. DR RefSeq; NP_438349.1; NC_000907.1. DR RefSeq; WP_005694105.1; NC_000907.1. DR STRING; 71421.HI0181; -. DR EnsemblBacteria; AAC21850; AAC21850; HI_0181. DR GeneID; 951090; -. DR KEGG; hin:HI0181; -. DR PATRIC; 20188857; VBIHaeInf48452_0185. DR eggNOG; ENOG4105TMB; Bacteria. DR eggNOG; COG2116; LUCA. DR KO; K06212; -. DR OMA; KGIGCNW; -. DR OrthoDB; EOG6QRW6X; -. DR PhylomeDB; P43756; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015499; F:formate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015724; P:formate transport; IBA:GO_Central. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000292; For/NO2_transpt. DR InterPro; IPR024002; For/NO2_transpt_CS. DR InterPro; IPR023999; Formate_transptr_FocA_put. DR Pfam; PF01226; Form_Nir_trans; 1. DR TIGRFAMs; TIGR00790; fnt; 1. DR TIGRFAMs; TIGR04060; formate_focA; 1. DR PROSITE; PS01005; FORMATE_NITRITE_TP_1; 1. DR PROSITE; PS01006; FORMATE_NITRITE_TP_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 284 Probable formate transporter. FT /FTId=PRO_0000094720. FT TOPO_DOM 1 39 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 40 56 Helical. {ECO:0000255}. FT TOPO_DOM 57 71 Extracellular. {ECO:0000255}. FT TRANSMEM 72 88 Helical. {ECO:0000255}. FT TOPO_DOM 89 119 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 120 136 Helical. {ECO:0000255}. FT TOPO_DOM 137 167 Extracellular. {ECO:0000255}. FT TRANSMEM 168 186 Helical. {ECO:0000255}. FT TOPO_DOM 187 194 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 195 210 Helical. {ECO:0000255}. FT TOPO_DOM 211 262 Extracellular. {ECO:0000255}. FT TRANSMEM 263 280 Helical. {ECO:0000255}. FT TOPO_DOM 281 284 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 284 AA; 30850 MW; 075E621E5C624BF1 CRC64; MASENQKLSS VALTPVEATD YAENTATYKA NKRPFLSFMS GISAGACIAL AFVFYTTTQT ASAGAPWGLT KLVGGLVFSL GVIMVVILGS ELFTSSTLTL VARVGGRITT TQMIRNWIVV YLGNFVGGLF IAAVIWFSGQ TMAANGQWGL TILATAQHKI HHTWFEAFNL GILCNIMVCV AVWMSYSGKT VTDKAFIMIM PIGLFVASGF EHCVANMFMI PMGIITAHFS TPEFWQQIGV DPMKYADLDL YHFIVKNLIP VTLGNIVGGA ICIGVFQRYL TKTH // ID FOLB_HAEIN Reviewed; 118 AA. AC P46362; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Dihydroneopterin aldolase {ECO:0000303|PubMed:9651328}; DE Short=DHNA; DE EC=4.1.2.25 {ECO:0000269|PubMed:9651328}; DE AltName: Full=7,8-dihydroneopterin 2'-epimerase; DE AltName: Full=7,8-dihydroneopterin aldolase; DE AltName: Full=7,8-dihydroneopterin epimerase; DE EC=5.1.99.8 {ECO:0000269|PubMed:9651328}; DE AltName: Full=Dihydroneopterin epimerase; GN Name=folB; OrderedLocusNames=HI_0265; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP REACTION MECHANISM. RX PubMed=9651328; DOI=10.1074/jbc.273.28.17418; RA Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.; RT "Biosynthesis of pteridines in Escherichia coli. Structural and RT mechanistic similarity of dihydroneopterin-triphosphate epimerase and RT dihydroneopterin aldolase."; RL J. Biol. Chem. 273:17418-17424(1998). CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6- CC hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin CC and D-erythro-dihydroneopterin as substrates for the formation of CC 6-hydroxymethyldihydropterin, but it can also catalyze the CC epimerization of carbon 2' of dihydroneopterin to CC dihydromonapterin. {ECO:0000269|PubMed:9651328}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8- CC dihydropterin + glycolaldehyde. {ECO:0000269|PubMed:9651328}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 7,8-dihydromonapterin. CC {ECO:0000269|PubMed:9651328}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=21 uM for 7,8-dihydroneopterin in aldolase reaction CC {ECO:0000269|PubMed:9651328}; CC KM=43 uM for 7,8-dihydroneopterin in epimerase reaction CC {ECO:0000269|PubMed:9651328}; CC KM=16 uM for 7,8-dihydromonapterin in aldolase reaction CC {ECO:0000269|PubMed:9651328}; CC KM=19 uM for 7,8-dihydromonapterin in epimerase reaction CC {ECO:0000269|PubMed:9651328}; CC Vmax=242 umol/h/mg enzyme toward 7,8-dihydroneopterin in CC aldolase reaction {ECO:0000269|PubMed:9651328}; CC Vmax=1.67 umol/h/mg enzyme toward 7,8-dihydroneopterin in CC epimerase reaction {ECO:0000269|PubMed:9651328}; CC Vmax=9.9 umol/h/mg enzyme toward 7,8-dihydromonapterin in CC aldolase reaction {ECO:0000269|PubMed:9651328}; CC Vmax=1.43 umol/h/mg enzyme toward 7,8-dihydromonapterin in CC epimerase reaction {ECO:0000269|PubMed:9651328}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2- CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate CC from 7,8-dihydroneopterin triphosphate: step 3/4. CC -!- SIMILARITY: Belongs to the DHNA 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; L42023; AAC21930.1; -; Genomic_DNA. DR RefSeq; NP_438434.1; NC_000907.1. DR RefSeq; WP_005656206.1; NC_000907.1. DR ProteinModelPortal; P46362; -. DR SMR; P46362; 1-115. DR STRING; 71421.HI0265; -. DR EnsemblBacteria; AAC21930; AAC21930; HI_0265. DR GeneID; 949403; -. DR KEGG; hin:HI0265; -. DR PATRIC; 20189057; VBIHaeInf48452_0280. DR eggNOG; ENOG4107ZVW; Bacteria. DR eggNOG; COG1539; LUCA. DR KO; K01633; -. DR OMA; WEQTIKQ; -. DR OrthoDB; EOG6ND0KG; -. DR PhylomeDB; P46362; -. DR UniPathway; UPA00077; UER00154. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR006156; Dihydroneopterin_aldolase. DR InterPro; IPR006157; FolB_dom. DR Pfam; PF02152; FolB; 1. DR SMART; SM00905; FolB; 1. DR TIGRFAMs; TIGR00525; folB; 1. DR TIGRFAMs; TIGR00526; folB_dom; 1. PE 1: Evidence at protein level; KW Complete proteome; Folate biosynthesis; Isomerase; Lyase; KW Reference proteome. FT CHAIN 1 118 Dihydroneopterin aldolase. FT /FTId=PRO_0000168272. FT REGION 72 73 Substrate binding. FT {ECO:0000250|UniProtKB:P0AC16}. FT ACT_SITE 98 98 Proton donor/acceptor. FT {ECO:0000250|UniProtKB:P0AC16}. FT BINDING 21 21 Substrate. FT {ECO:0000250|UniProtKB:P0AC16}. FT BINDING 53 53 Substrate. FT {ECO:0000250|UniProtKB:P0AC16}. SQ SEQUENCE 118 AA; 13577 MW; 158C716C473DC701 CRC64; MDRVFIEELT VFAQIGVYDW EQQIKQKLVF DLEMAWDCKQ AAETDDVVYC LNYAEVSQAI IDYVESKPFL LIERVAYEVA DLLESRYQLQ GLKIKLSKPK AVAQARNVGV LIVRGCLK // ID FOLC_HAEIN Reviewed; 437 AA. AC P43775; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Folylpolyglutamate synthase; DE EC=6.3.2.17; DE AltName: Full=Folylpoly-gamma-glutamate synthetase; DE Short=FPGS; DE AltName: Full=Tetrahydrofolylpolyglutamate synthase; DE Short=Tetrahydrofolate synthase; GN Name=folC; OrderedLocusNames=HI_1261; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Conversion of folates to polyglutamate derivatives. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L- CC glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1). CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate CC biosynthesis. CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22914.1; -; Genomic_DNA. DR PIR; C64113; C64113. DR RefSeq; NP_439416.1; NC_000907.1. DR RefSeq; WP_005694318.1; NC_000907.1. DR ProteinModelPortal; P43775; -. DR STRING; 71421.HI1261; -. DR EnsemblBacteria; AAC22914; AAC22914; HI_1261. DR GeneID; 950205; -. DR KEGG; hin:HI1261; -. DR PATRIC; 20191203; VBIHaeInf48452_1313. DR eggNOG; ENOG4105DPM; Bacteria. DR eggNOG; COG0285; LUCA. DR KO; K11754; -. DR OMA; VIDEWHC; -. DR OrthoDB; EOG6ZPSW2; -. DR PhylomeDB; P43775; -. DR UniPathway; UPA00850; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR InterPro; IPR001645; Folylpolyglutamate_synth. DR InterPro; IPR018109; Folylpolyglutamate_synth_CS. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR PANTHER; PTHR11136; PTHR11136; 2. DR Pfam; PF08245; Mur_ligase_M; 1. DR PIRSF; PIRSF001563; Folylpolyglu_synth; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01499; folC; 1. DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1. DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW One-carbon metabolism; Reference proteome. FT CHAIN 1 437 Folylpolyglutamate synthase. FT /FTId=PRO_0000168304. FT NP_BIND 55 61 ATP. {ECO:0000250}. SQ SEQUENCE 437 AA; 48826 MW; 04A493395E76CD43 CRC64; MNNMQLKATS PLAEWLSYLE KSHFKPIDLG LDRIKSVAEK LDLLHPVPYV ITVGGTNGKG TTCRLLETIL LNHGLRVGVY SSPHLLRYNE RVRIQNQDLP DEAHTASFAF IDENKTESLT YFEFSTLSAL HLFKQAKLDV VILEVGLGGR LDATNIVDSH LAVITSIDID HTDFLGDTRE AIAFEKAGIF RENCPVVIGE PNVPQTMLDQ AEKLHCQVAR RDVDWLFEQN AENWQWQNKK VRLENLPFCQ IPLANAATVL AAVQYLPFDI SEQTLRKSLQ EVELVGRFQA IKTDKREKLA DYLGVPVETL PTIIVDVGHN PHAAKYLSEK LTALKRSIEG KMIAVCGMLK DKDANGVFEH LTPIIDEWHC VTLGGYRGQS GDELVEKLKS HFPNIQATSD NSVMDGVCTA LKSAVKNDVV LVFGSFHTVA EFWAVVE // ID FOLD_HAEIN Reviewed; 282 AA. AC P44313; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 103. DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576}; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576}; DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576}; GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; GN OrderedLocusNames=HI_0609; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22268.1; -; Genomic_DNA. DR PIR; A64081; A64081. DR RefSeq; NP_438767.1; NC_000907.1. DR RefSeq; WP_005654480.1; NC_000907.1. DR ProteinModelPortal; P44313; -. DR SMR; P44313; 2-277. DR STRING; 71421.HI0609; -. DR EnsemblBacteria; AAC22268; AAC22268; HI_0609. DR GeneID; 950705; -. DR KEGG; hin:HI0609; -. DR PATRIC; 20189797; VBIHaeInf48452_0633. DR eggNOG; ENOG4105CN0; Bacteria. DR eggNOG; COG0190; LUCA. DR KO; K01491; -. DR OMA; GQPMALM; -. DR OrthoDB; EOG6K6VBB; -. DR PhylomeDB; P44313; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01576; THF_DHG_CYH; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom. DR InterPro; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 282 Bifunctional protein FolD. FT /FTId=PRO_0000199307. FT NP_BIND 166 168 NADP. {ECO:0000255|HAMAP-Rule:MF_01576}. FT BINDING 232 232 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01576}. SQ SEQUENCE 282 AA; 30460 MW; 0C39A118DEA5B888 CRC64; MAAKIISGTE LSKQIKANLA DKITHYIEQG KRAPGLAVIL VGADPASQIY VGNKRKSCEE VGILSKSYDL PETTTQNELL AIIDQLNADK NIDGILVQLP LPKQINAEAI IERIDPKKDV DGFHPYNVGR LCQRIPTLRA CTPYGVMKLL ETTGIDLHGK HAVIVGASNI VGRPMSLELL LAGATVTVTH RFTKNLENHV RQADILVVAV GKPNLISGDW IKESAVVIDV GINRVDGKLV GDVEFDKAAE KAAYITPVPG GVGPMTVAML MSNTLYAYEH NK // ID FRDC_HAEIN Reviewed; 132 AA. AC P44892; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Fumarate reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00708}; GN Name=frdC {ECO:0000255|HAMAP-Rule:MF_00708}; GN OrderedLocusNames=HI_0833; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Seems to be involved in the anchoring of the catalytic CC components of the fumarate reductase complex to the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00708}. CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a CC flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two CC hydrophobic anchor proteins (FrdC and FrdD). {ECO:0000255|HAMAP- CC Rule:MF_00708}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00708}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00708}. CC -!- SIMILARITY: Belongs to the FrdC family. {ECO:0000255|HAMAP- CC Rule:MF_00708}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22491.1; -; Genomic_DNA. DR PIR; F64097; F64097. DR RefSeq; NP_438993.2; NC_000907.1. DR ProteinModelPortal; P44892; -. DR STRING; 71421.HI0833; -. DR EnsemblBacteria; AAC22491; AAC22491; HI_0833. DR GeneID; 949847; -. DR KEGG; hin:HI0833; -. DR PATRIC; 20190321; VBIHaeInf48452_0874. DR eggNOG; ENOG4108WJH; Bacteria. DR eggNOG; COG3029; LUCA. DR KO; K00246; -. DR OMA; MTATWWQ; -. DR OrthoDB; EOG6NPM9V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00708; Fumarate_red_C; 1. DR InterPro; IPR003510; Fumarate_red_C. DR Pfam; PF02300; Fumarate_red_C; 1. DR PIRSF; PIRSF000180; FrdC; 1. DR ProDom; PD015900; Fumarate_red_C; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 132 Fumarate reductase subunit C. FT /FTId=PRO_0000196530. FT TRANSMEM 30 50 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00708}. FT TRANSMEM 70 90 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00708}. FT TRANSMEM 110 130 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00708}. SQ SEQUENCE 132 AA; 15265 MW; 03740E833BB58C4A CRC64; MSKRKKYVRP MTATWWQKLD FYKAYMLREA TSVFAVWFCI VLLYGVLCFA SNPMPGLGIL SFIEFLRNPI VVFLNIITLI ATLYHTVTYF LMTPKVMNII VKNERLPHTV VRNALWAVTA LVSVIALVLV YI // ID FIS_HAEIN Reviewed; 99 AA. AC P44966; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=DNA-binding protein Fis {ECO:0000255|HAMAP-Rule:MF_00166}; GN Name=fis {ECO:0000255|HAMAP-Rule:MF_00166}; OrderedLocusNames=HI_0980; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activates ribosomal RNA transcription. Plays a direct CC role in upstream activation of rRNA promoters. {ECO:0000255|HAMAP- CC Rule:MF_00166}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00166}. CC -!- SIMILARITY: Belongs to the transcriptional regulatory Fis family. CC {ECO:0000255|HAMAP-Rule:MF_00166}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22640.1; -; Genomic_DNA. DR PIR; A64106; A64106. DR RefSeq; NP_439143.1; NC_000907.1. DR RefSeq; WP_005651583.1; NC_000907.1. DR ProteinModelPortal; P44966; -. DR SMR; P44966; 12-98. DR STRING; 71421.HI0980; -. DR EnsemblBacteria; AAC22640; AAC22640; HI_0980. DR GeneID; 949985; -. DR KEGG; hin:HI0980; -. DR PATRIC; 20190621; VBIHaeInf48452_1023. DR eggNOG; ENOG4105VY0; Bacteria. DR eggNOG; COG2901; LUCA. DR KO; K03557; -. DR OMA; MSDNANL; -. DR OrthoDB; EOG67HJXZ; -. DR PhylomeDB; P44966; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000787; C:cytoplasmic nucleosome; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. 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 Gene3D; 1.10.10.60; -; 1. DR HAMAP; MF_00166; DNA_binding_Fis; 1. DR InterPro; IPR005412; Fis_DNA-bd. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR Pfam; PF02954; HTH_8; 1. DR PIRSF; PIRSF002097; DNA-binding_Fis; 1. DR PRINTS; PR01591; DNABINDNGFIS. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; SSF46689; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 99 DNA-binding protein Fis. FT /FTId=PRO_0000203884. FT DNA_BIND 75 94 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00166}. SQ SEQUENCE 99 AA; 11167 MW; 83D004DCE3B6406C CRC64; MLEQQRNSAD ALTVSVLNAQ SQVTSKPLRD SVKQALRNYL AQLDGQDVND LYELVLAEVE HPMLDMIMQY TRGNQTRAAN MLGINRGTLR KKLKKYGMG // ID FKBY_HAEIN Reviewed; 241 AA. AC P44760; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable FKBP-type peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Rotamase; GN OrderedLocusNames=HI_0574; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22232.1; -; Genomic_DNA. DR PIR; A64155; A64155. DR RefSeq; NP_438731.1; NC_000907.1. DR RefSeq; WP_005694170.1; NC_000907.1. DR ProteinModelPortal; P44760; -. DR STRING; 71421.HI0574; -. DR EnsemblBacteria; AAC22232; AAC22232; HI_0574. DR GeneID; 949620; -. DR KEGG; hin:HI0574; -. DR PATRIC; 20189703; VBIHaeInf48452_0594. DR eggNOG; ENOG4108V1T; Bacteria. DR eggNOG; COG0545; LUCA. DR KO; K03772; -. DR OMA; RNEPAKF; -. DR OrthoDB; EOG6DRPKW; -. DR PhylomeDB; P44760; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005528; F:FK506 binding; IBA:GO_Central. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central. DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GOC. DR Gene3D; 1.10.287.460; -; 1. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR InterPro; IPR000774; PPIase_FKBP_N. DR PANTHER; PTHR10516; PTHR10516; 2. DR Pfam; PF00254; FKBP_C; 1. DR Pfam; PF01346; FKBP_N; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Reference proteome; Rotamase. FT CHAIN 1 241 Probable FKBP-type peptidyl-prolyl cis- FT trans isomerase. FT /FTId=PRO_0000075373. FT DOMAIN 150 241 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. SQ SEQUENCE 241 AA; 26125 MW; 7AE029E4E747439F CRC64; MLKIQKLSIA ALMVSAVISG QVFAEDNTFD EKAASYAVGT LMGSQMKDLV DSHKEVIKYD NARILDGLKD ALEGKVDVRK DEKIQKTLES IEAKLVAASK AKAESIAKQA KEEGDKFRAE FAKGKDVKTT QSGLMYKIES AGKGDTIKST DTVKVHYTGK LPNGKVFDSS VERGQPVEFQ LDQVIKGWTE GLQLVKKGGK IQFVIAPELG YGEQGAGASI PPNSTLIFDV EVLDVNPKSE K // ID FMT_HAEIN Reviewed; 318 AA. AC P44787; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Methionyl-tRNA formyltransferase; DE EC=2.1.2.9; GN Name=fmt; OrderedLocusNames=HI_0623; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22283.1; -; Genomic_DNA. DR PIR; E64082; E64082. DR RefSeq; NP_438783.1; NC_000907.1. DR RefSeq; WP_005694641.1; NC_000907.1. DR ProteinModelPortal; P44787; -. DR SMR; P44787; 2-317. DR STRING; 71421.HI0623; -. DR EnsemblBacteria; AAC22283; AAC22283; HI_0623. DR GeneID; 949680; -. DR KEGG; hin:HI0623; -. DR PATRIC; 20189841; VBIHaeInf48452_0649. DR eggNOG; ENOG4105CAE; Bacteria. DR eggNOG; COG0223; LUCA. DR KO; K00604; -. DR OMA; GCINSHA; -. DR OrthoDB; EOG6B09WV; -. DR PhylomeDB; P44787; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; IBA:GOC. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_00182; Formyl_trans; 1. DR InterPro; IPR005794; Fmt. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR001555; GART_AS. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00460; fmt; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 318 Methionyl-tRNA formyltransferase. FT /FTId=PRO_0000082973. FT REGION 112 115 Tetrahydrofolate (THF) binding. FT {ECO:0000250}. SQ SEQUENCE 318 AA; 34789 MW; 217051C13BE9B14A CRC64; MKSLNIIFAG TPDFAAQHLQ AILNSQHNVI AVYTQPDKPA GRGKKLQASP VKQLAEQNNI PVYQPKSLRK EEAQSELKAL NADVMVVVAY GLILPKAVLD APRLGCLNVH GSILPRWRGA APIQRSIWAG DVQTGVTIMQ MDEGLDTGDM LHKVYCDILP TETSTSLYNK LAELAPSALI DVLDNLENGK FIAEKQDGSQ SNYAEKLSKE EAQLNWSLSA MQLERNIRAF NPWPIAYFST EDKDGNAHTL KVYQAKVLPH QDKPAGTILS ADKNGIQIAT VDGVLNLLQL QSAGKKPMSA QDLLNGRAEW FTIGKVLA // ID FTN1_HAEIN Reviewed; 162 AA. AC P43707; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 16-MAR-2016, entry version 104. DE RecName: Full=Probable bacterial non-heme ferritin; DE EC=1.16.3.2; GN Name=ftnA; Synonyms=rsgA-A; OrderedLocusNames=HI_1384; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 1-10. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Iron-storage protein. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + O(2) + 6 H(2)O = 4 (FeO(OH)) + 8 CC H(+). CC -!- SUBUNIT: Homooligomer of 24 subunits that assemble into a CC spherical protein shell (12 +/- 1 nM diameter) that can sequester CC at least 2000 iron atoms. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23031.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23031.1; ALT_INIT; Genomic_DNA. DR PIR; A64121; A64121. DR RefSeq; NP_439536.1; NC_000907.1. DR RefSeq; WP_005692004.1; NC_000907.1. DR ProteinModelPortal; P43707; -. DR STRING; 71421.HI1384; -. DR EnsemblBacteria; AAC23031; AAC23031; HI_1384. DR GeneID; 950297; -. DR KEGG; hin:HI1384; -. DR PATRIC; 20191459; VBIHaeInf48452_1440. DR eggNOG; ENOG41090A1; Bacteria. DR eggNOG; COG1528; LUCA. DR KO; K02217; -. DR OMA; CEDKGFE; -. DR OrthoDB; EOG6G4W12; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; PTHR11431; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; Iron; KW Iron storage; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 162 Probable bacterial non-heme ferritin. FT /FTId=PRO_0000201093. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 17 17 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 50 50 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 50 50 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 53 53 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 94 94 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 127 127 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. SQ SEQUENCE 162 AA; 18896 MW; CDF256FA7F02799A CRC64; MLNQIIINKL NDQINLEFYS SNVYLQMSAW CSKHGYEGAA TFLLRHADEE LEHMQKLFNY VSETSGMPIL GKIDAPKHDY SSLREVFEIT LEHEKLVTSK INELVEVTFE SKDYSTFNFL QWYVAEQHEE EKLFSGIIDR FNLVGEDGKG LFFIDRELAT LE // ID FTSA_HAEIN Reviewed; 425 AA. AC P45068; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033}; GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; GN OrderedLocusNames=HI_1142; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell division protein that is involved in the assembly CC of the Z ring. May serve as a membrane anchor for the Z ring. CC {ECO:0000255|HAMAP-Rule:MF_02033}. CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000255|HAMAP- CC Rule:MF_02033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_02033}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent CC manner. Targeted to the membrane through a conserved C-terminal CC amphiphatic helix. {ECO:0000255|HAMAP-Rule:MF_02033}. CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP- CC Rule:MF_02033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22797.1; -; Genomic_DNA. DR PIR; H64185; H64185. DR RefSeq; NP_439300.1; NC_000907.1. DR RefSeq; WP_005693456.1; NC_000907.1. DR ProteinModelPortal; P45068; -. DR STRING; 71421.HI1142; -. DR PRIDE; P45068; -. DR DNASU; 950107; -. DR EnsemblBacteria; AAC22797; AAC22797; HI_1142. DR GeneID; 950107; -. DR KEGG; hin:HI1142; -. DR PATRIC; 20190959; VBIHaeInf48452_1192. DR eggNOG; ENOG4105CIT; Bacteria. DR eggNOG; COG0849; LUCA. DR KO; K03590; -. DR OMA; HTAVIPF; -. DR OrthoDB; EOG6TR0B6; -. DR PhylomeDB; P45068; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_02033; FtsA; 1. DR InterPro; IPR020823; Cell_div_FtsA. DR InterPro; IPR003494; SHS2_FtsA. DR Pfam; PF02491; SHS2_FTSA; 1. DR PIRSF; PIRSF003101; FtsA; 1. DR SMART; SM00842; FtsA; 1. DR TIGRFAMs; TIGR01174; ftsA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Complete proteome; Membrane; Reference proteome. FT CHAIN 1 425 Cell division protein FtsA. FT /FTId=PRO_0000062737. SQ SEQUENCE 425 AA; 45836 MW; AF5C4B808D73CE9D CRC64; MVKGVETKTI VGLEVGTSKV VVVVGEVFPD GVVNVLGVGS CPSKGIDRGS ITDLDAVVGS IQRAIEAAES MADCQIMSVT LAITGEHIQS LNESGFVPIA ESEVTQEEID SALHTASSIK LPEGLSLLHV IPQEYAVDRQ MNIKNPLGLQ GVRLKAQVHL IACHQDWQNN LKKAVERCGL QVDKVVFSGF AATHSVLTED EKDLGVCLID FGAGTMNVMV YTNGALRFSK VIPYAGNIVT NDIAHACTIS RAEAERIKVN YASAFYPARL HGDKKIEVAS IGGRAPRSLT KSDLSLITSA RYTELLGVVK DELDKLKAEL EAKHIKFELI AGVVITGGGA QIEDLKECAS NVFHCQVRIA SPLNITGLTD YVNRPQYSTV VGLLQYNYSN SDDDLISGSD DSEGTFFESI WQGVKKIVNK VRSEF // ID FTSQ_HAEIN Reviewed; 254 AA. AC P45067; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Cell division protein FtsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN Name=ftsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN OrderedLocusNames=HI_1141; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. May control correct divisome assembly. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00911}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00911}. Note=Localizes to the division CC septum. {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00911}. CC -!- SIMILARITY: Contains 1 POTRA domain. {ECO:0000255|PROSITE- CC ProRule:PRU01115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22796.1; -; Genomic_DNA. DR PIR; G64185; G64185. DR RefSeq; NP_439299.1; NC_000907.1. DR RefSeq; WP_005693455.1; NC_000907.1. DR ProteinModelPortal; P45067; -. DR STRING; 71421.HI1141; -. DR EnsemblBacteria; AAC22796; AAC22796; HI_1141. DR GeneID; 950106; -. DR KEGG; hin:HI1141; -. DR PATRIC; 20190957; VBIHaeInf48452_1191. DR eggNOG; ENOG4105K7E; Bacteria. DR eggNOG; COG1589; LUCA. DR KO; K03589; -. DR OMA; WHATLGN; -. DR OrthoDB; EOG6XM7B0; -. DR PhylomeDB; P45067; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:InterPro. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00911; FtsQ_subfam; 1. DR InterPro; IPR005548; Cell_div_FtsQ/DivIB. DR InterPro; IPR026579; FtsQ. DR InterPro; IPR013685; POTRA_FtsQ_type. DR Pfam; PF03799; FtsQ; 1. DR Pfam; PF08478; POTRA_1; 1. DR PROSITE; PS51779; POTRA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 254 Cell division protein FtsQ. FT /FTId=PRO_0000160581. FT TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TOPO_DOM 49 254 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT DOMAIN 54 124 POTRA. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 254 AA; 29323 MW; 13B8D25862085DAF CRC64; MNILKRKTPQ NIRFGEQKPK YYFHIRAFAV LLGVFFLLGV YFNWQSILEK MDDKPISAFA LVGQNTFTTA DDIKESLLKM GELKGFWGQD VAPIQEQIEA LPWVKGAIVR KMWPNRLSIW VSEYQPVAFW NQNQFVTLDG IVFQLPSVRL TAKNLPYLGG PDYQSLKVIE TWNQIYINLK SNNIMAKGIN IDDRGAWQVQ LDNDIVLKLG RGDWKSKLER FVTIYPQIDV PENKKIDYID LRYTAGAAVG MVDR // ID FTSW_HAEIN Reviewed; 394 AA. AC P45064; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Putative lipid II flippase FtsW {ECO:0000255|HAMAP-Rule:MF_00913}; DE AltName: Full=Cell division protein FtsW {ECO:0000255|HAMAP-Rule:MF_00913}; GN Name=ftsW {ECO:0000255|HAMAP-Rule:MF_00913}; GN OrderedLocusNames=HI_1137; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein. Transports lipid-linked CC peptidoglycan precursors from the inner to the outer leaflet of CC the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00913}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00913}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00913}. Note=Localizes to the division septum. CC {ECO:0000255|HAMAP-Rule:MF_00913}. CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22792.1; -; Genomic_DNA. DR PIR; C64185; C64185. DR RefSeq; NP_439295.1; NC_000907.1. DR RefSeq; WP_010869137.1; NC_000907.1. DR STRING; 71421.HI1137; -. DR EnsemblBacteria; AAC22792; AAC22792; HI_1137. DR GeneID; 950104; -. DR KEGG; hin:HI1137; -. DR PATRIC; 20190949; VBIHaeInf48452_1187. DR eggNOG; ENOG4105CNI; Bacteria. DR eggNOG; COG0772; LUCA. DR KO; K03588; -. DR OMA; MEPDFGA; -. DR OrthoDB; EOG68M4JQ; -. DR PhylomeDB; P45064; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00913; FtsW_proteobact; 1. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; Cell_cycle_FtsW/RodA. DR InterPro; IPR013437; FtsW. DR PANTHER; PTHR30474; PTHR30474; 1. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR TIGRFAMs; TIGR02614; ftsW; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 394 Putative lipid II flippase FtsW. FT /FTId=PRO_0000062704. FT TOPO_DOM 1 27 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 49 66 Periplasmic. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 88 93 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 115 120 Periplasmic. {ECO:0000255}. FT TRANSMEM 121 141 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 142 155 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TRANSMEM 177 197 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 198 198 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 220 277 Periplasmic. {ECO:0000255}. FT TRANSMEM 278 298 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 299 322 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 344 353 Periplasmic. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00913}. FT TOPO_DOM 375 394 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 394 AA; 44552 MW; 820264F925036B36 CRC64; MEFLQNIKKN YDEWTRITPQ GLLYDRALFW LFVILLLIGL VAVTSASIPY SSRLFNDPFY FAKRDAIYVL LSLLTCYISL QISSSQWEKW HAKIFLFSVI LLLLVPFIGT SVNGAKRWIS LGILNFQPAE FAKLALTCFL ASYFTRRYDE VRSRHVSIFK PFIVMLVLGC FLLLQPDLGS TVVLFIIMSG MLFIVGAKIL QFVGLIALGG ILFVWLVLTA SYRLKRFIGF LEPFKEPYGT GFQLTNSLIA FGRGEITGEG LGNSIQKLDY LPEAHTDFIM AIIGEEFGFI GILIVILLLG LLIFRAMKIG RESLMLEQRF RGFFALGIGF WIFFQGFVNL GMALGMLPTK GLTFPLVSYG GSSIIIMSAT IGILLRIDHE NRLFRIGQAR LRDD // ID FTSY_HAEIN Reviewed; 414 AA. AC P44870; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. 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}; GN OrderedLocusNames=HI_0768; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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). Interaction with SRP-RNC leads to CC the transfer of the RNC complex to the Sec translocase for CC insertion into the membrane, the hydrolysis of GTP by both Ffh and CC FtsY, and the dissociation of the SRP-FtsY complex into the CC individual components. {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. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein; Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP- CC 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; L42023; AAC22426.1; -; Genomic_DNA. DR PIR; G64091; G64091. DR RefSeq; NP_438927.1; NC_000907.1. DR RefSeq; WP_005693162.1; NC_000907.1. DR ProteinModelPortal; P44870; -. DR SMR; P44870; 111-409. DR STRING; 71421.HI0768; -. DR EnsemblBacteria; AAC22426; AAC22426; HI_0768. DR GeneID; 950144; -. DR KEGG; hin:HI0768; -. DR PATRIC; 20190187; VBIHaeInf48452_0807. DR eggNOG; ENOG4105CCP; Bacteria. DR eggNOG; COG0552; LUCA. DR KO; K03110; -. DR OMA; NKAELMN; -. DR OrthoDB; EOG62K1ZH; -. DR PhylomeDB; P44870; -. DR Proteomes; UP000000579; 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 inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW GTP-binding; Membrane; Nucleotide-binding; Receptor; KW Reference proteome. FT CHAIN 1 414 Signal recognition particle receptor FT FtsY. FT /FTId=PRO_0000101132. FT NP_BIND 216 223 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 298 302 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 362 365 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. SQ SEQUENCE 414 AA; 46147 MW; DB2C457C651C52C0 CRC64; MNDIFIGLQL REHFMAEENK KGGFWASLFG RNKKQDEPKI EPIIEEEKIK DIEPSIEKFE ANDLVEEEKI QEISTALEPI EEIIEAKNLE DEFQPVVEIE TREKPSEGGF FSRLVKGLLK TKQNIGAGFR GFFLGKKIDD ELFEELEEQL LIADIGVPTT SKIIKNLTEH ASRKELQDAE LLYQQLKVEM ADILEPVAQP LEIDSTKKPY VILMVGVNGV GKTTTIGKLA RKFQAEGKSV MLAAGDTFRA AAVEQLQVWG ERNHIPVVAQ STGSDSASVI FDAMQSAAAR NIDILIADTA GRLQNKNNLM DELKKIVRVM KKYDETAPHE IMLTLDAGTG QNAISQAKLF NEAVGLTGIS LTKLDGTAKG GVIFAIADQF KLPIRYIGVG EKIEDLREFN AKEFIEALFV HEEE // ID FTSI_HAEIN Reviewed; 610 AA. AC P45059; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 110. DE RecName: Full=Peptidoglycan synthase FtsI {ECO:0000250|UniProtKB:P0AD68}; DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P0AD68}; DE AltName: Full=Penicillin-binding protein 3 {ECO:0000250|UniProtKB:P0AD68}; DE Short=PBP-3 {ECO:0000250|UniProtKB:P0AD68}; DE AltName: Full=Peptidoglycan glycosyltransferase 3 {ECO:0000250|UniProtKB:P0AD68}; GN Name=ftsI; OrderedLocusNames=HI_1132; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein that is required for the CC synthesis of peptidoglycan at the division septum. Catalyzes the CC synthesis of cross-linked peptidoglycan from the lipid-linked CC precursors. {ECO:0000250|UniProtKB:P0AD68}. CC -!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L- CC Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)- CC Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl CC diphosphate. {ECO:0000250|UniProtKB:P0AD68}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000250|UniProtKB:P0AD68}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0AD68}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P0AD68}; Periplasmic side CC {ECO:0000250|UniProtKB:P0AD68}. Note=Localizes to the division CC septum during the later stages of cell growth and throughout CC septation. {ECO:0000250|UniProtKB:P0AD68}. CC -!- SIMILARITY: Belongs to the transpeptidase 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; L42023; AAC22787.1; -; Genomic_DNA. DR PIR; G64184; G64184. DR RefSeq; NP_439290.1; NC_000907.1. DR RefSeq; WP_005693446.1; NC_000907.1. DR ProteinModelPortal; P45059; -. DR STRING; 71421.HI1132; -. DR DrugBank; DB00303; Ertapenem. DR EnsemblBacteria; AAC22787; AAC22787; HI_1132. DR GeneID; 950626; -. DR KEGG; hin:HI1132; -. DR PATRIC; 20190939; VBIHaeInf48452_1182. DR eggNOG; ENOG4105CJN; Bacteria. DR eggNOG; COG0768; LUCA. DR KO; K03587; -. DR OMA; LPIWSTY; -. DR OrthoDB; EOG6N0HHV; -. DR PhylomeDB; P45059; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; 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:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR005311; PBP_dimer. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF03717; PBP_dimer; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56519; SSF56519; 1. DR SUPFAM; SSF56601; SSF56601; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 610 Peptidoglycan synthase FtsI. FT /FTId=PRO_0000195457. FT TOPO_DOM 1 42 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 43 65 Helical. {ECO:0000255}. FT TOPO_DOM 66 610 Periplasmic. {ECO:0000305}. FT ACT_SITE 327 327 Acyl-ester intermediate. FT {ECO:0000250|UniProtKB:P0AD68}. SQ SEQUENCE 610 AA; 67166 MW; 8A1DA5538235C0A3 CRC64; MVKFNSSRKS GKSKKTIRKL TAPETVKQNK PQKVFEKCFM RGRYMLSTVL ILLGLCALVA RAAYVQSINA DTLSNEADKR SLRKDEVLSV RGSILDRNGQ LLSVSVPMSA IVADPKTMLK ENSLADKERI AALAEELGMT ENDLVKKIEK NSKSGYLYLA RQVELSKANY IRRLKIKGII LETEHRRFYP RVEEAAHVVG YTDIDGNGIE GIEKSFNSLL VGKDGSRTVR KDKRGNIVAH ISDEKKYDAQ DVTLSIDEKL QSMVYREIKK AVSENNAESG TAVLVDVRTG EVLAMATAPS YNPNNRVGVK SELMRNRAIT DTFEPGSTVK PFVVLTALQR GVVKRDEIID TTSFKLSGKE IVDVAPRAQQ TLDEILMNSS NRGVSRLALR MPPSALMETY QNAGLSKPTD LGLIGEQVGI LNANRKRWAD IERATVAYGY GITATPLQIA RAYATLGSFG VYRPLSITKV DPPVIGKRVF SEKITKDIVG ILEKVAIKNK RAMVEGYRVG VKTGTARKIE NGHYVNKYVA FTAGIAPISD PRYALVVLIN DPKAGEYYGG AVSAPVFSNI MGYALRANAI PQDAEAAENT TTKSAKRIVY IGEHKNQKVN // ID FTSK_HAEIN Reviewed; 529 AA. AC P45264; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=DNA translocase FtsK; GN Name=ftsK; OrderedLocusNames=HI_1592; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May function as a DNA motor that moves dsDNA in an ATP- CC dependent manner towards the dif recombination site, which is CC located within the replication terminus region. Translocation CC stops specifically at Xer-dif sites, where FtsK interacts with the CC Xer recombinase, allowing activation of chromosome unlinking by CC recombination. FtsK orienting polar sequences (KOPS) guide the CC direction of DNA translocation. FtsK can remove proteins from DNA CC as it translocates, but translocation stops specifically at XerCD- CC dif site, thereby preventing removal of XerC and XerD from dif (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: Although strongly related to FtsK, it lacks the CC typical transmembrane domains located at the N-terminal part of CC FtsK. CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FtsK domain. {ECO:0000255|PROSITE- CC ProRule:PRU00289}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23240.1; -; Genomic_DNA. DR PIR; G64131; G64131. DR ProteinModelPortal; P45264; -. DR SMR; P45264; 40-446. DR EnsemblBacteria; AAC23240; AAC23240; HI_1592. DR OMA; MILATHR; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 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 Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002543; FtsK_dom. DR InterPro; IPR018541; Ftsk_gamma. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF09397; Ftsk_gamma; 1. DR Pfam; PF01580; FtsK_SpoIIIE; 1. DR SMART; SM00843; Ftsk_gamma; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50901; FTSK; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Chromosome partition; KW Complete proteome; DNA-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 529 DNA translocase FtsK. FT /FTId=PRO_0000098261. FT DOMAIN 174 387 FtsK. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. FT NP_BIND 194 199 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00289}. SQ SEQUENCE 529 AA; 58768 MW; 0C0F882EADFE726D CRC64; MEAVQLDKNQ EPNYKGYSGS LIHPAFQQQT TKREKPSTPL PSLDLLLKYP PNEQRITPDE IMETSQRIEQ QLRNFNVKAS VKDVLVGPVV TRYELELQPG VKASKVTSID TDLARALMFR SIRVAEVIPG KPYIGIETPN LHRQMVPLRD VLDSNEFRDS KATLPIALGK DISGKPVIVD LAKMPHLLVA GSTGSGKSVG VNTMILSLLY RVQPEDVKFI MIDPKVVELS VYNDIPHLLT PVVTDMKKAA NALRWCVDEM ERRYQLLSAL RVRNIEGFNE KIDEYEAMGM PVPNPIWRLG DTMDAMPPAL KKLSYIVVIV DEFADLMMVA GKQIEELIAR LAQKARAIGI HLILATQRPS VDVITGLIKA NIPSRIAFTV ASKIDSRTIL DQGGAEALLG RGDMLYSGQG SSDLIRVHGA YMSDDEVINI ADDWRARGKP DYIDGILESA DDEESSEKGI SSGGELDPLF DEVMDFVINT GTTSVSSIQR KFSVGFNRAA RIMDQMEEQG IVSPMQNGKR EILSHRPEY // ID FPG_HAEIN Reviewed; 271 AA. AC P44948; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 122. 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=HI_0946; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22606.1; -; Genomic_DNA. DR PIR; A64104; A64104. DR RefSeq; NP_439106.1; NC_000907.1. DR RefSeq; WP_005693293.1; NC_000907.1. DR ProteinModelPortal; P44948; -. DR SMR; P44948; 2-269. DR STRING; 71421.HI0946; -. DR EnsemblBacteria; AAC22606; AAC22606; HI_0946. DR GeneID; 949949; -. DR KEGG; hin:HI0946; -. DR PATRIC; 20190549; VBIHaeInf48452_0987. DR eggNOG; ENOG4105ERD; Bacteria. DR eggNOG; COG0266; LUCA. DR KO; K10563; -. DR OMA; WHRRGKY; -. DR OrthoDB; EOG6QP131; -. DR PhylomeDB; P44948; -. DR Proteomes; UP000000579; 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 2 271 Formamidopyrimidine-DNA glycosylase. FT /FTId=PRO_0000170828. FT ZN_FING 235 269 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 57 57 Proton donor; for beta-elimination FT activity. {ECO:0000250}. FT ACT_SITE 259 259 Proton donor; for delta-elimination FT activity. {ECO:0000250}. FT BINDING 90 90 DNA. {ECO:0000250}. FT BINDING 109 109 DNA. {ECO:0000250}. FT BINDING 150 150 DNA. {ECO:0000250}. SQ SEQUENCE 271 AA; 30772 MW; 571E67EF1D0978E1 CRC64; MPELPEVETA LRGISPYLKN FTIEKVVVRQ PKLRWAVSEE LITLKNVKIV DLTRRAKYLI IHTEKGYIIG HLGMSGSVRI VPQDSAIDKH DHIDIVVNNG KLLRYNDPRR FGAWLWTENL DDFHLFLKLG PEPLSDEFNA EYLFKKSRQK STALKTFLMD NAVVVGVGNI YTNESLFICG IHPLKLAKNL TRNQCFSLVN TIKDVLRKAI IQGGTTLKDF LQPDGRPGYF AQELLVYGNK DKPCPKCGGK IESLIIGQRN SFFCPKCQKR G // ID FRDD_HAEIN Reviewed; 114 AA. AC P44891; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Fumarate reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00709}; GN Name=frdD {ECO:0000255|HAMAP-Rule:MF_00709}; GN OrderedLocusNames=HI_0832; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Seems to be involved in the anchoring of the catalytic CC components of the fumarate reductase complex to the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00709}. CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a CC flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two CC hydrophobic anchor proteins (FrdC and FrdD). {ECO:0000255|HAMAP- CC Rule:MF_00709}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00709}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00709}. CC -!- SIMILARITY: Belongs to the FrdD family. {ECO:0000255|HAMAP- CC Rule:MF_00709}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22490.1; -; Genomic_DNA. DR PIR; E64097; E64097. DR RefSeq; NP_438992.1; NC_000907.1. DR RefSeq; WP_005648338.1; NC_000907.1. DR ProteinModelPortal; P44891; -. DR SMR; P44891; 1-114. DR STRING; 71421.HI0832; -. DR EnsemblBacteria; AAC22490; AAC22490; HI_0832. DR GeneID; 949846; -. DR KEGG; hin:HI0832; -. DR PATRIC; 20190319; VBIHaeInf48452_0873. DR eggNOG; ENOG4108VP9; Bacteria. DR eggNOG; COG3080; LUCA. DR KO; K00247; -. DR OMA; GMWSAIV; -. DR OrthoDB; EOG6MPWX0; -. DR PhylomeDB; P44891; -. DR Proteomes; UP000000579; 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:0006106; P:fumarate metabolic process; IEA:InterPro. DR HAMAP; MF_00709; Fumarate_red_D; 1. DR InterPro; IPR003418; Fumarate_red_D. DR Pfam; PF02313; Fumarate_red_D; 1. DR PIRSF; PIRSF000179; FrdD; 1. DR ProDom; PD015693; Fumarate_red_D; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 114 Fumarate reductase subunit D. FT /FTId=PRO_0000196546. FT TRANSMEM 24 44 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00709}. FT TRANSMEM 50 70 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00709}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00709}. SQ SEQUENCE 114 AA; 12636 MW; C970ABB17E61E189 CRC64; MVDQNPKRSG EPPVWLMFGA GGTVSAIFLP VVILIIGLLL PFGLVDVHNL ITFAYSWIGK LVILVLTIFP MWCGLHRIHH GMHDLKVHVP AGGFIFYGLA TIYTVWVLFA VINL // ID FTN2_HAEIN Reviewed; 165 AA. AC P43708; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Probable bacterial non-heme ferritin-like protein; GN Name=ftnB; Synonyms=rsgA-B; OrderedLocusNames=HI_1385; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23032.1; -; Genomic_DNA. DR PIR; B64121; B64121. DR RefSeq; NP_439537.1; NC_000907.1. DR RefSeq; WP_005693978.1; NC_000907.1. DR ProteinModelPortal; P43708; -. DR STRING; 71421.HI1385; -. DR EnsemblBacteria; AAC23032; AAC23032; HI_1385. DR GeneID; 950298; -. DR KEGG; hin:HI1385; -. DR PATRIC; 20191461; VBIHaeInf48452_1441. DR eggNOG; ENOG41090A1; Bacteria. DR eggNOG; COG1528; LUCA. DR KO; K02217; -. DR OMA; NEFNASH; -. DR OrthoDB; EOG6G4W12; -. DR PhylomeDB; P43708; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; PTHR11431; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 165 Probable bacterial non-heme ferritin-like FT protein. FT /FTId=PRO_0000201094. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 17 17 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 50 50 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 50 50 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 53 53 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 94 94 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 127 127 Iron 2. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. SQ SEQUENCE 165 AA; 19021 MW; 47ABB48B11626D2F CRC64; MLSENVVKLL NDQMNLEFYS SNLYLQMSAW CDQQGFEGTA KFLSVHAAEE MQHMRKLFTY LNETGSLAVI SAIEAPAHEY KSLKEVIETT YEHEKLITSK INELVGKTFE EKDYSAFNFL QWYVEEQHEE EKLFSSILDK LNFLGEDGKG LFLIDKDLGN LSTKA // ID G3P_HAEIN Reviewed; 339 AA. AC P44304; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 116. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; DE Short=GAPDH {ECO:0000250|UniProtKB:P0A9B2}; DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P0A9B2}; DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2}; GN Name=gapA; Synonyms=gapDH; OrderedLocusNames=HI_0001; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of CC glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) CC using the cofactor NAD. The first reaction step involves the CC formation of a hemiacetal intermediate between G3P and a cysteine CC residue, and this hemiacetal intermediate is then oxidized to a CC thioester, with concomitant reduction of NAD to NADH. The reduced CC NADH is then exchanged with the second NAD, and the thioester is CC attacked by a nucleophilic inorganic phosphate to produce BPG. CC {ECO:0000250|UniProtKB:P0A9B2}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC {ECO:0000250|UniProtKB:P0A9B2}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9B2}. 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; L42023; AAC21680.1; -; Genomic_DNA. DR PIR; G64041; G64041. DR RefSeq; NP_438174.1; NC_000907.1. DR RefSeq; WP_005646416.1; NC_000907.1. DR ProteinModelPortal; P44304; -. DR SMR; P44304; 3-334. DR STRING; 71421.HI0001; -. DR PRIDE; P44304; -. DR EnsemblBacteria; AAC21680; AAC21680; HI_0001. DR GeneID; 950899; -. DR KEGG; hin:HI0001; -. DR PATRIC; 20188453; VBIHaeInf48452_0001. DR eggNOG; ENOG4105C17; Bacteria. DR eggNOG; COG0057; LUCA. DR KO; K00134; -. DR OMA; KWGEVGA; -. DR OrthoDB; EOG66TG3S; -. DR PhylomeDB; P44304; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10836; PTHR10836; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 339 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145661. FT NP_BIND 12 13 NAD. {ECO:0000250|UniProtKB:P00362}. FT REGION 149 151 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P0A9B2}. FT REGION 209 210 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250|UniProtKB:P0A9B2}. FT ACT_SITE 150 150 Nucleophile. FT {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 34 34 NAD. {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 78 78 NAD; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 120 120 NAD. {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 180 180 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 232 232 Glyceraldehyde 3-phosphate. FT {ECO:0000250|UniProtKB:P0A9B2}. FT BINDING 319 319 NAD. {ECO:0000250|UniProtKB:P0A9B2}. FT SITE 177 177 Activates thiol group during catalysis. FT {ECO:0000250|UniProtKB:P0A9B2}. SQ SEQUENCE 339 AA; 36052 MW; 87119EDEB114EDF0 CRC64; MAIKIGINGF GRIGRIVFRA AQHRDDIEVV GINDLIDVEY MAYMLKYDST HGRFDGTVEV KDGNLVVNGK TIRVTAERDP ANLNWGAIGV DIAVEATGLF LTDETARKHI TAGAKKVVLT GPSKDATPMF VRGVNFNAYA GQDIVSNASC TTNCLAPLAR VVHETFGIKD GLMTTVHATT ATQKTVDGPS AKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ALNGKLTGMA FRVPTPNVSV VDLTVNLEKP ASYDAIKQAI KDAAEGKTFN GELKGVLGYT EDAVVSTDFN GCALTSVFDA DAGIALTDSF VKLVSWYDNE TGYSNKVLDL VAHIYNYKG // ID FNR_HAEIN Reviewed; 257 AA. AC P45199; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Anaerobic regulatory protein; GN Name=fnr; OrderedLocusNames=HI_1425; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: It is involved in the activation of genes necessary for CC anaerobic respiration. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00060}. CC -!- SIMILARITY: Contains 1 HTH crp-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00387}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23062.1; -; Genomic_DNA. DR PIR; E64122; E64122. DR RefSeq; NP_439574.1; NC_000907.1. DR RefSeq; WP_005662331.1; NC_000907.1. DR ProteinModelPortal; P45199; -. DR STRING; 71421.HI1425; -. DR EnsemblBacteria; AAC23062; AAC23062; HI_1425. DR GeneID; 950327; -. DR KEGG; hin:HI1425; -. DR PATRIC; 20191545; VBIHaeInf48452_1482. DR eggNOG; ENOG4105DS0; Bacteria. DR eggNOG; COG0664; LUCA. DR KO; K01420; -. DR OMA; HVHKIMS; -. DR OrthoDB; EOG6RVFWF; -. DR PhylomeDB; P45199; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF13545; HTH_Crp_2; 1. DR PRINTS; PR00034; HTHCRP. DR SMART; SM00100; cNMP; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51206; SSF51206; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS00042; HTH_CRP_1; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Activator; Complete proteome; Cytoplasm; DNA-binding; Iron; KW Iron-sulfur; Metal-binding; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 257 Anaerobic regulatory protein. FT /FTId=PRO_0000100177. FT DOMAIN 167 240 HTH crp-type. {ECO:0000255|PROSITE- FT ProRule:PRU00387}. FT DNA_BIND 200 219 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00387}. FT REGION 23 32 Essential for the oxygen-regulated FT activity. {ECO:0000250}. FT REGION 143 162 Dimerization. {ECO:0000255}. FT METAL 23 23 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 26 26 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 32 32 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 125 125 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 257 AA; 28595 MW; 2D81E3CE180D5137 CRC64; MKNFVAGAQS GRKIQSGGCA IHCQDCSISQ LCIPFTLNEQ ELDQLDNIIE RKKPIQKSQV LFKAGDSLNS IYAIRSGTIK SYTISESGEE QITSFHLPGD LVGFDAITQM QHPSFAQALE TAMVCEIPFD ILDDLAGKMP KLRQQILRLM SSEIKSDQEM ILLLSKMNAE ERLAAFIHNL SKRYSARGFS AREFRLTMTR GDIGNYLGLT VETISRLLGR FQKLGVISVQ GKYITINDLN GLIELTGTNK TKITLVK // ID FRDB_HAEIN Reviewed; 256 AA. AC P44893; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Fumarate reductase iron-sulfur subunit; DE EC=1.3.5.1; GN Name=frdB; OrderedLocusNames=HI_0834; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000250}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; CC -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex CC containing four subunits: a flavoprotein, an iron-sulfur, and two CC hydrophobic anchor proteins. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22492.1; -; Genomic_DNA. DR RefSeq; NP_438994.1; NC_000907.1. DR RefSeq; WP_005639269.1; NC_000907.1. DR ProteinModelPortal; P44893; -. DR SMR; P44893; 7-255. DR STRING; 71421.HI0834; -. DR EnsemblBacteria; AAC22492; AAC22492; HI_0834. DR GeneID; 949848; -. DR KEGG; hin:HI0834; -. DR PATRIC; 20190323; VBIHaeInf48452_0875. DR eggNOG; ENOG4105E33; Bacteria. DR eggNOG; COG0479; LUCA. DR KO; K00245; -. DR OMA; FKNFFGS; -. DR OrthoDB; EOG6CK7MG; -. DR PhylomeDB; P44893; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome; KW Transport; Tricarboxylic acid cycle. FT CHAIN 1 256 Fumarate reductase iron-sulfur subunit. FT /FTId=PRO_0000158702. FT DOMAIN 7 97 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT DOMAIN 151 180 4Fe-4S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 58 58 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 63 63 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 66 66 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 78 78 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 160 160 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 163 163 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 166 166 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 170 170 Iron-sulfur 3 (3Fe-4S). {ECO:0000250}. FT METAL 216 216 Iron-sulfur 3 (3Fe-4S). {ECO:0000250}. FT METAL 222 222 Iron-sulfur 3 (3Fe-4S). {ECO:0000250}. FT METAL 226 226 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 256 AA; 28668 MW; 42E3851D0B6B355E CRC64; MANSPVMNVE VLRYNPEIDQ EPHLSTYQVP YDNQTSLLDA LGYIKDKLEP SLSYRWSCRM AICGSCGMMV NNKPKLACKT FLRDYSGHMR IEPLANFPIE RDLVVDLSHF IESLEAIKPY IIGNEAPALD GKPHPSKELQ VSRTKQTPAQ LEKYRQFSMC INCGLCYAAC PQFGLNPEFL GPAAITMAHR YNLDNRDHGK AKRMSLLNGK NGVWSCTFVG YCSEVCPKHV DPASAINQGK VESAKDYVIS MLKPKG // ID FTSE_HAEIN Reviewed; 218 AA. AC P44871; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Cell division ATP-binding protein FtsE; GN Name=ftsE; OrderedLocusNames=HI_0769; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular CC division. Important for assembly or stability of the septal ring. CC {ECO:0000250|UniProtKB:P0A9R7}. CC -!- SUBUNIT: Homodimer. Forms a membrane-associated complex with FtsX. CC {ECO:0000250|UniProtKB:P0A9R7}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0A9R7}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P0A9R7}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P0A9R7}. Note=Associated with the membrane CC through an interaction with FtsX. {ECO:0000250|UniProtKB:P0A9R7}. 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; L42023; AAC22427.1; -; Genomic_DNA. DR PIR; H64091; H64091. DR RefSeq; NP_438928.1; NC_000907.1. DR RefSeq; WP_005632750.1; NC_000907.1. DR ProteinModelPortal; P44871; -. DR STRING; 71421.HI0769; -. DR EnsemblBacteria; AAC22427; AAC22427; HI_0769. DR GeneID; 950167; -. DR KEGG; hin:HI0769; -. DR PATRIC; 20190189; VBIHaeInf48452_0808. DR eggNOG; ENOG4105CAK; Bacteria. DR eggNOG; COG2884; LUCA. DR KO; K09812; -. DR OMA; MLMERAS; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P44871; -. DR Proteomes; UP000000579; 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; 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; IPR005286; Cell_div_FtsE_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02673; FtsE; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; KW Cell membrane; Complete proteome; Membrane; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 218 Cell division ATP-binding protein FtsE. FT /FTId=PRO_0000092331. FT DOMAIN 2 218 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 218 AA; 24349 MW; 6E3DFE39C03F33EB CRC64; MIKFSNVSKA YHGATQPALQ GLNFHLPVGS MTYLVGHSGA GKSTLLKLIM GMEKANAGQI WFNGHDITRL SKYEIPFLRR QIGMVHQDYR LLTDRTVVEN VALPLIIAGM HPKDANTRAM ASLDRVGLRN KAHYLPPQIS GGEQQRVDIA RAIVHKPQLL LADEPTGNLD DELSLGIFNL FEEFNRLGMT VLIATHDINL IQQKPKPCLV LEQGYLRY // ID FTSL_HAEIN Reviewed; 107 AA. AC P45058; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Cell division protein FtsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN Name=ftsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN OrderedLocusNames=HI_1131; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. {ECO:0000255|HAMAP-Rule:MF_00910}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00910}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00910}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00910}. Note=Localizes to the division CC septum where it forms a ring structure. {ECO:0000255|HAMAP- CC Rule:MF_00910}. CC -!- SIMILARITY: Belongs to the FtsL family. {ECO:0000255|HAMAP- CC Rule:MF_00910}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22786.1; -; Genomic_DNA. DR PIR; F64184; F64184. DR RefSeq; NP_439289.1; NC_000907.1. DR RefSeq; WP_005647600.1; NC_000907.1. DR STRING; 71421.HI1131; -. DR DNASU; 950098; -. DR EnsemblBacteria; AAC22786; AAC22786; HI_1131. DR GeneID; 950098; -. DR KEGG; hin:HI1131; -. DR PATRIC; 20190937; VBIHaeInf48452_1181. DR eggNOG; COG3116; LUCA. DR KO; K03586; -. DR OMA; FICIIVT; -. DR OrthoDB; EOG6F81SK; -. DR PhylomeDB; P45058; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00910; FtsL; 1. DR InterPro; IPR011922; Cell_div_FtsL. DR Pfam; PF04999; FtsL; 1. DR TIGRFAMs; TIGR02209; ftsL_broad; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 107 Cell division protein FtsL. FT /FTId=PRO_0000087375. FT TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TRANSMEM 25 45 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TOPO_DOM 46 107 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. SQ SEQUENCE 107 AA; 12199 MW; 62DBCB30DAFB7367 CRC64; MSENNKPRYP LQQILVEDLF SSNKLVVLLL IGILVSAMGT IWITHKTRQL ISENGMLILQ RQALENEYRN LQVQEATEGD STRVESIAIS TLKMKVVSSE QEVEIRE // ID FTSZ_HAEIN Reviewed; 421 AA. AC P45069; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 106. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=HI_1143; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22798.1; -; Genomic_DNA. DR PIR; I64185; I64185. DR RefSeq; NP_439301.1; NC_000907.1. DR RefSeq; WP_005693457.1; NC_000907.1. DR ProteinModelPortal; P45069; -. DR SMR; P45069; 17-344. DR STRING; 71421.HI1143; -. DR EnsemblBacteria; AAC22798; AAC22798; HI_1143. DR GeneID; 950290; -. DR KEGG; hin:HI1143; -. DR PATRIC; 20190961; VBIHaeInf48452_1193. DR eggNOG; ENOG4105CDK; Bacteria. DR eggNOG; COG0206; LUCA. DR KO; K03531; -. DR OMA; IWGTSVD; -. DR OrthoDB; EOG6S7XZG; -. DR PhylomeDB; P45069; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 421 Cell division protein FtsZ. FT /FTId=PRO_0000114355. FT NP_BIND 26 30 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 132 134 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 163 163 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 167 167 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 211 211 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. SQ SEQUENCE 421 AA; 45022 MW; AA6579FE1BCCDE52 CRC64; MLYPEYPEYD NFNESGALIK VVGVGGGGGN AVNHMVMNMV KQEMGGTFVG ESSLTSEEHG RIVFYAVNTD AQALRKSQVQ QTVQIGGETT KGLGAGANPN IGRKAAEDDQ DEIRKMLEGA DMVFIAAGMG GGTGTGAAPV VAKIAKELGI LTVAVVTKPF TFEGKKRMQF AELGIKDLSQ YVDSMIIIPN QQIQKVLPKN AKLIDAFAAA NDVLRNSVMG ISDMITSPGL INVDFADVRT VMSVQGQAMI GFGSAVGEPG AGRAEEAARL AVRNDLLEKI DLSNAQGILV NITAGMDLVF EEFNIIGETI GSFASEEATV VVGTSLVPEM SDEIRVTIVA TGLGEIAGNE PIQVVRQGLS TQNIEGEGRV NIVPELHRRE SVEVSRTASE EYQRPLDKPI TDRLEAFKKN NFFNPAQREE N // ID FTSP_HAEIN Reviewed; 311 AA. AC P44847; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative cell division protein FtsP; DE Flags: Precursor; GN Name=ftsP; Synonyms=sufI; OrderedLocusNames=HI_0733; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell division protein that is required for growth during CC stress conditions. May be involved in protecting or stabilizing CC the divisomal assembly under conditions of stress (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Localizes to CC the division septum. {ECO:0000250}. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Belongs to the FtsP family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 plastocyanin-like domain. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. The C-terminus is CC much shorter than in related proteins. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22390.1; -; Genomic_DNA. DR PIR; H64157; H64157. DR ProteinModelPortal; P44847; -. DR STRING; 71421.HI0733; -. DR EnsemblBacteria; AAC22390; AAC22390; HI_0733. DR PATRIC; 20190103; VBIHaeInf48452_0767. DR eggNOG; ENOG4107QQV; Bacteria. DR eggNOG; COG2132; LUCA. DR OMA; GERYELI; -. DR OrthoDB; EOG6HB9PM; -. DR PhylomeDB; P44847; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.420; -; 2. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR SUPFAM; SSF49503; SSF49503; 2. DR PROSITE; PS51318; TAT; 1. PE 5: Uncertain; KW Cell cycle; Cell division; Complete proteome; Periplasm; KW Reference proteome; Signal. FT SIGNAL 1 29 Tat-type signal. {ECO:0000255|PROSITE- FT ProRule:PRU00648}. FT CHAIN 30 311 Putative cell division protein FtsP. FT /FTId=PRO_0000002994. FT DOMAIN 228 297 Plastocyanin-like. SQ SEQUENCE 311 AA; 34496 MW; 436173F59F1E1772 CRC64; MPRLSRRQLL KTAAISTALS TVPAPLLAAS REKLVVPPLI EVRRGRPIVL TMQETNYPLD GSHNVTVWGF NGNYLGPTIK IKSGSFAKLN YHNNLPQSVA LSIQGLQASG ELFGGAARVL KKGESWAPIV PIEQPAASCW YRSATLANSA YQTYRGLAGM WLIEDEQSLK ANLPNKYGVD DIPLILQDME FNNDGLQLFK QNQPHFVGNR LLVNGIEAPY LDVARGWIRL RLLNASLARA YDLRLDNDQE MLLIAQDLGF LPKAKSVKSL VLSPGERAEI LVNMMKLTTY LSLAEVNVAC TKNKKYVVLR R // ID FUCK_HAEIN Reviewed; 470 AA. AC P44399; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=L-fuculokinase {ECO:0000255|HAMAP-Rule:MF_00986}; DE EC=2.7.1.51 {ECO:0000255|HAMAP-Rule:MF_00986}; DE AltName: Full=L-fuculose kinase {ECO:0000255|HAMAP-Rule:MF_00986}; GN Name=fucK {ECO:0000255|HAMAP-Rule:MF_00986}; GN OrderedLocusNames=HI_0613; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of L-fuculose. CC {ECO:0000255|HAMAP-Rule:MF_00986}. CC -!- CATALYTIC ACTIVITY: ATP + L-fuculose = ADP + L-fuculose 1- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00986}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00986}; CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L- CC lactaldehyde and glycerone phosphate from L-fucose: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00986}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00986}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22272.1; -; Genomic_DNA. DR PIR; E64081; E64081. DR RefSeq; NP_438771.1; NC_000907.1. DR RefSeq; WP_005694547.1; NC_000907.1. DR ProteinModelPortal; P44399; -. DR STRING; 71421.HI0613; -. DR EnsemblBacteria; AAC22272; AAC22272; HI_0613. DR GeneID; 950556; -. DR KEGG; hin:HI0613; -. DR PATRIC; 20189809; VBIHaeInf48452_0637. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00879; -. DR OMA; ATNVRAM; -. DR OrthoDB; EOG6X9MHN; -. DR PhylomeDB; P44399; -. DR UniPathway; UPA00563; UER00625. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008737; F:L-fuculokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR HAMAP; MF_00986; Fuculokinase; 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; IPR013450; Fuculokinase. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR02628; fuculo_kin_coli; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; KW Fucose metabolism; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 470 L-fuculokinase. FT /FTId=PRO_0000059425. SQ SEQUENCE 470 AA; 51949 MW; 9FAEE26213E9AB7A CRC64; MAIALIFDCG ATNLRTIAIN EKGQILASHH LANNTKQGIE SSDYHIWDIE EIWQKLTSCA TQTLNQLMQQ GIDLKDIVGI SVTTFGVDGA PFDENDQQLY PIISWKCPRT IPVMENLSNQ LDIKSLYQRN GIGQYSFNTL FKLHWLKTHK PDVFQKMAKF VFISSMLTQR LTGQFTTDHT MAGTSMMTNL TSGNWDPSIL ASLGLSNNHF PPMRYAGEKV GKLRTPLAQK WGLNPVPVIS CGHDTQFAVF GSGAGLNQPV LSSGTWEILM ARTQHAEPRF EFVSQGLTTE FDAQSNCFNP AVQWVGSGVI EWLGKLLFSD VYGSDHYYTT MIKEGEKAFN AGKRAVNFEG IFSQLGQGNI SGLSMFATRG EIYVSALQHM ANKLKNGLSV LHQVSQFQAK SLICVGGGSK NVLWNQIRAN TLNLPIDVVD ISESTVLGAA MFTFAGVGIY ENVNAAQQAM QPTRKRIYPN // ID FUMC_HAEIN Reviewed; 464 AA. AC P71384; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743}; DE Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743}; DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743}; GN Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743}; GN OrderedLocusNames=HI_1398; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible addition of water to fumarate CC to give L-malate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00743}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)- CC malate from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743}. CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic CC A site, and the non-catalytic B site that may play a role in the CC transfer of substrate or product between the active site and the CC solvent. Alternatively, the B site may bind allosteric effectors CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Fumarase subfamily. {ECO:0000255|HAMAP-Rule:MF_00743}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23045.1; -; Genomic_DNA. DR RefSeq; NP_439551.1; NC_000907.1. DR RefSeq; WP_010869204.1; NC_000907.1. DR ProteinModelPortal; P71384; -. DR STRING; 71421.HI1398; -. DR PRIDE; P71384; -. DR EnsemblBacteria; AAC23045; AAC23045; HI_1398. DR GeneID; 950314; -. DR KEGG; hin:HI1398; -. DR PATRIC; 20191495; VBIHaeInf48452_1458. DR eggNOG; ENOG4105C9Q; Bacteria. DR eggNOG; COG0114; LUCA. DR KO; K01679; -. DR OMA; FELNVYN; -. DR OrthoDB; EOG6V1M4M; -. DR PhylomeDB; P71384; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IBA:GO_Central. DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR HAMAP; MF_00743; FumaraseC; 1. DR InterPro; IPR005677; Fum_hydII. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00979; fumC_II; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Cytoplasm; Lyase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 464 Fumarate hydratase class II. FT /FTId=PRO_0000161279. FT REGION 98 100 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT REGION 129 132 B site. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT REGION 139 141 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT REGION 187 188 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT REGION 324 326 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT ACT_SITE 188 188 Proton donor/acceptor. {ECO:0000250}. FT ACT_SITE 318 318 {ECO:0000250}. FT BINDING 319 319 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00743}. FT SITE 331 331 Important for catalytic activity. FT {ECO:0000250}. SQ SEQUENCE 464 AA; 50482 MW; AC836336DA7457CE CRC64; MAFRIEKDTM GEVQVLADKY WAAQTERSRN NFKIGPAASM PHEIIEAFGY LKKAAAFANH DLGVLPLEKR DLIALACDEI LANKLDDQFP LVIWQTGSGT QSNMNVNEVV ANRAHVLNGG KLGEKSIIHP NDDVNKSQSS NDTFPTAMHI AAYKKVVEHT IPCVERLQKT FAAKSEAFKN VVKIGRTHLM DATPLTLGQE FSAYAAQLDF GLKALKNTLP HLSQLALGGT AVGTGLNTPK GYDLKVVDYI AKFTALPFVT ADNKFEALAA HDAIVETHGA LRQLAMSLFK IANDIRLLAS GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EXMTMVCAQV FGNDTTIAFV GSQGHFQLNV FNPVMIANFL QSAQLLGDAC VSFDEHCAVG IEPNYPRIKQ QLENSLMLVT ALNTHIGYEN AAKIAKTAHK NGTTLREEAI NLGLVSAEDF DKWVRPEDMV GSLK // ID G6PD_HAEIN Reviewed; 494 AA. AC P44311; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 113. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=HI_0558; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- CC glucono-1,5-lactone + NADPH. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00966}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22213.1; -; Genomic_DNA. DR PIR; E64077; E64077. DR RefSeq; NP_438715.1; NC_000907.1. DR RefSeq; WP_005694154.1; NC_000907.1. DR ProteinModelPortal; P44311; -. DR STRING; 71421.HI0558; -. DR EnsemblBacteria; AAC22213; AAC22213; HI_0558. DR GeneID; 949608; -. DR KEGG; hin:HI0558; -. DR PATRIC; 20189671; VBIHaeInf48452_0578. DR eggNOG; ENOG4105D8W; Bacteria. DR eggNOG; COG0364; LUCA. DR KO; K00036; -. DR OMA; TIFEPIW; -. DR OrthoDB; EOG61308Z; -. DR PhylomeDB; P44311; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR23429; PTHR23429; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 494 Glucose-6-phosphate 1-dehydrogenase. FT /FTId=PRO_0000068122. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 46 46 NADP. {ECO:0000255|HAMAP-Rule:MF_00966}. FT BINDING 150 150 NADP. {ECO:0000255|HAMAP-Rule:MF_00966}. FT BINDING 180 180 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 184 184 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 218 218 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 237 237 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. FT BINDING 342 342 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00966}. SQ SEQUENCE 494 AA; 56189 MW; 142F81FFB87FBADF CRC64; MQTDNNCIVI FGASGDLTHR KLIPALYNLY KIGRLSENFS VLGVARSDLN DETFREKMRE ALIHNEETTP ETLDAFCSHL YYQAVNTSDA QDYGKLVPRL DDLHDKYQTC GNTFYYMSTP PSLYGVIPEC LAAHGLNTEE YGWKRIIVEK PFGYDEKTAQ TLDVQIHRFF EEHQIYRIDH YLGKETVQNL LVLRFSNGWF EPLWNRNFID YVEITGAESI GVEERGGYYD GSGAMRDMFQ NHLLQVLAMV AMEPPAIINA NSMRDEVAKV MHSLRPLTSE DMENNLVLGQ YTAAEINGKM EKGYLEEKGV PANSRTETYI ALRCEIENWR WAGVPFYVRT GKRLPARVTE IVIHFKTTPH PVFSQNAPEN KLIIRIQPDE AISMRFGLKK PGAGFEAKEV SMDFRYADLA GAQVLTAYER LLLDAMKGDA TLFARTDAVH AAWKFVQPIL DYKANGGRIH EYEAGTWGPV AADKLIAKQG KVWRKPSGLM KKKV // ID GALE_HAEIN Reviewed; 338 AA. AC P24325; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 09-DEC-2015, entry version 120. 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=HI_0351; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1956282; DOI=10.1111/j.1365-2958.1991.tb01874.x; RA Maskell D.J., Szabo M.J., Butler P.D., Williams A.E., Moxon E.R.; RT "Molecular analysis of a complex locus from Haemophilus influenzae RT involved in phase-variable lipopolysaccharide biosynthesis."; RL Mol. Microbiol. 5:1013-1022(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 controlling the internal galactose concentration, it may be linked CC to the biosynthesis of lipopolysaccharide surface molecules, which CC are important for the pathogenesis of H.influenzae. CC {ECO:0000269|PubMed:1956282}. 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; X57315; CAA40568.1; -; Genomic_DNA. DR EMBL; L42023; AAC22012.1; -; Genomic_DNA. DR PIR; A64063; A64063. DR RefSeq; NP_438515.1; NC_000907.1. DR RefSeq; WP_005694325.1; NC_000907.1. DR ProteinModelPortal; P24325; -. DR SMR; P24325; 2-337. DR STRING; 71421.HI0351; -. DR EnsemblBacteria; AAC22012; AAC22012; HI_0351. DR GeneID; 949642; -. DR KEGG; hin:HI0351; -. DR PATRIC; 20189249; VBIHaeInf48452_0370. DR eggNOG; ENOG4105CMR; Bacteria. DR eggNOG; COG1087; LUCA. DR KO; K01784; -. DR OMA; DTMIKHN; -. DR OrthoDB; EOG6WHNS9; -. DR PhylomeDB; P24325; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 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 1 338 UDP-glucose 4-epimerase. FT /FTId=PRO_0000183205. FT NP_BIND 11 12 NAD. {ECO:0000250}. FT NP_BIND 31 36 NAD. {ECO:0000250}. FT NP_BIND 58 59 NAD. {ECO:0000250}. FT NP_BIND 80 84 NAD. {ECO:0000250}. FT REGION 199 200 Substrate binding. {ECO:0000250}. FT REGION 216 218 Substrate binding. {ECO:0000250}. FT REGION 292 295 Substrate binding. {ECO:0000250}. FT ACT_SITE 149 149 Proton acceptor. {ECO:0000250}. FT BINDING 99 99 NAD. {ECO:0000250}. FT BINDING 124 124 NAD. {ECO:0000250}. FT BINDING 124 124 Substrate. {ECO:0000250}. FT BINDING 149 149 NAD. {ECO:0000250}. FT BINDING 149 149 Substrate. {ECO:0000250}. FT BINDING 153 153 NAD. {ECO:0000250}. FT BINDING 178 178 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 179 179 Substrate. {ECO:0000250}. FT BINDING 231 231 Substrate. {ECO:0000250}. FT VARIANT 285 285 A -> P (in strain: RM 7004). FT VARIANT 333 333 P -> S (in strain: RM 7004). SQ SEQUENCE 338 AA; 37165 MW; 449934B0E21C8A56 CRC64; MAILVTGGAG YIGSHTVVEL LNVGKEVVVL DNLCNSSPKS LERVKQITGK EAKFYEGDIL DRALLQKIFA ENEINSVIHF AGLKAVGESV QKPTEYYMNN VAGTLVLIQE MKKAGVWNFV FSSSATVYGD PKIIPITEDC EVGGTTNPYG TSKYMVEQIL RDTAKAEPKF SMTILRYFNP VGAHESGLIG EDPNGIPNNL LPYISQVAIG KLAQLSVFGS DYDTHDGTGV RDYIHVVDLA VGHLKALQRH ENDAGLHIYN LGTGHGYSVL DMVKAFEKAN NITIAYKLVE RRSGDIATCY SDPSLAAKEL GWVAERGLEK MMQDTWNWQK NNPKGYRD // ID FRDA_HAEIN Reviewed; 599 AA. AC P44894; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=Fumarate reductase flavoprotein subunit; DE EC=1.3.5.4; GN Name=frdA; OrderedLocusNames=HI_0835; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD covalently per subunit. {ECO:0000250}; CC -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex CC containing four subunits: a flavoprotein, an iron-sulfur, and two CC hydrophobic anchor proteins. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH 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; L42023; AAC22493.1; -; Genomic_DNA. DR PIR; H64097; H64097. DR RefSeq; NP_438995.1; NC_000907.1. DR RefSeq; WP_010869064.1; NC_000907.1. DR ProteinModelPortal; P44894; -. DR SMR; P44894; 1-571. DR STRING; 71421.HI0835; -. DR PRIDE; P44894; -. DR EnsemblBacteria; AAC22493; AAC22493; HI_0835. DR GeneID; 949849; -. DR KEGG; hin:HI0835; -. DR PATRIC; 20190325; VBIHaeInf48452_0876. DR eggNOG; ENOG4105C00; Bacteria. DR eggNOG; COG1053; LUCA. DR KO; K00244; -. DR OMA; AAPSIIH; -. DR OrthoDB; EOG6M3PC4; -. DR PhylomeDB; P44894; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR GO; GO:0009061; P:anaerobic respiration; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:InterPro. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR005884; Fum_red_fp. DR InterPro; IPR030664; SdhA/FrdA/AprA. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF56425; SSF56425; 1. DR TIGRFAMs; TIGR01176; fum_red_Fp; 1. DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; FAD; Flavoprotein; KW Oxidoreductase; Reference proteome; Transport. FT CHAIN 1 599 Fumarate reductase flavoprotein subunit. FT /FTId=PRO_0000158661. FT NP_BIND 9 23 FAD. {ECO:0000255}. FT ACT_SITE 233 233 {ECO:0000250}. FT ACT_SITE 249 249 {ECO:0000250}. FT MOD_RES 45 45 Tele-8alpha-FAD histidine. {ECO:0000250}. SQ SEQUENCE 599 AA; 65933 MW; 30D4D3B10059236F CRC64; MQTVNVDIAI VGAGGGGLRA AIAAAEANPN LKIALVSKVY PMRTHTVAAE GGAAAVIKEE DSYDKHFQDT VAGGDWLCEQ DVVEYFVQHS PVEMTQLERW GCPWSRKADG DVNVRRFGGM KIERTWFAAD KTGFHLLHTL FQTSIQYPQI QRFDEHFVLD ILVDDGHARG MVAMNMMEGS LVQINANAVV IATGGGCRAF KFNTNGGIVT GDGLSMAYRH GVPLRDMEFV QYHPTGLPNT GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPIGKPQN KYMELGPRDK VSQAFWQEWK KGNTLKTAKG VDVVHLDLRH LGEKYLHERL PFICELASAY EGVNPVNEPI PVRPVVHYTM GGIEVDFNSE TRIKGLFAVG ECASSGLHGA NRLGSNSLAE LVVLGRVAGE YAAQRAVEAQ SVNQSAVDAQ AKDVVARLEA LHKQEGNESW SEIRDEMGTV MEEGCGIYRD QASMQKAVDK IAELKERYKR IRVSDNSSVF NTDVLYTVEL GYILDVAQSI ANSAIERKES RGAHQRLDYT ERDDVNYLKH TLAFYNENGA PRIEYSPVKI TKSQPAKRVY GAEAEAQEAA AKAKEQANG // ID FRMA_HAEIN Reviewed; 378 AA. AC P44557; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase; DE EC=1.1.1.284; DE AltName: Full=Alcohol dehydrogenase class-3; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase class-III; DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase; DE Short=FALDH; DE Short=FDH; DE Short=GSH-FDH; DE EC=1.1.1.-; GN Name=frmA; Synonyms=adhC; OrderedLocusNames=HI_0185; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S- CC formylglutathione + NAD(P)H. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III 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; L42023; AAC21854.1; -; Genomic_DNA. DR PIR; H64052; H64052. DR RefSeq; NP_438353.1; NC_000907.1. DR RefSeq; WP_005694101.1; NC_000907.1. DR ProteinModelPortal; P44557; -. DR SMR; P44557; 7-377. DR STRING; 71421.HI0185; -. DR EnsemblBacteria; AAC21854; AAC21854; HI_0185. DR GeneID; 951091; -. DR KEGG; hin:HI0185; -. DR PATRIC; 20188865; VBIHaeInf48452_0189. DR eggNOG; ENOG4107QPD; Bacteria. DR eggNOG; COG1062; LUCA. DR KO; K00121; -. DR OMA; MITHVLK; -. DR OrthoDB; EOG6K9QDH; -. DR PhylomeDB; P44557; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 2. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; SSF50129; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; KW Reference proteome; Zinc. FT CHAIN 1 378 S-(hydroxymethyl)glutathione FT dehydrogenase. FT /FTId=PRO_0000160776. FT METAL 49 49 Zinc 1; catalytic. {ECO:0000250}. FT METAL 71 71 Zinc 1; catalytic. {ECO:0000250}. FT METAL 101 101 Zinc 2. {ECO:0000250}. FT METAL 104 104 Zinc 2. {ECO:0000250}. FT METAL 107 107 Zinc 2. {ECO:0000250}. FT METAL 115 115 Zinc 2. {ECO:0000250}. FT METAL 178 178 Zinc 1; catalytic. {ECO:0000250}. SQ SEQUENCE 378 AA; 40651 MW; A68677243681165E CRC64; MEIKQINSTI KSRAAVAFAP NQPLQIVEID VEMPRKGEVL IRNTHTGVCH TDAFTLSGSD PEGVFPVVLG HEGAGVVVAV GEGVLSVKPG DHVIPLYTAE CGECEFCRSG KTNLCVSVRD TQGKGLMPDC TTRFSYQGQP IYHYMGCSTF SEYSVVAEVS LAKINPEANH EQVCLLGCGV TTGIGAVHNT AKVQEGDSVA VFGLGAIGLA VVQGARQAKA GRIIAIDTNP AKFELAKQFG ATDCLNPNDY DKPIKDVLLD INKWGIDHTF ECIGNVNVMR QALESAHRGW GQSIIIGVAG AGQEISTRPF QLVTGRVWKG SAFGGVKGRS ELPQMVEDSM KGDIQLEPFV THTMPLDKIN EAFELMHEGK SIRTVIHY // ID FTSHL_HAEIN Reviewed; 381 AA. AC P45219; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH homolog; GN OrderedLocusNames=HI_1465; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000305}. CC -!- CAUTION: Missing the N-terminal trans-membrane domains found in CC paralogs. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23112.1; -; Genomic_DNA. DR PIR; B64125; B64125. DR RefSeq; NP_439616.1; NC_000907.1. DR RefSeq; WP_005694651.1; NC_000907.1. DR ProteinModelPortal; P45219; -. DR SMR; P45219; 1-140. DR STRING; 71421.HI1465; -. DR MEROPS; M41.001; -. DR EnsemblBacteria; AAC23112; AAC23112; HI_1465. DR GeneID; 950570; -. DR KEGG; hin:HI1465; -. DR PATRIC; 20191643; VBIHaeInf48452_1531. DR eggNOG; COG0465; LUCA. DR OMA; MFISEDS; -. DR OrthoDB; EOG6PKFBJ; -. DR PhylomeDB; P45219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. 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 SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1 381 ATP-dependent zinc metalloprotease FtsH FT homolog. FT /FTId=PRO_0000084634. FT METAL 159 159 Zinc. {ECO:0000255}. FT METAL 163 163 Zinc. {ECO:0000255}. FT METAL 237 237 Zinc. {ECO:0000255}. SQ SEQUENCE 381 AA; 42106 MW; CF689D40B15F7EE0 CRC64; MGRQRGAGLG GGHDEREQTL NQMLVEMDGF SGNDGVIVIA ATNRPDVLDP ALTRPGRFDR QVVVGLPDVK GREQILKVHM RKVSVAQDVD AMTLARGTPG YSGADLANLV NEAALFAARV NKRTVTMLEF EKAKDKINMG PERRTMIMTD KQKESTAYHE AGHAIVGYLV PEHDPVHKVT IIPRGRALGV TFFLPEGDQI SISQKQLESK LSTLYAGRLA EDLIYGEENI STGASNDIKV ATNIARNMVT QWGFSEKLGP ILYTEDEGEV FLGRSMAKAK HMSDETAHSI DEEVRAIVNR NYARAREILI DNMDILHAMK DALVKYETIE EEQIKQLMNR EPVTPPSGWG EPKTQQAAYA NSTTNDTKPE SAVENTDDFN V // ID FUCA_HAEIN Reviewed; 216 AA. AC P44777; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=L-fuculose phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987}; DE EC=4.1.2.17 {ECO:0000255|HAMAP-Rule:MF_00987}; DE AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987}; GN Name=fucA {ECO:0000255|HAMAP-Rule:MF_00987}; GN OrderedLocusNames=HI_0611; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the cleavage of L-fuculose 1-phosphate to CC glycerone phosphate and L-lactaldehyde. {ECO:0000255|HAMAP- CC Rule:MF_00987}. CC -!- CATALYTIC ACTIVITY: L-fuculose 1-phosphate = glycerone phosphate + CC (S)-lactaldehyde. {ECO:0000255|HAMAP-Rule:MF_00987}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00987}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00987}; CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L- CC lactaldehyde and glycerone phosphate from L-fucose: step 3/3. CC {ECO:0000255|HAMAP-Rule:MF_00987}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00987}. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00987}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22270.1; -; Genomic_DNA. DR PIR; C64081; C64081. DR RefSeq; NP_438769.1; NC_000907.1. DR RefSeq; WP_005694545.1; NC_000907.1. DR ProteinModelPortal; P44777; -. DR SMR; P44777; 1-210. DR STRING; 71421.HI0611; -. DR EnsemblBacteria; AAC22270; AAC22270; HI_0611. DR GeneID; 950000; -. DR KEGG; hin:HI0611; -. DR PATRIC; 20189805; VBIHaeInf48452_0635. DR eggNOG; ENOG4107W7X; Bacteria. DR eggNOG; COG0235; LUCA. DR KO; K01628; -. DR OMA; YATFGTH; -. DR OrthoDB; EOG6HQSSQ; -. DR PhylomeDB; P44777; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR HAMAP; MF_00987; FucA; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR004782; FucA. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. DR TIGRFAMs; TIGR01086; fucA; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Fucose metabolism; Lyase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 216 L-fuculose phosphate aldolase. FT /FTId=PRO_0000162928. FT ACT_SITE 73 73 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00987}. FT ACT_SITE 113 113 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00987}. FT METAL 73 73 Zinc. {ECO:0000255|HAMAP-Rule:MF_00987}. FT METAL 92 92 Zinc. {ECO:0000255|HAMAP-Rule:MF_00987}. FT METAL 94 94 Zinc. {ECO:0000255|HAMAP-Rule:MF_00987}. FT METAL 155 155 Zinc. {ECO:0000255|HAMAP-Rule:MF_00987}. SQ SEQUENCE 216 AA; 23944 MW; 4DBEEE21ED8EA6C6 CRC64; MNRAELSQKI IDTCLEMTKL GLNQGTAGNV SVRYKDGMLI TPTGMPYHLM KTENIVYVDG NGKHEENKLP SSEWQFHLSV YHTRPEANAV VHNHSIHCAG LSILEKPIPA IHYMVAVSGT DHIPCVPYAT FGSHKLASYV ATGIKESKAI LLAHHGLITC GENLDKALWL AQEVEVLASW YLKLLSTGLE IPLLSKEQMQ VVLGKFHTYG LRIEES // ID FUCI_HAEIN Reviewed; 589 AA. AC P44779; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=L-fucose isomerase {ECO:0000255|HAMAP-Rule:MF_01254}; DE EC=5.3.1.25 {ECO:0000255|HAMAP-Rule:MF_01254}; DE AltName: Full=6-deoxy-L-galactose isomerase {ECO:0000255|HAMAP-Rule:MF_01254}; DE AltName: Full=FucIase; GN Name=fucI {ECO:0000255|HAMAP-Rule:MF_01254}; GN OrderedLocusNames=HI_0614; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts the aldose L-fucose into the corresponding CC ketose L-fuculose. {ECO:0000255|HAMAP-Rule:MF_01254}. CC -!- CATALYTIC ACTIVITY: L-fucopyranose = L-fuculose. CC {ECO:0000255|HAMAP-Rule:MF_01254}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01254}; CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L- CC lactaldehyde and glycerone phosphate from L-fucose: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01254}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01254}. CC -!- SIMILARITY: Belongs to the L-fucose isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_01254}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22273.1; 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; L42023; AAC22273.1; ALT_INIT; Genomic_DNA. DR PIR; F64081; F64081. DR RefSeq; NP_438772.2; NC_000907.1. DR RefSeq; WP_010869020.1; NC_000907.1. DR ProteinModelPortal; P44779; -. DR STRING; 71421.HI0614; -. DR EnsemblBacteria; AAC22273; AAC22273; HI_0614. DR GeneID; 950887; -. DR KEGG; hin:HI0614; -. DR PATRIC; 20189811; VBIHaeInf48452_0638. DR eggNOG; ENOG4105EHF; Bacteria. DR eggNOG; COG2407; LUCA. DR KO; K01818; -. DR OMA; GAISYGH; -. DR OrthoDB; EOG6FJNCF; -. DR PhylomeDB; P44779; -. DR UniPathway; UPA00563; UER00624. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008736; F:L-fucose isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.14.10; -; 1. DR Gene3D; 3.40.275.10; -; 1. DR Gene3D; 3.40.50.1070; -; 1. DR HAMAP; MF_01254; Fucose_iso; 1. DR InterPro; IPR004216; Fuc/Ara_isomerase_C. DR InterPro; IPR015888; Fuc_isomerase_C. DR InterPro; IPR012888; Fucose_iso_N1. DR InterPro; IPR005763; Fucose_isomerase. DR InterPro; IPR009015; Fucose_isomerase_N/cen. DR InterPro; IPR012889; Fucose_isomerase_N2. DR Pfam; PF02952; Fucose_iso_C; 1. DR Pfam; PF07881; Fucose_iso_N1; 1. DR Pfam; PF07882; Fucose_iso_N2; 1. DR SUPFAM; SSF50443; SSF50443; 1. DR SUPFAM; SSF53743; SSF53743; 1. DR TIGRFAMs; TIGR01089; fucI; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Fucose metabolism; Isomerase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 589 L-fucose isomerase. FT /FTId=PRO_0000204148. FT ACT_SITE 340 340 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01254}. FT ACT_SITE 364 364 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01254}. FT METAL 340 340 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01254}. FT METAL 364 364 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01254}. FT METAL 527 527 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_01254}. SQ SEQUENCE 589 AA; 65401 MW; F2E8FF1C65FFFC90 CRC64; MALATQSNRI KIGIRPTIDG RRMGVRESLE TQTIRMAQSV AQLLQTHIRH TDGTFVECVV ADSTIGGVAE AAACADKFKR ENVGLTITVT PCWCYGSETI DMDPHMPKAI WGFNGTERPG AVYLAAALAG HSQLGLPAFS IYGTEVQEAD DTNIPEDVKE KLLRFARAGL AVASIRGKSY LSIGSVSMGI AGSIVNQAFF QEYLGMRNEY VDMMEIKRRL DRKIYDQEEV DLALSWVKQY CKEGVDVNSL ENQRNAEERA ELWENVVKMT IITRDLMVGN PKLATLNYAE EALGHNAIAA GFQGQRHWTD HLPNGDFMEA MLNSTYDWNG VRPPYILATE NDSLNAIGML FGHQLTGKAQ IFADVRTYWS QDSVERVTGW RPESGFIHLI NSGSAALDGT GEHQDAQGNP TLKPAWDVTE EEAKRCLENT RWCPAVHEYF RGGGLSSQFL TKGGIPFTIH RINLIKGLGP VLQIAEGWSI DLPQDVHNKL NQRTNETWPT TWFVPRLTGK GAFTDVYSVM ANWGANHCVA THGHVGADLI TLASMLRIPV CMHNVSEKNI FRPSAWNGFG QDKEGQDYRA CQNFGPLYK // ID GAL7_HAEIN Reviewed; 349 AA. AC P31764; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 119. DE RecName: Full=Galactose-1-phosphate uridylyltransferase; DE Short=Gal-1-P uridylyltransferase; DE EC=2.7.7.12; DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase; GN Name=galT; OrderedLocusNames=HI_0820; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x; RA Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.; RT "The gal locus from Haemophilus influenzae: cloning, sequencing and RT the use of gal mutants to study lipopolysaccharide."; RL Mol. Microbiol. 6:3051-3063(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + alpha-D-galactose 1- CC phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SIMILARITY: Belongs to the galactose-1-phosphate CC uridylyltransferase type 1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65934; CAA46730.1; -; Genomic_DNA. DR EMBL; L42023; AAC22479.1; -; Genomic_DNA. DR PIR; E64096; E64096. DR RefSeq; NP_438980.1; NC_000907.1. DR RefSeq; WP_005693184.1; NC_000907.1. DR ProteinModelPortal; P31764; -. DR SMR; P31764; 5-346. DR STRING; 71421.HI0820; -. DR EnsemblBacteria; AAC22479; AAC22479; HI_0820. DR GeneID; 950798; -. DR KEGG; hin:HI0820; -. DR PATRIC; 20190295; VBIHaeInf48452_0861. DR eggNOG; ENOG4105F0Z; Bacteria. DR eggNOG; COG1085; LUCA. DR KO; K00965; -. DR OMA; WHYAPFF; -. DR OrthoDB; EOG6CCH5M; -. DR PhylomeDB; P31764; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.428.10; -; 2. DR InterPro; IPR001937; GalP_UDPtransf1. DR InterPro; IPR019779; GalP_UDPtransf1_His-AS. DR InterPro; IPR005850; GalP_Utransf_C. DR InterPro; IPR005849; GalP_Utransf_N. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR11943; PTHR11943; 1. DR Pfam; PF02744; GalP_UDP_tr_C; 1. DR Pfam; PF01087; GalP_UDP_transf; 1. DR PIRSF; PIRSF000808; GalT; 1. DR SUPFAM; SSF54197; SSF54197; 2. DR TIGRFAMs; TIGR00209; galT_1; 1. DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Iron; Metal-binding; Nucleotidyltransferase; Reference proteome; KW Transferase; Zinc. FT CHAIN 1 349 Galactose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000169895. FT ACT_SITE 167 167 Tele-UMP-histidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU10033}. FT METAL 53 53 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 56 56 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 116 116 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 165 165 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10033}. FT METAL 183 183 Iron. {ECO:0000250}. FT METAL 282 282 Iron. {ECO:0000250}. FT METAL 297 297 Iron. {ECO:0000250}. FT METAL 299 299 Iron. {ECO:0000250}. FT VARIANT 221 221 I -> V (in strain: RM 7004). FT VARIANT 229 229 I -> V (in strain: RM 7004). FT VARIANT 334 334 E -> D (in strain: RM 7004). SQ SEQUENCE 349 AA; 40758 MW; 3BAB24B417E5ECBF CRC64; MTALFEPTEH PHRRYNPLID QWVLVSPHRA KRPWQGQQEK VNEEQKPSYD PTCYLCPSNK RITGELNPDY RKPYVFKNDF SALLEDTPAP EKSSDPLFQS SQARGESRVI CFSPDHSKTL PLLTALEIEE VIKVWQEQLR ELGAKYQWVQ IFENKGAAMG CSNPHPHGQI WANSFLPNEV AREDRTQRDY LLKHGSVMLV DYVKRELALK ERIVVETEHW IALVPYWAIW PFETLLLPKT HVKRLTELSD EQSKDLAVIL KKLTTKYDNL FETSFPYSMG FHAAPFNGED NEHWQLHAHF YPPLLRSATV RKFMVGYEML GENQRDLTAE QAAERLRALS EVHYKERTK // ID GALR_HAEIN Reviewed; 332 AA. AC P31766; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 109. DE RecName: Full=HTH-type transcriptional regulator GalR; DE AltName: Full=Galactose operon repressor; GN Name=galR; Synonyms=galS; OrderedLocusNames=HI_0821; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x; RA Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.; RT "The gal locus from Haemophilus influenzae: cloning, sequencing and RT the use of gal mutants to study lipopolysaccharide."; RL Mol. Microbiol. 6:3051-3063(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Repressor of the galactose operon. Binds galactose as an CC inducer. CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism CC [regulation]. CC -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65934; CAA46729.1; -; Genomic_DNA. DR EMBL; L42023; AAC22480.1; -; Genomic_DNA. DR PIR; F64096; F64096. DR RefSeq; NP_438981.1; NC_000907.1. DR RefSeq; WP_005663077.1; NC_000907.1. DR ProteinModelPortal; P31766; -. DR STRING; 71421.HI0821; -. DR EnsemblBacteria; AAC22480; AAC22480; HI_0821. DR GeneID; 949832; -. DR KEGG; hin:HI0821; -. DR PATRIC; 20190297; VBIHaeInf48452_0862. DR eggNOG; ENOG41060NJ; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; GVMRALH; -. DR OrthoDB; EOG6SJJMM; -. DR PhylomeDB; P31766; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000579; 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:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; DNA-binding; KW Galactose metabolism; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 332 HTH-type transcriptional regulator GalR. FT /FTId=PRO_0000107953. FT DOMAIN 1 56 HTH lacI-type. {ECO:0000255|PROSITE- FT ProRule:PRU00111}. FT DNA_BIND 4 23 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00111}. FT CONFLICT 35 35 V -> A (in Ref. 1; CAA46729). FT {ECO:0000305}. FT CONFLICT 38 38 Q -> R (in Ref. 1; CAA46729). FT {ECO:0000305}. FT CONFLICT 208 208 P -> L (in Ref. 1; CAA46729). FT {ECO:0000305}. SQ SEQUENCE 332 AA; 36708 MW; 0F431000946AF8A5 CRC64; MSTIRDVAKL ANVSVATVSR VLNHSLSVSE NTRLVVEQAI AQLAYQPNAN AQALAVQNTD TIGVVVTDVT DAFFAILVKA VDKVAEAHQK TILIGIGYHH AEKEREAINT LLRKRCSSLV VHSKALSDDE LSHYLNTVQG MVIINRVIKG YEHRCVSLDN QKGTYLATEM LIRYGHQHIA YIGSNHAIFD EVERRNGYLA ALKDHNYPII EQAITLNSPD FEGGEKAMID LLSYNKNLTA VVAYNDSMAA GAISVLNENN ISVPSQFSII GFDDMPIARY LIPKLTTIRY PIDLMATYAA KLALSLTDEK IITPPVVQFN PTLVRRFSVE SR // ID GCH1_HAEIN Reviewed; 218 AA. AC P43866; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=GTP cyclohydrolase 1; DE EC=3.5.4.16; DE AltName: Full=GTP cyclohydrolase I; DE Short=GTP-CH-I; GN Name=folE; OrderedLocusNames=HI_1447; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6- CC (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step CC 1/1. CC -!- SUBUNIT: Toroid-shaped homodecamer, composed of two pentamers of CC five dimers. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I 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; L42023; AAC23097.1; -; Genomic_DNA. DR PIR; A64124; A64124. DR RefSeq; NP_439599.1; NC_000907.1. DR RefSeq; WP_005666869.1; NC_000907.1. DR ProteinModelPortal; P43866; -. DR SMR; P43866; 4-217. DR STRING; 71421.HI1447; -. DR EnsemblBacteria; AAC23097; AAC23097; HI_1447. DR GeneID; 950345; -. DR KEGG; hin:HI1447; -. DR PATRIC; 20191599; VBIHaeInf48452_1509. DR eggNOG; ENOG4105EUJ; Bacteria. DR eggNOG; COG0302; LUCA. DR KO; K01495; -. DR OMA; RATHFCV; -. DR OrthoDB; EOG6XHC8G; -. DR PhylomeDB; P43866; -. DR UniPathway; UPA00848; UER00151. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00223; FolE; 1. DR InterPro; IPR001474; GTP_CycHdrlase_I. DR InterPro; IPR018234; GTP_CycHdrlase_I_CS. DR InterPro; IPR020602; GTP_CycHdrlase_I_dom. DR PANTHER; PTHR11109; PTHR11109; 1. DR Pfam; PF01227; GTP_cyclohydroI; 1. DR TIGRFAMs; TIGR00063; folE; 1. DR PROSITE; PS00859; GTP_CYCLOHYDROL_1_1; 1. DR PROSITE; PS00860; GTP_CYCLOHYDROL_1_2; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; One-carbon metabolism; Reference proteome; Zinc. FT CHAIN 1 218 GTP cyclohydrolase 1. FT /FTId=PRO_0000119411. FT METAL 109 109 Zinc. {ECO:0000250}. FT METAL 112 112 Zinc. {ECO:0000250}. FT METAL 180 180 Zinc. {ECO:0000250}. SQ SEQUENCE 218 AA; 24945 MW; BCC60F0038158D38 CRC64; MSKISLDALN VRNALIEKGI ETPMIDPTQA KNERRESIAK HMHEVMKLIG LDLRDDSLEE TPNRLAKMFI DEIFSGMDYA NFPKMTKIKN QMKVSEMVQV NDITLTSTCE HHFVTIDGKV CVAYYPKDWV IGLSKINRIV SFFAQRPQVQ ERLTEQLLTA FQTILETDDV AVYVKATHFC VKARGIRDTN SYTVTSAYGG VFLEDRDTRK EFLATVQK // ID FTSB_HAEIN Reviewed; 92 AA. AC P44035; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Cell division protein FtsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN Name=ftsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN OrderedLocusNames=HI_0673; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein. May link together the CC upstream cell division proteins, which are predominantly CC cytoplasmic, with the downstream cell division proteins, which are CC predominantly periplasmic. {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. CC {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00599}; Single-pass type II membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00599}. Note=Localizes to the division CC septum. {ECO:0000255|HAMAP-Rule:MF_00599}. CC -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000255|HAMAP- CC Rule:MF_00599}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22333.1; -; Genomic_DNA. DR PIR; H64011; H64011. DR RefSeq; NP_438833.1; NC_000907.1. DR RefSeq; WP_005661211.1; NC_000907.1. DR STRING; 71421.HI0673; -. DR EnsemblBacteria; AAC22333; AAC22333; HI_0673. DR GeneID; 950558; -. DR KEGG; hin:HI0673; -. DR PATRIC; 20189963; VBIHaeInf48452_0703. DR eggNOG; COG2919; LUCA. DR KO; K05589; -. DR OMA; DYVRVKD; -. DR OrthoDB; EOG6P5ZC4; -. DR PhylomeDB; P44035; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00599; FtsB; 1. DR InterPro; IPR023081; Cell_div_FtsB. DR InterPro; IPR007060; FtsL/DivIC. DR Pfam; PF04977; DivIC; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Coiled coil; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 92 Cell division protein FtsB. FT /FTId=PRO_0000214445. FT TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT TRANSMEM 4 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT TOPO_DOM 22 92 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00599}. FT COILED 28 63 {ECO:0000255|HAMAP-Rule:MF_00599}. SQ SEQUENCE 92 AA; 10916 MW; B30D25D34481F42B CRC64; MRLLILILLS VLVLFQYNFW FGSNGFLDYR QNAEKIKENQ AENEKLSQRN QRINAEIQGL TKGFEAIEER ARMQHGLVKE NEVFYHIVKE SK // ID FTSX_HAEIN Reviewed; 310 AA. AC P44872; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Cell division protein FtsX; GN Name=ftsX; OrderedLocusNames=HI_0770; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular CC division. {ECO:0000250}. CC -!- SUBUNIT: Forms a membrane-associated complex with FtsE. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC FtsX 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; L42023; AAC22428.1; -; Genomic_DNA. DR PIR; I64091; I64091. DR RefSeq; NP_438929.1; NC_000907.1. DR RefSeq; WP_005660149.1; NC_000907.1. DR STRING; 71421.HI0770; -. DR EnsemblBacteria; AAC22428; AAC22428; HI_0770. DR GeneID; 949837; -. DR KEGG; hin:HI0770; -. DR PATRIC; 20190191; VBIHaeInf48452_0809. DR eggNOG; ENOG4105CRP; Bacteria. DR eggNOG; COG2177; LUCA. DR KO; K09811; -. DR OMA; ITIFARR; -. DR OrthoDB; EOG60W7WW; -. DR PhylomeDB; P44872; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; ISS:UniProtKB. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR004513; ABC_transpt_FtsX. DR Pfam; PF02687; FtsX; 1. DR PIRSF; PIRSF003097; FtsX; 1. DR TIGRFAMs; TIGR00439; ftsX; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 310 Cell division protein FtsX. FT /FTId=PRO_0000166794. FT TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TOPO_DOM 53 176 Periplasmic. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TOPO_DOM 198 234 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TOPO_DOM 256 279 Periplasmic. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. FT TOPO_DOM 301 310 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 310 AA; 35033 MW; 4F1EB7D259257E38 CRC64; MSRSTDASVF VQTAYTLRAV WADLWQRKFG TLLTILVIAV SLTIPTVSYL MWKNLHLATT QFYPESELTI YLHKNLSEEN ANLVVEKIRQ QKGVESLNYV SRQESLKEFK SWSGFGEELE ILDDNPLPAV VIVKPTSEFN VSEKRDELRT NLNKIKGVQE VRLDNDWMEK LTALSWLIAH VAIFCTVLMT IAVFLVIGNS IRSDVYSSRS SIDVMKLLGA TDQFILRPYL YTGMIYALLG GLVAAIFSSF IISYFTSAVK YVTDIFAVQF SLNGLGVGEF VFLLVCCLIM GYVGAWIAAT RHIAMMERKE // ID FUR_HAEIN Reviewed; 146 AA. AC P44561; O30882; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=Ferric uptake regulation protein; DE Short=Ferric uptake regulator; GN Name=fur; OrderedLocusNames=HI_0190; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Biogroup aegyptius / F3031; RX PubMed=9727086; RA Smoot L.M., Bell E.C., Paz R.L., Corbin K.A., Hall D.D., RA Steenbergen J.N., Harner A.C., Actis L.A.; RT "Molecular and genetic analysis of iron uptake proteins in the RT Brazilian purpuric fever clone of Haemophilus influenzae biogroup RT aegyptius."; RL Front. Biosci. 3:D989-D996(1998). CC -!- FUNCTION: Acts as a global negative controlling element, employing CC Fe(2+) as a cofactor to bind the operator of the repressed genes. CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Fur 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; L42023; AAC21859.1; -; Genomic_DNA. DR EMBL; AF020350; AAB71196.1; -; Genomic_DNA. DR PIR; B64053; B64053. DR RefSeq; NP_438359.1; NC_000907.1. DR RefSeq; WP_010868953.1; NC_000907.1. DR ProteinModelPortal; P44561; -. DR SMR; P44561; 5-83. DR STRING; 71421.HI0190; -. DR EnsemblBacteria; AAC21859; AAC21859; HI_0190. DR GeneID; 951099; -. DR KEGG; hin:HI0190; -. DR PATRIC; 20188877; VBIHaeInf48452_0195. DR eggNOG; ENOG41090R7; Bacteria. DR eggNOG; COG0735; LUCA. DR KO; K03711; -. DR OMA; DERSDIG; -. DR OrthoDB; EOG6J48SS; -. DR PhylomeDB; P44561; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002481; FUR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01475; FUR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Iron; Metal-binding; KW Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc. FT CHAIN 1 146 Ferric uptake regulation protein. FT /FTId=PRO_0000095554. FT REGION 1 85 DNA-binding. {ECO:0000250}. FT REGION 86 146 Dimerization. {ECO:0000250}. FT COMPBIAS 88 91 His-rich. FT METAL 34 34 Zinc. {ECO:0000250}. FT METAL 82 82 Zinc. {ECO:0000250}. FT METAL 88 88 Iron. {ECO:0000250}. FT METAL 90 90 Iron. {ECO:0000250}. FT METAL 91 91 Zinc. {ECO:0000250}. FT METAL 94 94 Zinc. {ECO:0000250}. FT METAL 97 97 Zinc. {ECO:0000250}. FT METAL 102 102 Zinc. {ECO:0000250}. FT METAL 109 109 Iron. {ECO:0000250}. FT METAL 126 126 Iron. {ECO:0000250}. FT VARIANT 4 4 G -> E (in strain: F3031). FT VARIANT 44 44 F -> L (in strain: F3031). FT VARIANT 49 49 C -> S (in strain: F3031). SQ SEQUENCE 146 AA; 16961 MW; 517ED359ABD0173A CRC64; MSEGNIKLLK KVGLKITEPR LTILALMQNH KNEHFSAEDV YKIFLEQGCE IGLATVYRVL NQFDEAHIVI RHNFEGNKSV FELAPTEHHD HIICEDCGKV FEFTDNIIEQ RQREISEKYG IKLKTHNVYL YGKCSDINHC DENNSK // ID FTSH_HAEIN Reviewed; 635 AA. AC P71377; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 119. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; GN OrderedLocusNames=HI_1335; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. 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 inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000255|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000255|HAMAP-Rule:MF_01458}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22979.1; -; Genomic_DNA. DR RefSeq; NP_439486.1; NC_000907.1. DR RefSeq; WP_010869183.1; NC_000907.1. DR ProteinModelPortal; P71377; -. DR SMR; P71377; 140-394. DR STRING; 71421.HI1335; -. DR MEROPS; M41.001; -. DR EnsemblBacteria; AAC22979; AAC22979; HI_1335. DR GeneID; 950795; -. DR KEGG; hin:HI1335; -. DR PATRIC; 20191353; VBIHaeInf48452_1387. DR eggNOG; ENOG4105C3H; Bacteria. DR eggNOG; COG0465; LUCA. DR KO; K03798; -. DR OMA; IHGTFTN; -. DR OrthoDB; EOG6PKFBJ; -. DR PhylomeDB; P71377; -. DR Proteomes; UP000000579; 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; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Metal-binding; Metalloprotease; KW Nucleotide-binding; Protease; Reference proteome; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1 635 ATP-dependent zinc metalloprotease FtsH. FT /FTId=PRO_0000084633. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 26 97 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TRANSMEM 98 118 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT TOPO_DOM 119 635 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT NP_BIND 191 198 ATP. {ECO:0000255|HAMAP-Rule:MF_01458}. FT ACT_SITE 414 414 {ECO:0000255|HAMAP-Rule:MF_01458}. FT METAL 413 413 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 417 417 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. FT METAL 491 491 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01458}. SQ SEQUENCE 635 AA; 70030 MW; 70E6DD1E8293839D CRC64; MVKNLVLWVV VAVIMMTAYQ SFNSSSVENS TDYTTFVYDV SNGQVTAARF DANEITVTKT DGSKYSTVMP PLEDKKLLDD LLSKKVKVEG TPFERRGFLS QILISWFPML FLVGVWVFFM RQMQGGGGKA MSFGKSRAKM LNQDQIKVTF ADVAGCDEAK EEVGEIVDFL RDPNKFQNLG GKIPKGILMV GPPGTGKTLL ARAIAGEAKV PFFTISGSDF VEMFVGVGAS RVRDMFEQAK KNAPCLIFID EIDAVGRQRG AGLGGGHDER EQTLNQMLVE MDGFSGNDGV IVIAATNRPD VLDPALTRPG RFDRQVVVGL PDVKGREQIL KVHMRKVSVA QDVDAMTLAR GTPGYSGADL ANLVNEAALF AARVNKRTVT MLEFEKAKDK INMGPERRTM IMTDKQKEST AYHEAGHAIV GYLVPEHDPV HKVTIIPRGR ALGVTFFLPE GDQISISQKQ LESKLSTLYA GRLAEDLIYG EENISTGASN DIKVATNIAR NMVTQWGFSE KLGPILYTED EGEVFLGRSM AKAKHMSDET AHSIDEEVRA IVNRNYARAR EILIDNMDIL HAMKDALVKY ETIEEEQIKQ LMNREPVTPP SGWGEPKTQQ AAYANSTTND TKPESAVENT DDFNV // ID FUCM_HAEIN Reviewed; 144 AA. AC P44778; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=L-fucose mutarotase {ECO:0000255|HAMAP-Rule:MF_01662}; DE EC=5.1.3.29 {ECO:0000255|HAMAP-Rule:MF_01662}; DE AltName: Full=Fucose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01662}; DE AltName: Full=Type-2 mutarotase {ECO:0000255|HAMAP-Rule:MF_01662}; GN Name=fucU {ECO:0000255|HAMAP-Rule:MF_01662}; GN OrderedLocusNames=HI_0612; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the anomeric conversion of L-fucose. CC {ECO:0000255|HAMAP-Rule:MF_01662}. CC -!- CATALYTIC ACTIVITY: Alpha-L-fucose = beta-L-fucose. CC {ECO:0000255|HAMAP-Rule:MF_01662}. CC -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01662}. CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01662}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01662}. CC -!- SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01662}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22271.1; -; Genomic_DNA. DR PIR; D64081; D64081. DR RefSeq; NP_438770.1; NC_000907.1. DR RefSeq; WP_005648572.1; NC_000907.1. DR ProteinModelPortal; P44778; -. DR STRING; 71421.HI0612; -. DR EnsemblBacteria; AAC22271; AAC22271; HI_0612. DR GeneID; 949663; -. DR KEGG; hin:HI0612; -. DR PATRIC; 20189807; VBIHaeInf48452_0636. DR eggNOG; ENOG4105NWF; Bacteria. DR eggNOG; COG4154; LUCA. DR KO; K02431; -. DR OMA; ASSICAC; -. DR OrthoDB; EOG6D5G31; -. DR PhylomeDB; P44778; -. DR UniPathway; UPA00956; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042806; F:fucose binding; IEA:InterPro. DR GO; GO:0016854; F:racemase and epimerase activity; IEA:InterPro. DR GO; GO:0042354; P:L-fucose metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1650.10; -; 1. DR HAMAP; MF_01662; L_fucose_rotase; 1. DR InterPro; IPR023751; L-fucose_mutarotase. DR InterPro; IPR023750; RbsD-like. DR InterPro; IPR007721; RbsD_FucU. DR Pfam; PF05025; RbsD_FucU; 1. DR SUPFAM; SSF102546; SSF102546; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Fucose metabolism; Isomerase; Reference proteome. FT CHAIN 1 144 L-fucose mutarotase. FT /FTId=PRO_0000087383. FT REGION 131 133 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01662}. FT ACT_SITE 22 22 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01662}. FT BINDING 30 30 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01662}. FT BINDING 109 109 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01662}. SQ SEQUENCE 144 AA; 15750 MW; 3665520CDB7935B2 CRC64; MLKGIHPALS PELLKTLAEM GHGDEIVLAD AHFPAHSLHK NVIRADGISI DILLEAITPL FEFDAYVDAP LLMMKAVEGD SLDPNVETRY LNAIESAVGF TPNLTCLERF DFYTRAKQAY AVVVSGEIAK YGNIIIKKGV TPIL // ID FUCR_HAEIN Reviewed; 249 AA. AC P44780; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=L-fucose operon activator; GN Name=fucR; OrderedLocusNames=HI_0615; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transcriptional activator of the fuc operon. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH deoR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00349}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22274.1; -; Genomic_DNA. DR PIR; G64081; G64081. DR RefSeq; NP_438773.1; NC_000907.1. DR RefSeq; WP_005661551.1; NC_000907.1. DR ProteinModelPortal; P44780; -. DR STRING; 71421.HI0615; -. DR DNASU; 949664; -. DR EnsemblBacteria; AAC22274; AAC22274; HI_0615. DR GeneID; 949664; -. DR KEGG; hin:HI0615; -. DR PATRIC; 20189813; VBIHaeInf48452_0639. DR eggNOG; ENOG4107EDW; Bacteria. DR eggNOG; COG1349; LUCA. DR KO; K02430; -. DR OMA; VNIFSIE; -. DR OrthoDB; EOG6XSZXW; -. DR PhylomeDB; P44780; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014036; DeoR_C. DR InterPro; IPR001034; DeoR_HTH. DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00455; DeoRC; 1. DR Pfam; PF08220; HTH_DeoR; 1. DR PRINTS; PR00037; HTHLACR. DR SMART; SM00420; HTH_DEOR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00894; HTH_DEOR_1; 1. DR PROSITE; PS51000; HTH_DEOR_2; 1. PE 3: Inferred from homology; KW Activator; Carbohydrate metabolism; Complete proteome; DNA-binding; KW Fucose metabolism; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 249 L-fucose operon activator. FT /FTId=PRO_0000050249. FT DOMAIN 1 56 HTH deoR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. FT DNA_BIND 18 37 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. SQ SEQUENCE 249 AA; 28163 MW; AAA07C53B1965714 CRC64; MNYRDELILQ WVNQQGKASV IELAQHCDIS VETIRRDLNK LANKGLLHRT HGGAVSNKTK DLGSFFQTRK HINATAKRHI AQKALDLLYE NAVIGLDASS TSWYFAYLMP DIPCTVVTNS MFNINALVNK SNVKTIVTGG VYSAKYEAFY GPLSEYLLQR LHINFSVFSC SGIDKNGNIW ESNELNASLK RKMMEASERA YLLIDSSKFE KTSLIQLADL SKINTIFSDR SLPDNLQKYC EQHDIMTVL // ID G6PI_HAEIN Reviewed; 549 AA. AC P44312; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 11-NOV-2015, entry version 100. 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=HI_1576; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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=AAC23219.1; 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; L42023; AAC23219.1; ALT_INIT; Genomic_DNA. DR PIR; F64130; F64130. DR RefSeq; NP_439722.2; NC_000907.1. DR RefSeq; WP_010869249.1; NC_000907.1. DR ProteinModelPortal; P44312; -. DR SMR; P44312; 23-549. DR STRING; 71421.HI1576; -. DR EnsemblBacteria; AAC23219; AAC23219; HI_1576. DR GeneID; 950436; -. DR KEGG; hin:HI1576; -. DR PATRIC; 20191883; VBIHaeInf48452_1649. DR eggNOG; ENOG4107QP8; Bacteria. DR eggNOG; COG0166; LUCA. DR KO; K01810; -. DR OMA; SHLIAPY; -. DR OrthoDB; EOG64R61J; -. DR PhylomeDB; P44312; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1390.10; -; 1. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR023096; G6P_Isomerase_C. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; 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 1 549 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000180650. FT ACT_SITE 355 355 Proton donor. {ECO:0000250}. FT ACT_SITE 387 387 {ECO:0000250}. FT ACT_SITE 515 515 {ECO:0000250}. SQ SEQUENCE 549 AA; 61622 MW; F65348C667068F16 CRC64; MKNINPTHTH AWKSLEAHKA ELSNITIQDL FKQEKNRFDD YSLTFNNQIL IDFSKNNINQ TTLSHLRQLA QECALDSAKE AMFTGEKINR TENRAVLHTA LRNRTNTPVL VDGKDVMPEV NAVLAKMKDF CQRIISGEWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF VSNVDGTHIA ETLKKVNPET TLFLVASKTF TTQETMTNAQ SARDWLLKAA KDESAVAKHF AALSTNAKDV EKFGIDTNNM FEFWDWVGGR YSLWSAIGLS IALSIGFENF EALLNGAHEM DKHFLSTPIE QNIPTTLALV GLWNTNFLGA QTEAILPYDQ YLHRFAAYFQ QGNMESNGKY VDRDGNVIKN YQTGPIIWGE PGTNGQHAFY QLIHQGTTLI PCDFIAPAQR HNPLADHHNK LLSNFFAQTE ALAFGKTKEE VEAEFVKAGK SLDDVKNIVP FKVFTGNKPT NSILVQKITP FTLGALIAMY EHKIFVQGVI FNIFSFDQWG VELGKQLANR ILPELTDSEK VASHDSSTNG LINQFKAWR // ID GAL1_HAEIN Reviewed; 384 AA. AC P31767; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 114. DE RecName: Full=Galactokinase {ECO:0000255|HAMAP-Rule:MF_00246}; DE EC=2.7.1.6 {ECO:0000255|HAMAP-Rule:MF_00246}; DE AltName: Full=Galactose kinase {ECO:0000255|HAMAP-Rule:MF_00246}; GN Name=galK {ECO:0000255|HAMAP-Rule:MF_00246}; GN OrderedLocusNames=HI_0819; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x; RA Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.; RT "The gal locus from Haemophilus influenzae: cloning, sequencing and RT the use of gal mutants to study lipopolysaccharide."; RL Mol. Microbiol. 6:3051-3063(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to CC D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-galactose = ADP + alpha-D- CC galactose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00246}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22478.1; 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; X65934; CAA46731.1; -; Genomic_DNA. DR EMBL; L42023; AAC22478.1; ALT_INIT; Genomic_DNA. DR PIR; D64096; D64096. DR RefSeq; NP_438979.2; NC_000907.1. DR RefSeq; WP_010869061.1; NC_000907.1. DR ProteinModelPortal; P31767; -. DR STRING; 71421.HI0819; -. DR EnsemblBacteria; AAC22478; AAC22478; HI_0819. DR GeneID; 950587; -. DR KEGG; hin:HI0819; -. DR PATRIC; 20190293; VBIHaeInf48452_0860. DR eggNOG; ENOG4105CRD; Bacteria. DR eggNOG; COG0153; LUCA. DR KO; K00849; -. DR OMA; VMPCAIN; -. DR OrthoDB; EOG6DG2SH; -. DR PhylomeDB; P31767; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00246; Galactokinase; 1. DR InterPro; IPR000705; Galactokinase. DR InterPro; IPR022963; Galactokinase_bac. DR InterPro; IPR019741; Galactokinase_CS. DR InterPro; IPR019539; GalKase_gal-bd. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR006206; Mevalonate/galactokinase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10457; PTHR10457; 1. DR PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1. DR Pfam; PF10509; GalKase_gal_bdg; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF000530; Galactokinase; 1. DR PRINTS; PR00473; GALCTOKINASE. DR PRINTS; PR00959; MEVGALKINASE. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00131; gal_kin; 1. DR PROSITE; PS00106; GALACTOKINASE; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Galactose metabolism; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 384 Galactokinase. FT /FTId=PRO_0000184612. FT NP_BIND 123 129 ATP. {ECO:0000255|HAMAP-Rule:MF_00246}. FT REGION 34 37 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT ACT_SITE 173 173 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT METAL 129 129 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT METAL 161 161 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT BINDING 222 222 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00246}. FT SITE 28 28 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00246}. FT VARIANT 107 107 D -> H (in strain: RM 7004). FT VARIANT 145 145 D -> N (in strain: RM 7004). FT VARIANT 321 321 A -> V (in strain: RM 7004). FT VARIANT 331 331 A -> T (in strain: RM 7004). FT VARIANT 353 353 S -> A (in strain: RM 7004). SQ SEQUENCE 384 AA; 42132 MW; B28D552832858D34 CRC64; MTPIQNAQQI FNRQHKNLPE ITVYAPGRVN IIGEHTDYND GFVMPCAINF GTAVSGTKRD DHIWNVYAAD LDETDEFSLN VEIPKSEHKW ANYVRGVVKF IQERYPDFQQ GANLVISGNV PLSSGLSSSA ALEVAVGKFC QQLGDLPLSH TDIALNGQKA ENQFVGANCG NMDQLISALG QENHLLMIDC RSLETTPTPV PQDVAVIIVN SNVPHDLVTG EYNTRRQQCE EAAKFFGVKA LRDVSVEQFQ KREAELTALS PLAAKRARHV VTENQRVLDA VEALKNNDLT CLGKLMEASH DSMRDDFEIT VPQIDYLVEL AQLVIGKSGG ARMTGGGFGG CIVALAPHDK VDSVRKIIAD NYEKTTGLKE TFYVCTASQG VRVI // ID GALU_HAEIN Reviewed; 295 AA. AC P44878; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. 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; OrderedLocusNames=HI_0812; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22471.1; -; Genomic_DNA. DR PIR; G64095; G64095. DR RefSeq; NP_438972.1; NC_000907.1. DR RefSeq; WP_005693178.1; NC_000907.1. DR ProteinModelPortal; P44878; -. DR SMR; P44878; 2-289. DR STRING; 71421.HI0812; -. DR EnsemblBacteria; AAC22471; AAC22471; HI_0812. DR GeneID; 949826; -. DR KEGG; hin:HI0812; -. DR PATRIC; 20190279; VBIHaeInf48452_0853. DR eggNOG; ENOG4105C3Y; Bacteria. DR eggNOG; COG1210; LUCA. DR KO; K00963; -. DR OMA; VALMEVE; -. DR OrthoDB; EOG6Z9B3V; -. DR PhylomeDB; P44878; -. DR Proteomes; UP000000579; 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 1 295 UTP--glucose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000201358. SQ SEQUENCE 295 AA; 32279 MW; FED84173957E571B CRC64; MKAVIPVAGL GTRMLPATKA IPKEMLTLVD KPLIQYVVNE CVAAGIKEIV LVTHSSKNAI ENHFDTSFEL ETMLEKRVKR QLLEEVRSIC PKNVTIMHVR QGNAKGLGHA VLCGRPLVGN ESFAVMLPDV LLAEFSADQK KENLAAMIQR FNETGASQIM VTPVPQENVS SYGVADCGGI ELNGGESAKI NSIVEKPSIE DAPSNLAVVG RYVFSAAIWD LLEKTPIGVG DEIQLTDAID MLIEKETVEA FHMTGETFDC GDKIGYMEAF VEYGIRHEKL GKEFKSFIKN LAKTL // ID FUCP_HAEIN Reviewed; 428 AA. AC P44776; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=L-fucose permease; GN Name=fucP; OrderedLocusNames=HI_0610; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transport of L-fucose into the cell. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. FHS CC transporter (TC 2.A.1.7) 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; L42023; AAC22269.1; -; Genomic_DNA. DR PIR; B64081; B64081. DR RefSeq; NP_438768.1; NC_000907.1. DR RefSeq; WP_005694544.1; NC_000907.1. DR ProteinModelPortal; P44776; -. DR STRING; 71421.HI0610; -. DR EnsemblBacteria; AAC22269; AAC22269; HI_0610. DR GeneID; 950599; -. DR KEGG; hin:HI0610; -. DR PATRIC; 20189803; VBIHaeInf48452_0634. DR eggNOG; ENOG4105EDR; Bacteria. DR eggNOG; COG0738; LUCA. DR KO; K02429; -. DR OMA; VIAQVFY; -. DR OrthoDB; EOG6MSS4Q; -. DR PhylomeDB; P44776; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015150; F:fucose transmembrane transporter activity; IEA:InterPro. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR005275; Lfuc_permease_FucP. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR TIGRFAMs; TIGR00885; fucP; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cell inner membrane; Cell membrane; KW Complete proteome; Fucose metabolism; Membrane; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 428 L-fucose permease. FT /FTId=PRO_0000094502. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 204 224 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 339 359 Helical. {ECO:0000255}. FT TRANSMEM 371 391 Helical. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. SQ SEQUENCE 428 AA; 46988 MW; 93893FD9DC4EFB2F CRC64; MNAKVLEKKF IVPFVLITSL FALWGFANDI TNPMVAVFQT VMEIPASEAA LVQLAFYGGY GTMAIPAALF ASRYSYKAGI LLGLALYAIG AFLFWPAAQY EIFNFFLVSL YILTFGLAFL ETTANPYILA MGDPQTATRR LNFAQSFNPL GSITGMFVAS QLVLTNLESD KRDAAGNLIF HTLSEAEKMS IRTHDLAEIR DPYIALGFVV VAVFIIIGLK KMPAVKIEEA GQISFKTAVS RLAQKAKYRE GVIAQAFYVG VQIMCWTFIV QYAERLGFTK AEGQNFNIIA MAIFISSRFI STALMKYLKA EFMLMLFAIG GFLSILGVIF IDGVWGLYCL ILTSGFMPLM FPTIYGIALY GLKEESTLGA AGLVMAIVGG ALMPPLQGMI IDQGEVMGLP AVNFSFILPL ICFVVIAIYG FRAWKILK // ID GLMM_HAEIN Reviewed; 445 AA. AC P45164; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554}; DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554}; GN Name=glmM1 {ECO:0000255|HAMAP-Rule:MF_01554}; Synonyms=glmM-A, mrsA-A; GN OrderedLocusNames=HI_1337; GN and GN Name=glmM2 {ECO:0000255|HAMAP-Rule:MF_01554}; Synonyms=glmM-B, mrsA-B; GN OrderedLocusNames=HI_1463; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP- CC Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000255|HAMAP-Rule:MF_01554}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22984.1; -; Genomic_DNA. DR EMBL; L42023; AAC23110.1; -; Genomic_DNA. DR PIR; C64172; C64172. DR RefSeq; NP_439488.1; NC_000907.1. DR RefSeq; NP_439614.1; NC_000907.1. DR RefSeq; WP_005694655.1; NC_000907.1. DR ProteinModelPortal; P45164; -. DR STRING; 71421.HI1463; -. DR DNASU; 950893; -. DR EnsemblBacteria; AAC22984; AAC22984; HI_1337. DR EnsemblBacteria; AAC23110; AAC23110; HI_1463. DR GeneID; 950567; -. DR GeneID; 950893; -. DR KEGG; hin:HI1337; -. DR KEGG; hin:HI1463; -. DR PATRIC; 20191357; VBIHaeInf48452_1389. DR eggNOG; ENOG4107QJF; Bacteria. DR eggNOG; COG1109; LUCA. DR KO; K03431; -. DR OMA; NSHCDGR; -. DR OrthoDB; EOG6TN467; -. DR PhylomeDB; P45164; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR HAMAP; MF_01554_B; GlmM_B; 1. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR006352; GlmM_bact. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR TIGRFAMs; TIGR01455; glmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 445 Phosphoglucosamine mutase. FT /FTId=PRO_0000147896. FT ACT_SITE 102 102 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 102 102 Magnesium; via phosphate group. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 241 241 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 243 243 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 245 245 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT MOD_RES 102 102 Phosphoserine. {ECO:0000255|HAMAP- FT Rule:MF_01554}. SQ SEQUENCE 445 AA; 47372 MW; 0335916382F7DBF1 CRC64; MANRKYFGTD GVRGKVGAYP ITPDFALKLG WAAGKVLASQ GSKMVLIGKD TRISGYMLES ALEAGLAAAG LSAAFTGPMP TPAIAYLTRT FRAEAGIVIS ASHNPYYDNG IKFFSAKGTK LPDEIEEAIE AMLEQPMDCV ESAELGKASR INDAAGRYIE FCKGTFPAHL GLEGYKIVVD CANGATYHIA PNVLRELGAE VIEIGTDPNG LNINEKCGAT DVTALQAKVV ETKADVGLAY DGDGDRIMMV DHLGNKVDGD QILFIIAREA LRSGQLKGGV VGTLMSNMSL EIALKMLGVP FLRANVGDRY VLEKMVENDW TLGGENSGHI IIADKNTTGD GIVASLAVLA AMAQHKLSLN ELASAVKLFP QVLINVRFAG GENPLESDAV KSVAAEVEKR LEGKGRILLR KSGTEPLIRV MVECQDAELA QQCAEEIAEA VKKIN // ID GALM_HAEIN Reviewed; 340 AA. AC P31765; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 109. DE RecName: Full=Aldose 1-epimerase; DE EC=5.1.3.3; DE AltName: Full=Galactose mutarotase; DE AltName: Full=Type-1 mutarotase; GN Name=galM; Synonyms=mro; OrderedLocusNames=HI_0818; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x; RA Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.; RT "The gal locus from Haemophilus influenzae: cloning, sequencing and RT the use of gal mutants to study lipopolysaccharide."; RL Mol. Microbiol. 6:3051-3063(1992). CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It CC is active on D-glucose, L-arabinose, D-xylose, D-galactose, CC maltose and lactose (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose = beta-D-glucose. CC {ECO:0000255|PROSITE-ProRule:PRU10126}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the aldose epimerase 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; L42023; AAC22477.1; -; Genomic_DNA. DR EMBL; X65934; CAA46732.1; -; Genomic_DNA. DR PIR; C64096; C64096. DR RefSeq; NP_438978.1; NC_000907.1. DR RefSeq; WP_005693182.1; NC_000907.1. DR ProteinModelPortal; P31765; -. DR STRING; 71421.HI0818; -. DR EnsemblBacteria; AAC22477; AAC22477; HI_0818. DR GeneID; 949661; -. DR KEGG; hin:HI0818; -. DR PATRIC; 20190291; VBIHaeInf48452_0859. DR eggNOG; ENOG4105ENN; Bacteria. DR eggNOG; COG2017; LUCA. DR KO; K01785; -. DR OMA; SPNHPDW; -. DR OrthoDB; EOG69WFM5; -. DR PhylomeDB; P31765; -. DR UniPathway; UPA00242; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR018052; Ald1_epimerase_CS. DR InterPro; IPR013458; Ald_epimerase_bac. DR InterPro; IPR015443; Aldose_1-epimerase. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. DR Pfam; PF01263; Aldose_epim; 1. DR PIRSF; PIRSF005096; GALM; 1. DR SUPFAM; SSF74650; SSF74650; 1. DR TIGRFAMs; TIGR02636; galM_Leloir; 1. DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Reference proteome. FT CHAIN 1 340 Aldose 1-epimerase. FT /FTId=PRO_0000197445. FT ACT_SITE 172 172 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU10126}. FT ACT_SITE 305 305 Proton acceptor. {ECO:0000250}. FT BINDING 77 77 Substrate. {ECO:0000250}. FT BINDING 243 243 Substrate. {ECO:0000250}. FT VARIANT 42 42 V -> I (in strain: RM 7004). FT VARIANT 46 46 D -> G (in strain: RM 7004). FT VARIANT 58 58 D -> E (in strain: RM 7004). FT VARIANT 113 113 N -> K (in strain: RM 7004). SQ SEQUENCE 340 AA; 38102 MW; 4ECAE4FB8C498C7A CRC64; MLEQTTFNAP DGAPYQLITL QNENGMRVQF MDWGATWLSC KVPVNDTLRE VLLGCKVDNY PTHQSYLGAS VGRYANRIAN AQFELNGELI KLSSNQGKHQ LHGGEGFDKR RWNIQECGEN FVCFSLHSVD GDQGFPGNVD VSVTYTLTGD NSVKIEYAGM CDKDTALNLT NHTYFNLENA EQGSDVREHT LRLNADFYLP VDNEGIPNSP LKHVVNTSFD FRIAKPIKQD FLQGDQQATK GYDHSFIVNK AWQKPCVLLT SPTGDLSLEV RTSQAALQVY TGNYLAGTPT RNGELYADFS GIALETQCLP DTPNHPEWQN YGGIQKAGGR YYQWTEFKFK // ID GLGX_HAEIN Reviewed; 659 AA. AC P45178; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Glycogen operon protein GlgX homolog; DE EC=3.2.1.-; GN Name=glgX; OrderedLocusNames=HI_1358; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23005.1; -; Genomic_DNA. DR PIR; A64119; A64119. DR RefSeq; NP_439509.1; NC_000907.1. DR RefSeq; WP_005694002.1; NC_000907.1. DR ProteinModelPortal; P45178; -. DR STRING; 71421.HI1358; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR DNASU; 949470; -. DR EnsemblBacteria; AAC23005; AAC23005; HI_1358. DR GeneID; 949470; -. DR KEGG; hin:HI1358; -. DR PATRIC; 20191401; VBIHaeInf48452_1411. DR eggNOG; ENOG4108ESZ; Bacteria. DR eggNOG; COG1523; LUCA. DR KO; K02438; -. DR OMA; YSYNHGV; -. DR OrthoDB; EOG64BQ3X; -. DR PhylomeDB; P45178; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR011837; Glycogen_debranch_GlgX. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR10357; PTHR10357; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02922; CBM_48; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 2. DR SUPFAM; SSF81296; SSF81296; 1. DR TIGRFAMs; TIGR02100; glgX_debranch; 1. PE 3: Inferred from homology; KW Complete proteome; Glycogen biosynthesis; Glycosidase; Hydrolase; KW Reference proteome. FT CHAIN 1 659 Glycogen operon protein GlgX homolog. FT /FTId=PRO_0000054305. FT ACT_SITE 333 333 Nucleophile. {ECO:0000250}. FT ACT_SITE 369 369 Proton donor. {ECO:0000250}. FT SITE 441 441 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 659 AA; 75290 MW; E2B71F610E8B1CAC CRC64; MFKIYNNGNP IPMGYSQAVE NNVQITNFAL FSAAAIGVEL CLFDEQNQET RLPMVRTENV WHLAVTGVKT GTEYAFRIHG EFANPQKLIL DPYAKAVNGK PDLSSEESRS WFLLSDNRDN AHLAPRAVVI SEEFDWENDT SPNTPWAETI VYELHVKGFS QLNEKIPAAL RGTYTGLAHP VNLAYLKELG VTAVELLPVN FHINEPHLQA RGLQNYWGYN PLAMFAVEPK YAATNNPLAE FKTMVKAFHK AGIEVILDVV FNHSAESEQT YPTFSQRGID DQTYYWRNDQ GRYINWTGCG NMLNLSSDVG RKWVVDCLRY WVEQCHIDGF RFDLATVLGR DTPDFNSSAQ LFTDIKNEPS LQNIKLIAEP WDIGHYGYQV GNFPSYFAEW NDRFRDDLCR FWLWKSGEIG AFAERFAGSS DLFKKNDRLP HTTLNFITAH DGFTLKDLVS YNQKHNETNG EENRDGRNEN YSYNHGVEGS TESLSEPQKS AVENNRTFAQ SGLLMSLLLA NGTPMLLAGD EFGNTQYGNN NAYCQDNEIT WLKWANFNEE LFELTKQTIA LRKQIGSLNK DQWWSDENVQ WLNIVGEPMT VEDWQNQQTK ALQVVLDNRW LLLINAKAEG QMFHLPNRKW KPQIGTHNVT LEAQQAELSS MGFCMLNDE // ID GLNE_HAEIN Reviewed; 981 AA. AC P44419; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802}; DE EC=2.7.7.42 {ECO:0000255|HAMAP-Rule:MF_00802}; DE AltName: Full=Glutamine-synthetase adenylyltransferase; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_00802}; DE AltName: Full=[Glutamate--ammonia-ligase] adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00802}; GN Name=glnE {ECO:0000255|HAMAP-Rule:MF_00802}; GN OrderedLocusNames=HI_0069; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Adenylation and deadenylation of glutamate--ammonia CC ligase. {ECO:0000255|HAMAP-Rule:MF_00802}. CC -!- CATALYTIC ACTIVITY: ATP + [L-glutamate:ammonia ligase (ADP- CC forming)]-L-tyrosine = diphosphate + [L-glutamate:ammonia ligase CC (ADP-forming)]-O(4)-(5'-adenylyl)-L-tyrosine. {ECO:0000255|HAMAP- CC Rule:MF_00802}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00802}; CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000255|HAMAP- CC Rule:MF_00802}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21747.1; -; Genomic_DNA. DR PIR; G64046; G64046. DR RefSeq; NP_438242.1; NC_000907.1. DR RefSeq; WP_005693853.1; NC_000907.1. DR ProteinModelPortal; P44419; -. DR SMR; P44419; 49-476. DR STRING; 71421.HI0069; -. DR EnsemblBacteria; AAC21747; AAC21747; HI_0069. DR GeneID; 950967; -. DR KEGG; hin:HI0069; -. DR PATRIC; 20188593; VBIHaeInf48452_0070. DR eggNOG; ENOG4105CE6; Bacteria. DR eggNOG; COG1391; LUCA. DR KO; K00982; -. DR OMA; EFMVQYA; -. DR OrthoDB; EOG651SRZ; -. DR PhylomeDB; P44419; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase 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 HAMAP; MF_00802; GlnE; 1. DR InterPro; IPR023057; GlnE. DR InterPro; IPR005190; GlnE_rpt_dom. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR Pfam; PF08335; GlnD_UR_UTase; 2. DR Pfam; PF03710; GlnE; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1 981 Glutamate-ammonia-ligase FT adenylyltransferase. FT /FTId=PRO_0000209249. FT REGION 108 324 GlnE 1. FT REGION 646 866 GlnE 2. SQ SEQUENCE 981 AA; 112759 MW; 8B2B82376B814883 CRC64; MTALSALIEQ KLQSLGTILC QSFPELSPEK IHEAIQQNSN HPELPVYQLG YAIAMSDFVE KVLQKYPHLV KQWWEKSPCF ADCTAYIERL NKELANVHDE TALYQTLRQF RNIEMAKLSF CQSLNLATVE EIFVQLSQLA ESLIIAARDW LYHQACAEIG TPMDEQGNPQ QLYILGMGKL GGFELNFSSD IDLIFTYPSQ GETSVENTNA RRSVDNGKFF TRLGQRLISA LDEFTSDGFV YRTDMRLRPF GDSGVLVLSF SAMEQYYQDQ GRDWERYAMI KGRVLGAQTK DPNVSKLKKM LRPFVYRRYI DFSVIQSLRE MKGKIEREVR RRGLKDNIKL GAGGIREVEF IVQVFQLIRG GREINLQQHS LLKILPEITK LRLITEQQFH DLRESYIFLR RVENILQAIN DQQTQTLPTD EIDQIRLVEA CKTFTCLNEN NQTIEKHYPI ENWDDFYRTL QQKQEKVRAV FTQLIGDEQD ESSQTDSQWQ DFLEADFEDI EQTLLESSVS ENNIDEVLEK LAQFKDGLNH RVIGSRGRDV LSHLMPTVLA LIFEQENYRT LLPRILNIIE KISSRTTYLE LLLENPRALQ QVIELCAQSQ LISEQLAHYP ILLDELLNTE ALRHPLPFTQ YPAELHQYLL RLPPDDEEQL IDALRQFKQA TLLKVAAADI LGALPVMKVS DHLTYLAEAI IEVVVNLAWK QVSSRFGVPE HLQNNEKGFL VIGYGKLGGI ELGYKSDLDL VFLYDAVESQ TTGGKKVIDS NQFYLRLAQK IVSIFSINTS AGVLYEADMR LRPSGDAGLI GCSLSAFSHY QLNDAWTWEK QALVRARPVF GESSLKAKFE HIRQQVLSAS RDIEQLKQDV VEMRKKMFAH LSHSKHSEFN LKTDRGGITD IEFIAQYLML ANAPKKPQLT KWSDNVRIFD DMAEAKIISQ TDCDTLKQCY VDLRNTIHHL NLLGKSSVVE DSEFVKERSF IQAFWDRLFV S // ID GCH1L_HAEIN Reviewed; 251 AA. AC Q57354; O05008; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 17-FEB-2016, entry version 86. DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog; GN OrderedLocusNames=HI_0105; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBUNIT: Toroid-shaped homohexamer. In the hexamer, 3 dimers CC assemble to form a ring-like structure surrounding a central hole. CC {ECO:0000250|UniProtKB:P0AFP6}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21783.1; 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; L42023; AAC21783.1; ALT_INIT; Genomic_DNA. DR PIR; G64142; G64142. DR RefSeq; NP_438279.2; NC_000907.1. DR RefSeq; WP_005649665.1; NC_000907.1. DR ProteinModelPortal; Q57354; -. DR SMR; Q57354; 1-251. DR STRING; 71421.HI0105; -. DR EnsemblBacteria; AAC21783; AAC21783; HI_0105. DR GeneID; 951007; -. DR KEGG; hin:HI0105; -. DR PATRIC; 20188677; VBIHaeInf48452_0108. DR eggNOG; ENOG4107QNR; Bacteria. DR eggNOG; COG0327; LUCA. DR OMA; RVGWCTG; -. DR OrthoDB; EOG6N3CRB; -. DR PhylomeDB; Q57354; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002678; GTP_cyclohydrolase_I/Nif3. DR PANTHER; PTHR13799; PTHR13799; 1. DR Pfam; PF01784; NIF3; 1. DR SUPFAM; SSF102705; SSF102705; 1. DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 251 GTP cyclohydrolase 1 type 2 homolog. FT /FTId=PRO_0000147310. FT METAL 63 63 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 64 64 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 101 101 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 219 219 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 223 223 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 223 223 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. SQ SEQUENCE 251 AA; 27814 MW; 9DAC1A6AE9BE6636 CRC64; MNNLELEQLI NQKLSSDKIN DYAPNGLQVE GKTEIKKIIT GVTASQALIN YAISQNADAI LVHHGYFWKS ETPCIRGMKG KRIKALLVND INLYGYHLPL DVHPELGNNA QLAKLLDIEN LQPLEKGSVS IPVWGELKEP MTGKDFAEKI EKVLNRKPLI CIENGPHLIR KIGICTGGGQ GYIDLAAEQG CDAFITGEVS EQTIHSAREQ GLYFFSAGHH ATERYGIKAL GEWLAKEYGF DVEFKDIDNP A // ID GCVA_HAEIN Reviewed; 301 AA. AC P45099; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=Glycine cleavage system transcriptional activator homolog; GN Name=gcvA; OrderedLocusNames=HI_1194; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Not known, the gcv operon regulated by the E.coli CC homolog does not exist in H.influenzae, so it probably acts as a CC transcriptional regulator on some other operon. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22848.1; -; Genomic_DNA. DR PIR; B64189; B64189. DR RefSeq; NP_439350.1; NC_000907.1. DR ProteinModelPortal; P45099; -. DR STRING; 71421.HI1194m; -. DR EnsemblBacteria; AAC22848; AAC22848; HI_1194. DR GeneID; 950145; -. DR KEGG; hin:HI1194m; -. DR PATRIC; 20191067; VBIHaeInf48452_1246. DR eggNOG; ENOG4105ETT; Bacteria. DR eggNOG; ENOG410XS6G; LUCA. DR KO; K03566; -. DR OMA; TNALTDF; -. DR OrthoDB; EOG6G4VSC; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 301 Glycine cleavage system transcriptional FT activator homolog. FT /FTId=PRO_0000105628. FT DOMAIN 10 67 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 27 46 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 301 AA; 34528 MW; 9FA449EA8DB396C8 CRC64; MEILMYKRLP PLNSLKSFES AARYLSFTKA ADELCVTQAA VSHQIKLLEX FLGIDLFKRK NRSLELTELG KAYFVDINKI LRRLNEATER LLTLKTDPHL NISVPQTFGI QWLVPHLSEF NQLYPQIEVR LTGVDQDEGL LNKEIDLAIY YGLGNWQNLQ VDRLCEENLL ILASPELLAE NPIIQPEDLK KHTLIHIHTC DNWQAMANHL QLDDLNIQQG PLFSHTFMAL QAAIHGQGIV LANRLLALQE IENGSLQAVL PTNLPDPKSF YVVNHLDRLD DQKIQAFRQW IINSIKQEEN E // ID GLGB_HAEIN Reviewed; 730 AA. AC P45177; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB; DE EC=2.4.1.18; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme; DE AltName: Full=Glycogen branching enzyme; DE Short=BE; GN Name=glgB; OrderedLocusNames=HI_1357; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic CC linkages in glycogen by scission of a 1,4-alpha-linked CC oligosaccharide from growing alpha-1,4-glucan chains and the CC subsequent attachment of the oligosaccharide to the alpha-1,6 CC position. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan CC chain to a primary hydroxy group in a similar glucan chain. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB 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; L42023; AAC23004.1; -; Genomic_DNA. DR PIR; I64118; I64118. DR RefSeq; NP_439508.1; NC_000907.1. DR RefSeq; WP_005694003.1; NC_000907.1. DR ProteinModelPortal; P45177; -. DR SMR; P45177; 119-725. DR STRING; 71421.HI1357; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EnsemblBacteria; AAC23004; AAC23004; HI_1357. DR GeneID; 950275; -. DR KEGG; hin:HI1357; -. DR PATRIC; 20191399; VBIHaeInf48452_1410. DR eggNOG; ENOG4105C9C; Bacteria. DR eggNOG; COG0296; LUCA. DR KO; K00700; -. DR OMA; DDADHNT; -. DR OrthoDB; EOG6JX7GT; -. DR PhylomeDB; P45177; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR HAMAP; MF_00685; GlgB; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR006407; GlgB. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR10357; PTHR10357; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF02922; CBM_48; 1. DR PIRSF; PIRSF000463; GlgB; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR SUPFAM; SSF81296; SSF81296; 2. DR TIGRFAMs; TIGR01515; branching_enzym; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glycogen biosynthesis; KW Glycogen metabolism; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 730 1,4-alpha-glucan branching enzyme GlgB. FT /FTId=PRO_0000188710. FT ACT_SITE 405 405 Nucleophile. {ECO:0000250}. FT ACT_SITE 458 458 Proton donor. {ECO:0000250}. SQ SEQUENCE 730 AA; 83820 MW; 5B9575317F53769A CRC64; MTTAVTQAII DGFFDASNGD PFATLGMHET EQGIEIRTLL PDANRMVVIE RESGKEITEL DCVDERGFFV GVIPNCRQFF AYQLQVFWGN EAQIIEDPYR FHPMIDDLEQ WLLSEGSMLR PYEVLGAHFM ECDGVSGVNF RLWAPNARRV SIVGDFNYWD GRRHPMRFHS KSGVWELFLP KASLGQLYKF ELIDCHGNLR LKADPFAFSS QLRPDTASQV SALPNVVEMT EARKKANQGN QPISIYEVHL GSWRRNLENN FWLDYDQIAD ELIPYVKEMG FTHIEFLPLS EFPFDGSWGY QPLGLYSPTS RFGSPEAFRR LVKRAHEAGI NVILDWVPGH FPSDTHGLVA FDGTALYEHE DPREGYHQDW NTLIYNYGRN EVKNFLSSNA LYWLERFGVD GIRVDAVASM IYRDYSRAEG EWIPNQYGGR ENLEAIEFLK HTNWKIHSEM AGAISIAEES TSFAGVTHPS ENGGLGFNFK WNMGWMNDTL AYMKLDPIYR QYHHNKMTFG MVYQYSENFV LPLSHDEVVH GKYSLLGKMP GDTWQKFANL RAYYGYMWGY PGKKLLFMGN EFAQGREWNY EESLDWFLLD ENIGGGWHKG VLKLVKDLNQ IYQKNRPLFE LDNSPEGFDW LVVDDAANSV LAFERRSSNG ERIIVVSNFT PVPRHNYRIG VNVAGKYEEI LNTDSMYYEG SNVGNFGCVA SEQIESHGRE NSISVSIPPL ATVYLRLKTK // ID GLNA_HAEIN Reviewed; 472 AA. AC P43794; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Glutamine synthetase; DE EC=6.3.1.2; DE AltName: Full=Glutamate--ammonia ligase; GN Name=glnA; OrderedLocusNames=HI_0865; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- ENZYME REGULATION: The activity of this enzyme is controlled by CC adenylation under conditions of abundant glutamine. The fully CC adenylated enzyme complex is inactive (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two CC hexagons. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22524.1; -; Genomic_DNA. DR PIR; I64098; I64098. DR RefSeq; NP_439025.1; NC_000907.1. DR RefSeq; WP_005693212.1; NC_000907.1. DR ProteinModelPortal; P43794; -. DR SMR; P43794; 9-472. DR STRING; 71421.HI0865; -. DR EnsemblBacteria; AAC22524; AAC22524; HI_0865. DR GeneID; 949878; -. DR KEGG; hin:HI0865; -. DR PATRIC; 20190385; VBIHaeInf48452_0906. DR eggNOG; ENOG4105C5F; Bacteria. DR eggNOG; COG0174; LUCA. DR KO; K01915; -. DR OMA; ACFMPKP; -. DR OrthoDB; EOG6B360N; -. DR PhylomeDB; P43794; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR Gene3D; 3.10.20.70; -; 1. DR Gene3D; 3.30.590.10; -; 1. DR InterPro; IPR008147; Gln_synt_b-grasp. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR InterPro; IPR008146; Gln_synth_cat_dom. DR InterPro; IPR027303; Gln_synth_gly_rich_site. DR InterPro; IPR004809; Gln_synth_I. DR InterPro; IPR001637; Gln_synth_I_adenylation_site. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; SSF54368; 1. DR TIGRFAMs; TIGR00653; GlnA; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00182; GLNA_ADENYLATION; 1. DR PROSITE; PS00181; GLNA_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 472 Glutamine synthetase. FT /FTId=PRO_0000153238. FT MOD_RES 402 402 O-AMP-tyrosine. {ECO:0000250}. SQ SEQUENCE 472 AA; 52344 MW; 160DDD0F91B28046 CRC64; MPNANAIANV FKLIEENNVK FVLLRFTDIK GKEHGVSIPV SLVDEDMFED GKMFDGSSVE GWKTINKADM LLMPMAETAI VDPFAQIPTL SIRCSVYEPT TMQSYDRDPR SIAIRAENYM RSTGIADQAF FGPEPEFFLF DDVRFNVSMN KASFSIDDIE AAWNTNKKYE EGNNAYRPLK KGGYCAVAPI DSAHDIRSEM CLILEEMGLV IEAHHHEVAT AGQNEIATKF NTLTLKADET QIYKHVVQNV ALEHGKTACF MPKPITGDNG SGMHCNMSLS KDGKNIFQGD KYAGLSETAL YYIGGIIKHA KALNAFTNPS TNSYKRLVPG YEAPVLLAYS ASNRSASIRI PAVTNPKAIR VEARFPDPLA NPYLAFAALL MAGLDGVVNK IHPGDAMDKN LYDLPPEELK DIPAVASSLE EALNSLEKDY EFLTQGGVFA KDFIDAFISI KRKEVERLNM APHPVEFEMY YA // ID GLPE_HAEIN Reviewed; 105 AA. AC P44819; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Thiosulfate sulfurtransferase GlpE {ECO:0000255|HAMAP-Rule:MF_01009}; DE EC=2.8.1.1 {ECO:0000255|HAMAP-Rule:MF_01009}; GN Name=glpE {ECO:0000255|HAMAP-Rule:MF_01009}; GN OrderedLocusNames=HI_0679; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes, although with low efficiency, the sulfur CC transfer reaction from thiosulfate to cyanide. {ECO:0000255|HAMAP- CC Rule:MF_01009}. CC -!- CATALYTIC ACTIVITY: Thiosulfate + cyanide = sulfite + thiocyanate. CC {ECO:0000255|HAMAP-Rule:MF_01009}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01009}. CC -!- SIMILARITY: Belongs to the GlpE family. {ECO:0000255|HAMAP- CC Rule:MF_01009}. CC -!- SIMILARITY: Contains 1 rhodanese domain. {ECO:0000255|HAMAP- CC Rule:MF_01009}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22338.1; -; Genomic_DNA. DR PIR; H64085; H64085. DR RefSeq; NP_438839.1; NC_000907.1. DR RefSeq; WP_005694604.1; NC_000907.1. DR ProteinModelPortal; P44819; -. DR STRING; 71421.HI0679; -. DR EnsemblBacteria; AAC22338; AAC22338; HI_0679. DR GeneID; 949715; -. DR KEGG; hin:HI0679; -. DR PATRIC; 20189977; VBIHaeInf48452_0710. DR eggNOG; ENOG4105M78; Bacteria. DR eggNOG; COG0607; LUCA. DR KO; K02439; -. DR OMA; MDQFQHI; -. DR OrthoDB; EOG68DD6K; -. DR PhylomeDB; P44819; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.250.10; -; 1. DR HAMAP; MF_01009; Thiosulf_sulfurtr; 1. DR InterPro; IPR001763; Rhodanese-like_dom. DR InterPro; IPR023695; Thiosulf_sulfurTrfase. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 105 Thiosulfate sulfurtransferase GlpE. FT /FTId=PRO_0000200553. FT DOMAIN 15 103 Rhodanese. {ECO:0000255|HAMAP- FT Rule:MF_01009}. FT ACT_SITE 63 63 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01009}. SQ SEQUENCE 105 AA; 12033 MW; A3120E14BDD7245F CRC64; MPFKEITPQQ AWEMMQQGAI LVDIRDNMRF AYSHPKGAFH LTNQSFLQFE ELADFDSPII VSCYHGVSSR NVATFLVEQG YKNVFSMIGG FDGWCRAELP IDTTY // ID GLO2_HAEIN Reviewed; 238 AA. AC P71374; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000255|HAMAP-Rule:MF_01374}; DE EC=3.1.2.6 {ECO:0000255|HAMAP-Rule:MF_01374}; DE AltName: Full=Glyoxalase II {ECO:0000255|HAMAP-Rule:MF_01374}; DE Short=Glx II {ECO:0000255|HAMAP-Rule:MF_01374}; GN Name=gloB {ECO:0000255|HAMAP-Rule:MF_01374}; GN OrderedLocusNames=HI_1274; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D- CC lactoyl-glutathione to form glutathione and D-lactic acid. CC {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O = CC glutathione + a 2-hydroxy carboxylate. {ECO:0000255|HAMAP- CC Rule:MF_01374}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01374}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01374}; CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal CC degradation; (R)-lactate from methylglyoxal: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01374}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II family. {ECO:0000255|HAMAP-Rule:MF_01374}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22922.1; -; Genomic_DNA. DR PIR; G64113; G64113. DR RefSeq; NP_439427.1; NC_000907.1. DR RefSeq; WP_005694517.1; NC_000907.1. DR ProteinModelPortal; P71374; -. DR STRING; 71421.HI1274; -. DR EnsemblBacteria; AAC22922; AAC22922; HI_1274. DR GeneID; 950207; -. DR KEGG; hin:HI1274; -. DR PATRIC; 20191227; VBIHaeInf48452_1325. DR eggNOG; ENOG4108RW0; Bacteria. DR eggNOG; COG0491; LUCA. DR KO; K01069; -. DR OMA; NYIWLLQ; -. DR OrthoDB; EOG69GZQ4; -. DR PhylomeDB; P71374; -. DR UniPathway; UPA00619; UER00676. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01374; Glyoxalase_2; 1. DR InterPro; IPR032282; HAGH_C. DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF16123; HAGH_C; 1. DR Pfam; PF12706; Lactamase_B_2; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR03413; GSH_gloB; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 238 Hydroxyacylglutathione hydrolase. FT /FTId=PRO_0000192353. FT METAL 52 52 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 54 54 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 56 56 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 57 57 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 108 108 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 125 125 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 125 125 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. FT METAL 163 163 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01374}. SQ SEQUENCE 238 AA; 26850 MW; 63C845DA1DC739DE CRC64; MLFALPALND NYIWLYQREN LPLIIVDLPE TDKLFAWLEK QNATIEAVLL THEHDDHTQG VSAFKKRYPT VPIYGPQECE KKGATQIVNE GKILTANYQI DVIPTGGHTK QHVSFLVDNH LFCGDALFSA GCGRVFTGNY ALMFEGLQRL NTLPDETIVC PAHEYTLGNL AFAETVLVDK SAVEKSAVEK QRIFVETQRA ENKPSLPTTL KLEREINPFL QAKTLEEFTA LRKAKDIF // ID GLPT_HAEIN Reviewed; 480 AA. AC P96335; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 17-FEB-2016, entry version 106. DE RecName: Full=Glycerol-3-phosphate transporter; DE Short=G-3-P transporter; DE AltName: Full=G-3-P permease; GN Name=glpT; OrderedLocusNames=HI_0686; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B; RX PubMed=9714837; DOI=10.1016/S0378-1119(98)00259-5; RA Song X.M., Forsgren A., Janson H.; RT "Glycerol-3-phosphate transport in Haemophilus influenzae: cloning, RT sequencing, and transcription analysis of the glpT gene."; RL Gene 215:381-388(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi 772; RA Song X.M., Janson H.; RT "Different organization and regulation of the glpTQ operons between RT type b and nontypeable Haemophilus influenzae."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Responsible for glycerol-3-phosphate uptake. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22346.1; -; Genomic_DNA. DR EMBL; AF001172; AAC35741.1; -; Genomic_DNA. DR EMBL; AF132901; AAD38343.1; -; Genomic_DNA. DR RefSeq; NP_438846.1; NC_000907.1. DR RefSeq; WP_005650782.1; NC_000907.1. DR ProteinModelPortal; P96335; -. DR SMR; P96335; 5-475. DR STRING; 71421.HI0686; -. DR EnsemblBacteria; AAC22346; AAC22346; HI_0686. DR GeneID; 949719; -. DR KEGG; hin:HI0686; -. DR PATRIC; 20189991; VBIHaeInf48452_0717. DR eggNOG; ENOG4105CXY; Bacteria. DR eggNOG; COG2271; LUCA. DR KO; K02445; -. DR OMA; WAFNDDW; -. DR OrthoDB; EOG6M9DW7; -. DR PhylomeDB; P96335; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006820; P:anion transport; IBA:GO_Central. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR005267; G3P_transporter. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR021159; Sugar-P_transporter_CS. DR InterPro; IPR000849; Sugar_P_transporter. DR Pfam; PF07690; MFS_1; 1. DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00881; 2A0104; 1. DR TIGRFAMs; TIGR00712; glpT; 1. DR PROSITE; PS00942; GLPT; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Glycerol metabolism; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 480 Glycerol-3-phosphate transporter. FT /FTId=PRO_0000199879. FT TOPO_DOM 1 36 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 37 57 Helical; Name=1. {ECO:0000250}. FT TOPO_DOM 58 64 Periplasmic. {ECO:0000250}. FT TRANSMEM 65 85 Helical; Name=2. {ECO:0000250}. FT TOPO_DOM 86 94 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 95 113 Helical; Name=3. {ECO:0000250}. FT TOPO_DOM 114 121 Periplasmic. {ECO:0000250}. FT TRANSMEM 122 142 Helical; Name=4. {ECO:0000250}. FT TOPO_DOM 143 161 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 162 181 Helical; Name=5. {ECO:0000250}. FT TOPO_DOM 182 201 Periplasmic. {ECO:0000250}. FT TRANSMEM 202 219 Helical; Name=6. {ECO:0000250}. FT TOPO_DOM 220 274 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 275 295 Helical; Name=7. {ECO:0000250}. FT TOPO_DOM 296 300 Periplasmic. {ECO:0000250}. FT TRANSMEM 301 321 Helical; Name=8. {ECO:0000250}. FT TOPO_DOM 322 334 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 335 354 Helical; Name=9. {ECO:0000250}. FT TOPO_DOM 355 359 Periplasmic. {ECO:0000250}. FT TRANSMEM 360 396 Helical; Name=10. {ECO:0000250}. FT TOPO_DOM 397 415 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 416 437 Helical; Name=11. {ECO:0000250}. FT TOPO_DOM 438 442 Periplasmic. {ECO:0000250}. FT TRANSMEM 443 463 Helical; Name=12. {ECO:0000250}. FT TOPO_DOM 464 479 Cytoplasmic. {ECO:0000250}. SQ SEQUENCE 480 AA; 53045 MW; 6773C2E8013CB027 CRC64; MFGPFKPAPH IAELPAEKID STYKRLRWQV FAGIFFGYAA YYFVRANFDL AQPGLIQAGL YSKAELGVIG SAAGLAYGLS KFVMAGMSDR SNPRVFLPFG LLLSGLCMTL MGLFPWATSG IAIMWVMIFL NGWFQGMGWP PCGRTMVHWW SKSERGTIVS IWNTAHNIGG MVPGAMVLLA SAIFFSTHGI EAQAKDVWQQ SLYFPGIAAM IFAIPVYFVM RDTPQSCGLP SIEKWRNDYP DDYNEKTYEN DLTAKEIFVT YVLKNKLLWY IAIANVFVYL IRYGVLKWSP VYLSEVKHFN IKGTAWAYTI YELAAVPGTL LCGWVSDKVF KGKRGLTGFI FMILTTAAVV AYWMNPATPE AELANYSAWY ENPYQLTDFV LMTLIGFLIY GPVMLIGLHA LELAPKKAAG TAAGFTGLFG YLGGTVSASA VIGWAAQHYG WDGGFYVMIG GGVLAVLLLL IVMVEEGKHK AKLGDTYGTK // ID GLRX4_HAEIN Reviewed; 107 AA. AC P45085; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Glutaredoxin-4; DE Short=Grx4; DE AltName: Full=Monothiol glutaredoxin; GN Name=grxD; OrderedLocusNames=HI_1165; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Monothiol glutaredoxin involved in the biogenesis of CC iron-sulfur clusters. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00686}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22820.1; 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; L42023; AAC22820.1; ALT_INIT; Genomic_DNA. DR PIR; F64168; F64168. DR RefSeq; NP_439323.2; NC_000907.1. DR RefSeq; WP_010869143.1; NC_000907.1. DR ProteinModelPortal; P45085; -. DR SMR; P45085; 3-106. DR STRING; 71421.HI1165; -. DR EnsemblBacteria; AAC22820; AAC22820; HI_1165. DR GeneID; 949810; -. DR KEGG; hin:HI1165; -. DR PATRIC; 20191009; VBIHaeInf48452_1217. DR eggNOG; ENOG4105M2J; Bacteria. DR eggNOG; COG0278; LUCA. DR KO; K07390; -. DR OMA; TVHDFID; -. DR OrthoDB; EOG69GZQ4; -. DR PhylomeDB; P45085; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014434; Monothiol_GRX. DR InterPro; IPR004480; Monothiol_GRX-rel. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR10293; PTHR10293; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR PIRSF; PIRSF005894; Monothiol_GRX; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00365; TIGR00365; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Redox-active center; Reference proteome. FT CHAIN 1 107 Glutaredoxin-4. FT /FTId=PRO_0000102261. FT DOMAIN 4 106 Glutaredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT REGION 83 84 Glutathione binding. {ECO:0000250}. FT METAL 29 29 Iron-sulfur (2Fe-2S); shared with dimeric FT partner. {ECO:0000250}. FT BINDING 21 21 Glutathione. {ECO:0000250}. FT BINDING 58 58 Glutathione. {ECO:0000250}. FT BINDING 70 70 Glutathione; via amide nitrogen and FT carbonyl oxygen. {ECO:0000250}. SQ SEQUENCE 107 AA; 11941 MW; E20EF7B8C16DF9FC CRC64; METLDKIKKQ ISENPILIYM KGSPKLPSCG FPARASEALM HCKVPFGYVD ILQHPDIRAE LPTYANWPTF PQLWVEGELI GGCDIILEMY QAGELQTLLA EVAAKHA // ID GLYA_HAEIN Reviewed; 421 AA. AC P43844; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051}; DE EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; GN OrderedLocusNames=HI_0889; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22549.1; -; Genomic_DNA. DR PIR; D64100; D64100. DR RefSeq; NP_439050.1; NC_000907.1. DR RefSeq; WP_005693240.1; NC_000907.1. DR ProteinModelPortal; P43844; -. DR SMR; P43844; 1-419. DR STRING; 71421.HI0889; -. DR EnsemblBacteria; AAC22549; AAC22549; HI_0889. DR GeneID; 949894; -. DR KEGG; hin:HI0889; -. DR PATRIC; 20190435; VBIHaeInf48452_0931. DR eggNOG; ENOG4105C65; Bacteria. DR eggNOG; COG0112; LUCA. DR KO; K00600; -. DR OMA; MAIRCQH; -. DR OrthoDB; EOG6Z0QB2; -. DR PhylomeDB; P43844; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000579; 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 1 421 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113583. FT REGION 125 127 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 35 35 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 57 57 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 64 64 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 65 65 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 99 99 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 121 121 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 175 175 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 203 203 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 228 228 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 235 235 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 263 263 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 363 363 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 229 229 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00051}. SQ SEQUENCE 421 AA; 45904 MW; B73698800F583CA3 CRC64; MFTRNMTIAD YDPVLWQAIQ DENRRQEEHI ELIASENYAS PRVMEAQGSQ FTNKYAEGYP GKRYYGGCEY ADIVEQLAID RAKELFGADY VNVQPHSGSQ ANAAVYGALI NAGDTILGMD LAHGGHLTHG AKVSFSGKIY NSVLYGITAD GLIDYEDVRQ KALECKPKLI VAGFSAYSQV VDWAKMREIA DEVGAYLFVD MAHVAGLIAA GLYPNPLPHA HVVTTTTHKT LGGPRGGLIL SSCGDEEIYK KLQSSVFPAN QGGPLVHIIA AKAVCFKGAL EPQYKEYQAN VIKNAKAMVE VFKQRGYDVV SNGTENHLFL VSFIKQGLTG KAADAALGKA NITVNKNAVP NDPQKPFVTS GIRVGTPSVT RRGFNENDVR ELAGWMCDVL DALGKENEEQ VIAETKEKVL AICKRLPVYP K // ID GLND_HAEIN Reviewed; 863 AA. AC P43919; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277}; DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277}; DE Includes: DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277}; DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277}; DE Includes: DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277}; DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277}; GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; GN OrderedLocusNames=HI_1719; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII CC regulatory proteins (GlnB and homologs), in response to the CC nitrogen status of the cell that GlnD senses through the glutamine CC level. Under low glutamine levels, catalyzes the conversion of the CC PII proteins and UTP to PII-UMP and PPi, while under higher CC glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP CC (deuridylylation). Thus, controls uridylylation state and activity CC of the PII proteins, and plays an important role in the regulation CC of nitrogen assimilation and metabolism. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl- CC [protein-PII]. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- CATALYTIC ACTIVITY: Uridylyl-[protein-PII] + H(2)O = UMP + CC [protein-PII]. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277}; CC -!- ENZYME REGULATION: Uridylyltransferase (UTase) activity is CC inhibited by glutamine, while glutamine activates uridylyl- CC removing (UR) activity. {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- DOMAIN: Has four distinct domains: an N-terminal CC nucleotidyltransferase (NT) domain responsible for UTase activity, CC a central HD domain that encodes UR activity, and two C-terminal CC ACT domains that seem to have a role in glutamine sensing. CC {ECO:0000255|HAMAP-Rule:MF_00277}. CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- SIMILARITY: Contains 2 ACT domains. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000255|HAMAP- CC Rule:MF_00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23362.1; -; Genomic_DNA. DR PIR; B64138; B64138. DR RefSeq; NP_439860.1; NC_000907.1. DR RefSeq; WP_005694204.1; NC_000907.1. DR ProteinModelPortal; P43919; -. DR STRING; 71421.HI1719; -. DR EnsemblBacteria; AAC23362; AAC23362; HI_1719. DR GeneID; 950533; -. DR KEGG; hin:HI1719; -. DR PATRIC; 20192191; VBIHaeInf48452_1798. DR eggNOG; ENOG4105E1P; Bacteria. DR eggNOG; COG2844; LUCA. DR KO; K00990; -. DR OMA; HTLFWIA; -. DR OrthoDB; EOG6CCH44; -. DR PhylomeDB; P43919; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3210.10; -; 1. DR HAMAP; MF_00277; PII_uridylyl_transf; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase. DR InterPro; IPR010043; UTase/UR. DR Pfam; PF01842; ACT; 1. DR Pfam; PF08335; GlnD_UR_UTase; 1. DR Pfam; PF01966; HD; 1. DR PIRSF; PIRSF006288; PII_uridyltransf; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR01693; UTase_glnD; 1. DR PROSITE; PS51671; ACT; 2. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Multifunctional enzyme; KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1 863 Bifunctional FT uridylyltransferase/uridylyl-removing FT enzyme. FT /FTId=PRO_0000192736. FT DOMAIN 447 579 HD. {ECO:0000255|HAMAP-Rule:MF_00277}. FT DOMAIN 688 764 ACT 1. {ECO:0000255|HAMAP-Rule:MF_00277}. FT DOMAIN 794 863 ACT 2. {ECO:0000255|HAMAP-Rule:MF_00277}. FT REGION 1 328 Uridylyltransferase. FT REGION 329 687 Uridylyl-removing. SQ SEQUENCE 863 AA; 100173 MW; B6F679A70A01A651 CRC64; MLFSPTLSSL LTPSAVKIER ENLKQFELEN FSCYSIFELI ENRCDFYDAL LIQLWQEIGL SEQQGISLIA VGGYGRREMF PLSDLDFLIL VEQTPSHEIE EKITQFIQFL WDCGFEVGNS VRTLEQCELE GKQDITIATN LLEARFLTGN RPHFDVLNEL VKRADFWSKE DFFNAKVQEQ IERYQRYHNT AYNLEPDIKF SPGGLRDLHL LYWVALRHSG ALTLEAILQS GFIYPQEYQQ LQESRAFLFK VRFALHLILK RYDNRLLFDR QIKVSELLGF RGEGNPAVEK MMKCFFQALH RISLISNLLI QHYRENVLSS NQDTVIDQLD DDFQLINQSL CLRNSFVFQE KPARILDLFF YLTQYEHVNI HSDTLRQLQI SLEQLSQKLC EIPAAREKFL RLFNQSNAIK RAFMPMHQYG VLTAYLPQWQ AIEGLMQFDL FHIYTVDEHT LRVMLKLESF LPKGSAQEHP IAHRIFSQLS DRTLLYIAAL FHDIAKGRGG DHAELGAEDV ADFAQLHGLD RREIDTLAWL VQSHLLMSIT AQRRDIHDPE VVMNFAEAMQ NQVRLDYLTC LTVADICATN GNLWNSWKRS LFASLYEFTE QQFSQGMKEL LDYSEKSAEN RKLAQQILTQ DYSDITSISI EKLWTRCPED YFVRNTPKQI AWHTSLLVDF VEALLVKISN RFSLGGTEVF IYCQDQPHLF NKVVSTIGAK KFSIHDAQII TTQDGYVFDS FIITELNGEL VEFDRRRELE QALTVALQSE KLPALSIVPN RQLQHFTVQT DVRFLQENKK EHTEMELVAL DKAGLLAQVS QIFTELNLNL LNAKITTVGE KAEDFFILTN QFGQALAREE RERLNSVIIQ QIR // ID GLRX_HAEIN Reviewed; 87 AA. AC P45242; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Glutaredoxin; GN Name=grxA; Synonyms=grx; OrderedLocusNames=HI_1532; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in CC the presence of NADPH and glutathione reductase. Reduces low CC molecular weight disulfides and proteins (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23182.1; -; Genomic_DNA. DR PIR; I64127; I64127. DR RefSeq; NP_439681.1; NC_000907.1. DR RefSeq; WP_005628952.1; NC_000907.1. DR ProteinModelPortal; P45242; -. DR SMR; P45242; 1-83. DR STRING; 71421.HI1532; -. DR EnsemblBacteria; AAC23182; AAC23182; HI_1532. DR GeneID; 950394; -. DR KEGG; hin:HI1532; -. DR PATRIC; 20191789; VBIHaeInf48452_1603. DR eggNOG; ENOG41090BQ; Bacteria. DR eggNOG; COG0695; LUCA. DR KO; K03674; -. DR OMA; VGGCTEF; -. DR OrthoDB; EOG6Z3KS6; -. DR PhylomeDB; P45242; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR014025; Glutaredoxin_subgr. DR InterPro; IPR011902; GRXA. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02183; GRXA; 1. DR PROSITE; PS00195; GLUTAREDOXIN_1; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; Electron transport; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1 87 Glutaredoxin. FT /FTId=PRO_0000141591. FT DOMAIN 1 87 Glutaredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT DISULFID 11 14 Redox-active. {ECO:0000250}. SQ SEQUENCE 87 AA; 9670 MW; 27987F393D48C9DB CRC64; MFVVIFGRPG CPYCVRAKNL AEKLKGEVAD FDYRYVDIHA EGITKEDLSK SVGKPVETVP QIFIDEKPIG GCTDFEALMK EQFGIVA // ID GLTS_HAEIN Reviewed; 404 AA. AC P45240; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Sodium/glutamate symport carrier protein; DE AltName: Full=Glutamate permease; GN Name=gltS; OrderedLocusNames=HI_1530; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular CC glutamate. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GltS symporter 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; L42023; AAC23176.1; -; Genomic_DNA. DR PIR; G64127; G64127. DR RefSeq; NP_439679.1; NC_000907.1. DR RefSeq; WP_005693557.1; NC_000907.1. DR STRING; 71421.HI1530; -. DR EnsemblBacteria; AAC23176; AAC23176; HI_1530. DR GeneID; 950392; -. DR KEGG; hin:HI1530; -. DR PATRIC; 20191785; VBIHaeInf48452_1601. DR eggNOG; ENOG4105D6U; Bacteria. DR eggNOG; COG0786; LUCA. DR KO; K03312; -. DR OMA; TNIFRFQ; -. DR OrthoDB; EOG6FRCSX; -. DR PhylomeDB; P45240; -. DR Proteomes; UP000000579; 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:0015501; F:glutamate:sodium symporter activity; IEA:InterPro. DR InterPro; IPR004445; GltS. DR PANTHER; PTHR36178:SF1; PTHR36178:SF1; 1. DR Pfam; PF03616; Glt_symporter; 1. DR TIGRFAMs; TIGR00210; gltS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; Reference proteome; Sodium; Sodium transport; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 404 Sodium/glutamate symport carrier protein. FT /FTId=PRO_0000052334. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 161 181 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 277 297 Helical. {ECO:0000255}. FT TRANSMEM 307 327 Helical. {ECO:0000255}. FT TRANSMEM 338 358 Helical. {ECO:0000255}. FT TRANSMEM 373 393 Helical. {ECO:0000255}. SQ SEQUENCE 404 AA; 43371 MW; 8930C6BD39BDAC3C CRC64; MSYTFSTYET LALASLVLLL GYFLVKRINV LKTFNIPEPV VGGFIVAIGL LIWHKIDGTS FNFDKNLQTT MMLVFFTSIG LSANFSRLIK GGKPLVVFLF IAALLIFGQN VIGIASSMAL GIHPAYGLLA GSVTLTGGHG TGAAWADTFA HQFNLQGATE IAIACATFGL VFGGIIGGPV ARFLLNRQKQ GENPENDEVD DIQEAFEHPT YKRKITARSL IETIAMISVC LLIGQYLDVQ TKGTALQLPT FVWCLFTGVI VRNILTNIFR FQVAESAIDV LGSVGLSIFL AIALMSLRLW ELAGLAIDVL IVLAIQVAFM AAFAIFITYR AMGKDYDAVV LSAGHCGFGL GATPTAIANM QAVTSRFGPS HKAFLIVPMV GAFFIDLINA ALLKVSFAVV NILA // ID GMHBB_HAEIN Reviewed; 184 AA. AC P46452; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase; DE EC=3.1.3.82 {ECO:0000269|PubMed:25848029}; DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase; DE Short=HBP phosphatase; GN Name=gmhB; OrderedLocusNames=HI_0621.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. RN [3] RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. RX PubMed=12101286; RA Valvano M.A., Messner P., Kosma P.; RT "Novel pathways for biosynthesis of nucleotide-activated glycero- RT manno-heptose precursors of bacterial glycoproteins and cell surface RT polysaccharides."; RL Microbiology 148:1979-1989(2002). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=25848029; DOI=10.1073/pnas.1423570112; RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L., RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D., RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., RA Dunaway-Mariano D., Allen K.N., Farelli J.D.; RT "Panoramic view of a superfamily of phosphatases through substrate RT profiling."; RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015). CC -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7- CC bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1- CC phosphate by removing the phosphate group at the C-7 position in CC vitro. Also catalyzes the dephosphorylation of D-glycero-alpha-D- CC manno-heptose 1,7-bisphosphate, phospho-serine and fructose-1,6- CC biphosphate in vitro. {ECO:0000269|PubMed:25848029}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1,7- CC bisphosphate + H(2)O = D-glycero-beta-D-manno-heptose 1-phosphate CC + phosphate. {ECO:0000269|PubMed:25848029}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:25848029}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GmhB 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; L42023; AAC22281.1; -; Genomic_DNA. DR RefSeq; NP_438781.1; NC_000907.1. DR RefSeq; WP_005694551.1; NC_000907.1. DR ProteinModelPortal; P46452; -. DR SMR; P46452; 4-181. DR STRING; 71421.HI0621.1; -. DR EnsemblBacteria; AAC22281; AAC22281; HI_0621.1. DR GeneID; 949688; -. DR KEGG; hin:HI0621.1; -. DR PATRIC; 20189829; VBIHaeInf48452_0647. DR eggNOG; ENOG4108ZI0; Bacteria. DR eggNOG; COG0241; LUCA. DR KO; K03273; -. DR OMA; SFMIGDK; -. DR OrthoDB; EOG6QG8GT; -. DR PhylomeDB; P46452; -. DR BRENDA; 3.1.3.82; 2529. DR UniPathway; UPA00356; UER00438. DR UniPathway; UPA00976; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; ISS:GOC. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR004446; Heptose_bisP_phosphatase. DR InterPro; IPR006543; Histidinol-phos. DR PIRSF; PIRSF004682; GmhB; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00213; GmhB_yaeD; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Magnesium; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 184 D-glycero-beta-D-manno-heptose-1,7- FT bisphosphate 7-phosphatase. FT /FTId=PRO_0000209392. FT REGION 8 10 Substrate binding. {ECO:0000250}. FT REGION 16 19 Substrate binding. {ECO:0000250}. FT REGION 50 53 Substrate binding. {ECO:0000250}. FT REGION 106 107 Substrate binding. {ECO:0000250}. FT ACT_SITE 8 8 Nucleophile. {ECO:0000250}. FT ACT_SITE 10 10 Proton donor. {ECO:0000250}. FT METAL 8 8 Magnesium. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 10 10 Magnesium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 89 89 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 91 91 Zinc; via pros nitrogen. FT {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 103 103 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 105 105 Zinc. {ECO:0000250|UniProtKB:Q7WG29}. FT METAL 132 132 Magnesium. FT {ECO:0000250|UniProtKB:Q7WG29}. FT BINDING 133 133 Substrate. {ECO:0000250}. FT SITE 50 50 Stabilizes the phosphoryl group. FT {ECO:0000250}. FT SITE 106 106 Contributes to substrate recognition. FT {ECO:0000250}. FT SITE 107 107 Stabilizes the phosphoryl group. FT {ECO:0000250}. SQ SEQUENCE 184 AA; 20810 MW; 49D1D56DA6DF3DBD CRC64; MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT NQSGIARGYF SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK EDCDCRKPKS GMLLQAIKEL KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL VRTGKPVTGE GEGIADYVLD SIVDLPRILK RLKK // ID GLGC_HAEIN Reviewed; 437 AA. AC P43796; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-MAR-2003, sequence version 2. DT 11-MAY-2016, entry version 103. DE RecName: Full=Glucose-1-phosphate adenylyltransferase; DE EC=2.7.7.27; DE AltName: Full=ADP-glucose pyrophosphorylase; DE Short=ADPGlc PPase; DE AltName: Full=ADP-glucose synthase; GN Name=glgC; OrderedLocusNames=HI_1359; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the synthesis of ADP-glucose, a sugar donor CC used in elongation reactions on alpha-glucans. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate = CC diphosphate + ADP-glucose. CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23006.1; 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; L42023; AAC23006.1; ALT_INIT; Genomic_DNA. DR PIR; B64119; B64119. DR RefSeq; NP_439510.1; NC_000907.1. DR ProteinModelPortal; P43796; -. DR STRING; 71421.HI1359; -. DR EnsemblBacteria; AAC23006; AAC23006; HI_1359. DR GeneID; 950593; -. DR KEGG; hin:HI1359; -. DR PATRIC; 20191403; VBIHaeInf48452_1412. DR eggNOG; ENOG4107QQ4; Bacteria. DR eggNOG; COG0448; LUCA. DR KO; K00975; -. DR OMA; KAVAHHF; -. DR OrthoDB; EOG6W9X86; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 2. DR HAMAP; MF_00624; GlgC; 1. DR InterPro; IPR005836; ADP_Glu_pyroP_CS. DR InterPro; IPR011831; GlgC. DR InterPro; IPR023049; GlgC_bac. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 2. DR TIGRFAMs; TIGR02091; glgC; 1. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; KW Glycogen biosynthesis; Glycogen metabolism; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 437 Glucose-1-phosphate adenylyltransferase. FT /FTId=PRO_0000195299. SQ SEQUENCE 437 AA; 49107 MW; E5E2284ACE5AD1D9 CRC64; MEILMKSGDL NKYDLVKNAL VLVLAGGRGS RLHELTDKRA KPALYFGGNR RIIDFALSNC INSDLNRIGV VTQYAAHSLL LHLQTGWSFL PQERGEFVDM LPARQQIDDS TWYRGTADAV YQNMAIIKNH YRPKYILILA GDHIYKQDYS VMLMDHVNSG AKCTVGCIEV PRSEAHEFGV MAVNENLKVK AFVEKPKDPP AMVGKPDVSL ASMGIYVFDA DYLYKMLEQE VNTPQTSHDF GKDVLPKCLE EGALYAHPFS RSCMGRNTEG EIYWRDVGTL DSFWQSNIDL VSENPQLDIY DQSWPIRGNP IQAYPSKFFY KHSNVHPVDN SLIGGGCVIT DASISNSVLF DHIKIDAFSK VDHCVVLPQV KIGKNCVLKN CIIDRECEIP DGMQIGVDME EDKKRFRISS TGKVILVTSK MLKILEGHEI GEEGHLD // ID GLPG_HAEIN Reviewed; 192 AA. AC P44783; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Rhomboid protease GlpG; DE EC=3.4.21.105; DE AltName: Full=Intramembrane serine protease; GN Name=glpG; OrderedLocusNames=HI_0618; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), ACTIVE SITE, REACTION RP MECHANISM, AND SUBCELLULAR LOCATION. RX PubMed=17210913; DOI=10.1073/pnas.0609981104; RA Lemieux M.J., Fischer S.J., Cherney M.M., Bateman K.S., James M.N.G.; RT "The crystal structure of the rhomboid peptidase from Haemophilus RT influenzae provides insight into intramembrane proteolysis."; RL Proc. Natl. Acad. Sci. U.S.A. 104:750-754(2007). CC -!- FUNCTION: Rhomboid-type serine protease that catalyzes CC intramembrane proteolysis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cleaves type-1 transmembrane domains using a CC catalytic dyad composed of serine and histidine that are CC contributed by different transmembrane domains. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-10098079, EBI-10098079; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:17210913}; Multi-pass membrane protein CC {ECO:0000269|PubMed:17210913}. CC -!- SIMILARITY: Belongs to the peptidase S54 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; L42023; AAC22277.1; -; Genomic_DNA. DR PIR; I64081; I64081. DR RefSeq; NP_438776.1; NC_000907.1. DR RefSeq; WP_005648561.1; NC_000907.1. DR PDB; 2NR9; X-ray; 2.20 A; A=1-192. DR PDB; 3ODJ; X-ray; 2.84 A; A=1-192. DR PDBsum; 2NR9; -. DR PDBsum; 3ODJ; -. DR ProteinModelPortal; P44783; -. DR SMR; P44783; 4-192. DR IntAct; P44783; 1. DR STRING; 71421.HI0618; -. DR MEROPS; S54.024; -. DR EnsemblBacteria; AAC22277; AAC22277; HI_0618. DR GeneID; 950685; -. DR KEGG; hin:HI0618; -. DR PATRIC; 20189819; VBIHaeInf48452_0642. DR eggNOG; ENOG4105EBW; Bacteria. DR eggNOG; COG0705; LUCA. DR KO; K02441; -. DR OMA; PEGFFTM; -. DR OrthoDB; EOG60SCRR; -. DR PhylomeDB; P44783; -. DR BRENDA; 3.4.21.105; 2529. DR EvolutionaryTrace; P44783; -. DR Proteomes; UP000000579; 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 1.20.1540.10; -; 1. DR InterPro; IPR002610; Peptidase_S54_rhomboid. DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom. DR PANTHER; PTHR22936; PTHR22936; 1. DR Pfam; PF01694; Rhomboid; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Protease; Reference proteome; Serine protease; KW Transmembrane; Transmembrane helix. FT CHAIN 1 192 Rhomboid protease GlpG. FT /FTId=PRO_0000087516. FT TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 11 31 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 32 57 Periplasmic. {ECO:0000255}. FT TRANSMEM 58 78 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 79 82 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 83 103 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 104 107 Periplasmic. {ECO:0000255}. FT TRANSMEM 108 128 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 129 141 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 142 162 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 163 163 Periplasmic. {ECO:0000255}. FT TRANSMEM 164 184 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 185 192 Cytoplasmic. {ECO:0000255}. FT ACT_SITE 116 116 Nucleophile. FT {ECO:0000269|PubMed:17210913}. FT ACT_SITE 169 169 {ECO:0000269|PubMed:17210913}. FT HELIX 10 27 {ECO:0000244|PDB:2NR9}. FT HELIX 31 38 {ECO:0000244|PDB:2NR9}. FT HELIX 44 48 {ECO:0000244|PDB:2NR9}. FT HELIX 52 55 {ECO:0000244|PDB:2NR9}. FT HELIX 56 58 {ECO:0000244|PDB:2NR9}. FT HELIX 63 84 {ECO:0000244|PDB:2NR9}. FT HELIX 86 108 {ECO:0000244|PDB:2NR9}. FT HELIX 116 131 {ECO:0000244|PDB:2NR9}. FT TURN 144 148 {ECO:0000244|PDB:2NR9}. FT TURN 150 152 {ECO:0000244|PDB:2NR9}. FT HELIX 153 156 {ECO:0000244|PDB:2NR9}. FT HELIX 166 191 {ECO:0000244|PDB:2NR9}. SQ SEQUENCE 192 AA; 21657 MW; B76A7A658037217E CRC64; MKNFLAQQGK ITLILTALCV LIYLAQQLGF EDDIMYLMHY PAYEEQDSEV WRYISHTLVH LSNLHILFNL SWFFIFGGMI ERTFGSVKLL MLYVVASAIT GYVQNYVSGP AFFGLSGVVY AVLGYVFIRD KLNHHLFDLP EGFFTMLLVG IALGFISPLF GVEMGNAAHI SGLIVGLIWG FIDSKLRKNS LE // ID GLPQ_HAEIN Reviewed; 364 AA. AC Q06282; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Glycerophosphoryl diester phosphodiesterase; DE Short=Glycerophosphodiester phosphodiesterase; DE EC=3.1.4.46; DE AltName: Full=Immunoglobulin D-binding protein; DE Short=IgD-binding protein; DE AltName: Full=Surface-exposed lipoprotein D; DE Short=Protein D; DE Flags: Precursor; GN Name=glpQ; Synonyms=hpd; OrderedLocusNames=HI_0689; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi 772; RX PubMed=1987023; RA Janson H., Heden L.-O., Grubb A., Ruan M., Forsgren A.; RT "Protein D, an immunoglobulin D-binding protein of Haemophilus RT influenzae: cloning, nucleotide sequence, and expression in RT Escherichia coli."; RL Infect. Immun. 59:119-125(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Minna / Serotype B; RX PubMed=8104899; RA Janson H., Ruan M., Forsgren A.; RT "Limited diversity of the protein D gene (hpd) among encapsulated and RT nonencapsulated Haemophilus influenzae strains."; RL Infect. Immun. 61:4546-4552(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=3639, 3640, 6-7626, Eagan / Serotype B, HK695 / Serotype B, and RC NCTC 8468 / Serotype B; RX PubMed=7822043; RA Song X.-M., Forsgren A., Janson H.; RT "The gene encoding protein D (hpd) is highly conserved among RT Haemophilus influenzae type b and nontypeable strains."; RL Infect. Immun. 63:696-699(1995). RN [5] RP CHARACTERIZATION, DIACYLGLYCEROL AT CYS-19, AND PALMITOYLATION AT RP CYS-19. RC STRAIN=NTHi 772; RX PubMed=1548059; RA Janson H., Heden L.-O., Forsgren A.; RT "Protein D, the immunoglobulin D-binding protein of Haemophilus RT influenzae, is a lipoprotein."; RL Infect. Immun. 60:1336-1342(1992). CC -!- FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes CC deacylated phospholipids to G3P and the corresponding alcohols. CC Has a specific affinity for human immunoglobulin D myeloma CC protein. CC -!- CATALYTIC ACTIVITY: A glycerophosphodiester + H(2)O = an alcohol + CC sn-glycerol 3-phosphate. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. CC -!- PTM: Contains both ester- and amide-linked fatty acids. CC -!- MISCELLANEOUS: The sequence shown is that of strains NTHI 772 and CC RD / KW20. CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester CC phosphodiesterase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GP-PDE 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; L42023; AAC22348.1; -; Genomic_DNA. DR EMBL; M37487; AAA24998.1; -; Genomic_DNA. DR EMBL; L12445; AAA24999.1; -; Genomic_DNA. DR EMBL; Z35656; CAA84715.1; -; Genomic_DNA. DR EMBL; Z35657; CAA84716.1; -; Genomic_DNA. DR EMBL; Z35658; CAA84717.1; -; Genomic_DNA. DR EMBL; Z35659; CAA84718.1; -; Genomic_DNA. DR EMBL; Z35660; CAA84719.1; -; Genomic_DNA. DR EMBL; Z35661; CAA84720.1; -; Genomic_DNA. DR PIR; G64086; G64086. DR PIR; S59931; S59931. DR PIR; S59932; S59932. DR PIR; S59933; S59933. DR PIR; S59934; S59934. DR PIR; S59936; S59936. DR RefSeq; NP_438849.1; NC_000907.1. DR RefSeq; WP_005694613.1; NC_000907.1. DR ProteinModelPortal; Q06282; -. DR SMR; Q06282; 33-360. DR STRING; 71421.HI0689; -. DR EnsemblBacteria; AAC22348; AAC22348; HI_0689. DR GeneID; 949981; -. DR KEGG; hin:HI0689; -. DR PATRIC; 20189997; VBIHaeInf48452_0720. DR eggNOG; ENOG4106MZZ; Bacteria. DR eggNOG; COG0584; LUCA. DR KO; K01126; -. DR OMA; GRFYAID; -. DR OrthoDB; EOG65N189; -. DR PhylomeDB; Q06282; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Calcium; Cell outer membrane; Complete proteome; Glycerol metabolism; KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 18 FT CHAIN 19 364 Glycerophosphoryl diester FT phosphodiesterase. FT /FTId=PRO_0000012595. FT DOMAIN 35 360 GP-PDE. FT METAL 67 67 Calcium. {ECO:0000250}. FT METAL 69 69 Calcium. {ECO:0000250}. FT METAL 175 175 Calcium. {ECO:0000250}. FT LIPID 19 19 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:1548059}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:1548059}. FT VARIANT 13 13 A -> T (in strain: NCTC 8468). FT VARIANT 16 16 L -> V (in strain: NCTC 8468). FT VARIANT 25 25 N -> S (in strain: NCTC 8468). FT VARIANT 28 28 N -> K (in strain: 6-7626). FT VARIANT 34 34 D -> H (in strain: NCTC 8468). FT VARIANT 62 62 H -> Q (in strain: Eagan, 3639, 3640, 6- FT 7626, HK695 and Minna). FT VARIANT 63 63 S -> A (in strain: Eagan, 3639, 3640, FT NCTC 8468, 6-7626, HK695 and Minna). FT VARIANT 98 98 Y -> H (in strain: Eagan, 3639, 3640, FT NCTC 8468, 6-7626, HK695 and Minna). FT VARIANT 99 99 R -> H (in strain: NCTC 8468). FT VARIANT 144 144 K -> Q (in strain: 6-7626). FT VARIANT 168 168 K -> R (in strain: 6-7626). FT VARIANT 191 191 T -> A (in strain: Eagan, 3639, 3640, FT NCTC 8468, 6-7626, HK695 and Minna). FT VARIANT 253 253 P -> S (in strain: 6-7626). FT VARIANT 310 310 Q -> K (in strain: 6-7626). FT VARIANT 327 327 E -> A (in strain: Eagan, 3639, NCTC FT 8468, 6-7626, HK695 and Minna). FT VARIANT 338 338 A -> V (in strain: Eagan, 3640, HK695 and FT Minna). FT VARIANT 364 364 K -> E (in strain: 6-7626). SQ SEQUENCE 364 AA; 41902 MW; A6079B3ABF70E820 CRC64; MKLKTLALSL LAAGVLAGCS SHSSNMANTQ MKSDKIIIAH RGASGYLPEH TLESKALAFA QHSDYLEQDL AMTKDGRLVV IHDHFLDGLT DVAKKFPYRH RKDGRYYVID FTLKEIQSLE MTENFETKDG KQAQVYPNRF PLWKSHFRIH TFEDEIEFIQ GLEKSTGKKV GIYPEIKAPW FHHQNGKDIA TETLKVLKKY GYDKKTDMVY LQTFDFNELK RIKTELLPQM GMDLKLVQLI AYTDWKETQE KDPKGYWVNY NYDWMFKPGA MAEVVKYADG VGPGWYMLVN KEESKPDNIV YTPLVKELAQ YNVEVHPYTV RKDALPEFFT DVNQMYDALL NKSGATGVFT DFPDTGVEFL KGIK // ID GLPX_HAEIN Reviewed; 333 AA. AC P44811; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Fructose-1,6-bisphosphatase class 2; DE Short=FBPase class 2; DE EC=3.1.3.11; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2; GN Name=glpX; OrderedLocusNames=HI_0667; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to CC fructose 6-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FBPase class 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; L42023; AAC22322.1; -; Genomic_DNA. DR PIR; B64085; B64085. DR RefSeq; NP_438827.1; NC_000907.1. DR RefSeq; WP_005694623.1; NC_000907.1. DR ProteinModelPortal; P44811; -. DR STRING; 71421.HI0667; -. DR EnsemblBacteria; AAC22322; AAC22322; HI_0667. DR GeneID; 949705; -. DR KEGG; hin:HI0667; -. DR PATRIC; 20189951; VBIHaeInf48452_0697. DR eggNOG; ENOG4105CBT; Bacteria. DR eggNOG; COG1494; LUCA. DR KO; K02446; -. DR OMA; VIQGRLW; -. DR OrthoDB; EOG6R87CH; -. DR PhylomeDB; P44811; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro. DR InterPro; IPR004464; FBPase_class-2/SBPase. DR Pfam; PF03320; FBPase_glpX; 1. DR PIRSF; PIRSF004532; GlpX; 1. DR TIGRFAMs; TIGR00330; glpX; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase; KW Manganese; Metal-binding; Reference proteome. FT CHAIN 1 333 Fructose-1,6-bisphosphatase class 2. FT /FTId=PRO_0000201102. FT REGION 88 90 Substrate binding. {ECO:0000250}. FT REGION 164 166 Substrate binding. {ECO:0000250}. FT REGION 186 188 Substrate binding. {ECO:0000250}. FT METAL 33 33 Manganese 1. {ECO:0000250}. FT METAL 57 57 Manganese 1. {ECO:0000250}. FT METAL 85 85 Manganese 2. {ECO:0000250}. FT METAL 88 88 Manganese 2. {ECO:0000250}. FT METAL 213 213 Manganese 2. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000250}. FT BINDING 210 210 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 333 AA; 35534 MW; 510C21BEBF853D99 CRC64; MNRALAIEFS RVTEAAALAA YTWLGRGDKN AADDAAVKAM RYMLNLIHMD AEIVIGEGEI DEAPMLYVGE KVGSGLGELV SIAVDPIDGT HMTAMGQSNA ISVLAAGGKN TFLKAPDMYM EKLVVGSNVK GIIDLNLPLE QNLRRIASKL GKSLSDLTVM VLAKPRHDAV IKQIHNLGAK VLAIPDGDVA GSVLCCLPDA EVDLLYGIGG APEGVAAAAA IRALGGDMQA RLIPRNEVKS DTEENKKIAA NEIQRCAALG VKVNEVLKLE DLVRDDNLVF TATGITNGDL LKGISRKGNL ASTETILIRG KSRTIRKIQS IHYLDDLYKI LNI // ID GPDA_HAEIN Reviewed; 335 AA. AC P43798; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; GN OrderedLocusNames=HI_0605; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) = CC glycerone phosphate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22264.1; -; Genomic_DNA. DR PIR; F64080; F64080. DR RefSeq; NP_438763.1; NC_000907.1. DR RefSeq; WP_005694541.1; NC_000907.1. DR ProteinModelPortal; P43798; -. DR STRING; 71421.HI0605; -. DR EnsemblBacteria; AAC22264; AAC22264; HI_0605. DR GeneID; 949436; -. DR KEGG; hin:HI0605; -. DR PATRIC; 20189789; VBIHaeInf48452_0629. DR eggNOG; ENOG4105CSF; Bacteria. DR eggNOG; COG0240; LUCA. DR KO; K00057; -. DR OMA; RNHTAGR; -. DR OrthoDB; EOG6JDWF4; -. DR PhylomeDB; P43798; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC. DR GO; GO:0036439; F:glycerol-3-phosphate dehydrogenase [NADP+] activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW NAD; Oxidoreductase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome. FT CHAIN 1 335 Glycerol-3-phosphate dehydrogenase FT [NAD(P)+]. FT /FTId=PRO_0000137969. FT NP_BIND 12 17 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. FT REGION 259 260 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT ACT_SITE 195 195 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT BINDING 110 110 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 110 110 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00394}. FT BINDING 143 143 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 259 259 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. FT BINDING 285 285 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}. SQ SEQUENCE 335 AA; 36394 MW; 4913F8F2203B7CFC CRC64; MITSQTPITV LGAGSYGTAL AITFSRNGSP THLWGHNPAH IAQMQTERQN YRFLPDVIFP EDLHLESNLA QAMEYSQDIL IVVPSHAFGE ILIKIKPHLK AHHRLIWATK GLERNTGRLL QTVVEEQLGT QYPLAVLSGP TFAKELAQGL PSAITLAANN EQFAREFQSR IHCSKGFRVY INSDMTGVQL GGAIKNVIAI GAGISDGMGF GANARTALIT RGIAEITRLG ISLGANTNTF MGMSGLGDLV LTCTDNQSRN RRFGLMLGKG LDAQMAMENI GQVVEGFYNT KEAYLLAQRQ GVEMPITEQI YQMLFCGKSA QDVAISLLGR ACKGE // ID GLGA_HAEIN Reviewed; 476 AA. AC P45179; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Glycogen synthase; DE EC=2.4.1.21; DE AltName: Full=Starch [bacterial glycogen] synthase; GN Name=glgA; OrderedLocusNames=HI_1360; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP CC + (1,4-alpha-D-glucosyl)(n+1). CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. CC Bacterial/plant glycogen synthase 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; L42023; AAC23007.1; -; Genomic_DNA. DR PIR; C64119; C64119. DR RefSeq; NP_439511.1; NC_000907.1. DR RefSeq; WP_010869192.1; NC_000907.1. DR ProteinModelPortal; P45179; -. DR STRING; 71421.HI1360; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR DNASU; 950277; -. DR EnsemblBacteria; AAC23007; AAC23007; HI_1360. DR GeneID; 950277; -. DR KEGG; hin:HI1360; -. DR PATRIC; 20191405; VBIHaeInf48452_1413. DR eggNOG; ENOG4105CXW; Bacteria. DR eggNOG; COG0297; LUCA. DR KO; K00703; -. DR OMA; LLNAMRC; -. DR OrthoDB; EOG6JTC6Z; -. DR PhylomeDB; P45179; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro. DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00484; Glycogen_synth; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR011835; GS/SS. DR InterPro; IPR013534; Starch_synth_cat_dom. DR Pfam; PF08323; Glyco_transf_5; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR TIGRFAMs; TIGR02095; glgA; 1. PE 3: Inferred from homology; KW Complete proteome; Glycogen biosynthesis; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 476 Glycogen synthase. FT /FTId=PRO_0000188620. FT BINDING 15 15 ADP-glucose. {ECO:0000250}. SQ SEQUENCE 476 AA; 52975 MW; E4060E820E5D768D CRC64; MKILHVCSEL YPLLKTGGLA DVLGALPQAQ NQIGLDARFL LPAYPAITTG IPNTQVVAEF DNFAGHVVLR YGEYNGVGIY LIDAPHLYGR EGNPYHDAYY NDYGDNYKRF ALLGWVGAEL ATGLDSWWRA EVVHAHDWHA GLCVAYLFNK GKPAKSVFTI HNLAYQGQFS YHHLYEIGLP TGMFHVEGLE LFGQISYLKS GLFYSDASTA VSPTYAQEIT TPEFAYGLQG LLSGLKAQGR LVGILNGVDE NIWHPNVDQY IPHHYKLKYM AGKKKNKAEL QAYFNLPQDE SALAFVMVTR LTEQKGVDLL IESADEIVKQ GGQLMILGSG APHLEQGIRE LAERYPQNIA VKIGYDEALS HLMVAGGDVI LVPSRFEPCG LTQLYGLQYG TLPLVRKTGG LADTVVDSTS ESIKARTATG FVFESATPEA LRHCLQRAFA LWQKPRAWAM VRTDAMEQDF SWRKAAEQYR TLYERL // ID GLMU_HAEIN Reviewed; 456 AA. AC P43889; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 120. DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631}; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631}; DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631}; GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; GN OrderedLocusNames=HI_0642; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS, FUNCTION, MUTAGENESIS OF LYS-25; GLN-76; TYR-103; ASP-105; RP VAL-223 AND GLU-224, REACTION MECHANISM, AND SUBUNIT. RX PubMed=18029420; DOI=10.1110/ps.073135107; RA Mochalkin I., Lightle S., Zhu Y., Ohren J.F., Spessard C., RA Chirgadze N.Y., Banotai C., Melnick M., McDowell L.; RT "Characterization of substrate binding and catalysis in the potential RT antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase RT (GlmU)."; RL Protein Sci. 16:2657-2666(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS, AND SUBUNIT. RX PubMed=18218712; DOI=10.1110/ps.073271408; RA Mochalkin I., Lightle S., Narasimhan L., Bornemeier D., Melnick M., RA Vanderroest S., McDowell L.; RT "Structure of a small-molecule inhibitor complexed with GlmU from RT Haemophilus influenzae reveals an allosteric binding site."; RL Protein Sci. 17:577-582(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS. RA Melnick M., Mochalkin I., Lightle S., Narasimhan L., Mcdowell L., RA Sarver R.; RT "Discovery and initial sar of quinazoline inhibitors of GlmU from RT Haemophilus influenzae."; RL Submitted (OCT-2008) to the PDB data bank. RN [5] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOG. RX PubMed=22721802; DOI=10.1042/BJ20120596; RA Larsen N.A., Nash T.J., Morningstar M., Shapiro A.B., Joubran C., RA Blackett C.J., Patten A.D., Boriack-Sjodin P.A., Doig P.; RT "An aminoquinazoline inhibitor of the essential bacterial cell wall RT synthetic enzyme GlmU has a unique non-protein-kinase-like binding RT mode."; RL Biochem. J. 446:405-413(2012). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS. RX PubMed=25262942; DOI=10.1016/j.bmc.2014.08.017; RA Doig P., Boriack-Sjodin P.A., Dumas J., Hu J., Itoh K., Johnson K., RA Kazmirski S., Kinoshita T., Kuroda S., Sato T.O., Sugimoto K., RA Tohyama K., Aoi H., Wakamatsu K., Wang H.; RT "Rational design of inhibitors of the bacterial cell wall synthetic RT enzyme GlmU using virtual screening and lead-hopping."; RL Bioorg. Med. Chem. 22:6256-6269(2014). CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de CC novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- CC GlcNAc). The C-terminal domain catalyzes the transfer of acetyl CC group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) CC to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is CC converted into UDP-GlcNAc by the transfer of uridine 5- CC monophosphate (from uridine 5-triphosphate), a reaction catalyzed CC by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631, CC ECO:0000269|PubMed:18029420}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01631}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631, CC ECO:0000269|PubMed:18029420, ECO:0000269|PubMed:18218712, CC ECO:0000269|Ref.4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631, 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; L42023; AAC22302.1; -; Genomic_DNA. DR PIR; G64083; G64083. DR RefSeq; NP_438802.1; NC_000907.1. DR RefSeq; WP_005694502.1; NC_000907.1. DR PDB; 2V0H; X-ray; 1.79 A; A=1-456. DR PDB; 2V0I; X-ray; 1.89 A; A=1-456. DR PDB; 2V0J; X-ray; 2.00 A; A=1-456. DR PDB; 2V0K; X-ray; 2.30 A; A=1-456. DR PDB; 2V0L; X-ray; 2.20 A; A=1-456. DR PDB; 2VD4; X-ray; 1.90 A; A=1-456. DR PDB; 2W0V; X-ray; 1.99 A; A=1-456. DR PDB; 2W0W; X-ray; 2.59 A; A=1-456. DR PDB; 4E1K; X-ray; 2.00 A; A=1-456. DR PDB; 4KNR; X-ray; 2.10 A; A=1-456. DR PDB; 4KNX; X-ray; 1.90 A; A=1-456. DR PDB; 4KPX; X-ray; 2.21 A; A=1-456. DR PDB; 4KPZ; X-ray; 2.09 A; A=1-456. DR PDB; 4KQL; X-ray; 2.31 A; A=1-456. DR PDBsum; 2V0H; -. DR PDBsum; 2V0I; -. DR PDBsum; 2V0J; -. DR PDBsum; 2V0K; -. DR PDBsum; 2V0L; -. DR PDBsum; 2VD4; -. DR PDBsum; 2W0V; -. DR PDBsum; 2W0W; -. DR PDBsum; 4E1K; -. DR PDBsum; 4KNR; -. DR PDBsum; 4KNX; -. DR PDBsum; 4KPX; -. DR PDBsum; 4KPZ; -. DR PDBsum; 4KQL; -. DR ProteinModelPortal; P43889; -. DR SMR; P43889; 4-453. DR STRING; 71421.HI0642; -. DR BindingDB; P43889; -. DR EnsemblBacteria; AAC22302; AAC22302; HI_0642. DR GeneID; 949691; -. DR KEGG; hin:HI0642; -. DR PATRIC; 20189891; VBIHaeInf48452_0670. DR eggNOG; ENOG4105CAJ; Bacteria. DR eggNOG; COG1207; LUCA. DR KO; K04042; -. DR OMA; SITANYD; -. DR OrthoDB; EOG6Z6FQZ; -. DR PhylomeDB; P43889; -. DR BRENDA; 2.7.7.23; 2529. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR EvolutionaryTrace; P43889; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_01631; GlmU; 1. DR InterPro; IPR005882; Bifunctional_GlmU. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01173; glmU; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Magnesium; Metal-binding; Multifunctional enzyme; KW Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome; KW Repeat; Transferase. FT CHAIN 1 456 Bifunctional protein GlmU. FT /FTId=PRO_0000068703. FT REGION 1 229 Pyrophosphorylase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 11 14 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:18029420, FT ECO:0000269|PubMed:22721802, FT ECO:0000269|PubMed:25262942}. FT REGION 81 82 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:18029420, FT ECO:0000269|PubMed:25262942}. FT REGION 103 105 UDP-GlcNAc binding. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:18029420, FT ECO:0000269|PubMed:22721802, FT ECO:0000269|PubMed:25262942}. FT REGION 230 250 Linker. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 251 456 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT REGION 386 387 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT ACT_SITE 363 363 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 105 105 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT METAL 227 227 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 25 25 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 76 76 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:25262942}. FT BINDING 140 140 UDP-GlcNAc; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631, FT ECO:0000269|PubMed:18029420}. FT BINDING 154 154 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:18029420}. FT BINDING 169 169 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631, FT ECO:0000269|PubMed:18029420}. FT BINDING 227 227 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 333 333 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 351 351 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 366 366 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 377 377 UDP-GlcNAc. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 380 380 Acetyl-CoA; via amide nitrogen. FT {ECO:0000250|UniProtKB:P0ACC7, FT ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 405 405 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT BINDING 423 423 Acetyl-CoA; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01631}. FT BINDING 440 440 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01631}. FT MUTAGEN 25 25 K->A: No pyrophosphorylase activity. FT {ECO:0000269|PubMed:18029420}. FT MUTAGEN 76 76 Q->A: No pyrophosphorylase activity. FT {ECO:0000269|PubMed:18029420}. FT MUTAGEN 103 103 Y->A: Reduces the pyrophosphorylase FT activity. {ECO:0000269|PubMed:18029420}. FT MUTAGEN 105 105 D->A: No pyrophosphorylase activity. FT {ECO:0000269|PubMed:18029420}. FT MUTAGEN 223 223 V->A: Reduces slightly the FT pyrophosphorylase activity. FT {ECO:0000269|PubMed:18029420}. FT MUTAGEN 224 224 E->A: Reduces the pyrophosphorylase FT activity. {ECO:0000269|PubMed:18029420}. FT STRAND 6 11 {ECO:0000244|PDB:2V0H}. FT HELIX 17 19 {ECO:0000244|PDB:2V0H}. FT STRAND 21 23 {ECO:0000244|PDB:2V0H}. FT HELIX 25 27 {ECO:0000244|PDB:2V0H}. FT STRAND 28 30 {ECO:0000244|PDB:2V0H}. FT HELIX 35 45 {ECO:0000244|PDB:2V0H}. FT STRAND 51 55 {ECO:0000244|PDB:2V0H}. FT HELIX 59 65 {ECO:0000244|PDB:2V0H}. FT TURN 66 68 {ECO:0000244|PDB:2V0H}. FT STRAND 72 75 {ECO:0000244|PDB:2V0H}. FT HELIX 82 89 {ECO:0000244|PDB:2V0H}. FT HELIX 90 92 {ECO:0000244|PDB:2V0H}. FT STRAND 97 103 {ECO:0000244|PDB:2V0H}. FT HELIX 111 120 {ECO:0000244|PDB:2V0H}. FT STRAND 125 132 {ECO:0000244|PDB:2V0H}. FT STRAND 141 145 {ECO:0000244|PDB:2V0H}. FT STRAND 148 153 {ECO:0000244|PDB:2V0H}. FT TURN 155 157 {ECO:0000244|PDB:2V0H}. FT HELIX 160 163 {ECO:0000244|PDB:2V0H}. FT STRAND 167 176 {ECO:0000244|PDB:2V0H}. FT HELIX 177 184 {ECO:0000244|PDB:2V0H}. FT HELIX 198 200 {ECO:0000244|PDB:2V0H}. FT HELIX 201 207 {ECO:0000244|PDB:2V0H}. FT STRAND 212 216 {ECO:0000244|PDB:2V0H}. FT HELIX 221 223 {ECO:0000244|PDB:2V0H}. FT HELIX 229 249 {ECO:0000244|PDB:2V0H}. FT STRAND 253 255 {ECO:0000244|PDB:2V0H}. FT HELIX 257 259 {ECO:0000244|PDB:2V0H}. FT STRAND 260 268 {ECO:0000244|PDB:2V0H}. FT STRAND 276 286 {ECO:0000244|PDB:2V0H}. FT STRAND 297 303 {ECO:0000244|PDB:2V0H}. FT STRAND 314 320 {ECO:0000244|PDB:2V0H}. FT STRAND 328 332 {ECO:0000244|PDB:2V0H}. FT STRAND 336 338 {ECO:0000244|PDB:2W0W}. FT STRAND 343 352 {ECO:0000244|PDB:2V0H}. FT STRAND 360 372 {ECO:0000244|PDB:2V0H}. FT STRAND 383 386 {ECO:0000244|PDB:2V0H}. FT STRAND 388 391 {ECO:0000244|PDB:2V0H}. FT STRAND 395 397 {ECO:0000244|PDB:2V0H}. FT STRAND 408 415 {ECO:0000244|PDB:2V0H}. SQ SEQUENCE 456 AA; 49287 MW; 93B76552A8F9BD36 CRC64; MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN IHLIYGHGGD LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV VLYGDAPLIT KETLEKLIEA KPENGIALLT VNLDNPTGYG RIIRENGNVV AIVEQKDANA EQLNIKEVNT GVMVSDGASF KKWLARVGNN NAQGEYYLTD LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ NKQASKLLLE GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI KKSTVGKGSK VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD VFVGSDTQLV APVKVANGAT IGAGTTITRD VGENELVITR VAQRHIQGWQ RPIKKK // ID GLNB_HAEIN Reviewed; 112 AA. AC P43795; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Nitrogen regulatory protein P-II; GN Name=glnB; OrderedLocusNames=HI_0337; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: P-II indirectly controls the transcription of the CC glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed CC conversion of NR-I to NR-I-phosphate, the transcriptional CC activator of GlnA. When P-II is uridylylated to P-II-UMP, these CC events are reversed. When the ratio of Gln to 2-ketoglutarate CC decreases, P-II is uridylylated to P-II-UMP, which causes the CC deadenylation of glutamine synthetase by GlnE, so activating the CC enzyme (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- PTM: Uridylylated/deuridylylated by GlnD. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the P(II) protein family. CC {ECO:0000255|PROSITE-ProRule:PRU00675}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21999.1; -; Genomic_DNA. DR PIR; F64062; F64062. DR RefSeq; NP_438501.1; NC_000907.1. DR RefSeq; WP_005654045.1; NC_000907.1. DR ProteinModelPortal; P43795; -. DR SMR; P43795; 1-112. DR STRING; 71421.HI0337; -. DR PRIDE; P43795; -. DR EnsemblBacteria; AAC21999; AAC21999; HI_0337. DR GeneID; 949445; -. DR KEGG; hin:HI0337; -. DR PATRIC; 20189217; VBIHaeInf48452_0354. DR eggNOG; ENOG4108YZA; Bacteria. DR eggNOG; COG0347; LUCA. DR KO; K04751; -. DR OMA; AIEVKGF; -. DR OrthoDB; EOG69GZGV; -. DR PhylomeDB; P43795; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR002187; N-reg_PII. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR InterPro; IPR017918; N-reg_PII_CS. DR InterPro; IPR002332; N-reg_PII_urydylation_site. DR Pfam; PF00543; P-II; 1. DR PIRSF; PIRSF039144; GlnB; 1. DR PRINTS; PR00340; PIIGLNB. DR SMART; SM00938; P-II; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR PROSITE; PS00638; PII_GLNB_CTER; 1. DR PROSITE; PS51343; PII_GLNB_DOM; 1. DR PROSITE; PS00496; PII_GLNB_UMP; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 112 Nitrogen regulatory protein P-II. FT /FTId=PRO_0000139777. FT MOD_RES 51 51 O-UMP-tyrosine. {ECO:0000255|PROSITE- FT ProRule:PRU00675}. SQ SEQUENCE 112 AA; 12641 MW; B8CD67EFA9381D61 CRC64; MKKIEAMIKP FKLDDVRESL SDIGISGMTI TEVRGFGRQK GHTELYRGAE YMVDFLPKVK LEVVVPDELV DQCIEAIIET AQTGKIGDGK IFVYHVERAI RIRTGEENED AI // ID GLPA_HAEIN Reviewed; 563 AA. AC P43799; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit A; DE Short=G-3-P dehydrogenase; DE EC=1.1.5.3; GN Name=glpA; OrderedLocusNames=HI_0685; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone = CC glycerone phosphate + a quinol. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (anaerobic route): step 1/1. CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane CC bound GlpC. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Note=Loosely bound to CC the cytoplasmic membrane often occurring in vesicles associated CC with fumarate reductase. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-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; L42023; AAC22345.1; -; Genomic_DNA. DR PIR; E64086; E64086. DR RefSeq; NP_438845.1; NC_000907.1. DR RefSeq; WP_005694610.1; NC_000907.1. DR ProteinModelPortal; P43799; -. DR STRING; 71421.HI0685; -. DR EnsemblBacteria; AAC22345; AAC22345; HI_0685. DR GeneID; 949605; -. DR KEGG; hin:HI0685; -. DR PATRIC; 20189989; VBIHaeInf48452_0716. DR eggNOG; ENOG4107R5Y; Bacteria. DR eggNOG; COG0578; LUCA. DR KO; K00111; -. DR OMA; MGHRINK; -. DR OrthoDB; EOG651SR7; -. DR PhylomeDB; P43799; -. DR UniPathway; UPA00618; UER00673. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR InterPro; IPR017752; G3P_DH_GlpA_su. DR Pfam; PF01266; DAO; 1. DR Pfam; PF04324; Fer2_BFD; 1. DR PRINTS; PR01001; FADG3PDH. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR03377; glycerol3P_GlpA; 1. DR PROSITE; PS00977; FAD_G3PDH_1; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; FAD; KW Flavoprotein; Membrane; Oxidoreductase; Reference proteome. FT CHAIN 1 563 Anaerobic glycerol-3-phosphate FT dehydrogenase subunit A. FT /FTId=PRO_0000126095. FT NP_BIND 20 48 FAD. {ECO:0000255}. SQ SEQUENCE 563 AA; 61920 MW; 7E662A80F4E1EED6 CRC64; MGLSPSIYKD VGDLSSLSTD VIIIGGGATG AGIARDCALR GIDCILLERR DIATGATGRN HGLLHSGARY AVNDQESAEE CIKENRILRK IARHCVDETE GLFITLPEDS LDYQKTFLES CAKSGIDAQA IDPELAKIME PSVNPDLVGA VVVPDGSIDP FRLTASNMMD ATENGAKMFT YCEVKNLIRE GGKVIGVNAY DHKNRRERQF FAPLVVNAGG IWGQGIAEYA DLKIKMFPAK GALLVMGHRI NKLVINRCRK PADADILVPG DTICVIGTTS SRIPYDQIDN MEVTPEEVDI LFREGEKLAP SLRHTRVLRA YAGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI TGGKLMTYRL MAEWATDLVC KKLNKTARCV TAEQPLPGST ESRQETNQKV ISLPSTIRYS AVYRHGSRAT RLLEKERLDR SMVCECEAVT AGEVRYAVDE LDVNNLVDLR RRSRVGMGTC QAELCACRAA GLMNRFEVAT PRQSTTQLSA FMEERWRGIE PIAWGEAIRE AEFTSWMYAS VLGLNDVKPL DEQAQQGTDS NEF // ID GLPR_HAEIN Reviewed; 255 AA. AC P44784; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Glycerol-3-phosphate regulon repressor; GN Name=glpR; OrderedLocusNames=HI_0619; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Repressor of the glycerol-3-phosphate regulon. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH deoR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00349}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22278.1; -; Genomic_DNA. DR PIR; A64082; A64082. DR RefSeq; NP_438777.1; NC_000907.1. DR RefSeq; WP_005661561.1; NC_000907.1. DR ProteinModelPortal; P44784; -. DR STRING; 71421.HI0619; -. DR EnsemblBacteria; AAC22278; AAC22278; HI_0619. DR GeneID; 950682; -. DR KEGG; hin:HI0619; -. DR PATRIC; 20189821; VBIHaeInf48452_0643. DR eggNOG; ENOG4105E98; Bacteria. DR eggNOG; COG1349; LUCA. DR KO; K02444; -. DR OMA; QIPDHAS; -. DR OrthoDB; EOG6XSZXW; -. DR PhylomeDB; P44784; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014036; DeoR_C. DR InterPro; IPR001034; DeoR_HTH. DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00455; DeoRC; 1. DR Pfam; PF08220; HTH_DeoR; 1. DR PRINTS; PR00037; HTHLACR. DR SMART; SM00420; HTH_DEOR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00894; HTH_DEOR_1; 1. DR PROSITE; PS51000; HTH_DEOR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Glycerol metabolism; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 255 Glycerol-3-phosphate regulon repressor. FT /FTId=PRO_0000050253. FT DOMAIN 3 58 HTH deoR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. FT DNA_BIND 20 39 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. SQ SEQUENCE 255 AA; 28183 MW; EBBE589307BC3AB3 CRC64; MKQSLRHQKI IKLVEQSGYL STEELVAALD VSPQTIRRDL NILAELDLIR RHHGGAASPS SAENSDYVDR KQFFSLQKNN IAQEVAKLIP NGASLFIDIG TTPEAVANAL LGHEKLRIVT NNLNAAHLLR QNESFDIVMA GGSLRMDGGI IGEATVNFIS QFRLDFGILG ISAIDADGSL LDYDYHEVQV KRAIIESSRQ TLLVADHSKF TRQAIVRLGE LSDVEYLFTG DVPEGIVNYL KEQKTKLVLC NGKVR // ID GLMS_HAEIN Reviewed; 610 AA. AC P44708; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 118. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164}; DE EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164}; GN Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; GN OrderedLocusNames=HI_0429; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, CC converting fructose-6P into glucosamine-6P using glutamine as a CC nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|HAMAP- CC Rule:MF_00164}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22088.1; -; Genomic_DNA. DR PIR; D64067; D64067. DR RefSeq; NP_438590.1; NC_000907.1. DR RefSeq; WP_010868986.1; NC_000907.1. DR ProteinModelPortal; P44708; -. DR SMR; P44708; 2-610. DR STRING; 71421.HI0429; -. DR MEROPS; C44.971; -. DR PRIDE; P44708; -. DR EnsemblBacteria; AAC22088; AAC22088; HI_0429. DR GeneID; 950659; -. DR KEGG; hin:HI0429; -. DR PATRIC; 20189411; VBIHaeInf48452_0449. DR eggNOG; ENOG4105C46; Bacteria. DR eggNOG; COG0449; LUCA. DR KO; K00820; -. DR OMA; GEFFCAS; -. DR OrthoDB; EOG6KT2Q1; -. DR PhylomeDB; P44708; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00164; GlmS; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS. DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01135; glmS; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS51464; SIS; 2. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Reference proteome; Repeat; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000255|HAMAP- FT Rule:MF_00164}. FT CHAIN 2 610 Glutamine--fructose-6-phosphate FT aminotransferase [isomerizing]. FT /FTId=PRO_0000135339. FT DOMAIN 2 218 Glutamine amidotransferase type-2. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 278 426 SIS 1. {ECO:0000255|HAMAP-Rule:MF_00164}. FT DOMAIN 459 600 SIS 2. {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 2 2 Nucleophile; for GATase activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. FT ACT_SITE 605 605 For Fru-6P isomerization activity. FT {ECO:0000255|HAMAP-Rule:MF_00164}. SQ SEQUENCE 610 AA; 66832 MW; AAEE87EF0B4E6D3F CRC64; MCGIVGAVAQ RDVAEILING LHRLEYRGYD SAGVAVINKQ NELQRIRCLG KVKALDEAVS EKPLIGGTGI AHTRWATHGE PSETNAHPHS SGTFAVVHNG IIENHEELRE LLKSRGYVFL SQTDTEVIAH LVEWEMRTTD SLLDAVKKAV KQLTGAYGMV VMDSRHPEHL VAARSGSPLV IGLGIGENFL ASDQLALLSV TRRFIFLEEG DIAEITRRTV DIYDTHGNKA KREIHESNLE NDAAEKGKFR HFMQKEIYEQ PTALINTMEG RINHENVIVD SIGNGAKGIL EKVEHIQIVA CGTSYNAGMV ARYWFESLAG VSCDVEIASE FRYRKFVTRP NSLLITLSQS GETADTLAAL RLAKEKGYMA ALTICNVAGS SLVRESDLAF MTRAGVEVGV ASTKAFTTQL AALLMLVTAL GKVKGHISVE KEREIIKAMQ SLPAEIEKAL AFDTEIEALA EDFAEKHHAL FLGRGAFYPI AVEASLKLKE ISYIHAEAYA AGELKHGPLA LIDADMPVIV VAPNNELLEK VKSNIEEVRA RGGQLYVFAD KEAGFTPSEG MKIITMPKVN DIVAPIFYTI PMQLLSYYVA LIKGTDVDQP RNLAKSVTVE // ID GLPB_HAEIN Reviewed; 432 AA. AC P43800; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B; DE Short=Anaerobic G-3-P dehydrogenase subunit B; DE Short=Anaerobic G3Pdhase B; DE EC=1.1.5.3; GN Name=glpB; OrderedLocusNames=HI_0684; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. CC Uses fumarate or nitrate as electron acceptor (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone = CC glycerone phosphate + a quinol. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (anaerobic route): step 1/1. CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane CC bound GlpC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B 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; L42023; AAC22344.1; -; Genomic_DNA. DR RefSeq; NP_438844.1; NC_000907.1. DR RefSeq; WP_005694609.1; NC_000907.1. DR ProteinModelPortal; P43800; -. DR STRING; 71421.HI0684; -. DR DNASU; 950690; -. DR EnsemblBacteria; AAC22344; AAC22344; HI_0684. DR GeneID; 950690; -. DR KEGG; hin:HI0684; -. DR PATRIC; 20189987; VBIHaeInf48452_0715. DR eggNOG; ENOG4108KJ0; Bacteria. DR eggNOG; COG3075; LUCA. DR KO; K00112; -. DR OMA; VAINAQC; -. DR OrthoDB; EOG6K6V62; -. DR PhylomeDB; P43800; -. DR UniPathway; UPA00618; UER00673. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 2. DR HAMAP; MF_00753; Glycerol3P_GlpB; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR009158; G3P_DH_GlpB_su. DR Pfam; PF00890; FAD_binding_2; 1. DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1. DR SUPFAM; SSF51905; SSF51905; 4. DR TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Reference proteome. FT CHAIN 1 432 Anaerobic glycerol-3-phosphate FT dehydrogenase subunit B. FT /FTId=PRO_0000204563. SQ SEQUENCE 432 AA; 47251 MW; 6D99EEAC75549228 CRC64; MNFDVAIIGG GLAGLTCAIA LQQRGKRCVI INNGQAAIDF ASGSLDLLSR MPSTTYGENR AVENLKENIT ALRNELPAHP YSLLGAEKVL AKAQDFERLA NELHLDLIGS TEKNHWRVTG LGSLRGAWLS PNSVPTVQGN EPFPHKRIAV LGIEGYHDFQ PQLLAANLVL NPQFEHCEVT SGFLNIPQLD ELRKNAREFR SVNISQLLEH KLAFKDLVKE IIESAQGAEA VFLPACFGLE NQEFMTALRD ATKLALFELP TLPPSLLGMR QRIQLRHKFE SLGGLMINGD SALNATFEGN QVRCINTRLL EDEEITADNF VLASGSFFSK GLISEFDKIY EPVFESDIIG VEGFNNKDRF TWTAHRFAHP QPYQSAGVAI NAQCQVKKCG QFLTNLYAVG NVIGGFNALE LGCGSGVAVV TALAVADEIL AK // ID GREA_HAEIN Reviewed; 158 AA. AC P43881; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Transcription elongation factor GreA; DE AltName: Full=Transcript cleavage factor GreA; GN Name=greA; OrderedLocusNames=HI_1331; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GreA/GreB 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; L42023; AAC22976.1; -; Genomic_DNA. DR PIR; B64117; B64117. DR RefSeq; NP_439483.1; NC_000907.1. DR RefSeq; WP_005694444.1; NC_000907.1. DR ProteinModelPortal; P43881; -. DR SMR; P43881; 2-137. DR STRING; 71421.HI1331; -. DR PRIDE; P43881; -. DR EnsemblBacteria; AAC22976; AAC22976; HI_1331. DR GeneID; 950254; -. DR KEGG; hin:HI1331; -. DR PATRIC; 20191347; VBIHaeInf48452_1384. DR eggNOG; ENOG4108UKH; Bacteria. DR eggNOG; COG0782; LUCA. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR PhylomeDB; P43881; -. DR Proteomes; UP000000579; 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 Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 158 Transcription elongation factor GreA. FT /FTId=PRO_0000176928. SQ SEQUENCE 158 AA; 17478 MW; 847FDCD18B01F012 CRC64; MQQIPMTVRG AEQLREELDF LKNVRRPEII KAIAEAREHG DLKENAEYHA AREQQGFCEG RIQEIEGKLG NAQIIDVSKM PNNGKVIFGA TVVLVNTNTD EEVTYRIVGD DEADIKSGLI SVNSPIARGL IGKELDDTVN ITTPGGVVEF DIIEVNYI // ID GLPC_HAEIN Reviewed; 426 AA. AC P43801; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit C; DE Short=G-3-P dehydrogenase; GN Name=glpC; OrderedLocusNames=HI_0683; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Electron transfer protein; may also function as the CC membrane anchor for the GlpAB dimer. {ECO:0000250}. CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (anaerobic route): step 1/1. CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of GlpC. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Note=Loosely bound to CC the cytoplasmic membrane often occurring in vesicles associated CC with fumarate reductase. {ECO:0000250}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22343.1; -; Genomic_DNA. DR PIR; C64086; C64086. DR RefSeq; NP_438843.1; NC_000907.1. DR RefSeq; WP_005694608.1; NC_000907.1. DR ProteinModelPortal; P43801; -. DR STRING; 71421.HI0683; -. DR PRIDE; P43801; -. DR EnsemblBacteria; AAC22343; AAC22343; HI_0683. DR GeneID; 949971; -. DR KEGG; hin:HI0683; -. DR PATRIC; 20189985; VBIHaeInf48452_0714. DR eggNOG; ENOG4105CHG; Bacteria. DR eggNOG; COG0247; LUCA. DR KO; K00113; -. DR OMA; KEMPDNC; -. DR OrthoDB; EOG6W45NM; -. DR PhylomeDB; P43801; -. DR UniPathway; UPA00618; UER00673. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004017; Cys_rich_dom. DR InterPro; IPR017753; G3P_DH_GlpC_su. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF02754; CCG; 2. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR03379; glycerol3P_GlpC; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 426 Anaerobic glycerol-3-phosphate FT dehydrogenase subunit C. FT /FTId=PRO_0000159261. FT DOMAIN 21 53 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 67 99 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 32 32 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 35 35 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 38 38 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 42 42 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 79 79 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 82 82 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 85 85 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 89 89 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 426 AA; 48069 MW; A6EA5F33C6C4FC3C CRC64; MDNNIQRLID SAKQSLNSPE SYKYIDESFE SCIKCTACTA VCPVSRNNPL YPGPKQSGPD GERLRLKSAE LYDEALKYCT NCKRCEVACP SDVKIGDLIV RARNNHLAQS KKPLMNKLRD AILSNTDVMG KINTPLAPIV NTITGLKATK FMLEKTLNIS KKRTLPKYAF GTFRSWYMKN ALQDQQKFER KVAYFHGCYV NYNNPQLGKE FLKVFNAMNI GVMLLEKEKC CGLPLMVNGF PNRARNIAQF NTDYIGKMVD ENGIDVISEA SSCSLNLRDE YHHILGIDNA KVRPHIHMVT PFLYQLFKEG KTLPLKPLKL RVAYHTACHV DKAGWAPYTL EVLKKIPSLE IIMLPSQCCG IAGTYGFKSE NYEISQSIGK NLFDNINEGG FDYVISECQT CKWQIDMSSN VTCIHPLTLL CMSMDA // ID GLPF_HAEIN Reviewed; 264 AA. AC P44826; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=Glycerol uptake facilitator protein; GN Name=glpF; OrderedLocusNames=HI_0690; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. 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; L42023; AAC22350.1; -; Genomic_DNA. DR PIR; H64086; H64086. DR RefSeq; NP_438850.1; NC_000907.1. DR RefSeq; WP_005689987.1; NC_000907.1. DR ProteinModelPortal; P44826; -. DR SMR; P44826; 4-257. DR STRING; 71421.HI0690; -. DR EnsemblBacteria; AAC22350; AAC22350; HI_0690. DR GeneID; 949956; -. DR KEGG; hin:HI0690; -. DR PATRIC; 20189999; VBIHaeInf48452_0721. DR eggNOG; ENOG4105D8C; Bacteria. DR eggNOG; COG0580; LUCA. DR KO; K02440; -. DR OMA; WNETKDA; -. DR OrthoDB; EOG6TXQWK; -. DR PhylomeDB; P44826; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015254; F:glycerol channel activity; IBA:GO_Central. DR GO; GO:0015250; F:water channel activity; IBA:GO_Central. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0015793; P:glycerol transport; IBA:GOC. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central. DR GO; GO:0006833; P:water transport; IBA:GOC. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000425; MIP. DR InterPro; IPR022357; MIP_CS. DR PANTHER; PTHR19139; PTHR19139; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; SSF81338; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Glycerol metabolism; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 264 Glycerol uptake facilitator protein. FT /FTId=PRO_0000064083. FT TOPO_DOM 1 3 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 4 32 Helical; Name=M1. {ECO:0000250}. FT TOPO_DOM 33 37 Periplasmic. {ECO:0000250}. FT TRANSMEM 38 58 Helical; Name=M2. {ECO:0000250}. FT TOPO_DOM 59 61 Cytoplasmic. {ECO:0000250}. FT INTRAMEM 62 65 {ECO:0000250}. FT INTRAMEM 66 76 Helical; Name=M3. {ECO:0000250}. FT TOPO_DOM 77 82 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 83 106 Helical; Name=M4. {ECO:0000250}. FT TOPO_DOM 107 141 Periplasmic. {ECO:0000250}. FT TRANSMEM 142 167 Helical; Name=M5. {ECO:0000250}. FT TOPO_DOM 168 175 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 176 192 Helical; Name=M6. {ECO:0000250}. FT TOPO_DOM 193 196 Periplasmic. {ECO:0000250}. FT INTRAMEM 197 200 {ECO:0000250}. FT INTRAMEM 201 214 Helical; Name=M7. {ECO:0000250}. FT TOPO_DOM 215 229 Periplasmic. {ECO:0000250}. FT TRANSMEM 230 252 Helical; Name=M8. {ECO:0000250}. FT TOPO_DOM 253 264 Cytoplasmic. {ECO:0000250}. FT MOTIF 66 68 NPA 1. FT MOTIF 201 203 NPA 2. SQ SEQUENCE 264 AA; 27610 MW; 54941D2323D933D4 CRC64; MDKSLKANCI GEFLGTALLI FFGVGCVAAL KVAGASFGLW EISIMWGMGV ALAVYATAGL SGAHLNPAVT IALWKFACFD GKKVIPYIIS QMLGAFFAAA LVYALYRNVF IDYETVHNIV RGTQESLSLA GTFSTYPHPS LSIGGAFAVE FVITAILMAL IMALTDDGNG VPRGPLAPLL IGILIAVIGG AMGPLTGFAM NPARDFGPKF FAYLAGWGEL ALTGGREIPY FIVPMVAPVL GALAGAWLYK KAIGGNLPCN CGCE // ID GLPK_HAEIN Reviewed; 503 AA. AC P44400; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 102. 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}; GN OrderedLocusNames=HI_0691; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22351.1; -; Genomic_DNA. DR PIR; I64086; I64086. DR RefSeq; NP_438851.1; NC_000907.1. DR RefSeq; WP_005655029.1; NC_000907.1. DR ProteinModelPortal; P44400; -. DR SMR; P44400; 4-497. DR STRING; 71421.HI0691; -. DR EnsemblBacteria; AAC22351; AAC22351; HI_0691. DR GeneID; 949976; -. DR KEGG; hin:HI0691; -. DR PATRIC; 20190001; VBIHaeInf48452_0722. DR eggNOG; ENOG4107QVN; Bacteria. DR eggNOG; COG0554; LUCA. DR KO; K00864; -. DR OMA; GWVEHEP; -. DR OrthoDB; EOG6RZB46; -. DR PhylomeDB; P44400; -. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR HAMAP; MF_00186; Glycerol_kin; 1. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR005999; Glycerol_kin. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01311; glycerol_kin; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycerol metabolism; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 503 Glycerol kinase. FT /FTId=PRO_0000059458. FT NP_BIND 14 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT NP_BIND 412 416 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT REGION 84 85 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT REGION 246 247 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 14 14 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 18 18 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 136 136 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00186}. FT BINDING 268 268 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 311 311 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 315 315 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00186}. FT BINDING 330 330 ATP. {ECO:0000255|HAMAP-Rule:MF_00186}. SQ SEQUENCE 503 AA; 56141 MW; 11C9AA45917ABE5B CRC64; MTDKKYIIAL DQGTTSSRAV LLDHNANVVE IAQREFTQIY PRAGWVEHNP MEIWATQSST LNEVVAKAGI TSDEIAAIGI TNQRETTIVW EKSTGTPVYN AIVWQCRRTA DITDKLKADG HEEYIRNTTG LVVDPYFSGT KVKWILDNVE GAREKAERGE LLFGTVDTWL VWKLTQGRVH VTDYTNASRT MLFNIHTKQW DDKMLEILNI PRSMLPEVRN SSEIYGQTNI GGKGGVRIPV AGIAGDQQAA LYGHLCVHAG QAKNTYGTGC FMLLHTGNKA ITSKNGLLTT IACNAKGEPE YALEGSVFIA GASIQWLRDE LKIVHDSFDS EYFAQKVTDS NGVYVVPAFT GLGAPYWDPY ARGAIFGLSR GANRNHIVRA TLESIAYQTR DVLEAMQSDS GERLQYLRVD GGATNNNFLM QFQADILDVN VERPVVKEVT ALGAAYLAGL ATGFWKDLDE LRDKARVERT FSPDSDNEKR ERRYKGWKKA VKRSLEWAKE DEE // ID GLXK_HAEIN Reviewed; 378 AA. AC P44507; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Glycerate kinase; DE EC=2.7.1.31; GN Name=glxK; OrderedLocusNames=HI_0091; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + D-glycerate = ADP + 3-phospho-D- CC glycerate. CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21769.1; -; Genomic_DNA. DR PIR; C64142; C64142. DR RefSeq; NP_438264.1; NC_000907.1. DR RefSeq; WP_005649699.1; NC_000907.1. DR ProteinModelPortal; P44507; -. DR SMR; P44507; 1-374. DR STRING; 71421.HI0091; -. DR EnsemblBacteria; AAC21769; AAC21769; HI_0091. DR GeneID; 950989; -. DR KEGG; hin:HI0091; -. DR PATRIC; 20188645; VBIHaeInf48452_0092. DR eggNOG; ENOG4105BZW; Bacteria. DR eggNOG; COG1929; LUCA. DR KO; K00865; -. DR OMA; YGKTPMG; -. DR OrthoDB; EOG628F79; -. DR PhylomeDB; P44507; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008887; F:glycerate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0031388; P:organic acid phosphorylation; IEA:InterPro. DR Gene3D; 3.90.1510.10; -; 1. DR InterPro; IPR018193; Glyc_kinase_flavodox-like-dom. DR InterPro; IPR004381; Glycerate_kinase. DR PANTHER; PTHR21599; PTHR21599; 1. DR Pfam; PF02595; Gly_kinase; 1. DR PIRSF; PIRSF006078; GlxK; 1. DR SUPFAM; SSF110738; SSF110738; 1. DR TIGRFAMs; TIGR00045; TIGR00045; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 378 Glycerate kinase. FT /FTId=PRO_0000071533. SQ SEQUENCE 378 AA; 39759 MW; EBC57937BD8838A9 CRC64; MKFVIAPDSF KESLTALEVA TAIETGFKRV FPDADYVKLP MADGGEGTVQ SLVDATQGKL IECEVTAPLG DKVKSFFGLS GDGKTAIIEM AAASGLHLVP PEKRNPLLTT SYGTGELIKL ALDLGVESFI LGIGGSATND GGVGMLQALG MQCLDSQDKP IGFGGAELAN IVKIDVQQLD PRLQQVHIEV ACDVNNPLCG ECGASAIFGP QKGATPEMVK QLDAALSHFA EIAERDCGKQ IRDQAGAGAA GGMGGGLLLL PSVQLKAGIQ IVLDRLHLID YVKDADVVIT GEGRIDAQSI MGKTPIGVAR TAKQFNKPVI AIAGCLREDY DVVFDHGIDA VFPIIHQLGD LSDILKQGEQ NLISTAQNVA RVLAFKFH // ID GMHA_HAEIN Reviewed; 194 AA. AC P45093; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; DE EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067}; DE AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; GN Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067}; Synonyms=isn, lpcA; GN OrderedLocusNames=HI_1181; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP ROLE IN LOS BIOSYNTHESIS. RX PubMed=8655517; RA Brooke J.S., Valvano M.A.; RT "Molecular cloning of the Haemophilus influenzae gmhA (lpcA) gene RT encoding a phosphoheptose isomerase required for lipooligosaccharide RT biosynthesis."; RL J. Bacteriol. 178:3339-3341(1996). RN [4] RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. RX PubMed=12101286; RA Valvano M.A., Messner P., Kosma P.; RT "Novel pathways for biosynthesis of nucleotide-activated glycero- RT manno-heptose precursors of bacterial glycoproteins and cell surface RT polysaccharides."; RL Microbiology 148:1979-1989(2002). CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate CC in D-glycero-D-manno-heptose 7-phosphate. CC {ECO:0000305|PubMed:8655517}. CC -!- CATALYTIC ACTIVITY: D-sedoheptulose 7-phosphate = D-glycero-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00067}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00067}; CC -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7- CC phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7- CC phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from CC sedoheptulose 7-phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- MISCELLANEOUS: The reaction produces a racemic mixture of D- CC glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U17295; AAA95976.1; -; Genomic_DNA. DR EMBL; L42023; AAC22832.1; -; Genomic_DNA. DR PIR; G64168; G64168. DR RefSeq; NP_439337.1; NC_000907.1. DR RefSeq; WP_005694260.1; NC_000907.1. DR ProteinModelPortal; P45093; -. DR SMR; P45093; 1-192. DR STRING; 71421.HI1181; -. DR EnsemblBacteria; AAC22832; AAC22832; HI_1181. DR GeneID; 950026; -. DR KEGG; hin:HI1181; -. DR PATRIC; 20191039; VBIHaeInf48452_1232. DR eggNOG; ENOG4105F55; Bacteria. DR eggNOG; COG0279; LUCA. DR KO; K03271; -. DR OMA; EMHILMI; -. DR OrthoDB; EOG6384PC; -. DR PhylomeDB; P45093; -. DR BRENDA; 5.3.1.28; 2529. DR UniPathway; UPA00041; UER00436. DR UniPathway; UPA00976; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00067; GmhA; 1. DR InterPro; IPR004515; Phosphoheptose_Isoase. DR InterPro; IPR001347; SIS. DR Pfam; PF13580; SIS_2; 1. DR TIGRFAMs; TIGR00441; gmhA; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 194 Phosphoheptose isomerase. FT /FTId=PRO_0000136531. FT DOMAIN 37 194 SIS. {ECO:0000255|HAMAP-Rule:MF_00067}. FT REGION 52 54 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 93 94 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 119 121 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT METAL 61 61 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 65 65 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 172 172 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 180 180 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 172 172 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT CONFLICT 106 106 E -> D (in Ref. 1; AAA95976). FT {ECO:0000305}. SQ SEQUENCE 194 AA; 21379 MW; 198BDB6CA380A0D4 CRC64; MYLDQIKSEL VEAQDVLNKF ISDENNIKLI QEAALLISNS FKQGGKVLSC GNGGSHCDAM HFAEELTGRY RENRPGYPAI AISDASHLSC VSNDFGYEYV FSRYVEAVGQ KGDVLFGLST SGNSKNILNA IEAAKTKGMK VIAMTGKDGG KMAGLADVEI RVPHFRYADR IQEIHIKVIH ILMMLIEFEM AKQA // ID GRCA_HAEIN Reviewed; 127 AA. AC P44455; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Autonomous glycyl radical cofactor {ECO:0000255|HAMAP-Rule:MF_00806}; GN Name=grcA {ECO:0000255|HAMAP-Rule:MF_00806}; GN OrderedLocusNames=HI_0017; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Acts as a radical domain for damaged PFL and possibly CC other radical proteins. {ECO:0000255|HAMAP-Rule:MF_00806}. CC -!- SIMILARITY: Contains 1 glycine radical domain. {ECO:0000255|HAMAP- CC Rule:MF_00806}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21695.1; -; Genomic_DNA. DR PIR; C64140; C64140. DR RefSeq; NP_438190.1; NC_000907.1. DR RefSeq; WP_005628746.1; NC_000907.1. DR ProteinModelPortal; P44455; -. DR SMR; P44455; 67-127. DR STRING; 71421.HI0017; -. DR EnsemblBacteria; AAC21695; AAC21695; HI_0017. DR GeneID; 950913; -. DR KEGG; hin:HI0017; -. DR PATRIC; 20188485; VBIHaeInf48452_0017. DR eggNOG; ENOG4108VKA; Bacteria. DR eggNOG; COG3445; LUCA. DR KO; K06866; -. DR OMA; GQFEYRE; -. DR OrthoDB; EOG62C9MX; -. DR PhylomeDB; P44455; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008861; F:formate C-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central. DR HAMAP; MF_00806; GrcA; 1. DR InterPro; IPR019777; Form_AcTrfase_GR_CS. DR InterPro; IPR001150; Gly_radical. DR InterPro; IPR011140; Glycyl_radical_cofactor_GrcA. DR Pfam; PF01228; Gly_radical; 1. DR PIRSF; PIRSF000378; Gly_radicl_yfiD; 1. DR TIGRFAMs; TIGR04365; spare_glycyl; 1. DR PROSITE; PS00850; GLY_RADICAL_1; 1. DR PROSITE; PS51149; GLY_RADICAL_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Organic radical; Reference proteome. FT CHAIN 1 127 Autonomous glycyl radical cofactor. FT /FTId=PRO_0000166702. FT DOMAIN 5 127 Glycine radical. {ECO:0000255|HAMAP- FT Rule:MF_00806}. FT MOD_RES 102 102 Glycine radical. {ECO:0000255|HAMAP- FT Rule:MF_00806}. SQ SEQUENCE 127 AA; 14291 MW; A3B896D3A479DB0A CRC64; MIKGIQITQA ANDNLLNSFW LLDSEKNEAR CLCAKGEFAE DQVVAVSELG QIEYRELPVN VAPTVKVEGG QHLNVNVLRR ETLEDAVNNP DKYPQLTIRV SGYAVRFNSL TPEQQRDVIT RTFTESL // ID GST_HAEIN Reviewed; 209 AA. AC P44521; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Glutathione S-transferase; DE EC=2.5.1.18; GN Name=gst; OrderedLocusNames=HI_0111; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the GST superfamily. Beta family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21788.1; -; Genomic_DNA. DR PIR; A64049; A64049. DR RefSeq; NP_438285.1; NC_000907.1. DR RefSeq; WP_005693808.1; NC_000907.1. DR ProteinModelPortal; P44521; -. DR STRING; 71421.HI0111; -. DR EnsemblBacteria; AAC21788; AAC21788; HI_0111. DR GeneID; 951011; -. DR KEGG; hin:HI0111; -. DR PATRIC; 20188691; VBIHaeInf48452_0115. DR eggNOG; ENOG4108K3A; Bacteria. DR eggNOG; COG0625; LUCA. DR KO; K00799; -. DR OMA; ENADYEF; -. DR OrthoDB; EOG6H1Q01; -. DR PhylomeDB; P44521; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 209 Glutathione S-transferase. FT /FTId=PRO_0000185972. FT DOMAIN 1 81 GST N-terminal. FT DOMAIN 87 209 GST C-terminal. FT REGION 65 66 Glutathione binding. FT {ECO:0000250|UniProtKB:P0A9D2}. FT REGION 103 106 Glutathione binding. FT {ECO:0000250|UniProtKB:P0A9D2}. FT BINDING 10 10 Glutathione. FT {ECO:0000250|UniProtKB:P0A9D2}. FT BINDING 53 53 Glutathione; via amide nitrogen and FT carbonyl oxygen. FT {ECO:0000250|UniProtKB:P0A9D2}. SQ SEQUENCE 209 AA; 23925 MW; 0FA44B9415B52BEA CRC64; MKLYGLIGAC SFVPHVALEW VKIRENADYE FEPVTRELIK SPEFLSLNPR GAVPVLVDGD LVLSQNQAIL HYLDELYPNS KLFGSKTVRD KAKAARWLAF FNSDVHKSFV PLFRLPNYAK DNETLAHTIR QQAVEQILDQ LAVANEHLES HIYFGENISV ADAYLYIMLN WCKAVKIDFS HLTQLSAFMQ RVETDQAVEN VRKSEELKV // ID GPH_HAEIN Reviewed; 224 AA. AC P44755; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_00495}; DE Short=PGP {ECO:0000255|HAMAP-Rule:MF_00495}; DE Short=PGPase {ECO:0000255|HAMAP-Rule:MF_00495}; DE EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_00495}; GN Name=gph {ECO:0000255|HAMAP-Rule:MF_00495}; OrderedLocusNames=HI_0565; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2- CC phosphoglycolate. Is involved in the dissimilation of the CC intracellular 2-phosphoglycolate formed during the DNA repair of CC 3'-phosphoglycolate ends, a major class of DNA lesions induced by CC oxidative stress. {ECO:0000255|HAMAP-Rule:MF_00495}. CC -!- CATALYTIC ACTIVITY: 2-phosphoglycolate + H(2)O = glycolate + CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00495}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00495}; CC -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; CC glycolate from 2-phosphoglycolate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00495}. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC CbbY/CbbZ/Gph/YieH family. {ECO:0000255|HAMAP-Rule:MF_00495}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22223.1; -; Genomic_DNA. DR PIR; G64154; G64154. DR RefSeq; NP_438722.1; NC_000907.1. DR RefSeq; WP_005694158.1; NC_000907.1. DR ProteinModelPortal; P44755; -. DR SMR; P44755; 3-223. DR STRING; 71421.HI0565; -. DR EnsemblBacteria; AAC22223; AAC22223; HI_0565. DR GeneID; 949611; -. DR KEGG; hin:HI0565; -. DR PATRIC; 20189685; VBIHaeInf48452_0585. DR eggNOG; ENOG4108VXP; Bacteria. DR eggNOG; COG0546; LUCA. DR KO; K01091; -. DR OMA; RKPDARH; -. DR OrthoDB; EOG6HB9PJ; -. DR PhylomeDB; P44755; -. DR UniPathway; UPA00865; UER00834. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_00495; GPH_hydrolase_bact; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR000150; Hypothet_cof. DR InterPro; IPR006346; PGP_bact. DR InterPro; IPR023198; PGP_dom2. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR01449; PGP_bact; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; KW Metal-binding; Reference proteome. FT CHAIN 1 224 Phosphoglycolate phosphatase. FT /FTId=PRO_0000108029. FT ACT_SITE 11 11 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 11 11 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 13 13 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 177 177 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. SQ SEQUENCE 224 AA; 24774 MW; C251F0E6859A826B CRC64; MNTQFKLIGF DLDGTLVNSL PDLALSVNSA LAEFNLPQAP EELVLTWIGN GAPVLIARAL DWAKKQTGKV LTETEVKQVT ERFNFYYGEN LCNVSRLYPN VKETLEILKE KGYVLAVVTN KPTRHVQPVL AAFGIDHLFS EMLGGQSLPA IKPHPAPLYY LCGKFGFEPR QVLFVGDSKN DIIAGHAAGC AVVGLTYGYN YNIPIRESNP DWVFDDFAQL LSIL // ID GPMA_HAEIN Reviewed; 227 AA. AC P44865; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039}; DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039}; DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039}; GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; Synonyms=gpm; GN OrderedLocusNames=HI_0757; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_01039}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22416.1; -; Genomic_DNA. DR PIR; A64091; A64091. DR RefSeq; NP_438916.1; NC_000907.1. DR RefSeq; WP_005693156.1; NC_000907.1. DR ProteinModelPortal; P44865; -. DR SMR; P44865; 2-227. DR STRING; 71421.HI0757; -. DR EnsemblBacteria; AAC22416; AAC22416; HI_0757. DR GeneID; 949776; -. DR KEGG; hin:HI0757; -. DR PATRIC; 20190159; VBIHaeInf48452_0795. DR eggNOG; ENOG4105DKJ; Bacteria. DR eggNOG; COG0588; LUCA. DR KO; K01834; -. DR OMA; VKNQGKK; -. DR OrthoDB; EOG6C8N1H; -. DR PhylomeDB; P44865; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0043456; P:regulation of pentose-phosphate shunt; IBA:GO_Central. DR Gene3D; 3.40.50.1240; -; 1. DR HAMAP; MF_01039; PGAM_GpmA; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR005952; Phosphogly_mut1. DR PANTHER; PTHR11931; PTHR11931; 1. DR Pfam; PF00300; His_Phos_1; 2. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR TIGRFAMs; TIGR01258; pgm_1; 1. PE 3: Inferred from homology; KW Complete proteome; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 227 2,3-bisphosphoglycerate-dependent FT phosphoglycerate mutase. FT /FTId=PRO_0000179882. FT REGION 7 14 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 20 21 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 86 89 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 113 114 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT REGION 182 183 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT ACT_SITE 8 8 Tele-phosphohistidine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT ACT_SITE 86 86 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_01039}. FT BINDING 59 59 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT BINDING 97 97 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01039}. FT SITE 181 181 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01039}. SQ SEQUENCE 227 AA; 26049 MW; 3B846676BDFB561E CRC64; MELVFIRHGF SEWNAKNLFT GWRDVNLTER GVEEAKTAGK KLLDKGYEFD IAFTSVLTRA IKTCNIVLEE SHQLWIPQVK NWRLNERHYG ALQGLDKKAT AEQYGDEQVH IWRRSYDISP PDLDPQDPNS AHNDRRYANI PSDVVPNAEN LKLTLERALP FWEDQIAPAM LSGKRVLVVA HGNSLRALAK HIIGISDAEI MDFEIPTGQP LVLKLDDKLN YVEHYYL // ID GREB_HAEIN Reviewed; 158 AA. AC P43882; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Transcription elongation factor GreB {ECO:0000255|HAMAP-Rule:MF_00930}; DE AltName: Full=Transcript cleavage factor GreB {ECO:0000255|HAMAP-Rule:MF_00930}; GN Name=greB {ECO:0000255|HAMAP-Rule:MF_00930}; GN OrderedLocusNames=HI_0569; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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. GreB releases sequences of up to 9 CC nucleotides in length. {ECO:0000255|HAMAP-Rule:MF_00930}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. GreB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00930}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22227.1; -; Genomic_DNA. DR PIR; B64078; B64078. DR RefSeq; NP_438726.1; NC_000907.1. DR RefSeq; WP_005694166.1; NC_000907.1. DR ProteinModelPortal; P43882; -. DR SMR; P43882; 3-156. DR STRING; 71421.HI0569; -. DR EnsemblBacteria; AAC22227; AAC22227; HI_0569. DR GeneID; 950647; -. DR KEGG; hin:HI0569; -. DR PATRIC; 20189693; VBIHaeInf48452_0589. DR eggNOG; ENOG4108RRZ; Bacteria. DR eggNOG; COG0782; LUCA. DR KO; K04760; -. DR OMA; DQIFFGA; -. DR OrthoDB; EOG686NQ9; -. DR PhylomeDB; P43882; -. DR Proteomes; UP000000579; 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 HAMAP; MF_00930; GreB; 1. DR InterPro; IPR018151; TF_GreA/GreB_CS. 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 InterPro; IPR006358; Tscrpt_elong_fac_GreB. 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; TIGR01461; greB; 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 1 158 Transcription elongation factor GreB. FT /FTId=PRO_0000176930. FT COILED 53 75 {ECO:0000255|HAMAP-Rule:MF_00930}. SQ SEQUENCE 158 AA; 18464 MW; 611A427515F0B769 CRC64; MAKSNYITRQ GWLALDQELK FLWKEERPKV TQAVSDAAAL GDRSENAEYI YGKRRLREID RRVRFLTKRL EVLQIVDYNP KQEGKVFFGA WVELENEEGE TKQYRIVGCD EFAPAKNWIS IDSPVARALI GKTLDDEVRV ETPSGFITLY VNKIWYEK // ID GRPE_HAEIN Reviewed; 198 AA. AC P43732; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, 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}; GN OrderedLocusNames=HI_0071; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC21750.1; 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; L42023; AAC21750.1; ALT_INIT; Genomic_DNA. DR PIR; I64046; I64046. DR RefSeq; NP_438245.2; NC_000907.1. DR ProteinModelPortal; P43732; -. DR STRING; 71421.HI0071; -. DR EnsemblBacteria; AAC21750; AAC21750; HI_0071. DR GeneID; 950971; -. DR KEGG; hin:HI0071; -. DR PATRIC; 20188599; VBIHaeInf48452_0073. DR eggNOG; ENOG4105K90; Bacteria. DR eggNOG; COG0576; LUCA. DR KO; K03687; -. DR OMA; VCDSLDA; -. DR OrthoDB; EOG6FJNJ9; -. DR Proteomes; UP000000579; 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 1 198 Protein GrpE. FT /FTId=PRO_0000113793. SQ SEQUENCE 198 AA; 22298 MW; DDCA4C1B03D50EC0 CRC64; MSEQEQKVEI PEVEKQEEVV VEETQQAEHS QEFDPLEEAI ARVQELEEQL KTQIEEAANK EQDILLRSRA EIENLRRRTE QDVEKAHKFA LEKFSKDILN TIDNLERALA TPANKEDESV KALFDGVELT LKELVSTVGR FGVEAVGVVG EAFNPDLHQA ISMQPAEGFE TNQISVVLQK GYTLNGRVIR PAMVMVAA // ID GSHR_HAEIN Reviewed; 456 AA. AC P43783; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 123. DE RecName: Full=Glutathione reductase; DE Short=GR; DE Short=GRase; DE EC=1.8.1.7; GN Name=gor; OrderedLocusNames=HI_0161; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Maintains high levels of reduced glutathione in the CC cytosol. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 glutathione + NADP(+) = glutathione CC disulfide + NADPH. 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; U20229; AAA62137.1; -; Genomic_DNA. DR EMBL; L42023; AAC21833.1; -; Genomic_DNA. DR PIR; A64052; A64052. DR RefSeq; NP_438331.1; NC_000907.1. DR RefSeq; WP_005694117.1; NC_000907.1. DR ProteinModelPortal; P43783; -. DR SMR; P43783; 2-456. DR STRING; 71421.HI0161; -. DR EnsemblBacteria; AAC21833; AAC21833; HI_0161. DR GeneID; 951071; -. DR KEGG; hin:HI0161; -. DR PATRIC; 20188821; VBIHaeInf48452_0167. DR eggNOG; ENOG4105DC8; Bacteria. DR eggNOG; COG1249; LUCA. DR KO; K00383; -. DR OMA; YAEDYGF; -. DR OrthoDB; EOG6QCD6D; -. DR PhylomeDB; P43783; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0006749; P:glutathione metabolic process; 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; IPR006322; Glutathione_Rdtase_euk/bac. 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; TIGR01421; gluta_reduc_1; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; KW Oxidoreductase; Redox-active center; Reference proteome. FT CHAIN 1 456 Glutathione reductase. FT /FTId=PRO_0000067976. FT NP_BIND 34 42 FAD. {ECO:0000250}. FT ACT_SITE 445 445 Proton acceptor. {ECO:0000250}. FT DISULFID 42 47 Redox-active. {ECO:0000250}. SQ SEQUENCE 456 AA; 49329 MW; 846988C215FE949A CRC64; MTKHYDYIAI GGGSGGIASL NRAASYGKKC AIIEAKHLGG TCVNVGCVPK KVMFYGAHIA EAINNYAPDY GFDVEVKKFD FSKLIESRQA YISRIHTSYN NVLAKNNIDV INGFGKFVDA HTIEVTLADG TKEQVTADHI LIATGGRPYR PNIKGQEYGI DSDGFFALTE LPKRAAVIGA GYIAVELSGV LNSLGVETHL LVRRHAPMRN QDPLIVETLV EVLAQDGIQL HTNSTPSEIV KNADGSLTVR CDGQSDVTVD CVIWAAGRVP TTDKIGLENA GVETNEHGYV KVDKYQNTNV KGIYAVGDII ENGIELTPVA VAAGRRLSER LFNNKPTEYL DYSLVPTVVF SHPPIGTVGL TEPQAIEQYG AENVKVYKSS FTAMYTAVTQ HRQPCKMKLV CVGKDEKVVG LHGIGFGVDE MIQGFAVAIK MGATKADFDN TVAIHPTGSE EFVTMR // ID GYRA_HAEIN Reviewed; 880 AA. AC P43700; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 107. 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}; GN OrderedLocusNames=HI_1264; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22917.1; -; Genomic_DNA. DR PIR; E64113; E64113. DR RefSeq; NP_439419.1; NC_000907.1. DR RefSeq; WP_005694321.1; NC_000907.1. DR ProteinModelPortal; P43700; -. DR SMR; P43700; 31-519, 533-866. DR STRING; 71421.HI1264; -. DR DrugBank; DB06771; Besifloxacin. DR DrugBank; DB00827; Cinoxacin. DR DrugBank; DB00537; Ciprofloxacin. DR DrugBank; DB00467; Enoxacin. DR DrugBank; DB09047; Finafloxacin. DR DrugBank; DB04576; Fleroxacin. DR DrugBank; DB01155; Gemifloxacin. DR DrugBank; DB01137; Levofloxacin. DR DrugBank; DB00978; Lomefloxacin. DR DrugBank; DB00218; Moxifloxacin. DR DrugBank; DB01059; Norfloxacin. DR DrugBank; DB01165; Ofloxacin. DR DrugBank; DB00487; Pefloxacin. DR DrugBank; DB01208; Sparfloxacin. DR DrugBank; DB00685; Trovafloxacin. DR PRIDE; P43700; -. DR EnsemblBacteria; AAC22917; AAC22917; HI_1264. DR GeneID; 950199; -. DR KEGG; hin:HI1264; -. DR PATRIC; 20191209; VBIHaeInf48452_1316. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR KO; K02469; -. DR OMA; ETVDWVP; -. DR OrthoDB; EOG661H5V; -. DR PhylomeDB; P43700; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.268.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 1. 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 InterPro; IPR013757; Topo_IIA_A_a. 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 1 880 DNA gyrase subunit A. FT /FTId=PRO_0000145235. FT MOTIF 557 563 GyrA-box. {ECO:0000255|HAMAP- FT Rule:MF_01897}. FT ACT_SITE 123 123 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01897}. SQ SEQUENCE 880 AA; 97818 MW; 0B2E9DD34155A322 CRC64; MTDSIQSSIT PVNIEEELKS SYLDYAMSVI VGRALPDVRD GLKPVHRRVL FSMDREGNTA NKKYVKSARV VGDVIGKYHP HGDSAVYDTI VRMAQPFSLR YMLVDGQGNF GSIDGDAPAA MRYTEVRMQK ITQALLTDLD KETVNFSPNY DGELMIPDVL PTRIPALLAN GSSGIAVGMA TNIPPHNLNE VLNGCLAYID KNEITIDELM QHIPGPDFPT AALINGRKGI EEAYRTGRGK VYVRARATVE TNEKGREQII VSELPYQVNK AKLVEKIAEL IREKKIEGIS NITDLSNKEG IRIEIDIKRD AVGEVVLNHL YSLTQMQVTF GINMVALDHG QPRLFNLKEI IEAFVLHRRE VVTRRSIFEL RKARERTHIL EGLAVARSNI DEMIAIIRNS KNREEAATSI SSRSWTLHSD IINLLDASAR PDELEENLGI QGEQYYLSPA QVNAILELRL HRLTGIAFEE VIKEYEELLV KIADLLHILS SAERLMEVIR EELEEVKAQF GDDRLTEITA ASGDIDLEDL IAQEDVVVTL SHEGYVKYQP LTDYEAQRRG GKGKSATKMK EEDFIEKLLV ANTHDTILCF SSRGRLYWLK VYQLPQASRG ARGRPIVNIL PLQENERITA ILPVSAYEED KFVVMATAGG IVKKIALTEF SRPRSNGIIA LNLRDEDELI GVDITDGSNE IMLFSSQGRV VRFAENAVRA MGRLATGVRG IKLALTNDIS DDESAVEIED ISDDNAEASL DLNIDKVVSL VVPKGEGAIL TATQNGYGKR TQLSEYPTKS RNTKGVISIK VSERNGKVVA ATQVEETDQI MLITDAGTLV RTRVSEVSIV GRNTQGVRLI RTADDEHVVS LERVCDADED DSLEESSSEE // ID GUAA_HAEIN Reviewed; 523 AA. AC P44335; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 122. DE RecName: Full=GMP synthase [glutamine-hydrolyzing]; DE EC=6.3.5.2; DE AltName: Full=GMP synthetase; DE AltName: Full=Glutamine amidotransferase; GN Name=guaA; OrderedLocusNames=HI_0222; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21891.1; -; Genomic_DNA. DR PIR; I64055; I64055. DR RefSeq; NP_438394.1; NC_000907.1. DR RefSeq; WP_005694070.1; NC_000907.1. DR ProteinModelPortal; P44335; -. DR SMR; P44335; 3-523. DR STRING; 71421.HI0222; -. DR EnsemblBacteria; AAC21891; AAC21891; HI_0222. DR GeneID; 951140; -. DR KEGG; hin:HI0222; -. DR PATRIC; 20188965; VBIHaeInf48452_0235. DR eggNOG; ENOG4105CM0; Bacteria. DR eggNOG; COG0518; LUCA. DR eggNOG; COG0519; LUCA. DR KO; K01951; -. DR OMA; MSHGDSV; -. DR OrthoDB; EOG6JHRJV; -. DR PhylomeDB; P44335; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00344; GMP_synthase; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR022955; GMP_synthase. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 523 GMP synthase [glutamine-hydrolyzing]. FT /FTId=PRO_0000140131. FT DOMAIN 8 205 Glutamine amidotransferase type-1. FT DOMAIN 206 398 GMPS ATP-PPase. FT NP_BIND 233 239 ATP. {ECO:0000250}. FT ACT_SITE 85 85 Nucleophile. {ECO:0000250}. FT ACT_SITE 179 179 {ECO:0000250}. FT ACT_SITE 181 181 {ECO:0000250}. SQ SEQUENCE 523 AA; 58186 MW; 6361F38BC20CF154 CRC64; MTNIHYHKIL ILDFGSQYTQ LIARRVREIG VYCELWAWDV TEQQIREFAP TGIILSGSPE STTEENSPRA PEYVFNAGVP VLGICYGMQT MAMQLGGLTE TSDHREFGYA SVSLENSTAL FANLNDNLTA SEPKLDVWMS HGDKVTRLPE NFKVTGTTLT CPIAAMSDES RRFYGVQFHP EVTHTKKGLE LLTNFVVNIC GCETKWTAEN IIEDAVARIK EQVGDDEVIL GLSGGVDSSV VALLLHRAIG KNLHCVFVDN GLLRLHEGDQ VMEMFGDKFG LNITRVDAES RFLGELAGVS DPEAKRKIIG KVFVDVFDDE SKKLTNVKWL AQGTIYPDVI ESAASKTGKA HVIKSHHNVG GLPDYMKLGL VEPLRELFKD EVRKIGLALG LPAEMINRHP FPGPGLGVRV LGEVKKEYCD LLRRADAIFI EELRNSGWYE KTSQAFSVFL PVKSVGVMGD GRKYDWVISL RAVETIDFMT AHWAHLPYDL LGKVSNRIIN EVNGISRVVY DISGKPPATI EWE // ID HAP1_HAEIN Reviewed; 1409 AA. AC P44596; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 16-MAR-2016, entry version 104. DE RecName: Full=Adhesion and penetration protein autotransporter; DE EC=3.4.21.-; DE Contains: DE RecName: Full=Adhesion and penetration protein; DE Contains: DE RecName: Full=Adhesion and penetration protein translocator; DE AltName: Full=Helper peptide; DE Flags: Precursor; GN Name=hap; OrderedLocusNames=HI_0248; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable protease; promotes adherence and invasion by CC directly binding to a host cell structure. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Adhesion and penetration protein CC autotransporter: Periplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Adhesion and penetration protein: Secreted CC {ECO:0000305}. Cell surface {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Adhesion and penetration protein CC translocator: Cell outer membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Note=The cleaved C-terminal CC fragment (autotransporter domain) is localized in the outer CC membrane. {ECO:0000250}. CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides CC the autotransporter protein to the periplasmic space. Then, CC insertion of the C-terminal translocator domain in the outer CC membrane forms a hydrophilic pore for the translocation of the CC passenger domain to the bacterial cell surface, with subsequent CC cleavage (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 1 autotransporter (TC 1.B.12) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00556}. CC -!- SIMILARITY: Contains 1 peptidase S6 domain. {ECO:0000255|PROSITE- CC ProRule:PRU01028}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Erroneous termination; Positions=710; Note=Translated as Gln.; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; C64057; C64057. DR ProteinModelPortal; P44596; -. DR MEROPS; S06.006; -. DR OMA; YFIEREN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.20; -; 2. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR006315; OM_autotransptr_brl. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR000710; Peptidase_S6. DR InterPro; IPR030396; Peptidase_S6_dom. DR InterPro; IPR004899; Pertactin_central. DR InterPro; IPR033116; TRYPSIN_SER. DR Pfam; PF02395; Peptidase_S6; 1. DR Pfam; PF03212; Pertactin; 1. DR PRINTS; PR00921; IGASERPTASE. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF51126; SSF51126; 2. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS51691; PEPTIDASE_S6; 1. PE 3: Inferred from homology; KW Cell adhesion; Cell outer membrane; Complete proteome; Hydrolase; KW Membrane; Periplasm; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Transmembrane; Transmembrane beta strand; KW Zymogen. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1409 Adhesion and penetration protein FT autotransporter. FT /FTId=PRO_0000387595. FT CHAIN 26 ? Adhesion and penetration protein. FT /FTId=PRO_0000026954. FT CHAIN ? 1409 Adhesion and penetration protein FT translocator. {ECO:0000255}. FT /FTId=PRO_0000026955. FT DOMAIN 26 294 Peptidase S6. {ECO:0000255|PROSITE- FT ProRule:PRU01028}. FT DOMAIN 1156 1409 Autotransporter. {ECO:0000255|PROSITE- FT ProRule:PRU00556}. FT ACT_SITE 250 250 {ECO:0000250}. SQ SEQUENCE 1409 AA; 156815 MW; F51C219C312A146E CRC64; MKKTVFRLNF LTACVSLGIA SQAWAGHTYF GIDYQYYRDF AENKGKFTVG AKNIEVYNKE GQLVGTSMTK APMIDFSVVS RNGVAALVGD QYIVSVAHNG GYNDVDFGAE GRNPDQHRFT YQIVKRNNYQ AWERKHPYDG DYHMPRLHKF VTEAEPVGMT TNMDGKVYAD RENYPERVRI GSGRQYWRTD KDEETNVHSS YYVSGAYRYL TAGNTHTQSG NGNGTVNLSG NVVSPNHYGP LPTGGSKGDS GSPMFIYDAK KKQWLINAVL QTGHPFFGRG NGFQLIREEW FYNEVLAVDT PSVFQRYIPP INGHYSFVSN NDGTGKLTLT RPSKDGSKAK SEVGTVKLFN PSLNQTAKEH VKAAAGYNIY QPRMEYGKNI YLGDQGKGTL TIENNINQGA GGLYFEGNFV VKGKQNNITW QGAGVSIGQD ATVEWKVHNP ENDRLSKIGI GTLLVNGKGK NLGSLSAGNG KVILDQQADE AGQKQAFKEV GIVSGRATVQ LNSTDQVDPN NIYFGFRGGR LDLNGHSLTF KRIQNTDEGA MIVNHNTTQV ANITITGNES ITAPSNKKNI NKLDYSKEIA YNGWFGETDK NKHNGRLNLI YKPTTEDRTL LLSGGTNLKG DITQTKGKLF FSGRPTPHAY NHLDKRWSEM EGIPQGEIVW DYDWINRTFK AENFQIKGGS AVVSRNVSSI EGNWTVSNNA NATFGVVPNQ QNTICTRSDW TGLTTCKTVN LTDTKVINSI PITQINGSIN LTNNATVNIH GLAKLNGNVT LIDHSQFTLS NNATQTGNIK LSNHANATVN NATLNGNVHL TDSAQFSLKN SHFWHQIQGD KDTTVTLENA TWTMPSDTTL QNLTLNNSTV TLNSAYSASS NNAPRHRRSL ETETTPTSAE HRFNTLTVNG KLSGQGTFQF TSSLFGYKSD KLKLSNDAEG DYTLSVRNTG KEPVTLEQLT LIESLDNKPL SDKLKFTLEN DHVDAGALRY KLVKNKGEFR LHNPIKEQEL LNDLVRAEQA EQTLEAKQVE QTAEKQKSKA KARSRRAVLS DTPSAQSLLN ALEAKQVEQT TETQTSKPKT KKGRSKRALS AAFSDTPFDL SQLKVFEVKL EVINAQPQVK KEPQDQEEQG KQKELISRYS NSALSELSAT VNSMFSVQDE LDRLFVDQAQ SALWTNIAQD KRRYDSDAFR AYQQKTNLRQ IGVQKALDNG RIGAVFSHSR SDNTFDEQVK NHATLTMMSG FAQYQWGDLQ FGVNVGAGIS ASKMAEEQSR KIHRKAINYG VNASYQFRLG QLGIQPYLGV NRYFIERENY QSEEVKVQTP SLAFNRYNAG IRVDYTFTPT NNISVKPYFF VNYVDVSNAN VQTTVNSTML QQSFGRYWQK EVGLKAEILH FQLSAFISKS QGSQLGKQQN VGVKLGYRW // ID HFLK_HAEIN Reviewed; 410 AA. AC P44546; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 99. DE RecName: Full=Protein HflK; GN Name=hflK; OrderedLocusNames=HI_0151; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: HflC and HflK could encode or regulate a protease. CC {ECO:0000250}. CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK 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; L42023; AAC21822.1; -; Genomic_DNA. DR PIR; A64051; A64051. DR RefSeq; NP_438321.1; NC_000907.1. DR RefSeq; WP_005694434.1; NC_000907.1. DR ProteinModelPortal; P44546; -. DR STRING; 71421.HI0151; -. DR EnsemblBacteria; AAC21822; AAC21822; HI_0151. DR GeneID; 951061; -. DR KEGG; hin:HI0151; -. DR PATRIC; 20188795; VBIHaeInf48452_0154. DR eggNOG; ENOG4107QJR; Bacteria. DR eggNOG; COG0330; LUCA. DR KO; K04088; -. DR OMA; WNEPGGN; -. DR OrthoDB; EOG6J48MH; -. DR PhylomeDB; P44546; -. DR BioCyc; RETL1328306-WGS:GSTH-2838-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001107; Band_7. DR InterPro; IPR010201; HflK. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR PANTHER; PTHR10264:SF51; PTHR10264:SF51; 1. DR Pfam; PF01145; Band_7; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. DR TIGRFAMs; TIGR01933; hflK; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 410 Protein HflK. FT /FTId=PRO_0000094087. FT TRANSMEM 87 107 Helical. {ECO:0000255}. SQ SEQUENCE 410 AA; 45806 MW; FB6CCD1AF44FA09C CRC64; MENEMSQNGS DRDPWSKPGQ SNDQQPGNSS NNNGWNNNQN RGNQEQSPPD IEEIFNNLLK KLGGGNKKSG QNNGSSQGNT PFHFGKVIPL AVAIGAIIWG VNGFYTIKEA ERGVVLRFGE LHSIVQPGLN WKPTFVDKVL PVNVEQVKEL RTQGAMLTQD ENMVKVEMTV QYRVQDPAKY LFSVTNADDS LNQATDSALR YVIGHMSMND ILTTGRSVVR ENTWKALNEI IKSYDMGLEV IDVNFQSARP PEEVKDAFDD AIKAQEDEQR FIREAEAYAR EKEPIARGDA QRILEEATAY KDRIVLDAKG EVERLQRLLP EFKAAPDLLR ERLYIQTMEK VMANTPKVML DGNNGNNLTV LPLEQIMGKK SVTSAPSAVN SSPAFTAPER QNSYQPQPTT VAPIRQGRFN // ID GYRB_HAEIN Reviewed; 806 AA. AC P43701; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 116. 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}; GN OrderedLocusNames=HI_0567; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22225.1; -; Genomic_DNA. DR PIR; A64078; A64078. DR RefSeq; NP_438724.1; NC_000907.1. DR RefSeq; WP_010869008.1; NC_000907.1. DR ProteinModelPortal; P43701; -. DR SMR; P43701; 14-379. DR STRING; 71421.HI0567; -. DR PRIDE; P43701; -. DR EnsemblBacteria; AAC22225; AAC22225; HI_0567. DR GeneID; 949613; -. DR KEGG; hin:HI0567; -. DR PATRIC; 20189689; VBIHaeInf48452_0587. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR PhylomeDB; P43701; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 2. 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; 2. 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 1 806 DNA gyrase subunit B. FT /FTId=PRO_0000145313. FT DOMAIN 421 536 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 427 427 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 501 501 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01898}. FT METAL 501 501 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT METAL 503 503 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 452 452 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. FT SITE 455 455 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_01898}. SQ SEQUENCE 806 AA; 89885 MW; 0E9EC804D134B092 CRC64; MSETTNDNYG ASSIKVLKGL DAVRKRPGMY IGDTDDGTGL HHMVFEVVDN AIDEALAGHC SDIIVTIHDD NSVSVQDDGG GIPVDIHPEE GVSAAEVIMT VLHAGGKFDD NSYKVSGGLH GVGVSVVNAL SDKLQLTIRR QGHVHEQFYH LGEPQSPLTV IGETEATGTT VRFWPSSDIF AITTFDYKIL AKRLRELSFL NSGVSIRLID KRDGSEDHFH YEGGIQAFVE YLNKNKNPIH PKPFYFTAEK DGIGVEVALQ WNDGVNENVY CFTNNIPQRD GGTHLAGFRG ALTRSLNSYM ENEGMLKKEK VATSGDDARE GLVAIISVKV PDPKFSSQTK DKLVSSEVKS AVESAMNEKM QEYLLENPAD AKIIVNQIIM AARAREAARK AREMTRRKGA LDIAGLPGKL ADCQEKDPAL SELYLVEGDS AGGSAKVGRD RKTQAILPLK GKILNVEKAR FDKMLSSQEV GTLITALGCG IGRDEYNPDK LRYHHIIIMT DADVDGSHIR TLLLTFFYRQ MPELIERGYV YIAQPPLYKV KKGKQERYIK DADEMEQYEL TLALDGAELH ISTNAPAMNA LVFEKLVAEY NSVQKLIGRL NRHYPAPVLQ GLIYQSPISI EMMKEESAVE NWGKSFVEQL TAKETEAHQY SVRTQFNAER QVYEAVITVR KHGIDTDYFL NFDFVHGNEY AKIVSLNKQL NGLLEEGAYV IRGEKVQPVR SFEQAVEWLV KESRKGLEVQ RYKGLGEMNA DQLWETTMDP NSRRMLKVSI KDAVAADQLF TTLMGDEVEP RREFIELNAL RANLDV // ID HCAT_HAEIN Reviewed; 388 AA. AC P44629; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Probable 3-phenylpropionic acid transporter; GN Name=hcaT; OrderedLocusNames=HI_0308; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable permease involved in the uptake of 3- CC phenylpropionic acid. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the LacY/RafB permease family. HcaT 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; L42023; AAC21973.1; -; Genomic_DNA. DR PIR; F64147; F64147. DR RefSeq; NP_438475.1; NC_000907.1. DR RefSeq; WP_005694357.1; NC_000907.1. DR ProteinModelPortal; P44629; -. DR STRING; 71421.HI0308; -. DR EnsemblBacteria; AAC21973; AAC21973; HI_0308. DR GeneID; 950679; -. DR KEGG; hin:HI0308; -. DR PATRIC; 20189157; VBIHaeInf48452_0325. DR eggNOG; ENOG4105D8G; Bacteria. DR eggNOG; ENOG410XQVS; LUCA. DR KO; K05820; -. DR OMA; MDYGRVR; -. DR OrthoDB; EOG65QWFN; -. DR PhylomeDB; P44629; -. DR Proteomes; UP000000579; 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:0015293; F:symporter activity; IEA:UniProtKB-KW. DR InterPro; IPR026032; HcaT. DR InterPro; IPR024989; MFS_assoc_dom. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF12832; MFS_1_like; 1. DR PIRSF; PIRSF004925; HcaT; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00902; 2A0127; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 388 Probable 3-phenylpropionic acid FT transporter. FT /FTId=PRO_0000196190. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 5 31 Helical; Name=1. {ECO:0000250}. FT TOPO_DOM 32 37 Periplasmic. {ECO:0000250}. FT TRANSMEM 38 66 Helical; Name=2. {ECO:0000250}. FT TOPO_DOM 67 70 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 71 96 Helical; Name=3. {ECO:0000250}. FT TOPO_DOM 97 100 Periplasmic. {ECO:0000250}. FT TRANSMEM 101 119 Helical; Name=4. {ECO:0000250}. FT TOPO_DOM 120 130 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 131 153 Helical; Name=5. {ECO:0000250}. FT TOPO_DOM 154 156 Periplasmic. {ECO:0000250}. FT TRANSMEM 157 176 Helical; Name=6. {ECO:0000250}. FT TOPO_DOM 177 210 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 211 230 Helical; Name=7. {ECO:0000250}. FT TOPO_DOM 231 234 Periplasmic. {ECO:0000250}. FT TRANSMEM 235 259 Helical; Name=8. {ECO:0000250}. FT TOPO_DOM 260 269 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 270 289 Helical; Name=9. {ECO:0000250}. FT TOPO_DOM 290 292 Periplasmic. {ECO:0000250}. FT TRANSMEM 293 315 Helical; Name=10. {ECO:0000250}. FT TOPO_DOM 316 326 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 327 354 Helical; Name=11. {ECO:0000250}. FT TOPO_DOM 355 357 Periplasmic. {ECO:0000250}. FT TRANSMEM 358 378 Helical; Name=12. {ECO:0000250}. FT TOPO_DOM 379 388 Cytoplasmic. {ECO:0000250}. SQ SEQUENCE 388 AA; 43030 MW; 60A7258E1DC688D2 CRC64; MQVRPFYWLA LSFLGYYCAY GVFLPFFPAW LKSQQYGEEM IGLVIGSAYI FRFAGGLFFS SLIKKANHII IALRLLALAS AIIMAAMSLV AHNFWLLFIA IGLYASVNSA GMPIGDSLAS TWQRQIGLDY GKVRLIGSAA FILGVVVFGG MIGWVGEQNI VWILTALLSF YTIIQLLKPT IPPKDEIPED SVQNDVGFIA LLKNPMTLRV MIAVGLIQGS HAAYYVYSTI YWTSIGISVS QTSLLWGIGV LAEIVLFFFS RRLFQNISIS VLLYISALAC VGRWAVIGYI EDFWLIFLLQ LMHSLTYAVC HYAIVRYITT QPQSHIAKLQ GLYNGLSNGV LIAIFTAIAG MIYPTSPAMT FVFMSIIAAA AFFVIPRKLN AFLIVQHK // ID HFLC_HAEIN Reviewed; 295 AA. AC P44545; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 102. DE RecName: Full=Protein HflC; GN Name=hflC; OrderedLocusNames=HI_0150; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: HflC and HflK could regulate a protease. {ECO:0000250}. CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC 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; L42023; AAC21821.1; -; Genomic_DNA. DR PIR; I64050; I64050. DR RefSeq; NP_438320.1; NC_000907.1. DR RefSeq; WP_005660876.1; NC_000907.1. DR ProteinModelPortal; P44545; -. DR STRING; 71421.HI0150; -. DR MEROPS; I87.001; -. DR EnsemblBacteria; AAC21821; AAC21821; HI_0150. DR GeneID; 951060; -. DR KEGG; hin:HI0150; -. DR PATRIC; 20188793; VBIHaeInf48452_0153. DR eggNOG; ENOG4105EPW; Bacteria. DR eggNOG; COG0330; LUCA. DR KO; K04087; -. DR OMA; TRVDYVE; -. DR OrthoDB; EOG6B8XHM; -. DR PhylomeDB; P44545; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0052547; P:regulation of peptidase activity; IEA:InterPro. DR InterPro; IPR001107; Band_7. DR InterPro; IPR010200; HflC. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR Pfam; PF01145; Band_7; 1. DR PIRSF; PIRSF005651; HflC; 1. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. DR TIGRFAMs; TIGR01932; hflC; 2. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 295 Protein HflC. FT /FTId=PRO_0000094076. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 295 AA; 32902 MW; C5FC24E1ECCF42E3 CRC64; MRRFLLPVIF VIAAVVYSSI VVVTEGTRGI MLRFNKVQRD ADNKVVVYEP GLHFKVPLID SIKVLDARIR TLDGSATRFV TVEKKDLLVD SYVKWKISDF GRFYTSTGGG DYAQAANLLS RKVNDRLRSE IGSRTIKDIV SGTRGELMEG AKKALSSGQD STAELGIEVI DVRVKQINLP DEVSSSIYQR MRAERDAVAR EHRSQGKEKA AFIQADVDRK VTLILANANK TAQELRGSGD AAAAKLYSDA FAQEPQFFTF VRSLKAYEAS FANSDNIMIL KPDSDFFRFM QAPKK // ID HFQ_HAEIN Reviewed; 91 AA. AC P44437; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 97. DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436}; GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=HI_0411; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) CC and mRNAs to facilitate mRNA translational regulation in response CC to envelope stress, environmental stress and changes in metabolite CC concentrations. Also binds with high specificity to tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}. CC -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP- CC Rule:MF_00436}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22070.1; -; Genomic_DNA. DR PIR; D64066; D64066. DR RefSeq; NP_438573.1; NC_000907.1. DR RefSeq; WP_005693756.1; NC_000907.1. DR ProteinModelPortal; P44437; -. DR SMR; P44437; 4-70. DR STRING; 71421.HI0411; -. DR EnsemblBacteria; AAC22070; AAC22070; HI_0411. DR GeneID; 950678; -. DR KEGG; hin:HI0411; -. DR PATRIC; 20189373; VBIHaeInf48452_0430. DR eggNOG; ENOG4105KW8; Bacteria. DR eggNOG; COG1923; LUCA. DR KO; K03666; -. DR OMA; RRDGHAQ; -. DR OrthoDB; EOG68SW3W; -. DR PhylomeDB; P44437; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR HAMAP; MF_00436; Hfq; 1. DR InterPro; IPR005001; Hfq. DR InterPro; IPR010920; LSM_dom. DR SUPFAM; SSF50182; SSF50182; 1. DR TIGRFAMs; TIGR02383; Hfq; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding; Stress response. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 91 RNA-binding protein Hfq. FT /FTId=PRO_0000095642. SQ SEQUENCE 91 AA; 10250 MW; D5619D71B8236D60 CRC64; MAKGQSLQDP YLNALRRERI PVSIYLVNGI KLQGQIESFD QFVILLKNTV NQMVYKHAIS TVVPARSVSH HNNNHHTAPT EAVENVETQA E // ID HGP4_HAEIN Reviewed; 999 AA. AC Q57408; O86244; P96344; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 3. DT 17-FEB-2016, entry version 97. DE RecName: Full=Probable hemoglobin and hemoglobin-haptoglobin-binding protein 4; DE Flags: Precursor; GN OrderedLocusNames=HI_1565/HI_1567; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Acts as a receptor for hemoglobin or the CC hemoglobin/haptoglobin complex of the human host and is required CC for heme uptake. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: This protein is subject to phase-variable CC expression associated with alteration in the length of the CCAA CC repeat region. This mechanism is called slipped-strand mispairing. CC Addition or loss of CCAA repeat units would change the reading CC frame and result in introduction of stop codons downstream of the CC repeat region. This may be a mechanism of regulation and a way to CC avoid the immunological response of the host (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC Hemoglobin/haptoglobin binding protein subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23213.1; Type=Frameshift; Positions=49, 289; Note=The first frameshift is found in the repeats region.; Evidence={ECO:0000305}; CC Sequence=AAC23214.1; Type=Frameshift; Positions=49, 289; Note=The first frameshift is found in the repeats region.; 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; L42023; AAC23213.1; ALT_SEQ; Genomic_DNA. DR EMBL; L42023; AAC23214.1; ALT_SEQ; Genomic_DNA. DR PIR; A64130; A64130. DR ProteinModelPortal; Q57408; -. DR EnsemblBacteria; AAC23213; AAC23213; HI_1565. DR EnsemblBacteria; AAC23214; AAC23214; HI_1567. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR006970; PT. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF04886; PT; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Repeat; Signal; TonB box; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 999 Probable hemoglobin and hemoglobin- FT haptoglobin-binding protein 4. FT /FTId=PRO_0000034788. FT REPEAT 26 29 1. FT REPEAT 30 33 2. FT REPEAT 34 37 3. FT REPEAT 38 41 4. FT REPEAT 42 45 5. FT REPEAT 46 49 6. FT REGION 26 49 6 X 4 AA tandem repeats of P-T-N-Q. FT MOTIF 58 65 TonB box. FT MOTIF 982 999 TonB C-terminal box. SQ SEQUENCE 999 AA; 114315 MW; DAFCD4EB7000A876 CRC64; MTNFRLNVLA YSVMLGLTAS VAYAEPTNQP TNQPTNQPTN QPTNQPTNQN SNASEQLEQI NVLGSDNNND NTPPKIAETV KTASQLKRQQ VQDSRDLVRY ETGVTVVEAG RFGSSGYAIR GVDENRVAIT VDGLHQAETL SSQGFKELFE GYGNFNNTRN SVEIETLKVA KIAKGADSVK VGSGSLGGAV LFETKDARDF LTEKDWHIGY KAGYSTADNQ GLNAVTLAGR YQMFDALIMH SKRHGHELEN YDYKNGRDIQ GKEREKADPY TITKESTLVK FSFSPTENHR FTVASDTYLQ HSRGHDFSYN LVKTTYINKD EEELRHTNDL TKRKNVSFTY ENYTVTPFWD TLKLSYSQQR ITTRARTEDY CDGNEKCDSY KNPLGLQLKE GKVVDRNGDP VELKLVEDEQ GQKRHQVVDK YNNPFSVASG TNNDAFVGKQ LSPSEFWLDC SIFNCDKPVR VYKYQYSNQE PESKEVELNR TMEINGKKFA TYESNNYRDR YHMILPNSKG YLPLDYKERD LNTKTKQINL DLTKAFTLFE IENELSYGGV YAKTTKEMVN KAGYYGRNPT WWAERTLGKS LLNGLRTCKE DSSYNGLLCP RHEPKTSFLI PVETTTKSLY FADNIKLHNM LSVDLGYRYD DIKYQPEYIP GVTPKIADDM VRELFVPLPP ANGKDWQGNP VYTPEQIRKN AEENIAYIAQ EKRFKKHSYS LGATFDPLNF LRVQVKYSKG FRTPTSDELY FTFKHPDFTI LPNPNMKPEE AKNQEIALTF HHDWGFFSTN VFQTKYRQFI DLAYLGSRNL SNSVGGQAQA RDFQVYQNVN VDRAKVKGVE INSRLNIGYF FEKLDGFNVS YKFTYQRGRL DGNRPMNAIQ PKTSVIGLGY DHKEQRFGAD LYVTHVSAKK AKDTYNMFYK EQGYKDSAVR WRSDDYTLVD FVTYIKPVKN VTLQFGVYNL TDRKYLTWES ARSIKPFGTS NLINQGTGAG INRFYSPGRN YKLSAEITF // ID HEL_HAEIN Reviewed; 274 AA. AC P26093; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-MAY-2016, entry version 113. DE RecName: Full=Lipoprotein E; DE AltName: Full=Outer membrane protein P4; DE Short=OMP P4; DE Flags: Precursor; GN Name=hel; Synonyms=ompP4; OrderedLocusNames=HI_0693; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 263-274. RC STRAIN=RD / KW20B; RX PubMed=1715322; RA Green B.A., Farley J.E., Quinn-Dey T., Deich R.A., Zlotnick G.W.; RT "The e (P4) outer membrane protein of Haemophilus influenzae: biologic RT activity of anti-e serum and cloning and sequencing of the structural RT gene."; RL Infect. Immun. 59:3191-3198(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell outer 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; M68502; AAA51009.1; -; Genomic_DNA. DR EMBL; L42023; AAC22353.1; -; Genomic_DNA. DR PIR; B64087; B64087. DR RefSeq; NP_438853.1; NC_000907.1. DR RefSeq; WP_010869033.1; NC_000907.1. DR PDB; 3OCU; X-ray; 1.35 A; A=22-274. DR PDB; 3OCV; X-ray; 1.55 A; A=22-274. DR PDB; 3OCW; X-ray; 1.85 A; A=22-274. DR PDB; 3OCX; X-ray; 1.90 A; A=22-274. DR PDB; 3OCY; X-ray; 1.40 A; A=22-274. DR PDB; 3OCZ; X-ray; 1.35 A; A=22-274. DR PDB; 3SF0; X-ray; 1.35 A; A=22-274. DR PDBsum; 3OCU; -. DR PDBsum; 3OCV; -. DR PDBsum; 3OCW; -. DR PDBsum; 3OCX; -. DR PDBsum; 3OCY; -. DR PDBsum; 3OCZ; -. DR PDBsum; 3SF0; -. DR ProteinModelPortal; P26093; -. DR SMR; P26093; 31-274. DR STRING; 71421.HI0693; -. DR EnsemblBacteria; AAC22353; AAC22353; HI_0693. DR GeneID; 949723; -. DR KEGG; hin:HI0693; -. DR PATRIC; 20190007; VBIHaeInf48452_0725. DR eggNOG; ENOG4105CUR; Bacteria. DR eggNOG; COG2503; LUCA. DR OMA; LVKNCIK; -. DR OrthoDB; EOG6P8TN1; -. DR BioCyc; MetaCyc:MONOMER-8381; -. DR BRENDA; 3.1.3.2; 2529. DR EvolutionaryTrace; P26093; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR005519; Acid_phosphat_B-like. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006423; Lipo_e_P4. DR Pfam; PF03767; Acid_phosphat_B; 1. DR PIRSF; PIRSF019271; Acid_Ptase_C; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01533; lipo_e_P4; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 20 FT CHAIN 21 274 Lipoprotein E. FT /FTId=PRO_0000018178. FT LIPID 21 21 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 21 21 S-diacylglycerol cysteine. {ECO:0000305}. FT CONFLICT 30 30 G -> E (in Ref. 1; AAA51009). FT {ECO:0000305}. FT HELIX 30 38 {ECO:0000244|PDB:3OCU}. FT HELIX 41 49 {ECO:0000244|PDB:3OCU}. FT HELIX 51 70 {ECO:0000244|PDB:3OCU}. FT STRAND 78 83 {ECO:0000244|PDB:3OCU}. FT TURN 87 89 {ECO:0000244|PDB:3OCU}. FT HELIX 93 102 {ECO:0000244|PDB:3OCU}. FT HELIX 108 116 {ECO:0000244|PDB:3OCU}. FT HELIX 126 135 {ECO:0000244|PDB:3OCU}. FT STRAND 138 147 {ECO:0000244|PDB:3OCU}. FT TURN 148 151 {ECO:0000244|PDB:3OCU}. FT HELIX 152 162 {ECO:0000244|PDB:3OCU}. FT HELIX 169 171 {ECO:0000244|PDB:3OCU}. FT STRAND 172 177 {ECO:0000244|PDB:3OCU}. FT HELIX 182 190 {ECO:0000244|PDB:3OCU}. FT STRAND 193 202 {ECO:0000244|PDB:3OCU}. FT HELIX 203 206 {ECO:0000244|PDB:3OCU}. FT TURN 209 212 {ECO:0000244|PDB:3OCU}. FT HELIX 215 224 {ECO:0000244|PDB:3OCU}. FT HELIX 225 228 {ECO:0000244|PDB:3OCU}. FT TURN 230 232 {ECO:0000244|PDB:3OCU}. FT STRAND 233 235 {ECO:0000244|PDB:3OCU}. FT STRAND 239 242 {ECO:0000244|PDB:3OCZ}. FT HELIX 243 246 {ECO:0000244|PDB:3OCU}. FT HELIX 252 254 {ECO:0000244|PDB:3OCU}. FT HELIX 257 267 {ECO:0000244|PDB:3OCU}. SQ SEQUENCE 274 AA; 30431 MW; 047C693194155E6B CRC64; MKTTLKMTAL AALSAFVLAG CGSHQMKSEG HANMQLQQQA VLGLNWMQDS GEYKALAYQA YNAAKVAFDH AKVAKGKKKA VVADLDETML DNSPYAGWQV QNNKPFDGKD WTRWVDARQS RAVPGAVEFN NYVNSHNGKV FYVTNRKDST EKSGTIDDMK RLGFNGVEES AFYLKKDKSA KAARFAEIEK QGYEIVLYVG DNLDDFGNTV YGKLNADRRA FVDQNQGKFG KTFIMLPNAN YGGWEGGLAE GYFKKDTQGQ IKARLDAVQA WDGK // ID HGP3_HAEIN Reviewed; 1084 AA. AC P44836; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Probable hemoglobin and hemoglobin-haptoglobin-binding protein 3; DE Flags: Precursor; GN OrderedLocusNames=HI_0712; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Acts as a receptor for hemoglobin or the CC hemoglobin/haptoglobin complex of the human host and is required CC for heme uptake. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: This protein is subject to phase-variable CC expression associated with alteration in the length of the CCAA CC repeat region. This mechanism is called slipped-strand mispairing. CC Addition or loss of CCAA repeat units would change the reading CC frame and result in introduction of stop codons downstream of the CC repeat region. This may be a mechanism of regulation and a way to CC avoid the immunological response of the host (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC Hemoglobin/haptoglobin binding protein 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; L42023; AAC22369.1; -; Genomic_DNA. DR PIR; B64088; B64088. DR RefSeq; NP_438870.1; NC_000907.1. DR RefSeq; WP_010869038.1; NC_000907.1. DR ProteinModelPortal; P44836; -. DR STRING; 71421.HI0712; -. DR EnsemblBacteria; AAC22369; AAC22369; HI_0712. DR GeneID; 949735; -. DR KEGG; hin:HI0712; -. DR PATRIC; 20190045; VBIHaeInf48452_0743. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; NAFQNDY; -. DR OrthoDB; EOG6HB9KP; -. DR PhylomeDB; P44836; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR006970; PT. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF04886; PT; 2. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Repeat; Signal; TonB box; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 1084 Probable hemoglobin and hemoglobin- FT haptoglobin-binding protein 3. FT /FTId=PRO_0000034787. FT REPEAT 26 29 1. FT REPEAT 30 33 2. FT REPEAT 34 37 3. FT REPEAT 38 41 4. FT REPEAT 42 45 5. FT REPEAT 46 49 6. FT REPEAT 50 53 7. FT REPEAT 54 57 8. FT REPEAT 58 61 9. FT REPEAT 62 65 10. FT REPEAT 66 69 11. FT REPEAT 70 73 12. FT REGION 26 73 12 X 4 AA tandem repeats of Q-P-T-N. FT MOTIF 83 90 TonB box. FT MOTIF 1067 1084 TonB C-terminal box. SQ SEQUENCE 1084 AA; 123955 MW; 794DF91E0F53CFD9 CRC64; MTNFKFSLLA CSIAFALNAS TVYAAQPTNQ PTNQPTNQPT NQPTNQPTNQ PTNQPTNQPT NQPTNQPTNQ PTNQNSNVSE QLEQINVSGS SENINIKEKK VGETQISAKK LAKQQASDSR DLVRYETGIT VVETGRTGAS GYAVRGVDEN RVGIMVDGLR QAETLSSQGF KELFEGYGNF NNTRNSIEIE NVKTATITKG ADSLKSGSGA LGGSVIFETK DARDYLIDKD YYLSYKRGYQ TMNNQNLKTL TLAGRSKKFD ILIIDTTRDG HEIENYDYKI YPNKQADLRA VGPTREKADP YQITRQSTLI KLGFQPNENH RLSVALDDST LETKGIDLSY ALRPYSTAGN EKYGERIIND QSKRKNIQFS YENFSQTPFW DHIKLSYSSQ KITNKARSDE YCHQSTCNGV SNPQGLHLVE EGGVYKIVDK NGDKLTYNKN AGWYGQFQNK NGENVDNDID STGGSLDSVL IDCERLNCKN KFQVFVEKDE EGKDKYEYEE RDIIVETLPN GKKYGKITLK KGKTPLWDDV YQEESARFLF PKSYGYSTDF VNDRDLNTNT QQIKLDLDKE FSLWHTQHSL KYGGFYEKTL KSMVNHQYNT VANVQWWAGN FFCNKLENGK RTPAPDYSHR CSLMNTDKGK ETYLIPVTTK NNVLYFGDNV QLTSWLGLDL NYRYDHVKYL PSYDEKIPVP NGLITGLFKK FGPKDYVYGS KYSKPADYTD CTYNSDCYKK NFKDNLALLL RKTDYKHHSY NLGLNLDPTD WLRVQLKYAN GFRAPTSDEI YMTFKHPQFS IQPNTDLKAE TSKTKEVAFT FYKNSSYITL NAFQNDYRNF IDLVEVGPRP IEEGSTIAYP FHQNQNRDRA RVRGIEIASR LEMGDLFEKL QGFHLGYKFT YQKGRIKDNG LNPKYKEFLE LNKDKHPEYE AIARKPQPMN ALQPTTSVYN IGYDAPSQKW GVDMYITNVA AKKAKDSFNS QWTSMVKRKE KIYGNEKDAE ASTANGKEVK DSRGLWRNNR YTVIDTIAYW KPIKNLTFTA GVYNLTNKKY LTWDSARSIR HLGTINRVET ATGKGLNRFY APGRNYRMSV QFEF // ID HBPA_HAEIN Reviewed; 547 AA. AC P33950; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 109. DE RecName: Full=Heme-binding protein A; DE AltName: Full=Hemin-binding lipoprotein; DE Flags: Precursor; GN Name=hbpA; Synonyms=dppA; OrderedLocusNames=HI_0853; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=DL42 / Serotype B; RX PubMed=1339409; RA Hanson M.S., Slaughter C., Hansen E.J.; RT "The hbpA gene of Haemophilus influenzae type b encodes a heme-binding RT lipoprotein conserved among heme-dependent Haemophilus species."; RL Infect. Immun. 60:2257-2266(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=DL42 / Serotype B; RX PubMed=2041470; DOI=10.1111/j.1365-2958.1991.tb02107.x; RA Hanson M.S., Hansen E.J.; RT "Molecular cloning, partial purification, and characterization of a RT haemin-binding lipoprotein from Haemophilus influenzae type b."; RL Mol. Microbiol. 5:267-278(1991). CC -!- FUNCTION: Important role in heme acquisition or metabolism. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:2041470}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303, ECO:0000269|PubMed:2041470}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22512.1; 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; M88134; AAA73214.1; ALT_SEQ; Genomic_DNA. DR EMBL; M84028; AAA24962.1; -; Genomic_DNA. DR EMBL; L42023; AAC22512.1; ALT_INIT; Genomic_DNA. DR PIR; D64098; D64098. DR PIR; T45066; T45066. DR RefSeq; NP_439013.1; NC_000907.1. DR RefSeq; WP_010869071.1; NC_000907.1. DR ProteinModelPortal; P33950; -. DR SMR; P33950; 41-545. DR STRING; 71421.HI0853; -. DR TCDB; 3.A.1.5.27; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22512; AAC22512; HI_0853. DR GeneID; 949866; -. DR KEGG; hin:HI0853; -. DR PATRIC; 20190361; VBIHaeInf48452_0894. DR eggNOG; ENOG4105DEF; Bacteria. DR eggNOG; COG0747; LUCA. DR KO; K12368; -. DR OMA; FKAMKFP; -. DR OrthoDB; EOG63C0PB; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0042938; P:dipeptide transport; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000305}. FT CHAIN 19 547 Heme-binding protein A. FT /FTId=PRO_0000031790. FT LIPID 19 19 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 19 19 S-diacylglycerol cysteine. {ECO:0000305}. FT VARIANT 48 49 KA -> NS (in strain: DL42). FT VARIANT 181 181 T -> N (in strain: DL42). FT VARIANT 240 240 H -> N (in strain: DL42). FT VARIANT 343 343 T -> I (in strain: DL42). FT VARIANT 375 375 A -> V (in strain: DL42). SQ SEQUENCE 547 AA; 60661 MW; 7755E2164A40CB31 CRC64; MKLKATLTLA AATLVLAACD QSSSANKSTA QTEAKSSSNN TFVYCTAKAP LGFSPALIIE GTSYNASSQQ VYNRLVEFKK GSTDIEPALA ESWEISDDGL SYTFHLRKGV KFHTTKEFTP TRDFNADDVV FSFQRQLDPN HPYHNVSKGT YPYFKAMKFP ELLKSVEKVD DNTIRITLNK TDATFLASLG MDFISIYSAE YADSMLKAGK PETLDSRPVG TGPFVFVDYK TDQAIQYVAH ENYWKGRTPL DRLVISIVPD ATTRYAKLQA GTCDLILFPN VADLAKMKTD PKVQLLEQKG LNVAYIAFNT EKAPFDNVKV RQALNYAVDK KAIIEAVYQG AGTSAKNPLP PTIWSYNDEI QDYPYDPEKA KQLLAEAGYP NGFETDFWIQ PVIRASNPNP KRMAELIMAD WAKIGVKTNP VTYEWADYRK RAKEGELTAG IFGWSGDNGD PDNFLSPLLG SSNIGNSNMA RFNNSEFDAL LNEAIGLTNK EERAKLYKQA QVIVHNQAPW IPVAHSVGFA PLSPRVKGYV QSPFGYDAFY GVSVDGK // ID HIS1_HAEIN Reviewed; 303 AA. AC P43853; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=ATP phosphoribosyltransferase; DE Short=ATP-PRT; DE Short=ATP-PRTase; DE EC=2.4.2.17; GN Name=hisG; OrderedLocusNames=HI_0468; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a CC crucial role in the pathway because the rate of histidine CC biosynthesis seems to be controlled primarily by regulation of CC HisG enzymatic activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Feedback inhibited by histidine. {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. CC Long 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; L42023; AAC22127.1; -; Genomic_DNA. DR PIR; D64070; D64070. DR RefSeq; NP_438629.1; NC_000907.1. DR RefSeq; WP_005656529.1; NC_000907.1. DR ProteinModelPortal; P43853; -. DR SMR; P43853; 10-303. DR STRING; 71421.HI0468; -. DR PRIDE; P43853; -. DR EnsemblBacteria; AAC22127; AAC22127; HI_0468. DR GeneID; 949555; -. DR KEGG; hin:HI0468; -. DR PATRIC; 20189491; VBIHaeInf48452_0488. DR eggNOG; ENOG4105E21; Bacteria. DR eggNOG; COG0040; LUCA. DR KO; K00765; -. DR OMA; CDIVSSG; -. DR OrthoDB; EOG66MQT3; -. DR PhylomeDB; P43853; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.120; -; 1. DR HAMAP; MF_00079; HisG_Long; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long. DR InterPro; IPR013115; HisG_C. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR PANTHER; PTHR21403; PTHR21403; 1. DR Pfam; PF01634; HisG; 1. DR Pfam; PF08029; HisG_C; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR TIGRFAMs; TIGR00070; hisG; 1. DR TIGRFAMs; TIGR03455; HisG_C-term; 1. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 303 ATP phosphoribosyltransferase. FT /FTId=PRO_0000151852. SQ SEQUENCE 303 AA; 33821 MW; 08C14D1F6E98A31D CRC64; MTNTTMQPNR LRIALQKKGR LSQDCAILLK QCGVKINWNE QRLIAYAENL PIEILRVRDD DIPGLIFDGV VDLGIIGENV LEEEELGRRA ANETVTYKKL RQLDFGDCRL SLAVDRDCHY ENVKDLANRR IATSYPHLLK RYMNENGVSF KSCLLNGSVE VAPSAGIAYA ICDLVSSGAT LEANGLKEVD VIYRSKACLI QRAEPLESTK QALVDKLLTR IQGVQQAAES KYIMLHAPKE KLEKITALLP GVENPTILPL ASDTTRVAMH VVSQENLFWE TMEQLKEAGA SSILVLPIEK MME // ID HIS2_HAEIN Reviewed; 221 AA. AC P44434; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE; DE Includes: DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase; DE Short=PRA-CH; DE EC=3.5.4.19; DE Includes: DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=HI_0475; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-AMP + diphosphate. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- CC ribosylamino)methylideneamino)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22134.1; -; Genomic_DNA. DR PIR; A64071; A64071. DR RefSeq; NP_438636.1; NC_000907.1. DR RefSeq; WP_005649391.1; NC_000907.1. DR ProteinModelPortal; P44434; -. DR STRING; 71421.HI0475; -. DR PRIDE; P44434; -. DR EnsemblBacteria; AAC22134; AAC22134; HI_0475. DR GeneID; 949566; -. DR KEGG; hin:HI0475; -. DR PATRIC; 20189505; VBIHaeInf48452_0495. DR eggNOG; ENOG4105K8F; Bacteria. DR eggNOG; COG0139; LUCA. DR eggNOG; COG0140; LUCA. DR KO; K11755; -. DR OMA; ERSCFHQ; -. DR OrthoDB; EOG6PGKB6; -. DR PhylomeDB; P44434; -. DR UniPathway; UPA00031; UER00007. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01019; HisIE; 1. DR HAMAP; MF_01020; HisE; 1. DR InterPro; IPR023019; His_synth_HisIE. DR InterPro; IPR008179; PRib-ATP_PPHydrolase. DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR Pfam; PF01502; PRA-CH; 1. DR Pfam; PF01503; PRA-PH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 221 Histidine biosynthesis bifunctional FT protein HisIE. FT /FTId=PRO_0000136415. FT REGION 1 121 Phosphoribosyl-AMP cyclohydrolase. FT REGION 122 221 Phosphoribosyl-ATP pyrophosphohydrolase. SQ SEQUENCE 221 AA; 25097 MW; C79C7B68E297B529 CRC64; MNITKIDWQK VNGLLPVIIQ NISTREVLML GYMNEEALTK TIKERKVTFF SRTKQRLWTK GEISGNFLNV EEMSLDCDND TLLILVDPIG ATCHTGEYSC FHQFTSPQSE NKKQQFANWA WFIKLEQHLK EKKNADPSNS YTATLHAKGT KKIAQKVGEE GVETALAAVA QDKAEVISEA TDLVYHLTVL LHNQDLQWYE IIAKLQERHQ GIGLHPEGGN K // ID HEMY_HAEIN Reviewed; 428 AA. AC P44772; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Protein HemY homolog; GN Name=hemY; OrderedLocusNames=HI_0602; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a late step of protoheme IX synthesis. CC {ECO:0000250}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {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; L42023; AAC22260.1; -; Genomic_DNA. DR PIR; C64080; C64080. DR RefSeq; NP_438760.1; NC_000907.1. DR RefSeq; WP_005694537.1; NC_000907.1. DR STRING; 71421.HI0602; -. DR EnsemblBacteria; AAC22260; AAC22260; HI_0602. DR GeneID; 949653; -. DR KEGG; hin:HI0602; -. DR PATRIC; 20189781; VBIHaeInf48452_0625. DR eggNOG; ENOG410601J; Bacteria. DR eggNOG; COG3071; LUCA. DR KO; K02498; -. DR OMA; CTQITRL; -. DR OrthoDB; EOG6T1WNH; -. DR PhylomeDB; P44772; -. DR UniPathway; UPA00252; -. DR Proteomes; UP000000579; 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:0042168; P:heme metabolic process; IEA:InterPro. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR005254; Heme_biosyn_assoc_TPR_pro. DR InterPro; IPR010817; HemY_N. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF07219; HemY_N; 1. DR TIGRFAMs; TIGR00540; TPR_hemY_coli; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Porphyrin biosynthesis; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 428 Protein HemY homolog. FT /FTId=PRO_0000135278. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. SQ SEQUENCE 428 AA; 48776 MW; 8654FAC94689CB5C CRC64; MFRVLFLMLT LLVGLVAGPY ISGQQGYVRI ETANRIIEMS ITTLVIFFII SLAIIYAFEW GVTRFFRLSR SSYQWFSNRK RVKAQKQTLE GLVKMDEGDY AKAEKLIGKN AKHSAEPVLN LIKAAEAAQQ RGDEFSANRY LIEATELAGS DNLLVEIART RILLQQNKLP AARSSVDSLL EMARRNKEVL KLAVEIYLRS KAYQALDKIL DNVANSGLFN DEEFKDLRSK TENGLLDEKM NEEGIDGLLT WWNQQPRHRR NNIELKISLI QRLIDCNDHE SATELTFEIL KKLGDNTAIS LPLCTQITRL QPEDNSKLLK LIEKRAKRVD EKQKCCINRA LGYLYVRNNE FIKAADVFKN VIACPEQLEQ NDLMMASYVF EQAGDKALAE QVRQESLKSV MAIQDVIPES AEEKTEENST ALLESKSE // ID HGP2_HAEIN Reviewed; 999 AA. AC P44809; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 3. DT 16-MAR-2016, entry version 112. DE RecName: Full=Probable hemoglobin and hemoglobin-haptoglobin-binding protein 2; DE Flags: Precursor; GN OrderedLocusNames=HI_0661; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Acts as a receptor for hemoglobin or the CC hemoglobin/haptoglobin complex of the human host and is required CC for heme uptake. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: This protein is subject to phase-variable CC expression associated with alteration in the length of the CCAA CC repeat region. This mechanism is called slipped-strand mispairing. CC Addition or loss of CCAA repeat units would change the reading CC frame and result in introduction of stop codons downstream of the CC repeat region. This may be a mechanism of regulation and a way to CC avoid the immunological response of the host (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC Hemoglobin/haptoglobin binding protein subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22319.1; Type=Frameshift; Positions=6, 53; Note=In the leader peptide and the repeats region.; 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; L42023; AAC22319.1; ALT_SEQ; Genomic_DNA. DR PIR; I64084; I64084. DR RefSeq; NP_438821.1; NC_000907.1. DR ProteinModelPortal; P44809; -. DR STRING; 71421.HI0661; -. DR EnsemblBacteria; AAC22319; AAC22319; HI_0661. DR GeneID; 949701; -. DR KEGG; hin:HI0661; -. DR PATRIC; 20189937; VBIHaeInf48452_0690. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; YAEGFRT; -. DR OrthoDB; EOG6HB9KP; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR006970; PT. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF04886; PT; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Repeat; Signal; TonB box; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 999 Probable hemoglobin and hemoglobin- FT haptoglobin-binding protein 2. FT /FTId=PRO_0000034786. FT REPEAT 26 29 1. FT REPEAT 30 33 2. FT REPEAT 34 37 3. FT REPEAT 38 41 4. FT REPEAT 42 45 5. FT REPEAT 46 49 6. FT REPEAT 50 53 7. FT REGION 26 53 7 X 4 AA tandem repeats of Q-P-T-N. FT MOTIF 63 70 TonB box. FT MOTIF 982 999 TonB C-terminal box. SQ SEQUENCE 999 AA; 114690 MW; 1A17AAB220092B7D CRC64; MTNFRLNVLA YSVMLGLTAG VAYAAQPTNQ PTNQPTNQPT NQPTNQPTNQ PTNQNSNVSE QLEQINVSGS TENSDTKTPP KIAETVKTAK TLEREQANNI KDIVKYETGV TVVEAGRFGQ SGFAIRGVDE NRVAINIDGL RQAETLSSQG FKELFEGYGN FNNTRNGAEI ETLKEVNITK GADSIKNGSG SLGGSVIYKT KDARDYLINK DYYVSYKKGY ATENNQSFDT LTLAGRYKKF DVLVVTTSRN GHELENYGYK NYNDKIQGKK REKADPYKIE QDSTLLKLSF NPTENHRFTF AADLYEHRSR GQDLSYTLKY QRSGNETPEV DSRHTNDKTK RRNISFSYEN FSQTPFWDTL KLTYSDQRIK TRARTDEYCD AGVRHCEGTD NPTGLKVTNG KITRRDGSDL QFEEKNNTAK SSDKTYDFKK FIDTDKRVID DKLVLNNPSD TWYDCSIFNC ENNAKIKVFK GNNYYGYDGK WKEVDLEIKE LNGKKFAKIK DNDRKIKSIL PSSPGYLERL WQERDLDTNT QQLNLDLTKD FKIWHIEHNL QYGGSYNTAM KRMVNRAGND ASDVQWWATP TLGEDSWTGK PHTCATTYEW NANLCPRVDP EFSYLLPIKT TGKSVYLFDN FVITDYLSFD LGYRYDNIHY QPKYKHGITP KLPDDIVKGL FIPLPNNSNS DPNKVKENVQ QNIDYIAKQN KKYKAHSYSF VSTIDPTSFL RLQLKYSKGF RTPTSDEMYF TFKHPDFTIL PNTDLKPEIA KTKEIAFTLH NDDWGFISTS LFKTNYKNFI DLIFKKQETF KVGGSGRGET LPFSLYQNIN RDNASLKGIE INSKVFLGKM AKFMDGFNLS YKYTYQKGRM NGNIPMNAIQ PRTMVYGLGY DHPNHKFGFD FYTTHVASKN PEDTYNMFYK EENKKDSTIK WRSKSYTILD LIGYVQPIKN LTIRAGVYNL TNRKYITWDS ARSIRSFGTS NVIDQSTGLG INRFYAPGRN YKMSVQFEF // ID HIS7_HAEIN Reviewed; 362 AA. AC P44327; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 114. DE RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022}; DE Includes: DE RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022}; DE EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022}; DE Includes: DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022}; DE Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022}; DE EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022}; GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022}; GN OrderedLocusNames=HI_0471; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol CC + phosphate. {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9. CC {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- SIMILARITY: In the N-terminal section; belongs to the histidinol- CC phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC imidazoleglycerol-phosphate dehydratase family. CC {ECO:0000255|HAMAP-Rule:MF_01022}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22130.1; -; Genomic_DNA. DR PIR; F64070; F64070. DR RefSeq; NP_438632.1; NC_000907.1. DR RefSeq; WP_005693690.1; NC_000907.1. DR ProteinModelPortal; P44327; -. DR SMR; P44327; 2-160. DR STRING; 71421.HI0471; -. DR EnsemblBacteria; AAC22130; AAC22130; HI_0471. DR GeneID; 949564; -. DR KEGG; hin:HI0471; -. DR PATRIC; 20189497; VBIHaeInf48452_0491. DR eggNOG; ENOG4105ECC; Bacteria. DR eggNOG; COG0131; LUCA. DR eggNOG; COG0241; LUCA. DR KO; K01089; -. DR OMA; PEDTFWP; -. DR OrthoDB; EOG60PHGP; -. DR PhylomeDB; P44327; -. DR UniPathway; UPA00031; UER00011. DR UniPathway; UPA00031; UER00013. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1000; -; 1. DR HAMAP; MF_00076; HisB; 1. DR HAMAP; MF_01022; Bifunc_HisB; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR020566; His_synth_bifunc_HisB. DR InterPro; IPR005954; HisB_N. DR InterPro; IPR006543; Histidinol-phos. DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase. DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 2. DR Pfam; PF00475; IGPD; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01261; hisB_Nterm; 1. DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1. DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1. DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Lyase; Magnesium; Metal-binding; KW Multifunctional enzyme; Reference proteome; Zinc. FT CHAIN 1 362 Histidine biosynthesis bifunctional FT protein HisB. FT /FTId=PRO_0000158210. FT REGION 1 173 Histidinol-phosphatase. FT {ECO:0000255|HAMAP-Rule:MF_01022}. FT REGION 174 362 Imidazoleglycerol-phosphate dehydratase. FT {ECO:0000255|HAMAP-Rule:MF_01022}. FT ACT_SITE 8 8 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01022}. FT ACT_SITE 10 10 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01022}. FT METAL 8 8 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01022}. FT METAL 10 10 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01022}. FT METAL 91 91 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022}. FT METAL 93 93 Zinc; via pros nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01022}. FT METAL 99 99 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022}. FT METAL 101 101 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022}. FT METAL 128 128 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01022}. SQ SEQUENCE 362 AA; 41162 MW; A031E606EAD2EAE5 CRC64; MQPTLFIDRD GTLIDEPKTD FQIDSLEKLK LEPKVIPALL RLKAKYRFVI VSNQDGLGTD AFPQTDFDKP HNVMMALFES QGITFDEVLI CPHKPEENCL CRKPKIKLLD HYIRKNLFDI DRSFVIGDRE TDVQLAENLG IRAIQYDPQK MNWDLIAEKL LGETVTNCGK RPPRFAEVIR QTKETDIKVQ VWLDEAGVNE IKTGVGFFDH MLDQIATHGG FRMNVQCKGD LWIDEHHTVE DTALALGQAL KQAVGDKRGI ARFGFVLPMD ECKAECALDL SGRPWIKFNA CFKRDKVGDF STELTEHFFQ SLAFSMLATL HLNVTGNNDH HKIESLFKAF GRTLRQAIRI EGNEMPSSKG VL // ID HOLA_HAEIN Reviewed; 344 AA. AC P43747; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=DNA polymerase III subunit delta; DE EC=2.7.7.7; GN Name=holA; OrderedLocusNames=HI_0923; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 delta subunit seems to interact with the gamma subunit to CC transfer the beta subunit on the DNA (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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22583.1; -; Genomic_DNA. DR PIR; A64103; A64103. DR RefSeq; NP_439083.1; NC_000907.1. DR RefSeq; WP_005693269.1; NC_000907.1. DR ProteinModelPortal; P43747; -. DR STRING; 71421.HI0923; -. DR PRIDE; P43747; -. DR EnsemblBacteria; AAC22583; AAC22583; HI_0923. DR GeneID; 949921; -. DR KEGG; hin:HI0923; -. DR PATRIC; 20190501; VBIHaeInf48452_0964. DR eggNOG; ENOG4105DJF; Bacteria. DR eggNOG; COG1466; LUCA. DR KO; K02340; -. DR OMA; RQQGFDE; -. DR OrthoDB; EOG6BCSPJ; -. DR PhylomeDB; P43747; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR032780; DNA_pol3_delt_C. DR InterPro; IPR010372; DNA_pol3_delta_N. DR InterPro; IPR005790; DNA_polIII_delta. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF14840; DNA_pol3_delt_C; 1. DR Pfam; PF06144; DNA_pol3_delta; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01128; holA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed DNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 344 DNA polymerase III subunit delta. FT /FTId=PRO_0000105506. SQ SEQUENCE 344 AA; 39845 MW; 5048DF5A42A97B5F CRC64; MNRIFPEQLN HHLAQGLARV YLLQGQDPLL LSETEDTICQ VANLQGFDEK NTIQVDSQTD WAQLIESCQS IGLFFSKQIL SLNLPENFTA LLQKNLQELI SVLHKDVLLI LQVAKLAKGI EKQTWFITLN QYEPNTILIN CQTPTVENLP RWVKNRTKAM GLDADNEAIQ QLCYSYENNL LALKQALQLL DLLYPDHKLN YNRVISVVEQ SSIFTPFQWI DALLVGKANR AKRILKGLQA EDVQPVILLR TLQRELFTLL ELTKPQQRIV TTEKLPIQQI KTEFDRLKIW QNRRPLFLSA IQRLTYQTLY EIIQELANIE RLAKQEFSDE VWIKLADLSV KICL // ID HOLD_HAEIN Reviewed; 134 AA. AC P43750; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=DNA polymerase III subunit psi; DE EC=2.7.7.7; GN Name=holD; OrderedLocusNames=HI_0011; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 exact function of the psi subunit is unknown (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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21689.1; -; Genomic_DNA. DR PIR; E64042; E64042. DR RefSeq; NP_438184.1; NC_000907.1. DR RefSeq; WP_005663309.1; NC_000907.1. DR ProteinModelPortal; P43750; -. DR STRING; 71421.HI0011; -. DR EnsemblBacteria; AAC21689; AAC21689; HI_0011. DR GeneID; 950908; -. DR KEGG; hin:HI0011; -. DR PATRIC; 20188473; VBIHaeInf48452_0011. DR eggNOG; ENOG4108WPU; Bacteria. DR eggNOG; COG3050; LUCA. DR KO; K02344; -. DR OMA; IRFITVS; -. DR OrthoDB; EOG6WDSJJ; -. DR PhylomeDB; P43750; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; 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; 3.40.50.10220; -; 1. DR InterPro; IPR004615; DNA_pol_III_psi. DR InterPro; IPR018382; DNA_pol_III_psi_subgr. DR Pfam; PF03603; DNA_III_psi; 1. DR PIRSF; PIRSF029225; DNA_pol_III_psi; 1. DR SUPFAM; SSF102220; SSF102220; 1. DR TIGRFAMs; TIGR00664; DNA_III_psi; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed DNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 134 DNA polymerase III subunit psi. FT /FTId=PRO_0000105521. SQ SEQUENCE 134 AA; 15718 MW; EFBFED319F5B8623 CRC64; MNRRDLLLQE MGISQWELYR PEVLQGSVGI SVAENIRLIT VSDENISSSP LLADVLLSLN LKKENCLCLN YDQIQHMECK QPIRYWLLSE NSDQIDRTLP FCKQAEQVYR SPSWQQFQSN HQAKRALWQQ IQQP // ID HFLD_HAEIN Reviewed; 205 AA. AC P44796; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=High frequency lysogenization protein HflD homolog {ECO:0000255|HAMAP-Rule:MF_00695}; GN Name=hflD {ECO:0000255|HAMAP-Rule:MF_00695}; GN OrderedLocusNames=HI_0638; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000255|HAMAP-Rule:MF_00695}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00695}; Cytoplasmic side CC {ECO:0000255|HAMAP-Rule:MF_00695}. CC -!- SIMILARITY: Belongs to the HflD family. {ECO:0000255|HAMAP- CC Rule:MF_00695}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22298.1; -; Genomic_DNA. DR PIR; I64155; I64155. DR RefSeq; NP_438798.1; NC_000907.1. DR RefSeq; WP_005694504.1; NC_000907.1. DR ProteinModelPortal; P44796; -. DR SMR; P44796; 2-204. DR STRING; 71421.HI0638; -. DR EnsemblBacteria; AAC22298; AAC22298; HI_0638. DR GeneID; 950538; -. DR KEGG; hin:HI0638; -. DR PATRIC; 20189883; VBIHaeInf48452_0666. DR eggNOG; ENOG41075W9; Bacteria. DR eggNOG; COG2915; LUCA. DR KO; K07153; -. DR OMA; RADSETF; -. DR OrthoDB; EOG6J1DBP; -. DR PhylomeDB; P44796; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 1.10.3890.10; -; 1. DR HAMAP; MF_00695; HflD_protein; 1. DR InterPro; IPR007451; UPF0274. DR Pfam; PF04356; DUF489; 1. DR ProDom; PD037115; UPF0274; 1. DR SUPFAM; SSF101322; SSF101322; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW Membrane; Reference proteome. FT CHAIN 1 205 High frequency lysogenization protein FT HflD homolog. FT /FTId=PRO_0000071580. SQ SEQUENCE 205 AA; 23235 MW; 81F31B0186BF82DA CRC64; MKNYHDIVLA LAGVCQSAKL VHQLATESRA DSETFLTALN SLFITQPQRI EDVFGGEVRH LKLGLETLIH QLNAQGDQNL TRYWLSLLAL EGKLSKNSDA KQTLGNRISR LKEQEIHYAR DSETMLSIMA NIYSDIISPL GKKIHILGSP DYLRQELVQN KIRAVLLAGI RSAVLWKQMG GTKWQILFFR RKLLATAKQI YSSIY // ID HINT_HAEIN Reviewed; 116 AA. AC P44956; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Purine nucleoside phosphoramidase {ECO:0000250|UniProtKB:P0ACE7}; DE EC=3.9.1.- {ECO:0000250|UniProtKB:P0ACE7}; DE AltName: Full=Histidine triad nucleotide binding protein HI_0961; DE Short=HIT protein; GN OrderedLocusNames=HI_0961; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Hydrolyzes purine nucleotide phosphoramidates, including CC adenosine 5'monophosphoramidate (AMP-NH2), adenosine CC 5'monophosphomorpholidate (AMP-morpholidate), guanosine CC 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine CC 5'guanosine monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N- CC epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine CC tRNA ligase and lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine CC methyl ester)). {ECO:0000250|UniProtKB:P0ACE7}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0ACE7}. CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HIT domain. {ECO:0000255|PROSITE- CC ProRule:PRU00464}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22621.1; 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; L42023; AAC22621.1; ALT_INIT; Genomic_DNA. DR PIR; G64162; G64162. DR RefSeq; NP_439122.2; NC_000907.1. DR RefSeq; WP_005627389.1; NC_000907.1. DR ProteinModelPortal; P44956; -. DR STRING; 71421.HI0961; -. DR EnsemblBacteria; AAC22621; AAC22621; HI_0961. DR GeneID; 950594; -. DR KEGG; hin:HI0961; -. DR PATRIC; 20190581; VBIHaeInf48452_1003. DR eggNOG; ENOG4105K59; Bacteria. DR eggNOG; COG0537; LUCA. DR KO; K02503; -. DR OMA; IPTTNDV; -. DR OrthoDB; EOG69GZSV; -. DR PhylomeDB; P44956; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW Complete proteome; Hydrolase; Nucleotide-binding; Reference proteome. FT CHAIN 1 116 Purine nucleoside phosphoramidase. FT /FTId=PRO_0000109833. FT DOMAIN 6 115 HIT. {ECO:0000255|PROSITE- FT ProRule:PRU00464}. FT NP_BIND 30 32 Purine nucleotide phosphoramidate. FT {ECO:0000250|UniProtKB:P0ACE7}. FT NP_BIND 96 97 Purine nucleotide phosphoramidate. FT {ECO:0000250|UniProtKB:P0ACE7}. FT NP_BIND 101 103 Purine nucleotide phosphoramidate. FT {ECO:0000250|UniProtKB:P0ACE7}. FT MOTIF 99 105 Histidine triad motif. FT {ECO:0000250|UniProtKB:P0ACE7}. FT ACT_SITE 101 101 Tele-AMP-histidine intermediate. FT {ECO:0000250|UniProtKB:P0ACE7}. FT BINDING 88 88 Purine nucleotide phosphoramidate. FT {ECO:0000250|UniProtKB:P0ACE7}. SQ SEQUENCE 116 AA; 12887 MW; 904B9A3211757F12 CRC64; MAEETIFSKI IRKEIPANIV YQDELVTAFR DISPQAKTHI LIIPNKVIPT VNDVTEQDEV ALGRLFSVAA KLAKEEGVAE DGYRLIVNCN KHGGQEVFHL HMHLVGGEPL GRMLAK // ID HEMH_HAEIN Reviewed; 323 AA. AC P43868; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Ferrochelatase; DE EC=4.99.1.1; DE AltName: Full=Heme synthase; DE AltName: Full=Protoheme ferro-lyase; GN Name=hemH; Synonyms=visA; OrderedLocusNames=HI_1160; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+). CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ferrochelatase 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; L42023; AAC22815.1; -; Genomic_DNA. DR PIR; I64186; I64186. DR RefSeq; NP_439318.1; NC_000907.1. DR RefSeq; WP_005693475.1; NC_000907.1. DR ProteinModelPortal; P43868; -. DR STRING; 71421.HI1160; -. DR DNASU; 950120; -. DR EnsemblBacteria; AAC22815; AAC22815; HI_1160. DR GeneID; 950120; -. DR KEGG; hin:HI1160; -. DR PATRIC; 20190999; VBIHaeInf48452_1212. DR eggNOG; ENOG4105CFX; Bacteria. DR eggNOG; COG0276; LUCA. DR KO; K01772; -. DR OMA; WEEGSPL; -. DR OrthoDB; EOG6XHC5H; -. DR PhylomeDB; P43868; -. DR UniPathway; UPA00252; UER00325. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004325; F:ferrochelatase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central. DR HAMAP; MF_00323; Ferrochelatase; 1. DR InterPro; IPR001015; Ferrochelatase. DR InterPro; IPR019772; Ferrochelatase_AS. DR PANTHER; PTHR11108; PTHR11108; 1. DR Pfam; PF00762; Ferrochelatase; 1. DR TIGRFAMs; TIGR00109; hemH; 1. DR PROSITE; PS00534; FERROCHELATASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Heme biosynthesis; Iron; Lyase; KW Metal-binding; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 323 Ferrochelatase. FT /FTId=PRO_0000175147. FT METAL 196 196 Iron. {ECO:0000250}. FT METAL 277 277 Iron. {ECO:0000250}. SQ SEQUENCE 323 AA; 37089 MW; 8D61C4FEE599A74D CRC64; MTKPAKIGVL LANLGTPDSP TPKSISRYLW QFLTDPRVVD LPRCKWYPLL KAIILPLRSK RIAKNYQAIW TEQGSPLLAI SRQQKDALQA YLDNQNIDTQ VEIAMTYGNP SMQSAVKNLL KNQVERIIVL PLYPQYSSST TGAVFDAFAN ALKEERGLLP FDFIHSYHID ENYINALADS IKVRLKSDEF LLFSYHGIPL RYEKMGDYYR EHCKQTTIAV VNKLGLTENQ WRMTFQSRFG REEWLQPYTD KFLESAAAQN IQKIAVICPG FSVDCLETIE EIDEENRENF LNNGGQSYQY IPALNVEHAH IEMMGKLILE KLT // ID HIS4_HAEIN Reviewed; 249 AA. AC P44435; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=HI_0473; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho- CC beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5- CC ((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22132.1; -; Genomic_DNA. DR PIR; H64070; H64070. DR RefSeq; NP_438634.1; NC_000907.1. DR RefSeq; WP_005649383.1; NC_000907.1. DR ProteinModelPortal; P44435; -. DR STRING; 71421.HI0473; -. DR EnsemblBacteria; AAC22132; AAC22132; HI_0473. DR GeneID; 949519; -. DR KEGG; hin:HI0473; -. DR PATRIC; 20189501; VBIHaeInf48452_0493. DR eggNOG; ENOG4105CJV; Bacteria. DR eggNOG; COG0106; LUCA. DR KO; K01814; -. DR OMA; EWLHLVD; -. DR OrthoDB; EOG6H1Q3W; -. DR PhylomeDB; P44435; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA. DR InterPro; IPR023016; Isoase_HisA. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00007; TIGR00007; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Isomerase; Reference proteome. FT CHAIN 1 249 1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] FT imidazole-4-carboxamide isomerase. FT /FTId=PRO_0000142010. FT ACT_SITE 11 11 Proton acceptor. {ECO:0000250}. FT ACT_SITE 133 133 Proton donor. {ECO:0000250}. SQ SEQUENCE 249 AA; 26861 MW; 093933D96D11C2F6 CRC64; MKQSIIIPAL DLINGQVVRL HQGDYAKQTT YSDNPIKQFD NYVRQGAKQL HLVDLTGAKN PQSRQTALIG KIVEATQCKV QVGGGIRTEQ DVADLLAVGA NRVVIGSTAV THRSMVKNWF IKYGAEKFVL ALDVNINASG QKIVAISGWQ EESGVLLETL IEDFQTVGLQ QVLCTDISRD GTLTGSNIGL YQEICEKYPP IQFQSSGGIG SLADIEALKG TGVSGVIVGR ALLEGKFTLS EAIKCWQNG // ID HIS5_HAEIN Reviewed; 199 AA. AC P44340; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=2.4.2.-; DE AltName: Full=IGP synthase glutamine amidotransferase subunit; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; GN Name=hisH; OrderedLocusNames=HI_0472; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisH subunit provides the glutamine CC amidotransferase activity that produces the ammonia necessary to CC HisF for the synthesis of IGP and AICAR (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22131.1; -; Genomic_DNA. DR PIR; G64070; G64070. DR RefSeq; NP_438633.1; NC_000907.1. DR RefSeq; WP_005693689.1; NC_000907.1. DR ProteinModelPortal; P44340; -. DR STRING; 71421.HI0472; -. DR EnsemblBacteria; AAC22131; AAC22131; HI_0472. DR GeneID; 949532; -. DR KEGG; hin:HI0472; -. DR PATRIC; 20189499; VBIHaeInf48452_0492. DR eggNOG; ENOG4108UJE; Bacteria. DR eggNOG; COG0118; LUCA. DR KO; K02501; -. DR OMA; GMQMLLT; -. DR OrthoDB; EOG69KV05; -. DR PhylomeDB; P44340; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00278; HisH; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Histidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 199 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152379. FT DOMAIN 3 199 Glutamine amidotransferase type-1. FT ACT_SITE 78 78 Nucleophile. {ECO:0000250}. FT ACT_SITE 178 178 {ECO:0000250}. FT ACT_SITE 180 180 {ECO:0000250}. SQ SEQUENCE 199 AA; 22048 MW; C79126E93E1B55D9 CRC64; MINITIIDTG CANLSSVKFA FDRLGYNTEI TFDLNKIKSA DKLILPGVGT ANAAMYNLQE RQLIETIQNL TQPVLGICLG MQLMTEFSEE GNVPTLNLIS GKTNRIPDTG LPLPQMGWNR VQFVKNCPLF DGIVQNSHFY FVHSYAVSPN EHSVAISNYG VNFSAAIAKE NFYGVQFHPE RSGKNGALLL KNFVEKVPF // ID HPE_HAEIN Reviewed; 160 AA. AC P43961; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Surface-adhesin protein E; DE Flags: Precursor; GN Name=pe; OrderedLocusNames=HI_0178; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts as a multifunctional adhesin involved in direct CC interactions with host epithelial cells and host proteins. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Cell surface CC {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; L42023; AAC21855.1; -; Genomic_DNA. DR PIR; F64003; F64003. DR RefSeq; NP_438346.1; NC_000907.1. DR RefSeq; WP_005694109.1; NC_000907.1. DR PDB; 3ZH7; X-ray; 2.10 A; A=28-153. DR PDBsum; 3ZH7; -. DR STRING; 71421.HI0178; -. DR EnsemblBacteria; AAC21855; AAC21855; HI_0178. DR GeneID; 951088; -. DR KEGG; hin:HI0178; -. DR PATRIC; 20188851; VBIHaeInf48452_0182. DR OMA; WGDGIRT; -. DR OrthoDB; EOG67Q9B6; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR031939; Adhesin_E-like. DR InterPro; IPR016595; Adhesin_E_Pasteurellaceae. DR Pfam; PF16747; Adhesin_E; 1. DR PIRSF; PIRSF012320; Prplsmic_HI0178_prd; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Reference proteome; Signal; Virulence. FT SIGNAL 1 15 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 16 160 Surface-adhesin protein E. FT /FTId=PRO_0000013953. FT LIPID 16 16 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 16 16 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT STRAND 40 43 {ECO:0000244|PDB:3ZH7}. FT STRAND 46 58 {ECO:0000244|PDB:3ZH7}. FT STRAND 65 78 {ECO:0000244|PDB:3ZH7}. FT STRAND 81 83 {ECO:0000244|PDB:3ZH7}. FT STRAND 88 98 {ECO:0000244|PDB:3ZH7}. FT TURN 99 102 {ECO:0000244|PDB:3ZH7}. FT STRAND 103 115 {ECO:0000244|PDB:3ZH7}. FT STRAND 119 122 {ECO:0000244|PDB:3ZH7}. FT STRAND 130 133 {ECO:0000244|PDB:3ZH7}. FT STRAND 136 138 {ECO:0000244|PDB:3ZH7}. FT HELIX 139 151 {ECO:0000244|PDB:3ZH7}. SQ SEQUENCE 160 AA; 18360 MW; D0F685EBCC9085DF CRC64; MKKIILTLSL GLLTACSAQI QKAEQNDVKL APPTDVRSGY IRLVKNVNYY IDSESIWVDN QEPQIVHFDA VVNLDRGLYV YPEPKRYARS VRQYKILNCA NYHLTQIRTD FYDEFWGQGL RAAPKKQKKH TLSLTPDTTL YNAAQIICAN YGKAFSVDKK // ID HGP1_HAEIN Reviewed; 1063 AA. AC P44795; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 17-FEB-2016, entry version 111. DE RecName: Full=Probable hemoglobin and hemoglobin-haptoglobin-binding protein 1; DE Flags: Precursor; GN OrderedLocusNames=HI_0635; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Acts as a receptor for hemoglobin or the CC hemoglobin/haptoglobin complex of the human host and is required CC for heme uptake. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: This protein is subject to phase-variable CC expression associated with alteration in the length of the CCAA CC repeat region. This mechanism is called slipped-strand mispairing. CC Addition or loss of CCAA repeat units would change the reading CC frame and result in introduction of stop codons downstream of the CC repeat region. This may be a mechanism of regulation and a way to CC avoid the immunological response of the host (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. CC Hemoglobin/haptoglobin binding protein subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22294.1; Type=Frameshift; Positions=26; 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; L42023; AAC22294.1; ALT_SEQ; Genomic_DNA. DR PIR; B64083; B64083. DR RefSeq; NP_438795.2; NC_000907.1. DR ProteinModelPortal; P44795; -. DR STRING; 71421.HI0635; -. DR EnsemblBacteria; AAC22294; AAC22294; HI_0635. DR GeneID; 950591; -. DR KEGG; hin:HI0635; -. DR PATRIC; 20189877; VBIHaeInf48452_0663. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; DSSKHKY; -. DR OrthoDB; EOG6HB9KP; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 4. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR006970; PT. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF04886; PT; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Repeat; Signal; TonB box; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 1063 Probable hemoglobin and hemoglobin- FT haptoglobin-binding protein 1. FT /FTId=PRO_0000034785. FT REPEAT 26 29 1. FT REPEAT 30 33 2. FT REPEAT 34 37 3. FT REPEAT 38 41 4. FT REPEAT 42 45 5. FT REPEAT 46 49 6. FT REPEAT 50 53 7. FT REGION 26 53 7 X 4 AA tandem repeats of Q-P-T-N. FT MOTIF 63 70 TonB box. FT MOTIF 1046 1063 TonB C-terminal box. SQ SEQUENCE 1063 AA; 121161 MW; 370CB515523F2788 CRC64; MTNFKFSLLA CSIAFALNAS IAYAAQPTNQ PTNQPTNQPT NQPTNQPTNQ PTNQNSNVSE QLEQINVSGS SENINVKEKK VGETQISAKK LAKQQASDSR DLVRYETGIT VVETGRTGAS GYAVRGVDEN RVGIMVDGLR QAETLSSQGF KELFEGYGNF NNTRNSIEIE NVKTATITKG ADSLKSGSGA LGGSVIFETK DARDYLIDKD YYLSYKRGYQ TMNNQNLKTL TLAGRSKKFD ILIIDTTRDG HEIENYDYKI YPNKQADLRA VGPTREKADP YQITRQSTLI KLGFQPNENH RLSVALDDST LETKGIDLSY ALRPYSTANN EKYGERIIND QSKRKNIQFS YENFSQTPFW DHIKLSYSSQ KITNKARSDE YCHQSTCNGV SNPQGLHLVE EKGVYKIKDK YGGELESKEI GWSHEFKNSK GEDADKDISQ RSSLDSVLIN CEKLDCSKKF RIYQEYDENS SEKYTYDDRE IEVGTLPNGK KYGKIPLKKG KTPSWNGFPQ ETARFLFPKS YGYSTDFVND RDLNTHTQQI KLDLDKEFHL WHTQHQLKYG GLYEKTLKSM VNHQYNTAAN VQWWADYFFC ARAKGGNLGE KKTPHPNVSV AGCVNGTPLH SDIGKDTYLI PVTTKNNVLY FGDNVQLTSW LGLDLNYRYD HVKYLPGYDE KTPVPGGLIA GIFVPFNEKD VVYGAYVPSG YKDCRYNTEC YKKNFEENLA LLLRKTDYKH HSYNLGLNLD PTDWLRVQLK YANAFRAPTS DEIYMTFKHP DFSIGPNTNL KAETAKTKEV AFTFYKENSY LTLSAFQSDY RNFIDLVFEK NKQIDKGSAI EYPFYQNQNR DQARVRGIEI ASRLEMGDLF EKLQGFHLGY KLTYQKGRIK DNKLRSGYAE FLKLNPQYTA IASQDQPMNA LQPTTSVYNI GYDAPSKKWG MDVYITDVAA KKAKDSFNSQ WTSMVKRKEN IYGTERTVPA TQANGKDVKD SRGLWRNNRY TVIDTIAYWK PIKNLTFTAG VYNLTNKKYL TWDSARSVRH LGTINRVETA TGKGLNRFYA PGRNYRMSVQ FEF // ID HIS6_HAEIN Reviewed; 258 AA. AC P44436; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF; DE EC=4.1.3.-; DE AltName: Full=IGP synthase cyclase subunit; DE AltName: Full=IGP synthase subunit HisF; DE AltName: Full=ImGP synthase subunit HisF; DE Short=IGPS subunit HisF; GN Name=hisF; OrderedLocusNames=HI_0474; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisF subunit catalyzes the CC cyclization activity that produces IGP and AICAR from PRFAR using CC the ammonia provided by the HisH subunit (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22133.1; -; Genomic_DNA. DR PIR; I64070; I64070. DR RefSeq; NP_438635.1; NC_000907.1. DR RefSeq; WP_005693688.1; NC_000907.1. DR ProteinModelPortal; P44436; -. DR STRING; 71421.HI0474; -. DR EnsemblBacteria; AAC22133; AAC22133; HI_0474. DR GeneID; 949565; -. DR KEGG; hin:HI0474; -. DR PATRIC; 20189503; VBIHaeInf48452_0494. DR eggNOG; ENOG4105C0S; Bacteria. DR eggNOG; COG0107; LUCA. DR KO; K02500; -. DR OMA; KGTNFVN; -. DR OrthoDB; EOG6H1Q3W; -. DR PhylomeDB; P44436; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01013; HisF; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004651; HisF. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00735; hisF; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 258 Imidazole glycerol phosphate synthase FT subunit HisF. FT /FTId=PRO_0000142163. FT ACT_SITE 11 11 {ECO:0000255}. FT ACT_SITE 130 130 {ECO:0000255}. SQ SEQUENCE 258 AA; 28626 MW; ABC2F6351F1642C2 CRC64; MLAKRIIPCL DVRDGQVVKG VQFRNHEIIG DIVPLAQRYA QEGADELVFY DITASSDGRT VDKSWVERIA QVIDIPFCVA GGIKTIEDAE KLFAFGADKI SINSPALADP TLISRLADRF GVQAIVVGID SWFEQETGKY WVNQYTGDET RTRQTHWQLL DWVKEVQQCG AGEIVLNMMN QDGLRNGYDL AQLKLVRGVC RVPLIASGGA GKMVHFRDAF IEAKVDGALA ASVFHKQIIE IGELKSYLVQ SAIEIRSE // ID HIS82_HAEIN Reviewed; 366 AA. AC Q57004; P96340; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Histidinol-phosphate aminotransferase 2; DE EC=2.6.1.9; DE AltName: Full=Imidazole acetol-phosphate transaminase 2; GN Name=hisC2; OrderedLocusNames=HI_1166; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3- CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase 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; L42023; AAC22821.1; -; Genomic_DNA. DR PIR; D64187; D64187. DR RefSeq; NP_439324.1; NC_000907.1. DR RefSeq; WP_005694274.1; NC_000907.1. DR ProteinModelPortal; Q57004; -. DR STRING; 71421.HI1166; -. DR EnsemblBacteria; AAC22821; AAC22821; HI_1166. DR GeneID; 950769; -. DR KEGG; hin:HI1166; -. DR PATRIC; 20191011; VBIHaeInf48452_1218. DR eggNOG; ENOG4105CIH; Bacteria. DR eggNOG; COG0079; LUCA. DR KO; K00817; -. DR OMA; YGLPNHL; -. DR OrthoDB; EOG6JMMWS; -. DR PhylomeDB; Q57004; -. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01023; HisC_aminotrans_2; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR005861; HisP_aminotrans. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01141; hisC; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 366 Histidinol-phosphate aminotransferase 2. FT /FTId=PRO_0000153369. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 366 AA; 41053 MW; 8E671105AD669B05 CRC64; MQYINIANRG VKSLSPYQAG KPIEELEREL GISNIVKLAS NENPFGFPES AKKAIFEQLD KLTRYPDANG FELKQTIAKK FGVQPNQITL GNGSNDLLEL FAHTFATEGD EIMYSQYAFI VYPLVTKAIN AIVKEIPAKN WGHDLQGFLT ALSDKTKLIY IANPNNPTGN FLTSQEIEDF LAEVPENVIV VLDEAYTEFT RSEERVDSFS LLKKYSNLII SRSLSKAYGL AGLRIGYAVS NPEIADLLNR VRQPFNCNSL ALTAAVAVMN DDKFVEKVAE NNRIEMRRYE DFCQKNQLDY IPSKGNFITI DFKQPAAPIY DALLREGVIV RPIAGYGMPN HLRISIGLPE ENDKFFTALS KVLKFA // ID HLDE_HAEIN Reviewed; 476 AA. AC O05074; Q48046; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Bifunctional protein HldE {ECO:0000255|HAMAP-Rule:MF_01603}; DE Includes: DE RecName: Full=D-beta-D-heptose 7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603}; DE EC=2.7.1.167 {ECO:0000255|HAMAP-Rule:MF_01603}; DE AltName: Full=D-beta-D-heptose 7-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01603}; DE AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01603}; DE Includes: DE RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603}; DE EC=2.7.7.70 {ECO:0000255|HAMAP-Rule:MF_01603}; DE AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_01603}; GN Name=hldE {ECO:0000255|HAMAP-Rule:MF_01603}; Synonyms=rfaE, waaE; GN OrderedLocusNames=HI_1526; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-427, AND ROLE IN LOS RP BIOSYNTHESIS. RC STRAIN=NTHi 2019; RX PubMed=7868252; RA Lee N.-G., Sunshine M.G., Apicella M.A.; RT "Molecular cloning and characterization of the nontypeable Haemophilus RT influenzae 2019 rfaE gene required for lipopolysaccharide RT biosynthesis."; RL Infect. Immun. 63:818-824(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno- CC heptose 7-phosphate at the C-1 position to selectively form D- CC glycero-beta-D-manno-heptose-1,7-bisphosphate. CC {ECO:0000305|PubMed:7868252}. CC -!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D- CC manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno- CC heptose. {ECO:0000305|PubMed:7868252}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 7-phosphate + CC ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate + CC ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate CC kinase PfkB family. {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC cytidylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01603}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC43516.1; Type=Frameshift; Positions=331; 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; L42023; AAC23172.1; -; Genomic_DNA. DR EMBL; U17642; AAC43516.1; ALT_FRAME; Genomic_DNA. DR PIR; C64127; C64127. DR RefSeq; NP_439675.1; NC_000907.1. DR RefSeq; WP_005693548.1; NC_000907.1. DR ProteinModelPortal; O05074; -. DR STRING; 71421.HI1526; -. DR DNASU; 949890; -. DR EnsemblBacteria; AAC23172; AAC23172; HI_1526. DR GeneID; 949890; -. DR KEGG; hin:HI1526; -. DR PATRIC; 20191777; VBIHaeInf48452_1597. DR eggNOG; ENOG4105DW0; Bacteria. DR eggNOG; COG2870; LUCA. DR KO; K03272; -. DR OMA; EACYLAN; -. DR OrthoDB; EOG68Q0W4; -. DR PhylomeDB; O05074; -. DR UniPathway; UPA00356; UER00437. DR UniPathway; UPA00356; UER00439. DR UniPathway; UPA00976; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0033785; F:heptose 7-phosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01603; HldE; 1. DR InterPro; IPR023030; Bifunc_HldE. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR011913; RfaE_dom_I. DR InterPro; IPR011914; RfaE_dom_II. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR02198; rfaE_dom_I; 1. DR TIGRFAMs; TIGR02199; rfaE_dom_II; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 476 Bifunctional protein HldE. FT /FTId=PRO_0000080112. FT NP_BIND 195 198 ATP. {ECO:0000255|HAMAP-Rule:MF_01603}. FT REGION 1 318 Ribokinase. FT REGION 344 476 Cytidylyltransferase. FT ACT_SITE 264 264 {ECO:0000255|HAMAP-Rule:MF_01603}. FT CONFLICT 36 36 A -> R (in Ref. 2; AAC43516). FT {ECO:0000305}. FT CONFLICT 84 84 L -> H (in Ref. 2; AAC43516). FT {ECO:0000305}. FT CONFLICT 170 170 A -> G (in Ref. 2; AAC43516). FT {ECO:0000305}. FT CONFLICT 214 214 E -> K (in Ref. 2; AAC43516). FT {ECO:0000305}. FT CONFLICT 273 273 A -> T (in Ref. 2; AAC43516). FT {ECO:0000305}. FT CONFLICT 278 278 R -> C (in Ref. 2; AAC43516). FT {ECO:0000305}. SQ SEQUENCE 476 AA; 51946 MW; 4F241C08D2C6951E CRC64; MAQYSAEFKQ AKVLVLGDVM LDRYWFGATN RISPEAPVPV VRVQENEERA GGAANVAMNI ASLNVPVQLM GLIGQDETGS ALSLLLEKQK IDCNFVALET HPTITKLRIL SRHQQLLRLD FEEDFNNVDC KDLLAKLESA VKNYGALILS DYGKGTLKDV QKMIQIARKA NVPVLIDPKG TDFERYRGAT LLTPNMSEFE AVVGKCNTEE EIIEKGLKLI SDIELTALLV TRSEKGMTLL RPNQEPYHLP TVAKEVFDVT GAGDTVISVL ATALADGRSF EESCYLANVA AGIVVGKLGT STVSTVELEN AIHARPETGF GIMSEAELKD AVAQAKARGE KIVMTNGCFD ILHPGHISYL ENARKLGDRL IVAVNSDDSV KRLKGESRPI NNLENRMAVL AGLASVDWLV PFTEDTPQRL IGEILPDLLV KGGDYKPEEI AGSKEVWANG GDVKVLNFEN GCSTTNVIEK IKLLKD // ID HTPG_HAEIN Reviewed; 626 AA. AC P44516; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 2. DT 11-MAY-2016, entry version 114. DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505}; DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505}; DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505}; GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; GN OrderedLocusNames=HI_0104; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. CC {ECO:0000255|HAMAP-Rule:MF_00505}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}. CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. CC {ECO:0000255|HAMAP-Rule:MF_00505}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21778.1; 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; L42023; AAC21778.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_438278.1; NC_000907.1. DR RefSeq; WP_005693816.1; NC_000907.1. DR ProteinModelPortal; P44516; -. DR SMR; P44516; 3-625. DR STRING; 71421.HI0104; -. DR PRIDE; P44516; -. DR EnsemblBacteria; AAC21778; AAC21778; HI_0104. DR GeneID; 951006; -. DR KEGG; hin:HI0104; -. DR PATRIC; 20188675; VBIHaeInf48452_0107. DR eggNOG; ENOG4105CJX; Bacteria. DR eggNOG; COG0326; LUCA. DR KO; K04079; -. DR OMA; YLRFMRG; -. DR OrthoDB; EOG65TRNM; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.30.565.10; -; 1. DR HAMAP; MF_00505; HSP90; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR019805; Heat_shock_protein_90_CS. DR InterPro; IPR001404; Hsp90_fam. DR InterPro; IPR020575; Hsp90_N. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR11528; PTHR11528; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00183; HSP90; 1. DR PIRSF; PIRSF002583; Hsp90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS00298; HSP90; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; Stress response. FT CHAIN 1 626 Chaperone protein HtpG. FT /FTId=PRO_0000062990. FT REGION 1 339 A; substrate-binding. {ECO:0000255|HAMAP- FT Rule:MF_00505}. FT REGION 340 555 B. {ECO:0000255|HAMAP-Rule:MF_00505}. FT REGION 556 626 C. {ECO:0000255|HAMAP-Rule:MF_00505}. SQ SEQUENCE 626 AA; 71135 MW; 5BDBD29A1B2DC7E2 CRC64; MSQNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSNPALYEG DGDLRVRVSF DADKGTITIS DNGIGMTREQ VIDHLGTIAK SGTKEFLTAL GQDQAKNSQL IGQFGVGFYS AFIVADKVTV KTRAAGEEAD KAVLWESAGE GEYSVADIEK KSRGTDVILH LREDEKEFLN EWRLREIIGK YSDHIGLPVE MLTKEYDDEG KECGEKWEKI NKSDALWTRS KNDVSDEEYK AFYKHLSHDF VDPVTWAHNK VEGNQAYTSL LYVPAKAPWD LFNREHKHGL KLYVQRVFIM DDAEQFIPNY LRFMRGLIDS NDLPLNVSRE ILQDNKITAA LRKALTKRSL QMLEKLAKDD AEKYLQFWKE FGLVLKEGPA EDFANKETVA KLLRFASTHN DGSEQTVSLE DYILRMKEGQ KAIYYITADS YVAAKNSPHL ELFNKKGIEV LLLSDRIDEW MLSYLTEFDG KQLQSITKAD LDLGDLADKE SETQKQQDEA FGSFIERVKN LLGERVKTVR LTHNLTDTPA VVSTDNDQMT TQMAKLFAAA GQPVPEVKYT FELNPEHHLV KKVADIADET EFADWVELLL EQAMLAERGS LENPAAFIKR INKLLG // ID HIS81_HAEIN Reviewed; 367 AA. AC P44423; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Histidinol-phosphate aminotransferase 1; DE EC=2.6.1.9; DE AltName: Full=Imidazole acetol-phosphate transaminase 1; GN Name=hisC1; Synonyms=hisC; OrderedLocusNames=HI_0470; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3- CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase 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; L42023; AAC22129.1; -; Genomic_DNA. DR PIR; E64070; E64070. DR RefSeq; NP_438631.1; NC_000907.1. DR RefSeq; WP_005693691.1; NC_000907.1. DR ProteinModelPortal; P44423; -. DR SMR; P44423; 16-364. DR STRING; 71421.HI0470; -. DR PRIDE; P44423; -. DR EnsemblBacteria; AAC22129; AAC22129; HI_0470. DR GeneID; 949558; -. DR KEGG; hin:HI0470; -. DR PATRIC; 20189495; VBIHaeInf48452_0490. DR eggNOG; ENOG4105CIH; Bacteria. DR eggNOG; COG0079; LUCA. DR KO; K00817; -. DR OMA; IKPPYNI; -. DR OrthoDB; EOG651SWW; -. DR PhylomeDB; P44423; -. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01023; HisC_aminotrans_2; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR005861; HisP_aminotrans. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01141; hisC; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 367 Histidinol-phosphate aminotransferase 1. FT /FTId=PRO_0000153368. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 367 AA; 40794 MW; 8594237F1C530465 CRC64; MNDYNSHILQ WKKTIMTITT LSRQNIQALT PYQSARKLGG NGTIWLNANE YPTSPEFQLS GKDLNRYPEP QPQRVVQAYA NYAGVSTENV LVTRGGDEGI ELIIHTFCEP KQDAILFCPP TYGMYAVSAE TAGVLSKTVP LTDDFQLNLP EIKNHLNDVK VVFVCSPNNP TGNLLKQSDI LDLLQITAGK AIVVVDEAYI EFCPEASVIN LLKNYPHLAI IRTLSKAFAL AGLRCGFVLA NPELIDILSK VIAPYPIPVP SADLAEQALR PSNIATVQAL TQELLSNRQW LAKALLVLHQ VEKVYESEAN YLLIKCQNGQ AVFKALWEQG IILRDQNKTL HLQNCIRITV GTRNECEKVV EAIKEVK // ID HNS_HAEIN Reviewed; 134 AA. AC P43841; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=DNA-binding protein H-NS homolog; GN Name=hns; OrderedLocusNames=HI_1587; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds tightly to ds-DNA, increases its thermal stability CC and inhibits transcription. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the histone-like protein H-NS 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; L42023; AAC23235.1; -; Genomic_DNA. DR PIR; D64131; D64131. DR RefSeq; NP_439732.1; NC_000907.1. DR RefSeq; WP_005647241.1; NC_000907.1. DR ProteinModelPortal; P43841; -. DR SMR; P43841; 91-134. DR STRING; 71421.HI1587; -. DR EnsemblBacteria; AAC23235; AAC23235; HI_1587. DR GeneID; 950451; -. DR KEGG; hin:HI1587; -. DR PATRIC; 20191907; VBIHaeInf48452_1661. DR eggNOG; ENOG4108SAU; Bacteria. DR eggNOG; COG2916; LUCA. DR KO; K03746; -. DR OMA; LDDYAIN; -. DR OrthoDB; EOG6NPM97; -. DR PhylomeDB; P43841; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.1050; -; 1. DR Gene3D; 4.10.430.10; -; 1. DR InterPro; IPR027444; H-NS_C_dom. DR InterPro; IPR001801; Histone_HNS. DR InterPro; IPR027454; Histone_HNS_oligo_dom. DR Pfam; PF00816; Histone_HNS; 1. DR PIRSF; PIRSF002096; HnS; 1. DR SMART; SM00528; HNS; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 134 DNA-binding protein H-NS homolog. FT /FTId=PRO_0000168506. SQ SEQUENCE 134 AA; 15328 MW; F57CBA0C1496900B CRC64; MNELVRGLTN LRSLRAAVRE LTLEQAENAL EKLQTAIEEK RANEAELIKA ETERKERLAK YKELMEKEGI TPEELHEIFG TKTVSIRAKR APRPAKYAFI DENGEHKTWT GQGRTPRPIQ NALNKGKSLS DFEI // ID HOLB_HAEIN Reviewed; 327 AA. AC P43748; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 99. DE RecName: Full=DNA polymerase III subunit delta'; DE EC=2.7.7.7; GN Name=holB; OrderedLocusNames=HI_0455; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) 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 (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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22113.1; -; Genomic_DNA. DR RefSeq; NP_438616.1; NC_000907.1. DR RefSeq; WP_010868989.1; NC_000907.1. DR ProteinModelPortal; P43748; -. DR STRING; 71421.HI0455; -. DR EnsemblBacteria; AAC22113; AAC22113; HI_0455. DR GeneID; 949546; -. DR KEGG; hin:HI0455; -. DR PATRIC; 20189465; VBIHaeInf48452_0475. DR eggNOG; ENOG4107QRG; Bacteria. DR eggNOG; COG0470; LUCA. DR KO; K02341; -. DR OMA; CHSCHLM; -. DR OrthoDB; EOG6W9X5M; -. DR PhylomeDB; P43748; -. DR Proteomes; UP000000579; Chromosome. 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:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR004622; DNA_pol_HolB. DR InterPro; IPR015199; DNA_pol_III_delta_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF09115; DNApol3-delta_C; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00678; holB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed DNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 327 DNA polymerase III subunit delta'. FT /FTId=PRO_0000105514. SQ SEQUENCE 327 AA; 37039 MW; CEE4D452E371A298 CRC64; MTALYPWLMP IYHQIAQTFD EGLGHHAVLI KADSGLGVES LFNALAQKIM CVAQGDKPCG QCHSCHLMQA HSHPDYHELS PINGKDIGVD QVRDINEMVA QHAQQNGNKV VYVQGAERLT EAAANALLKT LEEPRPNTYF LLQADSSASL LATIYSRCQV WNLSVPNEEI AFEWLKSKSA VENQEILTAL AMNLGRPLLA LETLQEGFIE QRKNFLRQFW VFYRRRSPLE LLPLFDKERY VQQVDWILAF LSDCLKHKLE IDSHRQVADL GRGIEQFSDE QTALGLLQAI KIMQKVRSDL LTINGVNVEL MLLDGLTRLV TEVFETQ // ID HOLC_HAEIN Reviewed; 144 AA. AC P43749; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=DNA polymerase III subunit chi; DE EC=2.7.7.7; GN Name=holC; OrderedLocusNames=HI_1397; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-144. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3; RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., RA Benner J.S., Wilson G.G.; RT "Cloning, analysis and expression of the HindIII R-M-encoding genes."; RL Gene 150:75-80(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 (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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23044.1; -; Genomic_DNA. DR EMBL; L15391; AAA61957.1; -; Genomic_DNA. DR PIR; I64121; I64121. DR RefSeq; NP_439550.1; NC_000907.1. DR RefSeq; WP_005693964.1; NC_000907.1. DR ProteinModelPortal; P43749; -. DR STRING; 71421.HI1397; -. DR EnsemblBacteria; AAC23044; AAC23044; HI_1397. DR GeneID; 950308; -. DR KEGG; hin:HI1397; -. DR PATRIC; 20191493; VBIHaeInf48452_1457. DR eggNOG; ENOG4105MYG; Bacteria. DR eggNOG; COG2927; LUCA. DR KO; K02339; -. DR OMA; WQFEPSA; -. DR OrthoDB; EOG68H887; -. DR PhylomeDB; P43749; -. DR Proteomes; UP000000579; Chromosome. 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; 3.40.50.10110; -; 1. DR InterPro; IPR007459; DNA_pol3_chi. DR Pfam; PF04364; DNA_pol3_chi; 1. DR SUPFAM; SSF102400; SSF102400; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed DNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 144 DNA polymerase III subunit chi. FT /FTId=PRO_0000105518. SQ SEQUENCE 144 AA; 16636 MW; A4571B90253C9D45 CRC64; MAKTAQFYIL TENCTLTVEE IACNLAASIW RSGKKVLISC ESEAQALEID ERLWQRDPNE FVPHNLSGEA TQYPTPIEIS WLGKRNLQRR DLLINLQQEI PDFSHSFTQI IDFVPKDDAL KTQARERYKQ LRLQGWNLST ENVG // ID HTOA_HAEIN Reviewed; 466 AA. AC P45129; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Probable periplasmic serine protease do/HhoA-like; DE EC=3.4.21.-; DE Flags: Precursor; GN OrderedLocusNames=HI_1259; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 PDZ (DHR) domains. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22906.1; -; Genomic_DNA. DR PIR; A64113; A64113. DR RefSeq; NP_439414.1; NC_000907.1. DR RefSeq; WP_005694316.1; NC_000907.1. DR ProteinModelPortal; P45129; -. DR SMR; P45129; 40-369. DR STRING; 71421.HI1259; -. DR EnsemblBacteria; AAC22906; AAC22906; HI_1259. DR GeneID; 950193; -. DR KEGG; hin:HI1259; -. DR PATRIC; 20191199; VBIHaeInf48452_1311. DR eggNOG; ENOG4105C0H; Bacteria. DR eggNOG; COG0265; LUCA. DR KO; K04772; -. DR OMA; AFRYFFG; -. DR OrthoDB; EOG61ZTDN; -. DR PhylomeDB; P45129; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011782; Pept_S1C_Do. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001940; Peptidase_S1C. DR Pfam; PF00595; PDZ; 2. DR PRINTS; PR00834; PROTEASES2C. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 2. DR SUPFAM; SSF50494; SSF50494; 1. DR TIGRFAMs; TIGR02037; degP_htrA_DO; 1. DR PROSITE; PS50106; PDZ; 2. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Periplasm; Protease; Reference proteome; KW Repeat; Serine protease; Signal. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 466 Probable periplasmic serine protease FT do/HhoA-like. FT /FTId=PRO_0000026936. FT DOMAIN 270 361 PDZ 1. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT DOMAIN 367 458 PDZ 2. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 120 120 Charge relay system. {ECO:0000255}. FT ACT_SITE 150 150 Charge relay system. {ECO:0000255}. FT ACT_SITE 226 226 Charge relay system. {ECO:0000255}. SQ SEQUENCE 466 AA; 49434 MW; ED050A00047B5851 CRC64; MKKTRFVLNS IALGLSVLST SFVAHVAQAT LPSFVSEQNS LAPMLEKVQP AVVTLSVEGK AKVDSRSPFL DDIPEEFKFF FGDRFAEQFG GRGESKRNFR GLGSGVIINA SKGYVLTNNH VIDGADKITV QLQDGREFKA KLVGKDEQSD IALVQLEKPS NLTEIKFADS DKLRVGDFTV AIGNPFGLGQ TVTSGIVSAL GRSTGSDSGT YENYIQTDAA VNRGNSGGAL VNLNGELIGI NTAIISPSGG NAGIAFAIPS NQASNLVQQI LEFGQVRRGL LGIKGGELNA DLAKAFNVSA QQGAFVSEVL PKSAAEKAGL KAGDIITAMN GQKISSFAEI RAKIATTGAG KEISLTYLRD GKSHDVKMKL QADDSSQLSS KTELPALDGA TLKDYDAKGV KGIEITKIQP NSLAAQRGLK SGDIIIGINR QMIENIRELN KVLETEPSAV ALNILRGDSN FYLLVQ // ID HTPX_HAEIN Reviewed; 283 AA. AC P44840; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 112. DE RecName: Full=Protease HtpX {ECO:0000255|HAMAP-Rule:MF_00188}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188}; DE AltName: Full=Heat shock protein HtpX {ECO:0000255|HAMAP-Rule:MF_00188}; GN Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; GN OrderedLocusNames=HI_0720; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00188}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00188}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00188}. CC -!- SIMILARITY: Belongs to the peptidase M48B family. CC {ECO:0000255|HAMAP-Rule:MF_00188}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22378.1; -; Genomic_DNA. DR PIR; H64088; H64088. DR RefSeq; NP_438878.1; NC_000907.1. DR RefSeq; WP_005633091.1; NC_000907.1. DR ProteinModelPortal; P44840; -. DR SMR; P44840; 57-157. DR STRING; 71421.HI0720; -. DR MEROPS; M48.002; -. DR EnsemblBacteria; AAC22378; AAC22378; HI_0720. DR GeneID; 949740; -. DR KEGG; hin:HI0720; -. DR PATRIC; 20190063; VBIHaeInf48452_0752. DR eggNOG; ENOG4105D0M; Bacteria. DR eggNOG; COG0501; LUCA. DR KO; K03799; -. DR OMA; AWIASRF; -. DR OrthoDB; EOG6F55J5; -. DR PhylomeDB; P44840; -. DR Proteomes; UP000000579; 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:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00188; Pept_M48_protease_HtpX; 1. DR InterPro; IPR022919; Pept_M48_protease_HtpX. DR InterPro; IPR001915; Peptidase_M48. DR Pfam; PF01435; Peptidase_M48; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 283 Protease HtpX. FT /FTId=PRO_0000138865. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 33 53 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 147 167 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 190 210 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT ACT_SITE 140 140 {ECO:0000255|HAMAP-Rule:MF_00188}. FT METAL 139 139 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 143 143 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 218 218 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. SQ SEQUENCE 283 AA; 30780 MW; FAE062B1BE0E0818 CRC64; MMRILLFLAT NMAVMLVLGI ILSVTGIAGN STGGILIMAL LFGFAGSLIS LFLSKTMALR SVDGEVITQP RNQTERWLID TVSRQAQKAG IPMPDVAIYH SPDVNAFATG ATKSNSLVAV STGLLNNMTE AEAEAVLAHE ISHISNGDMV TMALLQGVLN TFVIFLSRVI ATAVASSRNN NGEETRSSGI YFLVSMVLEM LFGVLASIIA MWFSRYREFR ADAGSASLVG KEKMIMALQR LQQLHEPQNL EGSLNAFMIN GKRSELFMSH PPLEKRIEAL RNL // ID HXUC1_HAEIN Reviewed; 723 AA. AC P44600; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Heme/hemopexin utilization protein C; DE Flags: Precursor; GN Name=hxuC; OrderedLocusNames=HI_0262; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Required for utilization of free heme at low CC concentrations. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor 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; L42023; AAC21927.1; -; Genomic_DNA. DR PIR; C64058; C64058. DR RefSeq; NP_438431.1; NC_000907.1. DR RefSeq; WP_005694042.1; NC_000907.1. DR ProteinModelPortal; P44600; -. DR STRING; 71421.HI0262; -. DR TCDB; 1.B.14.2.11; the outer membrane receptor (omr) family. DR EnsemblBacteria; AAC21927; AAC21927; HI_0262. DR GeneID; 950895; -. DR KEGG; hin:HI0262; -. DR PATRIC; 20189051; VBIHaeInf48452_0277. DR eggNOG; ENOG4107ENK; Bacteria. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; RGNSNIT; -. DR OrthoDB; EOG6RJV1T; -. DR PhylomeDB; P44600; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 2. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR011276; TonB_haem/Hb_rcpt. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01785; TonB-hemin; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal; TonB box; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 723 Heme/hemopexin utilization protein C. FT /FTId=PRO_0000034792. FT MOTIF 706 723 TonB C-terminal box. SQ SEQUENCE 723 AA; 80776 MW; 91EB3AB0FFEA2984 CRC64; MRFSKLSLAI TTTLVTANAL AQSVELDSIN VIATRDPSRF AYTPEKQSKD SLLSKQATSV ADALEDIPNV DVRGGSRSIA QKPNIRGLSD NRVVQVIDGV RQNFDLAHRG SYFLPMSLIQ EIEVIKGPSS SLWGSGALGG VVAMRTPNAL DLLKNNDKFG VKIRQGYQTA NNLSEKDVSV FAANDKFDVL ISGFYNNADN LRTGKGNKLN NTAYKQFGGL AKFGWQINDA NRVELSHRET RFKQTAPSNN EVENELTNEQ ITDQIKKFHG QKDDLLPPTT QPSPSERSEF YSKVKTRLGS VSYLTDQQIP DQSTVFNYYL TPDNPYLNTH IALYNNKTIE KEQRKVSGVK DQTKLTTRGI NLRNSSELSH ISFVYGVDYM RDKIRTERGT NGSDAKFRAD PYNANSNTTG VYLIAHIPLF GEKLLVSPSV RYDHYDTSSK TVKYKDNHLS PATKLTWIVT NWLDFTAKYN EAFRAPSMQE RFVSGAHFGA NTLGLDHINR FVANPNLRPE TAKNKEITAN LHFDSLFKQG DKFKIEATYF RNDVKDFINL KIFNDAKTSA SAGANPNTNG ALLPKNSQYQ NITNARLSGI ELQAQYQTER LTLFTNYGST KGKDKDSGEA LSNIAASKIG VGVNYALVKD KFTVGATVTH YAAQRRVPKD HSVTYPSYIL TDLRATYAPL KGEWKNLRLD FALENLFDRK YQPAFSLMEG TGRNAKISAV YSF // ID HISX_HAEIN Reviewed; 427 AA. AC P44001; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=HI_0469; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine CC + 2 NADH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22128.1; -; Genomic_DNA. DR PIR; A64008; A64008. DR RefSeq; NP_438630.1; NC_000907.1. DR RefSeq; WP_005669329.1; NC_000907.1. DR ProteinModelPortal; P44001; -. DR SMR; P44001; 4-425. DR STRING; 71421.HI0469; -. DR PRIDE; P44001; -. DR EnsemblBacteria; AAC22128; AAC22128; HI_0469. DR GeneID; 949557; -. DR KEGG; hin:HI0469; -. DR PATRIC; 20189493; VBIHaeInf48452_0489. DR eggNOG; ENOG4105CEK; Bacteria. DR eggNOG; COG0141; LUCA. DR KO; K00013; -. DR OMA; TEIYRVG; -. DR OrthoDB; EOG6CVVCR; -. DR PhylomeDB; P44001; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01024; HisD; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 427 Histidinol dehydrogenase. FT /FTId=PRO_0000135777. FT ACT_SITE 321 321 Proton acceptor. {ECO:0000250}. FT ACT_SITE 322 322 Proton acceptor. {ECO:0000250}. FT METAL 254 254 Zinc. {ECO:0000250}. FT METAL 257 257 Zinc. {ECO:0000250}. FT METAL 355 355 Zinc. {ECO:0000250}. FT METAL 414 414 Zinc. {ECO:0000250}. FT BINDING 127 127 NAD. {ECO:0000250}. FT BINDING 185 185 NAD. {ECO:0000250}. FT BINDING 208 208 NAD. {ECO:0000250}. FT BINDING 232 232 Substrate. {ECO:0000250}. FT BINDING 254 254 Substrate. {ECO:0000250}. FT BINDING 257 257 Substrate. {ECO:0000250}. FT BINDING 322 322 Substrate. {ECO:0000250}. FT BINDING 355 355 Substrate. {ECO:0000250}. FT BINDING 409 409 Substrate. {ECO:0000250}. FT BINDING 414 414 Substrate. {ECO:0000250}. SQ SEQUENCE 427 AA; 46339 MW; FC5C5D8675654462 CRC64; MQTIIWNHLS ETEKRKVIMR PVQQNGKNIQ QAVNAIRENV AYNGDRALFE LCEKFDGVKL DKLIVSADEI QAASSRISVK LRNAIEQAKT NIEAFHKAQQ NQEIDLEIQE GVRCQVVTRP ISCVGLYIPG GSAPLFSTVL MLAIPAKIAG CKKIVLCSPP PISDEILYTA HLCGVETIYA IGGAQAVFAM AQGTESVAKV DKIFGPGNAF VTEAKRQVAQ NSTAIDMPAG PSEVLVIADE SADPEFVASD LLSQAEHGAD SQVILVATCE TLAKETALAI ERQLALLPRA ETVRKALNHS RIFIAESLEQ AVEISNEYAP EHLIVQTKNA RKLLPYLDNA GSIFLGAYSP ESMGDYASGT NHVLPTYGYT KTYSSLGLAD FSKRMTVQEL TPKGFKNLAE TVEVMAEAEQ LAAHKMAVSV RLAKLNI // ID HLDD_HAEIN Reviewed; 308 AA. AC P45048; Q48228; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 110. DE RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE EC=5.1.3.20 {ECO:0000255|HAMAP-Rule:MF_01601}; DE AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=ADP-hep 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601}; DE Short=AGME {ECO:0000255|HAMAP-Rule:MF_01601}; GN Name=hldD {ECO:0000255|HAMAP-Rule:MF_01601}; Synonyms=rfaD; GN OrderedLocusNames=HI_1114; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN LOS BIOSYNTHESIS. RC STRAIN=NTHi 2019; RX PubMed=9119477; RA Nichols W.A., Gibson B.W., Melaugh W., Lee N.-G., Sunshine M., RA Apicella M.A.; RT "Identification of the ADP-L-glycero-D-manno-heptose-6-epimerase RT (rfaD) and heptosyltransferase II (rfaF) biosynthesis genes from RT nontypeable Haemophilus influenzae 2019."; RL Infect. Immun. 65:1377-1386(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero- CC beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an CC epimerization at carbon 6 of the heptose. CC {ECO:0000305|PubMed:9119477}. CC -!- CATALYTIC ACTIVITY: ADP-D-glycero-D-manno-heptose = ADP-L-glycero- CC D-manno-heptose. {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- COFACTOR: CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01601}; CC Note=Binds 1 NADP(+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01601}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D- CC manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose CC from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core CC biosynthesis. CC -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_01601}. CC -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a CC smaller C-terminal substrate-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01601}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. HldD subfamily. {ECO:0000255|HAMAP-Rule:MF_01601}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L76100; AAA98766.1; -; Genomic_DNA. DR EMBL; L42023; AAC22768.1; -; Genomic_DNA. DR PIR; F64183; F64183. DR RefSeq; NP_439271.1; NC_000907.1. DR RefSeq; WP_005632797.1; NC_000907.1. DR ProteinModelPortal; P45048; -. DR SMR; P45048; 1-306. DR STRING; 71421.HI1114; -. DR PRIDE; P45048; -. DR EnsemblBacteria; AAC22768; AAC22768; HI_1114. DR GeneID; 950083; -. DR KEGG; hin:HI1114; -. DR PATRIC; 20190901; VBIHaeInf48452_1163. DR eggNOG; ENOG4105CUI; Bacteria. DR eggNOG; COG0451; LUCA. DR KO; K03274; -. DR OMA; KGRYQSF; -. DR OrthoDB; EOG6384GP; -. DR PhylomeDB; P45048; -. DR UniPathway; UPA00356; UER00440. DR UniPathway; UPA00976; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01601; Heptose_epimerase; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR011912; Heptose_epim. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR02197; heptose_epim; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; NADP; KW Reference proteome. FT CHAIN 1 308 ADP-L-glycero-D-manno-heptose-6- FT epimerase. FT /FTId=PRO_0000205798. FT NP_BIND 10 11 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT NP_BIND 31 32 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT NP_BIND 75 79 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT REGION 200 203 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT ACT_SITE 139 139 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 38 38 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 53 53 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 92 92 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 143 143 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 168 168 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 169 169 NADP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 177 177 NADP. {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 179 179 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01601}. FT BINDING 186 186 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 208 208 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT BINDING 271 271 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01601}. FT CONFLICT 67 67 G -> D (in Ref. 1; AAA98766). FT {ECO:0000305}. FT CONFLICT 299 299 T -> A (in Ref. 1; AAA98766). FT {ECO:0000305}. SQ SEQUENCE 308 AA; 34781 MW; 475F6BAACC4FAF5C CRC64; MIIVTGGAGF IGSNIVKALN DLGRKDILVV DNLKDGTKFA NLVDLDIADY CDKEDFIASI IAGDEFGDID AVFHEGACSA TTEWDGKYIM HNNYEYSKEL LHYCLDREIP FFYASSAATY GDTKVFREER EFEGPLNVYG YSKFLFDQYV RNILPEAKSP VCGFRYFNVY GPRENHKGSM ASVAFHLNNQ ILKGENPKLF AGSEHFRRDF VYVGDVAAVN IWCWQNGISG IYNLGTGNAE SFRAVADAVV KFHGKGEIET IPFPEHLKSR YQEYTQADLT KLRSTGYDKP FKTVAEGVTE YMAWLNRK // ID HMRM_HAEIN Reviewed; 464 AA. AC P45272; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Multidrug resistance protein HmrM; DE AltName: Full=Multidrug-efflux transporter; DE AltName: Full=Na(+)/drug antiporter; GN Name=hmrM; Synonyms=norM; OrderedLocusNames=HI_1612; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=14695443; DOI=10.1111/j.1348-0421.2003.tb03467.x; RA Xu X.-J., Su X.-Z., Morita Y., Kuroda T., Mizushima T., Tsuchiya T.; RT "Molecular cloning and characterization of the HmrM multidrug efflux RT pump from Haemophilus influenzae Rd."; RL Microbiol. Immunol. 47:937-943(2003). CC -!- FUNCTION: Multidrug efflux pump that functions as a Na(+)/drug CC antiporter. Confers resistance to norfloxacin, acriflavine, CC doxorubicin, ethidium bromide, tetraphenylphosphonium chloride, CC daunomycin, berberine and sodium deoxycholate. CC {ECO:0000269|PubMed:14695443}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) CC (TC 2.A.66.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23256.1; -; Genomic_DNA. DR PIR; B64173; B64173. DR RefSeq; NP_439754.1; NC_000907.1. DR RefSeq; WP_005693623.1; NC_000907.1. DR STRING; 71421.HI1612; -. DR DNASU; 950466; -. DR EnsemblBacteria; AAC23256; AAC23256; HI_1612. DR GeneID; 950466; -. DR KEGG; hin:HI1612; -. DR PATRIC; 20191955; VBIHaeInf48452_1685. DR eggNOG; ENOG4107QI1; Bacteria. DR eggNOG; COG0534; LUCA. DR KO; K03327; -. DR OMA; SIVFMLP; -. DR OrthoDB; EOG6423C5; -. DR PhylomeDB; P45272; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042895; F:antibiotic transporter activity; IBA:GO_Central. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042891; P:antibiotic transport; IBA:GO_Central. DR GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central. DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Antiport; Cell inner membrane; Cell membrane; KW Complete proteome; Ion transport; Membrane; Reference proteome; KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 464 Multidrug resistance protein HmrM. FT /FTId=PRO_0000164219. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 134 154 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 248 268 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT TRANSMEM 348 368 Helical. {ECO:0000255}. FT TRANSMEM 391 411 Helical. {ECO:0000255}. FT TRANSMEM 423 443 Helical. {ECO:0000255}. SQ SEQUENCE 464 AA; 51307 MW; 55E8CBA13CB4DB23 CRC64; MNFRLLSQYH ADIKKLIKIS LPILLAQIAQ NSMGLADTIM AGRVSSTDMA AISIGASIWM PLMFFGQGLL LALPPTISYL NGSGQHHRIA HQVRQGIWLV LGVSIPLGLL IYFCEIPLQY MQMESKMSDL ARDYLHAMLW GLPAYLMLIN FRCLNDGIEK TKPAMVITFL GLLINIPLNY IFIYGKFGMP AFGAVGCGIA TAIVNWAMCL MMIFYSYTNT QERSLKVFSQ LIEMPNPKTL KKLLRLGLPI AIAICCEVAL YALTSLMLSP LGATIVASHQ ITLNTSSFIF MFPMSIGMAT TILVGQALGA GSPQNAKKIG YAALLLGLTV TIVTALITIF FRYEIASIFV TDEIVIAMAA NLLLFAALYQ FSDTIQMVVG GILRGYKDTK VILYITLFSY WVIGVPLGYT LGRTDWLVPH IDAKGFWIAF VVSLTFAAFL LSLRMKKMQA MNDNAILQRL EKLK // ID HOFB_HAEIN Reviewed; 464 AA. AC P44622; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Protein transport protein HofB homolog; GN Name=hofB; Synonyms=hopB; OrderedLocusNames=HI_0298; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the GSP E 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; L42023; AAC21962.1; -; Genomic_DNA. DR PIR; E64060; E64060. DR RefSeq; NP_438465.1; NC_000907.1. DR RefSeq; WP_005694368.1; NC_000907.1. DR ProteinModelPortal; P44622; -. DR STRING; 71421.HI0298; -. DR EnsemblBacteria; AAC21962; AAC21962; HI_0298. DR GeneID; 949957; -. DR KEGG; hin:HI0298; -. DR PATRIC; 20189135; VBIHaeInf48452_0314. DR eggNOG; ENOG4107QHF; Bacteria. DR eggNOG; COG2804; LUCA. DR KO; K02504; -. DR OMA; QRVTAKN; -. DR OrthoDB; EOG63Z76W; -. DR PhylomeDB; P44622; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR007831; GSPII_E_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR Pfam; PF05157; T2SSE_N; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00662; T2SP_E; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 464 Protein transport protein HofB homolog. FT /FTId=PRO_0000207306. FT NP_BIND 264 271 ATP. {ECO:0000255}. SQ SEQUENCE 464 AA; 52984 MW; 4923156BE45BD6A2 CRC64; MTSYALLHTQ RVTAKNGEVF TISPDLWERN QQQQSLLLRY FALPLKEENN RLWLGVDSLS NLSACETIAF ITGKPVEPIL LESSQLKELL QQLTPNQMQV EEQVKFYQHQ ETHFEQEDDE PVIRLLNQIF ESALQKNASD IHLETLADQF QVRFRIDGVL QPQPLISKIF ANRIISRLKL LAKLDISENR LPQDGRFQFK TTFSDILDFR LSTLPTHWGE KIVLRAQQNK PVELSFSELG MTENQQQAFQ RVLSQPQGLI LVTGPTGSGK SISLYTALQW LNTPDKHIMT AEDPIEIELD GIIQSQINPQ IGLDFNRLLR TFLRQDPDII MLGEIRDEES AMIALRAAQT GHLVLSTLHT NDAISAISRL QQLGIQQYEI KNSLLLVIAQ RLVRKLCSKC GGNLANSCDC HQGYRGRIGV YQFLHWQQND YQTDFKNLRA SGLEKVSQGI TDEKEIERVL GKNL // ID HPPK_HAEIN Reviewed; 160 AA. AC P43777; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 115. DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; DE EC=2.7.6.3; DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; DE Short=PPPK; DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; DE Short=HPPK; GN Name=folK; OrderedLocusNames=HI_0064; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=10080886; DOI=10.1006/jmbi.1999.2623; RA Hennig M., Dale G.E., D'Arcy A., Danel F., Fischer S., Gray C.P., RA Jolidon S., Mueller F., Page M.G.P., Pattison P., Oefner C.; RT "The structure and function of the 6-hydroxymethyl-7,8-dihydropterin RT pyrophosphokinase from Haemophilus influenzae."; RL J. Mol. Biol. 287:211-219(1999). CC -!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP CC + 6-hydroxymethyl-7,8-dihydropterin diphosphate. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2- CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate CC from 7,8-dihydroneopterin triphosphate: step 4/4. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the HPPK 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; L42023; AAC21742.1; -; Genomic_DNA. DR RefSeq; NP_438237.1; NC_000907.1. DR RefSeq; WP_005693858.1; NC_000907.1. DR PDB; 1CBK; X-ray; 2.02 A; A/B=1-160. DR PDBsum; 1CBK; -. DR ProteinModelPortal; P43777; -. DR SMR; P43777; 1-160. DR STRING; 71421.HI0064; -. DR EnsemblBacteria; AAC21742; AAC21742; HI_0064. DR GeneID; 950962; -. DR KEGG; hin:HI0064; -. DR PATRIC; 20188583; VBIHaeInf48452_0065. DR eggNOG; ENOG4105K8U; Bacteria. DR eggNOG; COG0801; LUCA. DR KO; K00950; -. DR OMA; DWFLNAA; -. DR OrthoDB; EOG6XHC8G; -. DR PhylomeDB; P43777; -. DR UniPathway; UPA00077; UER00155. DR EvolutionaryTrace; P43777; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.70.560; -; 1. DR InterPro; IPR000550; Hppk. DR Pfam; PF01288; HPPK; 1. DR SUPFAM; SSF55083; SSF55083; 1. DR TIGRFAMs; TIGR01498; folK; 1. DR PROSITE; PS00794; HPPK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Folate biosynthesis; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 160 2-amino-4-hydroxy-6- FT hydroxymethyldihydropteridine FT pyrophosphokinase. FT /FTId=PRO_0000168250. FT STRAND 2 10 {ECO:0000244|PDB:1CBK}. FT HELIX 15 27 {ECO:0000244|PDB:1CBK}. FT STRAND 32 37 {ECO:0000244|PDB:1CBK}. FT STRAND 41 43 {ECO:0000244|PDB:1CBK}. FT STRAND 49 51 {ECO:0000244|PDB:1CBK}. FT STRAND 54 63 {ECO:0000244|PDB:1CBK}. FT HELIX 67 80 {ECO:0000244|PDB:1CBK}. FT STRAND 95 101 {ECO:0000244|PDB:1CBK}. FT STRAND 106 110 {ECO:0000244|PDB:1CBK}. FT STRAND 112 114 {ECO:0000244|PDB:1CBK}. FT HELIX 116 120 {ECO:0000244|PDB:1CBK}. FT HELIX 122 131 {ECO:0000244|PDB:1CBK}. FT HELIX 143 146 {ECO:0000244|PDB:1CBK}. FT HELIX 147 150 {ECO:0000244|PDB:1CBK}. SQ SEQUENCE 160 AA; 18299 MW; 136CD15F8844FDDD CRC64; MITAYIALGS NLNTPVEQLH AALKAISQLS NTHLVTTSSF YKSKPLGPQD QPDYVNAVAK IETELSPLKL LDELQRIENE QGRVRLRRWG ERTLDLDILL YGNEIIQNER LTIPHYDMHN REFVIVPLFE IASDLVLPNS QIITELVKQF ADHKMIKLNP // ID HSCB_HAEIN Reviewed; 174 AA. AC Q57006; P96333; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Co-chaperone protein HscB homolog; GN Name=hscB; OrderedLocusNames=HI_0375; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Co-chaperone involved in the maturation of iron-sulfur CC cluster-containing proteins. Seems to help targeting proteins to CC be folded toward HscA (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 J 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; L42023; AAC22032.1; -; Genomic_DNA. DR PIR; D64150; D64150. DR RefSeq; NP_438536.1; NC_000907.1. DR RefSeq; WP_005693789.1; NC_000907.1. DR ProteinModelPortal; Q57006; -. DR STRING; 71421.HI0375; -. DR EnsemblBacteria; AAC22032; AAC22032; HI_0375. DR GeneID; 949448; -. DR KEGG; hin:HI0375; -. DR PATRIC; 20189295; VBIHaeInf48452_0393. DR eggNOG; ENOG4108SWN; Bacteria. DR eggNOG; COG1076; LUCA. DR KO; K04082; -. DR OMA; FNPFQIF; -. DR OrthoDB; EOG66F07J; -. DR PhylomeDB; Q57006; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0051259; P:protein oligomerization; IEA:InterPro. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 1.20.1280.20; -; 1. DR HAMAP; MF_00682; HscB; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR004640; HscB. DR InterPro; IPR009073; HscB_oligo_C. DR PANTHER; PTHR14021; PTHR14021; 1. DR Pfam; PF07743; HSCB_C; 1. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; SSF46565; 1. DR SUPFAM; SSF47144; SSF47144; 1. DR TIGRFAMs; TIGR00714; hscB; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Reference proteome. FT CHAIN 1 174 Co-chaperone protein HscB homolog. FT /FTId=PRO_0000070971. FT DOMAIN 3 75 J. SQ SEQUENCE 174 AA; 20431 MW; 13BB2F423408EDD4 CRC64; MFNPFQIFDL PVDFQLDEKV LNARYLKLQK ALHPDNFVSS NALDQRVAMQ KSTEVNDALK TLKDPILRAE AIIALNTGEQ LDLEQKSTQD VAFLMQQLQW REQLEEVERQ QDERALNAFA KEIKQETQSL LTALFESLKS QQWARASQYC DKLRFTHKLS EEIERVEERI FELD // ID HOFC_HAEIN Reviewed; 406 AA. AC P44621; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Protein transport protein HofC homolog; GN Name=hofC; Synonyms=hopC; OrderedLocusNames=HI_0297; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GSP F 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; L42023; AAC21961.1; -; Genomic_DNA. DR PIR; D64060; D64060. DR RefSeq; NP_438464.1; NC_000907.1. DR RefSeq; WP_005694369.1; NC_000907.1. DR STRING; 71421.HI0297; -. DR EnsemblBacteria; AAC21961; AAC21961; HI_0297. DR GeneID; 950200; -. DR KEGG; hin:HI0297; -. DR PATRIC; 20189133; VBIHaeInf48452_0313. DR eggNOG; ENOG4105D7Q; Bacteria. DR eggNOG; COG1459; LUCA. DR KO; K02505; -. DR OMA; KIATHRS; -. DR OrthoDB; EOG6Z6FTM; -. DR PhylomeDB; P44621; -. DR Proteomes; UP000000579; 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:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR003004; GspF/PilC. DR InterPro; IPR018076; T2SS_F. DR InterPro; IPR001992; Type_2_secretion_system_CS. DR Pfam; PF00482; T2SSF; 2. DR PRINTS; PR00812; BCTERIALGSPF. DR PROSITE; PS00874; T2SP_F; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 406 Protein transport protein HofC homolog. FT /FTId=PRO_0000207846. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 214 234 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. SQ SEQUENCE 406 AA; 46291 MW; 429D83B7C10F8F82 CRC64; MTKKLFYYQA SNPLNQKQKG SIIADTKQQA HFQLISRGLT HIKLQQNWQF GAKPKNSEIS ELLNQLATLL QSAIPLKNSL QILQQNCTQI VLNEWLERLL QSIESGLAFS QAIEQQGKYL TQQEIQLIQV GEMTGKLAVV CKKIATHRSQ SLALQRKLQK IMLYPSMVLG ISLLLTLALL LFIVPQFAEM YSGNNAELPT ITAILLSISN FLKQNIGILL FFVLSFFLFY YFYLKRQTWF YQKKNQLISI TPIFGTIQKL SRLVNFSQSL QIMLQAGVPL NQALDSFLPR TQTWQTKKTL VNDIVLDKEV RSILQWVSQG YAFSNSVSSD LFPMEAQQML QIGEQSGKLA LMLEHIAENY QEKLNHQIDL LSQMLEPLMM VIIGSLIGII MMGMYLPIFN MGSVIQ // ID HRPA_HAEIN Reviewed; 1304 AA. AC P45018; P44108; P44109; P71368; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 114. DE RecName: Full=ATP-dependent RNA helicase HrpA homolog; DE EC=3.6.4.13; GN Name=hrpA; OrderedLocusNames=HI_1070; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH CC subfamily. {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; L42023; AAC22728.1; -; Genomic_DNA. DR PIR; G64165; G64165. DR PIR; I64019; I64019. DR RefSeq; NP_439228.2; NC_000907.1. DR ProteinModelPortal; P45018; -. DR STRING; 71421.HI1070; -. DR EnsemblBacteria; AAC22728; AAC22728; HI_1070. DR GeneID; 950050; -. DR KEGG; hin:HI1070; -. DR PATRIC; 20190803; VBIHaeInf48452_1114. DR eggNOG; ENOG4105CQ7; Bacteria. DR eggNOG; COG1643; LUCA. DR KO; K03578; -. DR OMA; YIKLMTD; -. DR OrthoDB; EOG6PP9H5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0044822; F:poly(A) RNA binding; IBA:GO_Central. DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR011709; DUF1605. DR InterPro; IPR007502; Helicase-assoc_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR024590; HrpA_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010222; RNA_helicase_HrpA. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF11898; DUF3418; 1. DR Pfam; PF04408; HA2; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07717; OB_NTP_bind; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00847; HA2; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01967; DEAH_box_HrpA; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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. FT CHAIN 1 1304 ATP-dependent RNA helicase HrpA homolog. FT /FTId=PRO_0000055179. FT DOMAIN 93 257 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 281 448 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 106 113 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 203 206 DEAH box. SQ SEQUENCE 1304 AA; 149626 MW; 179B59B57FBA5867 CRC64; MKNSSVKHTL TPLQQSLFSQ LNDIMLVDQR RLSARIHGIG KIKSQEAQQA VAAEIQQQIE QARLRVEQRK SAVQNPIVFP ESLPVSQRKV EIQKLISEHQ VIVVAGETGS GKTTQLPKMC LELGFGNLGM IGHTQPRRIA ARSVAARIAE ELETELGGLV GYKVRFNDQI SDNTQIKLMT DGILLAEIQN DRFLNQYSCL IIDEAHERSL NNDFILGYLK QLLPRRRRDL KLIITSATID VERFSKHFNN APIIEVSGRT YPVEVRYRPV VEEDDQDQLQ GILNAVDELQ AEGRGDILIF MNGEREIRDT AEALQKQNLK HTEILPLFAR LSAQEQNKIF HPSGLNRIVL ATNVAETSLT VPSIKYVIDP GTARISRYSY RTKVQRLPIE PISQASANQR KGRCGRVSEG ICIRLYSEED FNSRPEFTDP EILRTNLASV ILQMTALGLD DIEAFPFVDA PDERHIQDGV KLLEELGAFE TVQTKSGEKR LLTRVGRQLA QLPVDPRLAK MILSAVNFGC VYEMMIIVSA LSIQDPRERP QEKQQASDEK HRRFADKKSD FLAFLNLWRY LQEQQKESSK NQFRRQCQKD FLNYLRIREW QDIYHQIRLT VREMSLPINS EKAEYQQIHT ALLSGLLSHI GLKEAEKQQY LGARNAHFAI FPNSVLFKKQ PKWVMAAELV ETSKLWGRMV AEIEPEWIEP LAEHLIKKSY SVPLWSKSRG AVIADEKVTL YGVPIVAVRP VNYGAIDPTV SREIFIQSAL VEGGWNTKHK FFKENQRLVR EVEELEHKSR RRDILVDDRT LFEFYDQRIG TEVVSQKHFD TWWKKAQQKD PELLNFEHSF LINDDAEQVS KLDFPNFWHQ GNLKLKLTYQ FEPGTDADGV TVHIPLPLLN QVEMTGFDWQ IPGLREELVI ALIKSLPKSY RRNFVPAPNY AQAFLSRAVP LEKPLLDTLI YELRRMTGVT VEAEHWNWEQ IPSHLKMTFR VVDENGKKIA ESMNLDELKF NLKDRVQESI SAVADDGIEQ SGLHIWSFAD LPQCYEQKQR GFSVKAFPAI VDEKDAVGIK LFETEFEQSV AMQQGLRRLL LLNVPSPIKY LHEKLPNKAK LGLYFTPFGR VLDLIDDCIA CAVDKLIADF GGFVWDEAGF EKLRDFVREN LNEVTVDIAQ KVEQILTLTY QLNQRLKGKM DFTMAFALSD IKSQLAGLVY QGFVQKSGYD RLPDLQRYLQ AVDKRIDKLA QDVNRDRAAM LRVEQVQQAY QQLLAKLPKS KPISDEVAEI RYMIEELRVS LFAQQLGTKY QISDKRIGNI ISQY // ID HSCA_HAEIN Reviewed; 619 AA. AC P44669; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Chaperone protein HscA homolog; GN Name=hscA; OrderedLocusNames=HI_0373; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur CC cluster-containing proteins. Has a low intrinsic ATPase activity CC which is markedly stimulated by HscB (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; L42023; AAC22031.1; -; Genomic_DNA. DR PIR; B64064; B64064. DR RefSeq; NP_438534.1; NC_000907.1. DR RefSeq; WP_005693792.1; NC_000907.1. DR ProteinModelPortal; P44669; -. DR SMR; P44669; 388-615. DR STRING; 71421.HI0373; -. DR TCDB; 9.A.41.1.1; the capsular polysaccharide exporter (cps-e) family. DR EnsemblBacteria; AAC22031; AAC22031; HI_0373. DR GeneID; 949476; -. DR KEGG; hin:HI0373; -. DR PATRIC; 20189291; VBIHaeInf48452_0391. DR eggNOG; ENOG4105C9I; Bacteria. DR eggNOG; COG0443; LUCA. DR KO; K04044; -. DR OMA; LRGIPAM; -. DR OrthoDB; EOG6JMMSV; -. DR PhylomeDB; P44669; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1270.10; -; 1. DR Gene3D; 2.60.34.10; -; 1. DR HAMAP; MF_00679; HscA; 1. 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 InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF100920; SSF100920; 1. DR SUPFAM; SSF100934; SSF100934; 1. DR TIGRFAMs; TIGR01991; HscA; 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 Reference proteome. FT CHAIN 1 619 Chaperone protein HscA homolog. FT /FTId=PRO_0000078630. SQ SEQUENCE 619 AA; 66917 MW; A9047BAC5F804C2E CRC64; MALLQIAEPG QAAAPHQHRL AVGIDLGTTN SLVASVRSGQ SVILNDEQER SLVPSVVHYG VEEKKVGLEA FEQASLDPKN TVISVKRLIG RSLSDVQSRY SSLPYEFVAS ENGLPLIITA QGAKSPIEVS SDILSRLNHI AEQRLGGELS GVVITVPAYF DDAQRQSTKD AARLAGLNVL RLLNEPTAAA LAYGLDSGQE GIIAVYDLGG GTFDISILRL SKGIFEVLAT GGDTALGGDD FDHLIADWVI EQTKLKPQTA NQQRELITLA NQAKITLTNE KSAVISWQDF SVEISREQFN ELIYPLVKRS LLTCRRALKD ANVESEEVQA VVMVGGSTRV PYVREQVGEF FGKTPLTSID PDKVVALGAA IQADILVGNK TDSDMLLLDV VPLSLGIETM GGLVEKIIPR NTTIPVARAQ EFTTFKDGQT AMTVHVLQGE RELVDDCRSL GRFTLRGIPP MAAGAAHIRV TYQVDADGLL SVTAMEKSTK VQASIQIKPS YGLTDEEVTA MIKSSFDNAQ EDLQARELAE QRVEADRVIE SVIVALQADG AELLSTDEFH HIETVLKQLM DVKQGSDRDA IAQGIKALDT ATQEFAARRM NASINKALTG KNLSDIENP // ID HSLR_HAEIN Reviewed; 131 AA. AC P44754; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Heat shock protein 15 homolog; DE Short=HSP15; GN Name=hslR; OrderedLocusNames=HI_0562; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the recycling of free 50S ribosomal subunits CC that still carry a nascent chain. Binds RNA more specifically than CC DNA. Binds with very high affinity to the free 50S ribosomal CC subunit. Does not bind it when it is part of the 70S ribosome (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HSP15 family. {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; L42023; AAC22220.1; -; Genomic_DNA. DR PIR; F64154; F64154. DR RefSeq; NP_438719.1; NC_000907.1. DR RefSeq; WP_005654696.1; NC_000907.1. DR ProteinModelPortal; P44754; -. DR SMR; P44754; 5-107. DR STRING; 71421.HI0562; -. DR EnsemblBacteria; AAC22220; AAC22220; HI_0562. DR GeneID; 949610; -. DR KEGG; hin:HI0562; -. DR PATRIC; 20189679; VBIHaeInf48452_0582. DR eggNOG; ENOG4105VEJ; Bacteria. DR eggNOG; COG1188; LUCA. DR KO; K04762; -. DR OMA; RFYKTRT; -. DR OrthoDB; EOG64NB4B; -. DR PhylomeDB; P44754; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:InterPro. DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro. DR GO; GO:0034605; P:cellular response to heat; IEA:InterPro. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR025708; HSP15. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF01479; S4; 1. DR PIRSF; PIRSF016821; HSP15; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; RNA-binding. FT CHAIN 1 131 Heat shock protein 15 homolog. FT /FTId=PRO_0000201744. FT DOMAIN 6 67 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. SQ SEQUENCE 131 AA; 15505 MW; 881BB444C3ABD776 CRC64; MAEKEVRLDK WLWAARFYKT RSIAKAMIES GKVHYNNQRA KVSKIVEVGA MLKLRQGNEE KEIKIIALSD QRRGAPEAQL LYQETESSVK KREEIAWARK NNSLSMPHPD RRPNKKERRD LLKFKHQDKF E // ID HSLV_HAEIN Reviewed; 175 AA. AC P43772; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 116. DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248}; DE EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248}; GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248}; GN OrderedLocusNames=HI_0496; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15037245; DOI=10.1016/j.jsb.2003.11.003; RA Kwon A.-R., Trame C.B., McKay D.B.; RT "Kinetics of protein substrate degradation by HslUV."; RL J. Struct. Biol. 146:141-147(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLU. RX PubMed=11106733; DOI=10.1016/S0092-8674(00)00166-5; RA Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., RA McKay D.B.; RT "Crystal and solution structures of an HslUV protease-chaperone RT complex."; RL Cell 103:633-643(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH POTASSIUM OR RP SODIUM. RX PubMed=11717526; DOI=10.1107/S090744490101575X; RA Sousa M.C., McKay D.B.; RT "Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, RT revealing a cation-binding site near the catalytic site."; RL Acta Crystallogr. D 57:1950-1954(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU RP AND INHIBITOR, AND ENZYME REGULATION. RX PubMed=12054822; DOI=10.1016/S0022-2836(02)00145-6; RA Sousa M.C., Kessler B.M., Overkleeft H.S., McKay D.B.; RT "Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: RT corroboration of a proposed mechanism of allosteric activation of HslV RT by HslU."; RL J. Mol. Biol. 318:779-785(2002). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLU; RP MAGNESIUM; ADP AND INHIBITOR. RX PubMed=12823960; DOI=10.1016/S0022-2836(03)00580-1; RA Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.; RT "Structure and reactivity of an asymmetric complex between HslV and I- RT domain deleted HslU, a prokaryotic homolog of the eukaryotic RT proteasome."; RL J. Mol. Biol. 330:185-195(2003). CC -!- FUNCTION: Protease subunit of a proteasome-like degradation CC complex believed to be a general protein degrading machinery. CC -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- ENZYME REGULATION: Allosterically activated by HslU binding. CC {ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:12054822}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.3 uM for Arc-H(6)-SulA(CT) {ECO:0000269|PubMed:15037245}; CC Note=Arc-H(6)-SulA(CT) is a construct consisting of the Arc CC repressor protein fused to 6 His residues and the 11 carboxy CC terminal residues of SulA.; CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP. CC {ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:11106733, CC ECO:0000269|PubMed:11717526, ECO:0000269|PubMed:12054822, CC ECO:0000269|PubMed:12823960}. CC -!- INTERACTION: CC P43773:hslU; NbExp=4; IntAct=EBI-1030290, EBI-1030296; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00248}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22153.1; -; Genomic_DNA. DR PIR; C64072; C64072. DR RefSeq; NP_438654.1; NC_000907.1. DR RefSeq; WP_005649427.1; NC_000907.1. DR PDB; 1G3I; X-ray; 3.41 A; G/H/I/J/K/L/M/N/O/P/Q/R=2-175. DR PDB; 1G3K; X-ray; 1.90 A; A/B/C=2-175. DR PDB; 1JJW; X-ray; 1.90 A; A/B/C=2-175. DR PDB; 1KYI; X-ray; 3.10 A; G/H/I/J/K/L/M/N/O/P/Q/R=2-175. DR PDB; 1OFH; X-ray; 2.50 A; G/H/I/L/M/N=2-175. DR PDB; 1OFI; X-ray; 3.20 A; G/H/I/L/M/N=2-175. DR PDBsum; 1G3I; -. DR PDBsum; 1G3K; -. DR PDBsum; 1JJW; -. DR PDBsum; 1KYI; -. DR PDBsum; 1OFH; -. DR PDBsum; 1OFI; -. DR ProteinModelPortal; P43772; -. DR SMR; P43772; 2-174. DR DIP; DIP-6176N; -. DR IntAct; P43772; 1. DR STRING; 71421.HI0496; -. DR MEROPS; T01.006; -. DR EnsemblBacteria; AAC22153; AAC22153; HI_0496. DR GeneID; 949571; -. DR KEGG; hin:HI0496; -. DR PATRIC; 20189543; VBIHaeInf48452_0514. DR eggNOG; ENOG4108R5P; Bacteria. DR eggNOG; COG5405; LUCA. DR KO; K01419; -. DR OMA; IMKGNAR; -. DR OrthoDB; EOG6ND0PJ; -. DR PhylomeDB; P43772; -. DR EvolutionaryTrace; P43772; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00248; HslV; 1. DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PIRSF; PIRSF039093; HslV; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm; KW Hydrolase; Metal-binding; Protease; Reference proteome; Sodium; KW Threonine protease. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 175 ATP-dependent protease subunit HslV. FT /FTId=PRO_0000148111. FT ACT_SITE 2 2 FT METAL 158 158 Sodium; via carbonyl oxygen. FT METAL 161 161 Sodium; via carbonyl oxygen. FT METAL 164 164 Sodium; via carbonyl oxygen. FT STRAND 4 9 {ECO:0000244|PDB:1G3K}. FT STRAND 12 17 {ECO:0000244|PDB:1G3K}. FT STRAND 21 23 {ECO:0000244|PDB:1G3K}. FT STRAND 26 30 {ECO:0000244|PDB:1G3K}. FT STRAND 35 38 {ECO:0000244|PDB:1G3K}. FT TURN 39 42 {ECO:0000244|PDB:1G3K}. FT STRAND 43 49 {ECO:0000244|PDB:1G3K}. FT HELIX 51 67 {ECO:0000244|PDB:1G3K}. FT TURN 68 70 {ECO:0000244|PDB:1G3K}. FT HELIX 72 85 {ECO:0000244|PDB:1G3K}. FT HELIX 89 91 {ECO:0000244|PDB:1G3K}. FT STRAND 95 99 {ECO:0000244|PDB:1G3K}. FT STRAND 104 108 {ECO:0000244|PDB:1G3K}. FT TURN 109 111 {ECO:0000244|PDB:1G3K}. FT STRAND 112 114 {ECO:0000244|PDB:1G3K}. FT STRAND 121 125 {ECO:0000244|PDB:1G3K}. FT HELIX 128 141 {ECO:0000244|PDB:1G3K}. FT HELIX 146 160 {ECO:0000244|PDB:1G3K}. FT STRAND 169 173 {ECO:0000244|PDB:1G3K}. SQ SEQUENCE 175 AA; 19012 MW; CEA1C77B7AB2724C CRC64; MTTIVSVRRN GQVVVGGDGQ VSLGNTVMKG NARKVRRLYN GKVLAGFAGG TADAFTLFEL FERKLEMHQG HLLKSAVELA KDWRTDRALR KLEAMLIVAD EKESLIITGI GDVVQPEEDQ ILAIGSGGNY ALSAARALVE NTELSAHEIV EKSLRIAGDI CVFTNTNFTI EELPN // ID HPRT_HAEIN Reviewed; 179 AA. AC P45078; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Hypoxanthine phosphoribosyltransferase; DE Short=HPRT; DE EC=2.4.2.8; GN Name=hpt; OrderedLocusNames=HI_1153; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts preferentially on hypoxanthine; has very low CC activity towards guanine. Inactive towards xanthine (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho- CC alpha-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 -!- SUBUNIT: Homotetramer. 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; L42023; AAC22808.1; -; Genomic_DNA. DR PIR; D64168; D64168. DR RefSeq; NP_439311.1; NC_000907.1. DR RefSeq; WP_005693468.1; NC_000907.1. DR ProteinModelPortal; P45078; -. DR SMR; P45078; 3-177. DR STRING; 71421.HI1153; -. DR EnsemblBacteria; AAC22808; AAC22808; HI_1153. DR GeneID; 950117; -. DR KEGG; hin:HI1153; -. DR PATRIC; 20190981; VBIHaeInf48452_1203. DR eggNOG; ENOG4108UGV; Bacteria. DR eggNOG; COG0634; LUCA. DR KO; K00760; -. DR OMA; TMDWMAV; -. DR OrthoDB; EOG693GNP; -. DR PhylomeDB; P45078; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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 1 179 Hypoxanthine phosphoribosyltransferase. FT /FTId=PRO_0000139634. FT NP_BIND 101 110 IMP. {ECO:0000250}. FT NP_BIND 160 161 IMP. {ECO:0000250}. FT ACT_SITE 105 105 Proton acceptor. {ECO:0000250}. FT METAL 161 161 Magnesium. {ECO:0000250}. FT BINDING 133 133 IMP. {ECO:0000250}. FT BINDING 155 155 IMP; via carbonyl oxygen. {ECO:0000250}. SQ SEQUENCE 179 AA; 20370 MW; 65F8C1314942BFE7 CRC64; MKKHHVDVLI SENDVHARIA ELGAQITKFY QEKQIDNLVV VGLLRGSFMF MADIVRQINL PVEIEFMTTS SYGTGMTTNH DVRITKDLDG DIKGKHVLIV EDIIDTGYTL EKVRDILNLR EPASLTICTL LDKPSRREVE VPVEWVGFEI PDEFVVGYGI DYAQRHRNLG YIGKVVLEE // ID HSLO_HAEIN Reviewed; 293 AA. AC P44877; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=33 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00117}; DE AltName: Full=Heat shock protein 33 homolog {ECO:0000255|HAMAP-Rule:MF_00117}; DE Short=HSP33 {ECO:0000255|HAMAP-Rule:MF_00117}; GN Name=hslO {ECO:0000255|HAMAP-Rule:MF_00117}; GN OrderedLocusNames=HI_0810; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Redox regulated molecular chaperone. Protects both CC thermally unfolding and oxidatively damaged proteins from CC irreversible aggregation. Plays an important role in the bacterial CC defense system toward oxidative stress. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- PTM: Under oxidizing conditions two disulfide bonds are formed CC involving the reactive cysteines. Under reducing conditions zinc CC is bound to the reactive cysteines and the protein is inactive. CC {ECO:0000255|HAMAP-Rule:MF_00117}. CC -!- SIMILARITY: Belongs to the HSP33 family. {ECO:0000255|HAMAP- CC Rule:MF_00117}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22469.1; -; Genomic_DNA. DR PIR; H64158; H64158. DR RefSeq; NP_438970.1; NC_000907.1. DR RefSeq; WP_005693176.1; NC_000907.1. DR ProteinModelPortal; P44877; -. DR SMR; P44877; 11-239. DR STRING; 71421.HI0810; -. DR EnsemblBacteria; AAC22469; AAC22469; HI_0810. DR GeneID; 950307; -. DR KEGG; hin:HI0810; -. DR PATRIC; 20190275; VBIHaeInf48452_0851. DR eggNOG; ENOG4105F4C; Bacteria. DR eggNOG; COG1281; LUCA. DR KO; K04083; -. DR OMA; DMQCECC; -. DR OrthoDB; EOG651SSJ; -. DR PhylomeDB; P44877; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.10.287.480; -; 1. DR Gene3D; 3.55.30.10; -; 1. DR Gene3D; 3.90.1280.10; -; 1. DR HAMAP; MF_00117; HslO; 1. DR InterPro; IPR000397; Heat_shock_Hsp33. DR InterPro; IPR016154; Heat_shock_Hsp33_C. DR InterPro; IPR016153; Heat_shock_Hsp33_N. DR InterPro; IPR023212; Hsp33_helix_hairpin_bin_dom. DR Pfam; PF01430; HSP33; 1. DR PIRSF; PIRSF005261; Heat_shock_Hsp33; 1. DR SUPFAM; SSF118352; SSF118352; 1. DR SUPFAM; SSF64397; SSF64397; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Disulfide bond; KW Redox-active center; Reference proteome; Zinc. FT CHAIN 1 293 33 kDa chaperonin. FT /FTId=PRO_0000192180. FT DISULFID 237 239 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. FT DISULFID 271 274 Redox-active. {ECO:0000255|HAMAP- FT Rule:MF_00117}. SQ SEQUENCE 293 AA; 33103 MW; 05C25281B6CCE96A CRC64; MTNQQDYTQD NDKLYRYLFQ HRAVRGEWVR LNKTFTDTLN THQYPKAVQD LLGEMMVATN LLTATLKFAG NITVQIQGDG PLRLALVNGN DQQQIRALAR VDGNITENMS LHNMIGKGVL VITIAPKEGE RYQGVISLDK PTITECLEDY FVRSEQLQTQ LIIRTGEYEG KPVAAGMLLQ IMPDGSGTPE DFEHLTTLAA TVKDEELFGL PAEELLYRLY HEETVNLYPA QDVQFFCGCS AERSSSALLL ISDEEIDEIL AEHKGRIDMQ CECCGTHYFF NKEAIEKLKS TRV // ID HXUB1_HAEIN Reviewed; 565 AA. AC P44601; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Heme/hemopexin transporter protein HuxB; DE Flags: Precursor; GN Name=hxuB; OrderedLocusNames=HI_0263; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Likely functions in the release of soluble HxuA from the CC cell. {ECO:0000250}. CC -!- FUNCTION: Probable member of a two partner secretion pathway (TPS) CC in which it mediates the secretion of HuxA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane. CC -!- DOMAIN: Probably a beta-barrel protein. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TPS (TC 1.B.20) family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 POTRA domain. {ECO:0000255|PROSITE- CC ProRule:PRU01115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21928.1; -; Genomic_DNA. DR PIR; D64058; D64058. DR RefSeq; NP_438432.1; NC_000907.1. DR RefSeq; WP_005694040.1; NC_000907.1. DR ProteinModelPortal; P44601; -. DR STRING; 71421.HI0263; -. DR EnsemblBacteria; AAC21928; AAC21928; HI_0263. DR GeneID; 949385; -. DR KEGG; hin:HI0263; -. DR PATRIC; 20189053; VBIHaeInf48452_0278. DR eggNOG; ENOG4108D1Y; Bacteria. DR eggNOG; COG2831; LUCA. DR OMA; NADKHQF; -. DR OrthoDB; EOG6SZ1CV; -. DR PhylomeDB; P44601; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR013686; Polypept-transport_assoc_ShlB. DR Pfam; PF08479; POTRA_2; 1. DR PROSITE; PS51779; POTRA; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Ion transport; Membrane; KW Porin; Protein transport; Reference proteome; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 26 {ECO:0000250}. FT CHAIN 27 565 Heme/hemopexin transporter protein HuxB. FT /FTId=PRO_0000021470. FT DOMAIN 73 150 POTRA. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 565 AA; 62824 MW; B83F82558F7F5A91 CRC64; MKMRPRYSVI ASAVSLGFVL SKSVMALDRP DTGSLNRELE QRQIQSEAKP SGELFNQTAN SPYTAQYKQG LKFPLKQVQI LDRNNQEVVT DELAHILKNY VGKEVSLSDL SNLANEISEF YRHNNYLVAK AILPPQEIEQ GTVKILLLKG NVGEIRLQNH SALSNKFVSR LSNTTVNASE FILKDELEKF ALTINDVPGV NAGLQLSAGK KVGEANLLIK INDAKRFSSY VSVDNQGNKY TGRYRLAAGT KVSNLNGWGD ELKLDLMSSN QANLKNARID YSSLIDGYST RFGVTANYLD YKLGGNFKSL QSQGHSHTLG AYLLHPTIRT PNFRLSTKVS FNHQNLTDKQ QAVYVKQKRK INSLTAGIDG SWNLIKDGTT YFSLSTLFGN LANQTSEKKQ YTKEDFQPQS HFTVYNYRLS HEQILPKSFA FNIGINGQFA DKTLESSQKM LLGGLSGVRG HQAGAASVDE GHLIQTEFKH YLPVFSQSVL VSSLFYDYGL GKYYKNSQFL EKGVKNSVKL QSVGAGLSLS DAGSYAINVS VAKPLDNNIN NADKHQFWLS MIKTF // ID HSLU_HAEIN Reviewed; 444 AA. AC P43773; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 124. DE RecName: Full=ATP-dependent protease ATPase subunit HslU; DE AltName: Full=Unfoldase HslU; GN Name=hslU; OrderedLocusNames=HI_0497; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLV RP AND ATP. RX PubMed=11106733; DOI=10.1016/S0092-8674(00)00166-5; RA Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., RA McKay D.B.; RT "Crystal and solution structures of an HslUV protease-chaperone RT complex."; RL Cell 103:633-643(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE. RX PubMed=11468391; DOI=10.1107/S0907444901007673; RA Trame C.B., McKay D.B.; RT "Structure of Haemophilus influenzae HslU protein in crystals with RT one-dimensional disorder twinning."; RL Acta Crystallogr. D 57:1079-1090(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLV; RP MAGNESIUM; ADP AND INHIBITOR. RX PubMed=12823960; DOI=10.1016/S0022-2836(03)00580-1; RA Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.; RT "Structure and reactivity of an asymmetric complex between HslV and I- RT domain deleted HslU, a prokaryotic homolog of the eukaryotic RT proteasome."; RL J. Mol. Biol. 330:185-195(2003). CC -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; CC this subunit has chaperone activity. The binding of ATP and its CC subsequent hydrolysis by HslU are essential for unfolding of CC protein substrates subsequently hydrolyzed by HslV. HslU CC recognizes the N-terminal part of its protein substrates and CC unfolds these before they are guided to HslV for hydrolysis. CC -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on CC each side by a ring-shaped HslU homohexamer. The assembly of the CC HslU/HslV complex is dependent on binding of ATP. CC {ECO:0000269|PubMed:11106733, ECO:0000269|PubMed:11468391, CC ECO:0000269|PubMed:12823960}. CC -!- INTERACTION: CC P43772:hslV; NbExp=4; IntAct=EBI-1030296, EBI-1030290; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22154.1; -; Genomic_DNA. DR RefSeq; NP_438655.1; NC_000907.1. DR RefSeq; WP_010868991.1; NC_000907.1. DR PDB; 1G3I; X-ray; 3.41 A; A/B/C/D/E/F/S/T/U/V/W/X=1-444. DR PDB; 1G41; X-ray; 2.30 A; A=1-444. DR PDB; 1IM2; X-ray; 2.80 A; A=1-444. DR PDB; 1KYI; X-ray; 3.10 A; A/B/C/D/E/F/S/T/U/V/W/X=1-444. DR PDB; 1OFH; X-ray; 2.50 A; A/B/C=1-107, A/B/C=244-444. DR PDB; 1OFI; X-ray; 3.20 A; A/B/C=1-107, A/B/C=244-444. DR PDBsum; 1G3I; -. DR PDBsum; 1G41; -. DR PDBsum; 1IM2; -. DR PDBsum; 1KYI; -. DR PDBsum; 1OFH; -. DR PDBsum; 1OFI; -. DR ProteinModelPortal; P43773; -. DR SMR; P43773; 1-444. DR DIP; DIP-6175N; -. DR IntAct; P43773; 1. DR STRING; 71421.HI0497; -. DR EnsemblBacteria; AAC22154; AAC22154; HI_0497. DR GeneID; 950614; -. DR KEGG; hin:HI0497; -. DR PATRIC; 20189545; VBIHaeInf48452_0515. DR eggNOG; ENOG4105C4N; Bacteria. DR eggNOG; COG1220; LUCA. DR KO; K03667; -. DR OMA; RLHTTIE; -. DR OrthoDB; EOG6NPM7G; -. DR PhylomeDB; P43773; -. DR EvolutionaryTrace; P43773; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro. DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00249; HslU; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR019489; Clp_ATPase_C. DR InterPro; IPR004491; HslU. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11262:SF3; PTHR11262:SF3; 2. DR Pfam; PF00004; AAA; 1. DR Pfam; PF07724; AAA_2; 1. DR Pfam; PF10431; ClpB_D2-small; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM01086; ClpB_D2-small; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00390; hslU; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 444 ATP-dependent protease ATPase subunit FT HslU. FT /FTId=PRO_0000160508. FT NP_BIND 60 65 ATP. {ECO:0000269|PubMed:11106733}. FT NP_BIND 306 309 ATP. {ECO:0000269|PubMed:11106733}. FT BINDING 18 18 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:11106733}. FT BINDING 257 257 ATP. {ECO:0000250}. FT BINDING 322 322 ATP. {ECO:0000250}. FT BINDING 394 394 ATP. {ECO:0000250}. FT HELIX 6 14 {ECO:0000244|PDB:1G41}. FT HELIX 21 39 {ECO:0000244|PDB:1G41}. FT TURN 42 47 {ECO:0000244|PDB:1G41}. FT STRAND 53 56 {ECO:0000244|PDB:1G41}. FT STRAND 58 62 {ECO:0000244|PDB:1G3I}. FT HELIX 63 73 {ECO:0000244|PDB:1G41}. FT STRAND 78 82 {ECO:0000244|PDB:1G41}. FT HELIX 83 86 {ECO:0000244|PDB:1G41}. FT HELIX 92 94 {ECO:0000244|PDB:1OFH}. FT HELIX 97 117 {ECO:0000244|PDB:1G41}. FT STRAND 123 128 {ECO:0000244|PDB:1IM2}. FT HELIX 228 230 {ECO:0000244|PDB:1G41}. FT STRAND 231 234 {ECO:0000244|PDB:1IM2}. FT HELIX 237 251 {ECO:0000244|PDB:1G41}. FT STRAND 253 257 {ECO:0000244|PDB:1G41}. FT HELIX 259 262 {ECO:0000244|PDB:1G41}. FT STRAND 269 271 {ECO:0000244|PDB:1G41}. FT HELIX 272 287 {ECO:0000244|PDB:1G41}. FT STRAND 290 293 {ECO:0000244|PDB:1G41}. FT STRAND 296 299 {ECO:0000244|PDB:1G41}. FT HELIX 300 302 {ECO:0000244|PDB:1IM2}. FT STRAND 304 309 {ECO:0000244|PDB:1G41}. FT STRAND 312 314 {ECO:0000244|PDB:1OFH}. FT HELIX 316 318 {ECO:0000244|PDB:1G41}. FT HELIX 321 324 {ECO:0000244|PDB:1G41}. FT STRAND 329 332 {ECO:0000244|PDB:1G41}. FT HELIX 338 346 {ECO:0000244|PDB:1G41}. FT HELIX 352 361 {ECO:0000244|PDB:1G41}. FT TURN 362 364 {ECO:0000244|PDB:1G41}. FT STRAND 366 369 {ECO:0000244|PDB:1G41}. FT HELIX 371 387 {ECO:0000244|PDB:1G41}. FT HELIX 392 394 {ECO:0000244|PDB:1G41}. FT HELIX 395 410 {ECO:0000244|PDB:1G41}. FT HELIX 411 413 {ECO:0000244|PDB:1G41}. FT STRAND 418 421 {ECO:0000244|PDB:1G41}. FT HELIX 423 430 {ECO:0000244|PDB:1G41}. FT TURN 431 435 {ECO:0000244|PDB:1G41}. FT HELIX 437 443 {ECO:0000244|PDB:1G41}. SQ SEQUENCE 444 AA; 49372 MW; C346EA478E4094CE CRC64; MSEMTPREIV SELDQHIIGQ ADAKRAVAIA LRNRWRRMQL QEPLRHEVTP KNILMIGPTG VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDSAMKL VRQQEIAKNR ARAEDVAEER ILDALLPPAK NQWGEVENHD SHSSTRQAFR KKLREGQLDD KEIEIDVSAG VSMGVEIMAP PGMEEMTNQL QSLFQNLGSD KTKKRKMKIK DALKALIDDE AAKLINPEEL KQKAIDAVEQ NGIVFIDEID KICKKGEYSG ADVSREGVQR DLLPLVEGST VSTKHGMVKT DHILFIASGA FQVARPSDLI PELQGRLPIR VELTALSAAD FERILTEPHA SLTEQYKALM ATEGVNIAFT TDAVKKIAEA AFRVNEKTEN IGARRLHTVM ERLMDKISFS ASDMNGQTVN IDAAYVADAL GEVVENEDLS RFIL // ID HSRA_HAEIN Reviewed; 463 AA. AC P44903; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Probable transport protein HsrA; GN Name=hsrA; OrderedLocusNames=HI_0852; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. EmrB 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; L42023; AAC22509.1; -; Genomic_DNA. DR PIR; B64160; B64160. DR RefSeq; NP_439012.1; NC_000907.1. DR RefSeq; WP_010869070.1; NC_000907.1. DR ProteinModelPortal; P44903; -. DR STRING; 71421.HI0852; -. DR EnsemblBacteria; AAC22509; AAC22509; HI_0852. DR GeneID; 949865; -. DR KEGG; hin:HI0852; -. DR PATRIC; 20190359; VBIHaeInf48452_0893. DR eggNOG; ENOG4105C0R; Bacteria. DR eggNOG; ENOG410XNN3; LUCA. DR OMA; MTERESY; -. DR OrthoDB; EOG651SWK; -. DR PhylomeDB; P44903; -. DR Proteomes; UP000000579; 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:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004638; Drug-R_transpt_efflux_EmrB. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR TIGRFAMs; TIGR00711; efflux_EmrB; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 463 Probable transport protein HsrA. FT /FTId=PRO_0000173410. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 82 102 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TRANSMEM 267 287 Helical. {ECO:0000255}. FT TRANSMEM 298 318 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. FT TRANSMEM 393 413 Helical. {ECO:0000255}. FT TRANSMEM 429 449 Helical. {ECO:0000255}. SQ SEQUENCE 463 AA; 50003 MW; D725EFFD50F9F23F CRC64; MTTESNAYRG LAWVAAMALF MQSLDATILN TALPAISSDL HKPAFEMQMA IIAYSLAVAL FIPLTAWAAA KFGTLTVFRS AVFTFILGSV ACAAASNLES LILARVIQGI GGAFMMPVAR LAIIQAVPKQ QLVNAWNLMA TAGLIGPILG PILGGWLVIH ASWHWIFLIN IPIGALGILA SGSVMNNIKG KAEKLDWTGF LLFALGLVGI TLGLDLLGES QHNSSVTYSI LVVGILLLVT YCGYAKNNEN AILPLSLFRT RTFRLGIIAN IFIRLSASGV PFLLPLMFQL SFGYSAEMSG WLLAPIALIS VMLKILIGRI LNRWGYKTTL ISSALLMAGS VISMAWLDKQ SSLTWIICNL MWYGACMSII FTSINTLAVG DLSKQQSGTG STVLSIVQQV GIGFGIAVSS IILNLYRHFF SASDCLPQAF SYTFLTSSLF VIALVWSLMK LHKHDGDHLR KMP // ID ILVD_HAEIN Reviewed; 612 AA. AC P44851; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=HI_0738; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- CC oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22397.1; -; Genomic_DNA. DR PIR; G64089; G64089. DR RefSeq; NP_438897.1; NC_000907.1. DR RefSeq; WP_005693142.1; NC_000907.1. DR STRING; 71421.HI0738; -. DR EnsemblBacteria; AAC22397; AAC22397; HI_0738. DR GeneID; 949825; -. DR KEGG; hin:HI0738; -. DR PATRIC; 20190117; VBIHaeInf48452_0774. DR eggNOG; ENOG4105C01; Bacteria. DR eggNOG; COG0129; LUCA. DR KO; K01687; -. DR OMA; QGRNMAG; -. DR OrthoDB; EOG6MSS24; -. DR PhylomeDB; P44851; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IBA:GO_Central. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR004404; DihydroxyA_deHydtase. DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR PANTHER; PTHR21000; PTHR21000; 2. DR Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00110; ilvD; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Lyase; Metal-binding; Reference proteome. FT CHAIN 1 612 Dihydroxy-acid dehydratase. FT /FTId=PRO_0000103469. FT METAL 122 122 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. FT METAL 195 195 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. SQ SEQUENCE 612 AA; 65823 MW; 42CE1C8F7E0A09A1 CRC64; MPKLRSATST QGRNMAGARA LWRATGMKEN DFGKPIIAVV NSFTQFVPGH VHLKDMGQLV AAEIEKAGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRDLI ADSVEYMVNA HCADAMVCIS NCDKITPGML MAAMRLNIPT IFVSGGPMEA GKTKLSDQLI RLDLVDAMIE AADPNVSDER IDAIERSACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGS MLATHADRKE LFLKAGRQIV ELCKRYYEQD DASVLPRSIG TFDAFENAMS LDIAMGGSSN TVLHLLAAAQ EAGVDFKMED IDRLSRKVPC LSKIAPNTNK YHMEDVHRAG GIMGLLGELD RAGLIHKNTH TVLGMSMGEQ LDQYDIIRNQ DEELHKFFRA GPAGIRTTQA FSQDCRWDTV DNDRVNGCIR NKENAISQEG GLAVLFGNLA EDGCIVKTAG VDESIWKFTG TAIVFESQED AVAGILGGKV KEGHVVVIRY EGPKGGPGMQ EMLYPTSYLK SMGLGKKCAL LTDGRFSGGT SGLSIGHVSP EAASGGAIGL VRNGDIINID IPNRAINLEI SNEELATRRA EQDQKGWQPA NREREVSFAL KVFGHFATSA DKGAVRDKTL LK // ID HXUA1_HAEIN Reviewed; 905 AA. AC P44602; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Heme/hemopexin-binding protein; DE AltName: Full=Heme:hemopexin utilization protein A; DE Flags: Precursor; GN Name=hxuA; OrderedLocusNames=HI_0264; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds heme/hemopexin complexes. CC -!- SUBCELLULAR LOCATION: Secreted. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21929.1; -; Genomic_DNA. DR PIR; E64058; E64058. DR RefSeq; NP_438433.1; NC_000907.1. DR RefSeq; WP_005694039.1; NC_000907.1. DR PDB; 4I84; X-ray; 1.50 A; A/B=24-324. DR PDBsum; 4I84; -. DR ProteinModelPortal; P44602; -. DR STRING; 71421.HI0264; -. DR EnsemblBacteria; AAC21929; AAC21929; HI_0264. DR GeneID; 949388; -. DR KEGG; hin:HI0264; -. DR PATRIC; 20189055; VBIHaeInf48452_0279. DR eggNOG; ENOG4105IB0; Bacteria. DR eggNOG; COG3210; LUCA. DR OMA; NSHIKIV; -. DR OrthoDB; EOG6MWN64; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR008638; Filamn_hemagglutn_N. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF05860; Haemagg_act; 1. DR SMART; SM00912; Haemagg_act; 1. DR SUPFAM; SSF51126; SSF51126; 2. DR TIGRFAMs; TIGR01901; adhes_NPXG; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Repeat; Secreted; KW Signal; Transport. FT SIGNAL 1 21 {ECO:0000250}. FT CHAIN 22 905 Heme/hemopexin-binding protein. FT /FTId=PRO_0000021467. FT STRAND 28 35 {ECO:0000244|PDB:4I84}. FT STRAND 37 42 {ECO:0000244|PDB:4I84}. FT STRAND 45 50 {ECO:0000244|PDB:4I84}. FT STRAND 52 61 {ECO:0000244|PDB:4I84}. FT STRAND 69 73 {ECO:0000244|PDB:4I84}. FT STRAND 80 85 {ECO:0000244|PDB:4I84}. FT STRAND 87 89 {ECO:0000244|PDB:4I84}. FT STRAND 91 93 {ECO:0000244|PDB:4I84}. FT STRAND 95 106 {ECO:0000244|PDB:4I84}. FT STRAND 111 113 {ECO:0000244|PDB:4I84}. FT STRAND 118 120 {ECO:0000244|PDB:4I84}. FT STRAND 122 130 {ECO:0000244|PDB:4I84}. FT STRAND 136 138 {ECO:0000244|PDB:4I84}. FT STRAND 144 146 {ECO:0000244|PDB:4I84}. FT STRAND 159 162 {ECO:0000244|PDB:4I84}. FT STRAND 164 167 {ECO:0000244|PDB:4I84}. FT STRAND 169 181 {ECO:0000244|PDB:4I84}. FT STRAND 183 186 {ECO:0000244|PDB:4I84}. FT STRAND 192 203 {ECO:0000244|PDB:4I84}. FT STRAND 208 212 {ECO:0000244|PDB:4I84}. FT HELIX 214 216 {ECO:0000244|PDB:4I84}. FT STRAND 222 225 {ECO:0000244|PDB:4I84}. FT STRAND 227 238 {ECO:0000244|PDB:4I84}. FT STRAND 242 245 {ECO:0000244|PDB:4I84}. FT STRAND 248 251 {ECO:0000244|PDB:4I84}. FT STRAND 253 257 {ECO:0000244|PDB:4I84}. FT STRAND 266 276 {ECO:0000244|PDB:4I84}. FT STRAND 281 291 {ECO:0000244|PDB:4I84}. FT STRAND 298 302 {ECO:0000244|PDB:4I84}. FT STRAND 307 323 {ECO:0000244|PDB:4I84}. SQ SEQUENCE 905 AA; 98833 MW; 2424013EB437A99D CRC64; MYKLNVISLI ILTTYTGATY ASARDLPQGS SVVVGEANVS TIGNKMTIDQ KTPTTQIDWH SFDIGQNKEV EFKQPDANSV AYNRVTGGNA SQIQGKLTAN GKVYLANPNG VIITQGAEIN VAGLFATTKD LERISENGNG NGNKFTRKLK DGQVVKEGQV INKGKIKAKD FVVLNGDKVI NEGEIDATNN GKVYLSSGYN FTFTLSDSSI SVALEDNAVQ SIVQNEGIIK AGDITLNAKG RNQALDSLVM NNGVLEATKV SNKNGKVVLS ADDVQLNNKS DIKGESEVVF TNEPKNKIKI TSQTGSKVTS PKINFTGKSV NINGDFGRDD SKAHYNEEHK RLDTEVNIDV PDNENIRIAE KDNTGTGTGT DSFIQTGALS SLLANNGKVN LKGKDVNISG RIHIDSFRGS DSLLKLTNQG HIKINHADIH STGRLFFITS LQNEKDSQSD ITITDSKINL GNGAMGLGRS LDKENCDNQR WCRTETSQRK KFDVHMRNVV FDQVDDVVVA GGFKKVNLDN IVATGKTNFY IDGGVSRNNS RYEYGVLDLD KRTLLSELDQ RRRRWKYYND LDLDMNKAYW HRFDMFATKN TGRSTIKDTE INISNSKINL KNGFVHLLAE KIKLDNSKID ITFDKDNSQD ISTQINRLGM NGKVSMVNSH IKIVGDEKSD ISAKAPYATM FLIGELIGEK SSIFVKSHQG YTFRTDGDTK IAGKNSKDDL KITAINTGGR TGKEVIINGA PGSIDNDANI ANMAFTIGDN ANTKTTIENA DITALAPNGG TAYLSSKGVE IEVNPNSNFT FFELPREKNF NQTKIKGDST KLSERGFARL YDKINGVRAS NLSAEQLNVT DASEKIINTK LVSSLDVEKL VSVAVCDAGK GCEEQQFGDK GNNTKVSVGE LETEQ // ID IF1_HAEIN Reviewed; 72 AA. AC P44322; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 99. DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; GN OrderedLocusNames=HI_0548; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC22206.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22206.1; ALT_INIT; Genomic_DNA. DR PIR; H64076; H64076. DR RefSeq; NP_438706.2; NC_000907.1. DR RefSeq; WP_005627617.1; NC_000907.1. DR ProteinModelPortal; P44322; -. DR SMR; P44322; 2-72. DR STRING; 71421.HI0548; -. DR EnsemblBacteria; AAC22206; AAC22206; HI_0548. DR GeneID; 25058530; -. DR GeneID; 949386; -. DR KEGG; hin:HI0548; -. DR PATRIC; 20189649; VBIHaeInf48452_0567. DR eggNOG; ENOG4105K9U; Bacteria. DR eggNOG; COG0361; LUCA. DR KO; K02518; -. DR OMA; KGRIIWR; -. DR OrthoDB; EOG6384SC; -. DR PhylomeDB; P44322; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00075; IF_1; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006196; RNA-binding_domain_S1_IF1. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR004368; TIF_IF1. DR Pfam; PF01176; eIF-1a; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00008; infA; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 72 Translation initiation factor IF-1. FT /FTId=PRO_0000095797. FT DOMAIN 2 72 S1-like. {ECO:0000255|HAMAP- FT Rule:MF_00075}. SQ SEQUENCE 72 AA; 8285 MW; A68E02A0395104A9 CRC64; MAKEDCIEMQ GTILETLPNT MFRVELENGH VVTAHISGKM RKNYIRILTG DKVTVEMTPY DLSKGRIIFR SR // ID IF2_HAEIN Reviewed; 829 AA. AC P44323; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=Translation initiation factor IF-2; GN Name=infB; OrderedLocusNames=HI_1284; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22933.1; -; Genomic_DNA. DR PIR; E64114; E64114. DR RefSeq; NP_439436.1; NC_000907.1. DR RefSeq; WP_010869172.1; NC_000907.1. DR ProteinModelPortal; P44323; -. DR STRING; 71421.HI1284; -. DR PRIDE; P44323; -. DR EnsemblBacteria; AAC22933; AAC22933; HI_1284. DR GeneID; 950215; -. DR KEGG; hin:HI1284; -. DR PATRIC; 20191251; VBIHaeInf48452_1336. DR eggNOG; ENOG4107QHU; Bacteria. DR eggNOG; COG0532; LUCA. DR KO; K02519; -. DR OMA; DNRTGGY; -. DR OrthoDB; EOG67HJSV; -. DR PhylomeDB; P44323; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. 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; IPR013575; IF2_assoc_dom_bac. DR InterPro; IPR006847; IF2_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR000178; TF_IF2_bacterial-like. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF08364; IF2_assoc; 1. DR Pfam; PF04760; IF2_N; 1. DR SUPFAM; SSF50447; SSF50447; 2. DR SUPFAM; SSF52156; SSF52156; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00487; IF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. 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 1 829 Translation initiation factor IF-2. FT /FTId=PRO_0000137207. FT DOMAIN 328 498 tr-type G. FT NP_BIND 337 344 GTP. {ECO:0000250}. FT NP_BIND 384 388 GTP. {ECO:0000250}. FT NP_BIND 438 441 GTP. {ECO:0000250}. FT REGION 337 344 G1. {ECO:0000250}. FT REGION 362 366 G2. {ECO:0000250}. FT REGION 384 387 G3. {ECO:0000250}. FT REGION 438 441 G4. {ECO:0000250}. FT REGION 474 476 G5. {ECO:0000250}. SQ SEQUENCE 829 AA; 90552 MW; 75B20AC4CF610AF7 CRC64; MTEDVKADAP KKLSIQRRTK TTVSSTTTGG KSKEVQVEVR KKRTVKTDIA QQEEAKLKAQ QEAEAKKIAE QKAAEEKARL EAEKAKAETA KPVKSAVDSK AKSVESEKEK RKAGEAELRR KAEELARQKA EEQARRAVEE AKRYAEADDS DNESSSEDYS DYNLSSRYAL EAEDEEDRRN ENRGRGKNKV AKAKKGGRDD ENSKNSKNER ESNRKNQKDA KFGKGKNGKK GAALQQAFTK PAQVVKSDVV IGETITVAEL ANKMAVKATE IIKMMMKMGE MVTINQVIDQ ETAQLVAEEL GHKVILRNEN ELEEAVLGDR DVNAEKVTRA PVVTIMGHVD HGKTSLLDYI RKAKVAAGEA GGITQHIGAY HVEMDDGKMI TFLDTPGHAA FTSMRARGAK ATDIVVLVVA ADDGVMPQTI EAIQHAKAAG APLVVAVNKI DKPEANLDRV EQELLQHDVI SEKFGGDVQF VPVSAKKGTG VDDLLDAILL QSEVLELTAV KDGMASGVVI ESYLDKGRGP VATILVQSGT LRKGDIVLCG FEYGRVRAMR DENGKEVDEA GPSIPVELLG LSGVPAAGDE ATVVRDEKKA REVALYRQGK FREVKLARQQ KAKLENMFSN MSEGDVAELN VIVKADVQGS VEAIVQALNE LSTNEVKVKV VGSGVGGITE TDATLATASN AIIVGFNVRA DATARRVIEA ENIDLRYYSI IYELLNEIKA AMSGMLEPEF KQEIIGLAEV RDVFRHPKFG AIAGCMVTEG VVKRNNPIRV LRDNVVIFEG ELESLRRFKD DVSEVRNGME CGIGVKNYND VKVGDQIEVF EVVEVKRSI // ID ILVE_HAEIN Reviewed; 343 AA. AC P54689; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Branched-chain-amino-acid aminotransferase; DE Short=BCAT; DE EC=2.6.1.42; GN Name=ilvE; OrderedLocusNames=HI_1193; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2- CC oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate = (S)-3-methyl- CC 2-oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-valine + 2-oxoglutarate = 3-methyl-2- CC oxobutanoate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 4/4. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22845.1; -; Genomic_DNA. DR PIR; A64189; A64189. DR RefSeq; NP_439349.1; NC_000907.1. DR RefSeq; WP_005694252.1; NC_000907.1. DR ProteinModelPortal; P54689; -. DR STRING; 71421.HI1193; -. DR EnsemblBacteria; AAC22845; AAC22845; HI_1193. DR GeneID; 950143; -. DR KEGG; hin:HI1193; -. DR PATRIC; 20191065; VBIHaeInf48452_1245. DR eggNOG; ENOG4105CM2; Bacteria. DR eggNOG; COG0115; LUCA. DR KO; K00826; -. DR OMA; NFFGITH; -. DR OrthoDB; EOG67MF3R; -. DR PhylomeDB; P54689; -. DR UniPathway; UPA00047; UER00058. DR UniPathway; UPA00048; UER00073. DR UniPathway; UPA00049; UER00062. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR018300; Aminotrans_IV_CS. DR InterPro; IPR005786; B_amino_transII. DR PANTHER; PTHR11825; PTHR11825; 1. DR Pfam; PF01063; Aminotran_4; 1. DR PIRSF; PIRSF006468; BCAT1; 1. DR SUPFAM; SSF56752; SSF56752; 1. DR TIGRFAMs; TIGR01123; ilvE_II; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; KW Branched-chain amino acid biosynthesis; Complete proteome; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 343 Branched-chain-amino-acid FT aminotransferase. FT /FTId=PRO_0000103267. FT MOD_RES 182 182 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 343 AA; 37900 MW; 2B22577EE0E47112 CRC64; MKDLDWNNLG FSYIKTDYRF IAHWKDGKWD EGKLTTDSTL HIHEGSTALH YGQQCFEGLK AYRCKDGSIN LFRPQANAER MQRTADRLLM PRVPTELFVR ACKEVVKANQ DWLGPYGSGA TLYLRPFLIG VGENIGVKTA PEFIFSVFCC PVGAYFKGGL APSNFITTDY DRAAPMGTGG VKVGGNYAAS LLPHELAAEQ GTPERKFADA IYLDPKTHTK IEEVGAANFF GITKDNKFIT PKSESILPSI TKYSLLHIAK ERLGMEAIEG DVYIDQLDQF VEAGACGTAA VITPVGGIQH NGKFHVFDSE TEVGPVTRRL YDELTGIQFG DIEAPEGWIV KVE // ID ILVH_HAEIN Reviewed; 163 AA. AC P45260; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Acetolactate synthase small subunit; DE EC=2.2.1.6; DE AltName: Full=Acetohydroxy-acid synthase small subunit; DE Short=AHAS; DE Short=ALS; GN Name=ilvH; OrderedLocusNames=HI_1584; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. CC -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23232.1; -; Genomic_DNA. DR PIR; B64131; B64131. DR RefSeq; NP_439729.1; NC_000907.1. DR RefSeq; WP_005647229.1; NC_000907.1. DR ProteinModelPortal; P45260; -. DR SMR; P45260; 2-160. DR STRING; 71421.HI1584; -. DR PRIDE; P45260; -. DR EnsemblBacteria; AAC23232; AAC23232; HI_1584. DR GeneID; 950447; -. DR KEGG; hin:HI1584; -. DR PATRIC; 20191901; VBIHaeInf48452_1658. DR eggNOG; ENOG4108ZP8; Bacteria. DR eggNOG; COG0440; LUCA. DR KO; K01653; -. DR OMA; PYGIREI; -. DR OrthoDB; EOG6X3W8W; -. DR PhylomeDB; P45260; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR004789; Acetalactate_synth_ssu. DR InterPro; IPR019455; Acetolactate_synth_ssu_C. DR InterPro; IPR002912; ACT_dom. DR Pfam; PF10369; ALS_ss_C; 1. DR TIGRFAMs; TIGR00119; acolac_sm; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 163 Acetolactate synthase small subunit. FT /FTId=PRO_0000151412. FT DOMAIN 4 79 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 163 AA; 18087 MW; 4F6AFBE71FDD8A32 CRC64; MRRILSVLLE NESGALSRVV GLFSQRAFNI ESLTVAPTDD PTLSRMTIEA VGDAQALEQI EKQLHKLVDV FKVVNLSEQE HIEREIVLAK VRAVGSSRDE IKRLADIFRG QIVDVTPKSY TIQLSGTNDK VDAFISALKE ETTLLEIVRS GLISVSRGEK NIL // ID IHFB_HAEIN Reviewed; 94 AA. AC P43724; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Integration host factor subunit beta; DE Short=IHF-beta; GN Name=ihfB; Synonyms=himD; OrderedLocusNames=HI_1221; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is one of the two subunits of integration CC host factor, a specific DNA-binding protein that functions in CC genetic recombination as well as in transcriptional and CC translational control. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22874.1; -; Genomic_DNA. DR PIR; A64111; A64111. DR RefSeq; NP_439377.1; NC_000907.1. DR RefSeq; WP_005694284.1; NC_000907.1. DR ProteinModelPortal; P43724; -. DR SMR; P43724; 40-92. DR STRING; 71421.HI1221; -. DR EnsemblBacteria; AAC22874; AAC22874; HI_1221. DR GeneID; 950562; -. DR KEGG; hin:HI1221; -. DR PATRIC; 20191121; VBIHaeInf48452_1273. DR eggNOG; ENOG41080YA; Bacteria. DR eggNOG; COG0776; LUCA. DR KO; K05788; -. DR OMA; RDRVNIY; -. DR OrthoDB; EOG615VS6; -. DR PhylomeDB; P43724; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IBA:GO_Central. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 4.10.520.10; -; 1. DR HAMAP; MF_00381; IHF_beta; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR InterPro; IPR005685; IHF_beta. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR TIGRFAMs; TIGR00988; hip; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transcription; Transcription regulation; Translation regulation. FT CHAIN 1 94 Integration host factor subunit beta. FT /FTId=PRO_0000105053. SQ SEQUENCE 94 AA; 10454 MW; 3EAA97B915B63EAF CRC64; MTKSELMEKL SAKQPTLPAK EIENMVKGIL EFISQSLENG DRVEVRGFGS FSLHHRQPRL GRNPKTGDSV NLSAKSVPYF KAGKELKARV DVQA // ID ILVC_HAEIN Reviewed; 492 AA. AC P44822; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 114. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase; GN Name=ilvC; OrderedLocusNames=HI_0682; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22342.1; -; Genomic_DNA. DR PIR; B64086; B64086. DR RefSeq; NP_438842.1; NC_000907.1. DR RefSeq; WP_005654301.1; NC_000907.1. DR ProteinModelPortal; P44822; -. DR SMR; P44822; 3-490. DR STRING; 71421.HI0682; -. DR PRIDE; P44822; -. DR EnsemblBacteria; AAC22342; AAC22342; HI_0682. DR GeneID; 949478; -. DR KEGG; hin:HI0682; -. DR PATRIC; 20189983; VBIHaeInf48452_0713. DR eggNOG; ENOG4105C6M; Bacteria. DR eggNOG; COG0059; LUCA. DR KO; K00053; -. DR OMA; KLFEMNR; -. DR OrthoDB; EOG625K07; -. DR PhylomeDB; P44822; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 2. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 492 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151314. FT ACT_SITE 132 132 {ECO:0000255}. SQ SEQUENCE 492 AA; 54239 MW; 16D504256D7FF18E CRC64; MANYFNTLNL RQKLDQLGRC RFMDREEFAD EANFLKGKKI VIVGCGAQGL NQGLNMRDSG LDISYALRPE AIAEKRASFQ RATENGFKVG TYEELIPTAD LVVNLTPDKQ HSKVVADVMP LMKKDSAFGY SHGFNIVEVG EEIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE NDPKGEGMAI AKAWAAATGG HKAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSIVCYDKL VADGKDPAYA GKLIQYGWET ITEALKQGGI TLMMDRLSNS AKLRAFELAE QIKESLGFLY YKHMDDIISG HFSATMMADW ANGDKDLFAW REATGKTAFE NAPKYDGKIS EQEYFDNGVL MIAMVKAGVE LAFDAMVASG IYEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG NYLFSNVATP ILAKEIIPNL QKGDLGEPTP AVEVDNITLR DVNDAIRNHP VELIGQELRG YMTDMKRIAV AG // ID IOJAP_HAEIN Reviewed; 102 AA. AC P44471; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Ribosomal silencing factor RsfS {ECO:0000255|HAMAP-Rule:MF_01477}; GN Name=rsfS {ECO:0000255|HAMAP-Rule:MF_01477}; GN OrderedLocusNames=HI_0034; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Functions as a ribosomal silencing factor. Interacts CC with ribosomal protein L14 (rplN), blocking formation of CC intersubunit bridge B8. Prevents association of the 30S and 50S CC ribosomal subunits and the formation of functional ribosomes, thus CC repressing translation. {ECO:0000255|HAMAP-Rule:MF_01477}. CC -!- SUBUNIT: Interacts with ribosomal protein L14 (rplN). CC {ECO:0000255|HAMAP-Rule:MF_01477}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01477}. CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000255|HAMAP- CC Rule:MF_01477}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21712.1; -; Genomic_DNA. DR PIR; H64140; H64140. DR RefSeq; NP_438207.1; NC_000907.1. DR RefSeq; WP_005635481.1; NC_000907.1. DR ProteinModelPortal; P44471; -. DR STRING; 71421.HI0034; -. DR EnsemblBacteria; AAC21712; AAC21712; HI_0034. DR GeneID; 950928; -. DR KEGG; hin:HI0034; -. DR PATRIC; 20188519; VBIHaeInf48452_0034. DR eggNOG; ENOG4105KEM; Bacteria. DR eggNOG; COG0799; LUCA. DR KO; K09710; -. DR OMA; HVEGSEN; -. DR OrthoDB; EOG6J48TR; -. DR PhylomeDB; P44471; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central. DR GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IBA:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR HAMAP; MF_01477; Iojap_RsfS; 1. DR InterPro; IPR004394; Iojap/RsfS/C7orf30. DR PANTHER; PTHR21043; PTHR21043; 1. DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Repressor; KW Translation regulation. FT CHAIN 1 102 Ribosomal silencing factor RsfS. FT /FTId=PRO_0000168677. SQ SEQUENCE 102 AA; 11386 MW; BB84F9E4F385B5B7 CRC64; MALVEFLMET LDGLKGTDIV HFDVRGKSSI TDNMIICTGT SSRQVSAMAD NLITECKKAG FETFGEEGKN TADWIVVDLG QAIVHIMQRD AREMYQLEKL WA // ID IF3_HAEIN Reviewed; 172 AA. AC P43814; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080}; GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; GN OrderedLocusNames=HI_1318; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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=AAC22963.1; 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; L42023; AAC22963.1; ALT_INIT; Genomic_DNA. DR PIR; B64116; B64116. DR RefSeq; NP_439469.1; NC_000907.1. DR ProteinModelPortal; P43814; -. DR SMR; P43814; 7-79, 83-172. DR STRING; 71421.HI1318m; -. DR PRIDE; P43814; -. DR EnsemblBacteria; AAC22963; AAC22963; HI_1318. DR GeneID; 950242; -. DR KEGG; hin:HI1318m; -. DR PATRIC; 20191319; VBIHaeInf48452_1370. DR eggNOG; ENOG4108UUX; Bacteria. DR eggNOG; COG0290; LUCA. DR KO; K02520; -. DR OMA; HDFNVKV; -. DR OrthoDB; EOG63JRGJ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.80; -; 1. DR Gene3D; 3.30.110.10; -; 1. DR HAMAP; MF_00080; IF_3; 1. DR InterPro; IPR019813; Translation_initiation_fac3_CS. DR InterPro; IPR001288; Translation_initiation_fac_3. DR InterPro; IPR019815; Translation_initiation_fac_3_C. DR InterPro; IPR019814; Translation_initiation_fac_3_N. DR PANTHER; PTHR10938; PTHR10938; 1. DR Pfam; PF00707; IF3_C; 1. DR Pfam; PF05198; IF3_N; 1. DR SUPFAM; SSF54364; SSF54364; 1. DR SUPFAM; SSF55200; SSF55200; 1. DR TIGRFAMs; TIGR00168; infC; 1. DR PROSITE; PS00938; IF3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 172 Translation initiation factor IF-3. FT /FTId=PRO_0000177523. FT SITE 100 100 Important for 30S binding. {ECO:0000250}. FT SITE 103 103 Important for 30S binding. {ECO:0000250}. SQ SEQUENCE 172 AA; 19631 MW; BC97FB87D1D77001 CRC64; MNRPNRINEE IRVKEVRLID QNGEQAGIVS IQQALEMMAE QAELDLVEIS PNAEPPVCRI MNYGKFLYEK SKTAKEQKKK QKVVQVKEIK FRPGTDEGDY QVKLRSLIRF LEDGDKAKIT VRFRGREMAH QDIGLDVLER VKNDLAEISV VESAPGKLEG RQAVMVLAPK KK // ID IGA0_HAEIN Reviewed; 1694 AA. AC P44969; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 122. DE RecName: Full=Immunoglobulin A1 protease autotransporter; DE EC=3.4.21.72; DE Contains: DE RecName: Full=Immunoglobulin A1 protease; DE Short=IGA1 protease; DE Contains: DE RecName: Full=Immunoglobulin A1 protease translocator; DE AltName: Full=Helper peptide; DE Flags: Precursor; GN Name=iga; Synonyms=iga1; OrderedLocusNames=HI_0990; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Serotype D; RA Wright A., Fishman Y., Tai F., Plaut A.G.; RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP CHARACTERIZATION OF CLEAVAGE SITE SPECIFICITY. RX PubMed=2105270; RA Grundy F.J., Plaut A.G., Wright A.; RT "Localization of the cleavage site specificity determinant of RT Haemophilus influenzae immunoglobulin A1 protease genes."; RL Infect. Immun. 58:320-331(1990). CC -!- FUNCTION: Virulence factor; cleaves host immunoglobulin A CC producing intact Fc and Fab fragments. CC -!- CATALYTIC ACTIVITY: Cleavage of immunoglobulin A molecules at CC certain Pro-|-Xaa bonds in the hinge region. No small molecule CC substrates are known. CC -!- SUBCELLULAR LOCATION: Immunoglobulin A1 protease autotransporter: CC Periplasm {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Immunoglobulin A1 protease: Secreted. Cell CC surface. CC -!- SUBCELLULAR LOCATION: Immunoglobulin A1 protease translocator: CC Cell outer membrane {ECO:0000250}; Multi-pass membrane protein CC {ECO:0000250}. Note=The cleaved C-terminal fragment CC (autotransporter domain) is localized in the outer membrane. CC {ECO:0000250}. CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides CC the autotransporter protein to the periplasmic space. Then, CC insertion of the C-terminal translocator domain in the outer CC membrane forms a hydrophilic pore for the translocation of the CC passenger domain to the bacterial cell surface, with subsequent CC cleavage (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 1 autotransporter (TC 1.B.12) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00556}. CC -!- SIMILARITY: Contains 1 peptidase S6 domain. {ECO:0000255|PROSITE- CC ProRule:PRU01028}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X59800; CAB56789.1; -; Genomic_DNA. DR EMBL; L42023; AAC22651.1; -; Genomic_DNA. DR PIR; H64106; H64106. DR RefSeq; NP_439153.1; NC_000907.1. DR RefSeq; WP_005693332.1; NC_000907.1. DR PDB; 3H09; X-ray; 1.75 A; A/B=26-1014. DR PDBsum; 3H09; -. DR ProteinModelPortal; P44969; -. DR STRING; 71421.HI0990; -. DR EnsemblBacteria; AAC22651; AAC22651; HI_0990. DR GeneID; 950762; -. DR KEGG; hin:HI0990; -. DR PATRIC; 20190641; VBIHaeInf48452_1033. DR eggNOG; ENOG4108BMY; Bacteria. DR eggNOG; COG3468; LUCA. DR KO; K01347; -. DR OMA; AAPQDYM; -. DR OrthoDB; EOG66F02T; -. DR BRENDA; 3.4.21.72; 2529. DR EvolutionaryTrace; P44969; -. DR PMAP-CutDB; P44969; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.20; -; 1. DR Gene3D; 2.40.128.130; -; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR000710; Peptidase_S6. DR InterPro; IPR030396; Peptidase_S6_dom. DR InterPro; IPR004899; Pertactin_central. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF02395; Peptidase_S6; 1. DR Pfam; PF03212; Pertactin; 1. DR PRINTS; PR00921; IGASERPTASE. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF51126; SSF51126; 3. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. DR PROSITE; PS51691; PEPTIDASE_S6; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; Hydrolase; KW Membrane; Periplasm; Protease; Reference proteome; Secreted; KW Serine protease; Signal; Transmembrane; Transmembrane beta strand; KW Virulence; Zymogen. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1694 Immunoglobulin A1 protease FT autotransporter. FT /FTId=PRO_0000387598. FT CHAIN 26 1014 Immunoglobulin A1 protease. FT /FTId=PRO_0000026958. FT CHAIN 1015 1694 Immunoglobulin A1 protease translocator. FT {ECO:0000255}. FT /FTId=PRO_0000026959. FT DOMAIN 26 332 Peptidase S6. {ECO:0000255|PROSITE- FT ProRule:PRU01028}. FT DOMAIN 1442 1694 Autotransporter. {ECO:0000255|PROSITE- FT ProRule:PRU00556}. FT ACT_SITE 288 288 {ECO:0000305}. FT CONFLICT 253 254 EN -> GV (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 272 272 G -> A (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 464 464 G -> E (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 866 866 S -> T (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 1036 1036 A -> D (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 1074 1074 A -> G (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 1421 1421 A -> G (in Ref. 1; CAB56789). FT {ECO:0000305}. FT CONFLICT 1545 1545 H -> T (in Ref. 1; CAB56789). FT {ECO:0000305}. FT STRAND 30 32 {ECO:0000244|PDB:3H09}. FT HELIX 34 42 {ECO:0000244|PDB:3H09}. FT STRAND 55 57 {ECO:0000244|PDB:3H09}. FT STRAND 63 69 {ECO:0000244|PDB:3H09}. FT HELIX 77 79 {ECO:0000244|PDB:3H09}. FT TURN 82 84 {ECO:0000244|PDB:3H09}. FT STRAND 88 91 {ECO:0000244|PDB:3H09}. FT STRAND 94 97 {ECO:0000244|PDB:3H09}. FT STRAND 106 109 {ECO:0000244|PDB:3H09}. FT STRAND 111 113 {ECO:0000244|PDB:3H09}. FT HELIX 130 133 {ECO:0000244|PDB:3H09}. FT STRAND 134 139 {ECO:0000244|PDB:3H09}. FT STRAND 148 150 {ECO:0000244|PDB:3H09}. FT HELIX 154 162 {ECO:0000244|PDB:3H09}. FT STRAND 169 172 {ECO:0000244|PDB:3H09}. FT HELIX 191 193 {ECO:0000244|PDB:3H09}. FT TURN 195 197 {ECO:0000244|PDB:3H09}. FT STRAND 200 205 {ECO:0000244|PDB:3H09}. FT STRAND 207 218 {ECO:0000244|PDB:3H09}. FT STRAND 229 236 {ECO:0000244|PDB:3H09}. FT STRAND 243 246 {ECO:0000244|PDB:3H09}. FT STRAND 248 251 {ECO:0000244|PDB:3H09}. FT STRAND 257 261 {ECO:0000244|PDB:3H09}. FT HELIX 273 275 {ECO:0000244|PDB:3H09}. FT STRAND 291 296 {ECO:0000244|PDB:3H09}. FT TURN 297 300 {ECO:0000244|PDB:3H09}. FT STRAND 301 311 {ECO:0000244|PDB:3H09}. FT HELIX 313 316 {ECO:0000244|PDB:3H09}. FT STRAND 319 324 {ECO:0000244|PDB:3H09}. FT HELIX 327 337 {ECO:0000244|PDB:3H09}. FT STRAND 338 354 {ECO:0000244|PDB:3H09}. FT STRAND 357 362 {ECO:0000244|PDB:3H09}. FT STRAND 365 368 {ECO:0000244|PDB:3H09}. FT STRAND 376 378 {ECO:0000244|PDB:3H09}. FT HELIX 379 384 {ECO:0000244|PDB:3H09}. FT STRAND 388 401 {ECO:0000244|PDB:3H09}. FT STRAND 410 412 {ECO:0000244|PDB:3H09}. FT STRAND 414 422 {ECO:0000244|PDB:3H09}. FT STRAND 426 430 {ECO:0000244|PDB:3H09}. FT STRAND 432 434 {ECO:0000244|PDB:3H09}. FT STRAND 439 442 {ECO:0000244|PDB:3H09}. FT STRAND 451 462 {ECO:0000244|PDB:3H09}. FT STRAND 465 467 {ECO:0000244|PDB:3H09}. FT STRAND 471 474 {ECO:0000244|PDB:3H09}. FT STRAND 476 481 {ECO:0000244|PDB:3H09}. FT STRAND 491 493 {ECO:0000244|PDB:3H09}. FT STRAND 497 499 {ECO:0000244|PDB:3H09}. FT STRAND 504 510 {ECO:0000244|PDB:3H09}. FT HELIX 516 518 {ECO:0000244|PDB:3H09}. FT STRAND 519 521 {ECO:0000244|PDB:3H09}. FT STRAND 526 529 {ECO:0000244|PDB:3H09}. FT STRAND 535 538 {ECO:0000244|PDB:3H09}. FT STRAND 541 544 {ECO:0000244|PDB:3H09}. FT STRAND 547 550 {ECO:0000244|PDB:3H09}. FT STRAND 558 562 {ECO:0000244|PDB:3H09}. FT HELIX 571 573 {ECO:0000244|PDB:3H09}. FT STRAND 577 579 {ECO:0000244|PDB:3H09}. FT STRAND 600 602 {ECO:0000244|PDB:3H09}. FT TURN 603 606 {ECO:0000244|PDB:3H09}. FT STRAND 607 611 {ECO:0000244|PDB:3H09}. FT STRAND 630 638 {ECO:0000244|PDB:3H09}. FT HELIX 639 653 {ECO:0000244|PDB:3H09}. FT STRAND 660 663 {ECO:0000244|PDB:3H09}. FT STRAND 673 678 {ECO:0000244|PDB:3H09}. FT STRAND 685 688 {ECO:0000244|PDB:3H09}. FT STRAND 690 693 {ECO:0000244|PDB:3H09}. FT STRAND 695 707 {ECO:0000244|PDB:3H09}. FT HELIX 728 730 {ECO:0000244|PDB:3H09}. FT HELIX 732 734 {ECO:0000244|PDB:3H09}. FT STRAND 745 754 {ECO:0000244|PDB:3H09}. FT STRAND 759 762 {ECO:0000244|PDB:3H09}. FT STRAND 766 775 {ECO:0000244|PDB:3H09}. FT STRAND 780 785 {ECO:0000244|PDB:3H09}. FT STRAND 791 794 {ECO:0000244|PDB:3H09}. FT TURN 796 798 {ECO:0000244|PDB:3H09}. FT STRAND 801 804 {ECO:0000244|PDB:3H09}. FT HELIX 810 813 {ECO:0000244|PDB:3H09}. FT STRAND 819 823 {ECO:0000244|PDB:3H09}. FT STRAND 825 827 {ECO:0000244|PDB:3H09}. FT STRAND 832 842 {ECO:0000244|PDB:3H09}. FT STRAND 844 846 {ECO:0000244|PDB:3H09}. FT STRAND 851 854 {ECO:0000244|PDB:3H09}. FT STRAND 858 861 {ECO:0000244|PDB:3H09}. FT STRAND 866 882 {ECO:0000244|PDB:3H09}. FT TURN 886 888 {ECO:0000244|PDB:3H09}. FT STRAND 894 911 {ECO:0000244|PDB:3H09}. FT HELIX 912 914 {ECO:0000244|PDB:3H09}. FT STRAND 919 926 {ECO:0000244|PDB:3H09}. FT STRAND 928 938 {ECO:0000244|PDB:3H09}. FT STRAND 946 950 {ECO:0000244|PDB:3H09}. FT STRAND 959 965 {ECO:0000244|PDB:3H09}. FT STRAND 976 980 {ECO:0000244|PDB:3H09}. FT STRAND 983 987 {ECO:0000244|PDB:3H09}. SQ SEQUENCE 1694 AA; 185539 MW; C52427013F93178C CRC64; MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGRFSVG ATNVEVRDKN NHSLGNVLPN GIPMIDFSVV DVDKRIATLI NPQYVVGVKH VSNGVSELHF GNLNGNMNNG NAKSHRDVSS EENRYFSVEK NEYPTKLNGK AVTTEDQTQK RREDYYMPRL DKFVTEVAPI EASTASSDAG TYNDQNKYPA FVRLGSGSQF IYKKGDNYSL ILNNHEVGGN NLKLVGDAYT YGIAGTPYKV NHENNGLIGF GNSKEEHSDP KGILSQDPLT NYAVLGDSGS PLFVYDREKG KWLFLGSYDF WAGYNKKSWQ EWNIYKPEFA KTVLDKDTAG SLTGSNTQYN WNPTGKTSVI SNGSESLNVD LFDSSQDTDS KKNNHGKSVT LRGSGTLTLN NNIDQGAGGL FFEGDYEVKG TSDSTTWKGA GVSVADGKTV TWKVHNPKSD RLAKIGKGTL IVEGKGENKG SLKVGDGTVI LKQQADANNK VKAFSQVGIV SGRSTVVLND DKQVDPNSIY FGFRGGRLDA NGNNLTFEHI RNIDDGARLV NHNTSKTSTV TITGESLITD PNTITPYNID APDEDNPYAF RRIKDGGQLY LNLENYTYYA LRKGASTRSE LPKNSGESNE NWLYMGKTSD EAKRNVMNHI NNERMNGFNG YFGEEEGKNN GNLNVTFKGK SEQNRFLLTG GTNLNGDLKV EKGTLFLSGR PTPHARDIAG ISSTKKDQHF AENNEVVVED DWINRNFKAT NINVTNNATL YSGRNVANIT SNITASDNAK VHIGYKAGDT VCVRSDYTGY VTCTTDKLSD KALNSFNATN VSGNVNLSGN ANFVLGKANL FGTISGTGNS QVRLTENSHW HLTGDSNVNQ LNLDKGHIHL NAQNDANKVT TYNTLTVNSL SGNGSFYYLT DLSNKQGDKV VVTKSATGNF TLQVADKTGE PTKNELTLFD ASNATRNNLN VSLVGNTVDL GAWKYKLRNV NGRYDLYNPE VEKRNQTVDT TNITTPNNIQ ADVPSVPSNN EEIARVETPV PPPAPATPSE TTETVAENSK QESKTVEKNE QDATETTAQN GEVAEEAKPS VKANTQTNEV AQSGSETEET QTTEIKETAK VEKEEKAKVE KDEIQEAPQM ASETSPKQAK PAPKEVSTDT KVEETQVQAQ PQTQSTTVAA AEATSPNSKP AEETQPSEKT NAEPVTPVVS KNQTENTTDQ PTEREKTAKV ETEKTQEPPQ VASQASPKQE QSETVQPQAV LESENVPTVN NAEEVQAQLQ TQTSATVSTK QPAPENSINT GSATAITETA EKSDKPQTET AASTEDASQH KANTVADNSV ANNSESSDPK SRRRRSISQP QETSAEETTA ASTDETTIAD NSKRSKPNRR SRRSVRSEPT VTNGSDRSTV ALRDLTSTNT NAVISDAMAK AQFVALNVGK AVSQHISQLE MNNEGQYNVW VSNTSMNENY SSSQYRRFSS KSTQTQLGWD QTISNNVQLG GVFTYVRNSN NFDKASSKNT LAQVNFYSKY YADNHWYLGI DLGYGKFQSN LKTNHNAKFA RHTAQFGLTA GKAFNLGNFG ITPIVGVRYS YLSNANFALA KDRIKVNPIS VKTAFAQVDL SYTYHLGEFS VTPILSARYD TNQGSGKINV NQYDFAYNVE NQQQYNAGLK LKYHNVKLSL IGGLTKAKQA EKQKTAELKL SFSF // ID ILVA_HAEIN Reviewed; 513 AA. AC P46493; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=L-threonine dehydratase biosynthetic IlvA; DE EC=4.3.1.19; DE AltName: Full=Threonine deaminase; GN Name=ilvA; OrderedLocusNames=HI_0738.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate CC and ammonia from threonine in a two-step reaction. The first step CC involved a dehydration of threonine and a production of enamine CC intermediates (aminocrotonate), which tautomerizes to its imine CC form (iminobutyrate). Both intermediates are unstable and short- CC lived. The second step is the nonenzymatic hydrolysis of the CC enamine/imine intermediates to form 2-ketobutyrate and free CC ammonia. In the low water environment of the cell, the second step CC is accelerated by RidA (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from L-threonine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ACT-like domains. {ECO:0000255|PROSITE- CC ProRule:PRU01008}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22398.1; -; Genomic_DNA. DR RefSeq; NP_438898.1; NC_000907.1. DR RefSeq; WP_010869046.1; NC_000907.1. DR ProteinModelPortal; P46493; -. DR SMR; P46493; 10-512. DR STRING; 71421.HI0738.1; -. DR EnsemblBacteria; AAC22398; AAC22398; HI_0738.1. DR GeneID; 950764; -. DR KEGG; hin:HI0738.1; -. DR PATRIC; 20190119; VBIHaeInf48452_0775. DR eggNOG; ENOG4105C7B; Bacteria. DR eggNOG; COG1171; LUCA. DR KO; K01754; -. DR OMA; DEVCAAM; -. DR OrthoDB; EOG6ZSP7D; -. DR PhylomeDB; P46493; -. DR UniPathway; UPA00047; UER00054. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006566; P:threonine metabolic process; ISS:UniProtKB. DR InterPro; IPR001721; ACT-like_dom. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR005787; Thr_deHydtase_biosynth. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR Pfam; PF00585; Thr_dehydrat_C; 2. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1. DR PROSITE; PS51672; ACT_LIKE; 2. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Isoleucine biosynthesis; Lyase; KW Pyridoxal phosphate; Reference proteome; Repeat. FT CHAIN 1 513 L-threonine dehydratase biosynthetic FT IlvA. FT /FTId=PRO_0000185574. FT DOMAIN 340 411 ACT-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU01008}. FT DOMAIN 433 504 ACT-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU01008}. FT REGION 190 193 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 90 90 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 316 316 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 63 63 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 513 AA; 56663 MW; DF42CA8B6FDE4CD7 CRC64; MKNLLTNPQP SQSDYINAIV KLGSRVYEAA QVTPLQKMGK LSERLHNNIW IKREDRQPVN SFKLRGAYAM ISSLSAEQKA AGVIAASAGN HAQGVALSAK QLGLKALIVM PQNTPSIKVD AVRGFGGEVL LHGANFDEAK AKAIELSKEK NMTFIPPFDH PLVIAGQGTL AMEMLQQVAD LDYVFVQVGG GGLAAGVAIL LKQFMPEIKI IGVESKDSAC LKAALDKGEP TDLTHIGLFA DGVAVKRIGD ETFRLCQQYL DDMVLVDSDE VCAAMKDLFE NVRAVAEPSG ALGLAGLKKY VKQNHIEGKN MAAILSGANL NFHTLRYVSE RCEIGENREA LLAVTMPEQP GSFLKFAYVL GNRAVTEFSY RYADDKRACV FVGVRTTNEQ EKADIIADLT KNGFDVEDMS DDDIAKTHVR YLMGGRAAND NERLYTFEFP EQKGALLKFL ETLQNRWNIS LFHYRAHGAD YGNILAGFQI EQREQAEFEQ GLAQLNYVFE DVTKSKSYRY FLR // ID ISPG_HAEIN Reviewed; 368 AA. AC P44667; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000255|HAMAP-Rule:MF_00159}; DE EC=1.17.7.3 {ECO:0000255|HAMAP-Rule:MF_00159}; DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00159}; GN Name=ispG {ECO:0000255|HAMAP-Rule:MF_00159}; Synonyms=gcpE; GN OrderedLocusNames=HI_0368; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- CATALYTIC ACTIVITY: (E)-4-hydroxy-3-methylbut-2-en-1-yl CC diphosphate + H(2)O + oxidized flavodoxin = 2-C-methyl-D- CC erythritol 2,4-cyclodiphosphate + reduced flavodoxin. CC {ECO:0000255|HAMAP-Rule:MF_00159}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 5/6. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP- CC Rule:MF_00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22026.1; -; Genomic_DNA. DR PIR; H64063; H64063. DR RefSeq; NP_438529.1; NC_000907.1. DR RefSeq; WP_005693796.1; NC_000907.1. DR ProteinModelPortal; P44667; -. DR STRING; 71421.HI0368; -. DR EnsemblBacteria; AAC22026; AAC22026; HI_0368. DR GeneID; 949471; -. DR KEGG; hin:HI0368; -. DR PATRIC; 20189281; VBIHaeInf48452_0386. DR eggNOG; ENOG4105C4E; Bacteria. DR eggNOG; COG0821; LUCA. DR KO; K03526; -. DR OMA; HNGMKIA; -. DR OrthoDB; EOG67Q96Z; -. DR PhylomeDB; P44667; -. DR UniPathway; UPA00056; UER00096. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00159; IspG; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR016425; IspG_bac. DR InterPro; IPR004588; IspG_bac-typ. DR Pfam; PF04551; GcpE; 1. DR PIRSF; PIRSF004640; IspG; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR00612; ispG_gcpE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 368 4-hydroxy-3-methylbut-2-en-1-yl FT diphosphate synthase (flavodoxin). FT /FTId=PRO_0000190585. FT METAL 271 271 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 274 274 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 306 306 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. FT METAL 313 313 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00159}. SQ SEQUENCE 368 AA; 40116 MW; DC99EA15A50ED01B CRC64; MSAFQPTIKR RESTKIYVGN VPIGGDAPIA VQSMTNTRTT DVEATVAQIK SLERVGADIV RVSVPTMDAA EAFKQIKQQV NVPLVADIHF DYRIALKVAE YGVDCLRINP GNIGREDRVR AVVDCARDKN IPIRIGVNAG SLEKDLQEKY GEPTPEALLE SALRHVEILD RLNFDQFKVS VKASDVFLAV ESYRLLAKAI KQPLHLGITE AGGARAGAVK SAVGLGMLLA EGIGDTLRVS LAADPVEEIK VGFDILKSLR IRSRGINFIA CPTCSRQEFD VIGTVNALEQ RLEDIITPMD VSIIGCVVNG PGEALVSDLG VTGGNKKSGY YLDGERQKER FDNEDIVNQL EAKIRAKVAR QDPKNRII // ID IMDH_HAEIN Reviewed; 488 AA. AC P44334; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 122. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964}; DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964}; GN Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; GN OrderedLocusNames=HI_0221; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; CC -!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP- CC Rule:MF_01964}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|HAMAP- CC Rule:MF_01964}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21890.1; -; Genomic_DNA. DR PIR; H64055; H64055. DR RefSeq; NP_438392.1; NC_000907.1. DR RefSeq; WP_005694071.1; NC_000907.1. DR ProteinModelPortal; P44334; -. DR SMR; P44334; 3-486. DR STRING; 71421.HI0221; -. DR PRIDE; P44334; -. DR EnsemblBacteria; AAC21890; AAC21890; HI_0221. DR GeneID; 951137; -. DR KEGG; hin:HI0221; -. DR PATRIC; 20188961; VBIHaeInf48452_0233. DR eggNOG; ENOG4105CP4; Bacteria. DR eggNOG; COG0516; LUCA. DR eggNOG; COG0517; LUCA. DR KO; K00088; -. DR OMA; SSMGYCG; -. DR OrthoDB; EOG6B62F4; -. DR PhylomeDB; P44334; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD; KW Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; KW Repeat. FT CHAIN 1 488 Inosine-5'-monophosphate dehydrogenase. FT /FTId=PRO_0000093697. FT DOMAIN 94 150 CBS 1. {ECO:0000255|HAMAP-Rule:MF_01964}. FT DOMAIN 154 215 CBS 2. {ECO:0000255|HAMAP-Rule:MF_01964}. FT NP_BIND 249 251 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}. FT NP_BIND 299 301 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}. FT REGION 339 341 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT REGION 362 363 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT REGION 386 390 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT ACT_SITE 306 306 Thioimidate intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT ACT_SITE 402 402 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT METAL 301 301 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 303 303 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 306 306 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 470 470 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 471 471 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 472 472 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 249 249 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 304 304 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 416 416 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}. SQ SEQUENCE 488 AA; 51981 MW; B477F22344E4BE8B CRC64; MSLRIKQEAL TFDDVLLVPA HSTVLPNTAN LSTQLTKEIR LNIPMLSAAM DTVTETKLAI SLAQEGGIGF IHKNMTIERQ ADRVRKVKKF ESGIVSEPVT VLPNLTLAEL AEMVKKNGFA GYPVVDGENN LIGIITGRDT RFVKDLSKTV SQVMTKKEDL VTVKEGASRE EILELMHQHR VEKVLVVNDS FKLKGMITVK DFQKAEQKPN ACKDEFGRLR VGAAVGAGAG NEERIDALVK AGVDVLLIDS SHGHSEGVLQ RVRETRAKYP NLPIVAGNVA TAEGAIALAD AGASAVKVGI GPGSICTTRI VTGVGVPQIT AIADAAAALK DRGIPVIADG GIRFSGDIAK AIAAGASCVM VGSMFAGTEE APGEIELYQG RAFKSYRGMG SLGAMAKGSS DRYFQSDNAA DKLVPEGIEG RIPYKGYLKE IIHQQMGGLR SCMGLTGCAT IDELRTKAEF VRISGAGIKE SHVHDVAITK EAPNYRMG // ID ISCA_HAEIN Reviewed; 107 AA. AC P44672; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Iron-binding protein IscA; DE AltName: Full=Iron-sulfur cluster assembly protein; GN Name=iscA; OrderedLocusNames=HI_0376; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Is able to transfer iron-sulfur clusters to apo- CC ferredoxin. Multiple cycles of [2Fe2S] cluster formation and CC transfer are observed, suggesting that IscA acts catalytically. CC Recruits intracellular free iron so as to provide iron for the CC assembly of transient iron-sulfur cluster in IscU in the presence CC of IscS, L-cysteine and the thioredoxin reductase system (By CC similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per dimer. The dimer may bind additional CC iron ions. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the HesB/IscA 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; L42023; AAC22033.1; -; Genomic_DNA. DR PIR; E64150; E64150. DR RefSeq; NP_438537.1; NC_000907.1. DR RefSeq; WP_005693788.1; NC_000907.1. DR ProteinModelPortal; P44672; -. DR SMR; P44672; 1-97. DR STRING; 71421.HI0376; -. DR EnsemblBacteria; AAC22033; AAC22033; HI_0376. DR GeneID; 950630; -. DR KEGG; hin:HI0376; -. DR PATRIC; 20189297; VBIHaeInf48452_0394. DR eggNOG; ENOG4108Z4V; Bacteria. DR eggNOG; COG0316; LUCA. DR KO; K13628; -. DR OMA; LAYSVDY; -. DR OrthoDB; EOG6VXF8J; -. DR PhylomeDB; P44672; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central. DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central. DR Gene3D; 2.60.300.12; -; 1. DR InterPro; IPR000361; FeS_biogenesis. DR InterPro; IPR016092; FeS_cluster_insertion. DR InterPro; IPR017870; FeS_cluster_insertion_CS. DR InterPro; IPR031108; ISCA-like. DR InterPro; IPR011302; IscA_proteobacteria. DR PANTHER; PTHR10072:SF48; PTHR10072:SF48; 1. DR Pfam; PF01521; Fe-S_biosyn; 1. DR SUPFAM; SSF89360; SSF89360; 1. DR TIGRFAMs; TIGR02011; IscA; 1. DR TIGRFAMs; TIGR00049; TIGR00049; 1. DR PROSITE; PS01152; HESB; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Metal-binding; Reference proteome. FT CHAIN 1 107 Iron-binding protein IscA. FT /FTId=PRO_0000077009. FT METAL 35 35 Iron. {ECO:0000250}. FT METAL 99 99 Iron. {ECO:0000250}. FT METAL 101 101 Iron. {ECO:0000250}. SQ SEQUENCE 107 AA; 11722 MW; DC420D931D497992 CRC64; MGITLTEKAA QRVKAFLDNR GKGIGLRLGV KTSGCSGLAY VLEFVDVLNS EDQVFEQYGV NIIVDPKSLV YLNGIELDYV KEGLNEGFKY NNPNVKESCG CGESFHV // ID ISCS_HAEIN Reviewed; 404 AA. AC Q57337; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 11-NOV-2015, entry version 107. DE RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331}; DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331}; GN Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331}; GN OrderedLocusNames=HI_0378; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Master enzyme that delivers sulfur to a number of CC partners involved in Fe-S cluster assembly, tRNA modification or CC cofactor biosynthesis. Catalyzes the removal of elemental sulfur CC atoms from cysteine to produce alanine. Functions as a sulfur CC delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S CC scaffold assembly protein, as well as other S acceptor proteins. CC {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S- CC sulfanyl-acceptor. {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00331}; CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, interacts CC with other sulfur acceptors. {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00331}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22035.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22035.1; ALT_INIT; Genomic_DNA. DR PIR; D64064; D64064. DR RefSeq; NP_438539.2; NC_000907.1. DR RefSeq; WP_010868979.1; NC_000907.1. DR ProteinModelPortal; Q57337; -. DR SMR; Q57337; 2-392. DR STRING; 71421.HI0378; -. DR EnsemblBacteria; AAC22035; AAC22035; HI_0378. DR GeneID; 949479; -. DR KEGG; hin:HI0378; -. DR PATRIC; 20189301; VBIHaeInf48452_0396. DR eggNOG; ENOG4105C3J; Bacteria. DR eggNOG; COG1104; LUCA. DR KO; K04487; -. DR OMA; EPIQSGG; -. DR OrthoDB; EOG62RSBK; -. DR PhylomeDB; Q57337; -. DR UniPathway; UPA00266; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00331; Cys_desulf_IscS; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR010240; Cys_deSase_IscS. DR InterPro; IPR016454; Cysteine_dSase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF005572; NifS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR02006; IscS; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 404 Cysteine desulfurase IscS. FT /FTId=PRO_0000150268. FT REGION 75 76 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT REGION 203 205 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT ACT_SITE 328 328 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT METAL 328 328 Iron-sulfur (2Fe-2S); via persulfide FT group; shared with IscU. FT {ECO:0000255|HAMAP-Rule:MF_00331}. FT BINDING 155 155 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT BINDING 183 183 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT BINDING 243 243 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00331}. FT MOD_RES 206 206 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00331}. SQ SEQUENCE 404 AA; 44855 MW; 594A78806D1DFA50 CRC64; MKLPIYLDYA ATCPVDERVA KKMMAFLTID GTFGNPASRS HKFGWQAEEA VDIARNQIAD LIGADSREIV FTSGATESDN LAIKGAAHFY QTKGKHIITC KTEHKAVLDT CRQLEREGFE VTYLSPEADG LIDLEKFKAA LRPDTILASI MHANNEIGVL QDIKAIGELC RANKTIFHVD ATQSVGKVEI NLEELAVDLM SMSSHKLYGP KGVGALYVRR KPRVRLEAII HGGGHERGMR SGTLPVHQIV GMGEAYRIAK EEMASEMPRL KALRDRLYNG LKDIEETYVN GSMEHRLDSN LNISFNYVEG ESLMMALRDI AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFTLGRY TTEEEIDYTI NLMKGAVEKL RALSPLWDMF KEGIDLNTIE WSAH // ID ISPA_HAEIN Reviewed; 295 AA. AC P45204; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Farnesyl diphosphate synthase; DE Short=FPP synthase; DE EC=2.5.1.10; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; GN Name=ispA; OrderedLocusNames=HI_1438; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + (2E,6E)-farnesyl diphosphate. 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 -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23087.1; -; Genomic_DNA. DR PIR; C64123; C64123. DR RefSeq; NP_439590.1; NC_000907.1. DR RefSeq; WP_010869214.1; NC_000907.1. DR ProteinModelPortal; P45204; -. DR SMR; P45204; 4-294. DR STRING; 71421.HI1438; -. DR EnsemblBacteria; AAC23087; AAC23087; HI_1438. DR GeneID; 950833; -. DR KEGG; hin:HI1438; -. DR PATRIC; 20191581; VBIHaeInf48452_1500. DR eggNOG; ENOG4105CTB; Bacteria. DR eggNOG; COG0142; LUCA. DR KO; K00795; -. DR OMA; KSHAILE; -. DR OrthoDB; EOG6TN43W; -. DR PhylomeDB; P45204; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isoprene biosynthesis; Magnesium; KW Metal-binding; Reference proteome; Transferase. FT CHAIN 1 295 Farnesyl diphosphate synthase. FT /FTId=PRO_0000123983. FT METAL 85 85 Magnesium 1. {ECO:0000250}. FT METAL 85 85 Magnesium 2. {ECO:0000250}. FT METAL 91 91 Magnesium 1. {ECO:0000250}. FT METAL 91 91 Magnesium 2. {ECO:0000250}. FT METAL 223 223 Magnesium 3. {ECO:0000250}. FT BINDING 46 46 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 49 49 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 78 78 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 96 96 Geranyl diphosphate. {ECO:0000250}. FT BINDING 97 97 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 180 180 Geranyl diphosphate. {ECO:0000250}. FT BINDING 181 181 Geranyl diphosphate. {ECO:0000250}. FT BINDING 220 220 Geranyl diphosphate. {ECO:0000250}. FT BINDING 237 237 Geranyl diphosphate. {ECO:0000250}. SQ SEQUENCE 295 AA; 32407 MW; A64DE650266E670F CRC64; MGHFSEELQQ VQTRINRFLE AQFEGIESHN APLLEAMKYA LLLGGKRVRP FLVYATGQML GAEKQTLDYA AAAIEAIHAY SLIHDDLPAM DDDNLRRGHP TCHIQFDEAT AILAGDALQS FAFEILTKTP NISTEQKLAL IQILAQGAGV QGMCLGQSLD LISEHKQISL SELELIHRNK TGALLIAALK LGFICSPHFT DKRLEQSLTQ YAEAIGLAFQ VQDDILDIEG DSAEIGKQVG ADLDLDKSTY PKLLGLSGAK QKAQDLYQSA LSELEKIPFD TTVRALAEFI ITRKS // ID IHFA_HAEIN Reviewed; 96 AA. AC P43723; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Integration host factor subunit alpha; DE Short=IHF-alpha; GN Name=ihfA; Synonyms=himA; OrderedLocusNames=HI_1313; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is one of the two subunits of integration CC host factor, a specific DNA-binding protein that functions in CC genetic recombination as well as in transcriptional and CC translational control. {ECO:0000250}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22959.1; -; Genomic_DNA. DR PIR; A64116; A64116. DR RefSeq; NP_439464.1; NC_000907.1. DR RefSeq; WP_005652847.1; NC_000907.1. DR ProteinModelPortal; P43723; -. DR SMR; P43723; 4-93. DR STRING; 71421.HI1313; -. DR EnsemblBacteria; AAC22959; AAC22959; HI_1313. DR GeneID; 949629; -. DR KEGG; hin:HI1313; -. DR PATRIC; 20191309; VBIHaeInf48452_1365. DR eggNOG; ENOG4108ZUF; Bacteria. DR eggNOG; COG0776; LUCA. DR KO; K04764; -. DR OMA; FDLRDKK; -. DR OrthoDB; EOG615VS6; -. DR PhylomeDB; P43723; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IBA:GO_Central. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 4.10.520.10; -; 1. DR HAMAP; MF_00380; IHF_alpha; 1. DR InterPro; IPR000119; Hist_DNA-bd. DR InterPro; IPR020816; Histone-like_DNA-bd_CS. DR InterPro; IPR010992; IHF-like_DNA-bd_dom. DR InterPro; IPR005684; IHF_alpha. DR Pfam; PF00216; Bac_DNA_binding; 1. DR PRINTS; PR01727; DNABINDINGHU. DR SMART; SM00411; BHL; 1. DR SUPFAM; SSF47729; SSF47729; 1. DR TIGRFAMs; TIGR00987; himA; 1. DR PROSITE; PS00045; HISTONE_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transcription; Transcription regulation; Translation regulation. FT CHAIN 1 96 Integration host factor subunit alpha. FT /FTId=PRO_0000105010. SQ SEQUENCE 96 AA; 10907 MW; 891091C0CE6355EA CRC64; MATITKLDII EYLSDKYHLS KQDTKNVVEN FLEEIRLSLE SGQDVKLSGF GNFELRDKSS RPGRNPKTGD VVPVSARRVV TFKPGQKLRA RVEKTK // ID ILVI_HAEIN Reviewed; 573 AA. AC P45261; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Acetolactate synthase large subunit; DE Short=AHAS; DE EC=2.2.1.6; DE AltName: Full=Acetohydroxy-acid synthase large subunit; DE Short=ALS; GN Name=ilvI; OrderedLocusNames=HI_1585; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. CC -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}. CC -!- MISCELLANEOUS: Contains 1 molecule of FAD per monomer. The role of CC this cofactor is not clear considering that the reaction does not CC involve redox chemistry (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23233.1; -; Genomic_DNA. DR PIR; C64131; C64131. DR RefSeq; NP_439730.1; NC_000907.1. DR RefSeq; WP_005671546.1; NC_000907.1. DR ProteinModelPortal; P45261; -. DR STRING; 71421.HI1585; -. DR EnsemblBacteria; AAC23233; AAC23233; HI_1585. DR GeneID; 950449; -. DR KEGG; hin:HI1585; -. DR PATRIC; 20191903; VBIHaeInf48452_1659. DR eggNOG; ENOG4105C7K; Bacteria. DR eggNOG; COG0028; LUCA. DR KO; K01652; -. DR OMA; MVWPMVP; -. DR OrthoDB; EOG6KT2NW; -. DR PhylomeDB; P45261; -. DR BRENDA; 2.2.1.6; 2529. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR012846; Acetolactate_synth_lsu. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00118; acolac_lg; 1. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; Magnesium; Metal-binding; KW Reference proteome; Thiamine pyrophosphate; Transferase. FT CHAIN 1 573 Acetolactate synthase large subunit. FT /FTId=PRO_0000090795. FT NP_BIND 261 282 FAD. {ECO:0000250}. FT NP_BIND 304 323 FAD. {ECO:0000250}. FT REGION 396 476 Thiamine pyrophosphate binding. FT METAL 447 447 Magnesium. {ECO:0000250}. FT METAL 474 474 Magnesium. {ECO:0000250}. FT BINDING 51 51 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 153 153 FAD. {ECO:0000250}. SQ SEQUENCE 573 AA; 62620 MW; CA055388605F60BE CRC64; MKKLSGAEMV VQSLRDEGVE YVFGYPGGAV LDIYDAIHTL GGIEHILVRH EQAAVHMADG YARSTGKVGC VLVTSGPGAT NAITGILTAY TDSVPMVIIS GQVMSNLIGS DAFQECDMLG ISRPVVKHSF IVKKAEDIPS TLKKAFYIAS TGRPGPVVVD IPKDTVNPNF KYPYEYPEYV ELRSYNPTVN GHKGQIKKAL KALLVAKKPI LFVGGGAITA ECSEQLIQFA QRLNLPVTSS LMGLGAYPST DKQFLGMLGM HGTLEANTAM HESDLILGIG VRFDDRTTNN LEKYCPNAKV IHIDIDPTSI SKNVPVAIPI VGNAKNVLEE FLGLLNEEGL KSQTDLESWW QEINQWKAKK CLEFDRTSGV IKPQQVVEAV YRLTKGQAYV ASDVGQHQMF AALHYPFDEP RHWINSGGAG TMGFGFPAAL GVKLAHPEGT VVCVTGDGSI QMNIQELSTA TQYGIPVVII CLNNHFLGMV KQWQDLIYSG RHSQTYMNSL PDFAKLAESY GHVGIKIATP DELESKLQEA FSIKNKLVFV DINVDESEHV YPMQIRGGAM NEMILSKPQE ETN // ID ILVY_HAEIN Reviewed; 292 AA. AC P44821; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=HTH-type transcriptional activator IlvY; GN Name=ilvY; OrderedLocusNames=HI_0681; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein activates the transcription of the ilvC CC gene in the presence of acetolactate or acetohydroxybutyrate. IlvY CC is also a negative regulator of its own expression (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22340.1; -; Genomic_DNA. DR PIR; A64086; A64086. DR RefSeq; NP_438841.1; NC_000907.1. DR RefSeq; WP_005694606.1; NC_000907.1. DR ProteinModelPortal; P44821; -. DR STRING; 71421.HI0681; -. DR DNASU; 949718; -. DR EnsemblBacteria; AAC22340; AAC22340; HI_0681. DR GeneID; 949718; -. DR KEGG; hin:HI0681; -. DR PATRIC; 20189981; VBIHaeInf48452_0712. DR eggNOG; ENOG4105EMY; Bacteria. DR eggNOG; COG0583; LUCA. DR KO; K02521; -. DR OMA; KTATQNH; -. DR OrthoDB; EOG6C8MV8; -. DR PhylomeDB; P44821; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Activator; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; KW DNA-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 292 HTH-type transcriptional activator IlvY. FT /FTId=PRO_0000105658. FT DOMAIN 1 58 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 18 37 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 292 AA; 33548 MW; 6FAD81E275D44244 CRC64; MEFTDLQIFI HLSDTKNFTK TATQNHMSPS TLSRQIQRLE DELGKTLFIR DNRQVKLTEY GEKFLQFAKT EWQNWQQFKQ QLKDESDELC GEIKLFCSVT ASYSHLPHVL KEFRQRYPKV EIQLTTGDPA LALELIQAQQ VDLALAGKPN NLPSSVVFHK IDDISLSLIA PRVACLATQL LQEKPIDWQQ MPFIFPVEGH ARQRIEQWLR EKQIKHPKIY ATVAGHEGIV PMVGLGFGLA MLPDAVIDSS PMNNQISRLN LDKPIEPFEL GICTQKRNLE QPLVRAFWAM LE // ID IPYR_HAEIN Reviewed; 176 AA. AC P44529; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Inorganic pyrophosphatase; DE EC=3.6.1.1; DE AltName: Full=Pyrophosphate phospho-hydrolase; DE Short=PPase; GN Name=ppa; OrderedLocusNames=HI_0124; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21798.1; -; Genomic_DNA. DR PIR; G64049; G64049. DR RefSeq; NP_438296.1; NC_000907.1. DR RefSeq; WP_005630160.1; NC_000907.1. DR ProteinModelPortal; P44529; -. DR STRING; 71421.HI0124; -. DR EnsemblBacteria; AAC21798; AAC21798; HI_0124. DR GeneID; 951032; -. DR KEGG; hin:HI0124; -. DR PATRIC; 20188739; VBIHaeInf48452_0128. DR eggNOG; ENOG4105F0N; Bacteria. DR eggNOG; COG0221; LUCA. DR KO; K01507; -. DR OMA; HPEKYTF; -. DR OrthoDB; EOG6NKR4X; -. DR PhylomeDB; P44529; -. DR Proteomes; UP000000579; 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 1 176 Inorganic pyrophosphatase. FT /FTId=PRO_0000137500. FT METAL 67 67 Magnesium 1. {ECO:0000250}. FT METAL 72 72 Magnesium 1. {ECO:0000250}. FT METAL 72 72 Magnesium 2. {ECO:0000250}. FT METAL 104 104 Magnesium 1. {ECO:0000250}. SQ SEQUENCE 176 AA; 19725 MW; ECDEDE557F28446F CRC64; MADFNQILTP GDVDAGIINV VNEIPEGSCH KIEWNRKVAA FQLDRVEPAI FAKPTNYGFI PQTLDEDGDE LDVLLITRQP LATGVFLEAK VIGVMKFVDD GEVDDKIVCV PADDRDTGNA YNSLADLPAN LIKQIEFHFN NYKALKKPGS TKVTHWGDVE EAKEVIRESI KRWNER // ID ISCU_HAEIN Reviewed; 126 AA. AC Q57074; O05020; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 17-FEB-2016, entry version 95. DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; DE AltName: Full=Sulfur acceptor protein IscU; GN Name=iscU; OrderedLocusNames=HI_0377; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP STRUCTURE BY NMR OF THE APO PROTEIN AND IN COMPLEX WITH ZN(2+), RP SUBUNIT, AND COFACTOR. RX PubMed=15522305; DOI=10.1016/j.jmb.2004.08.038; RA Ramelot T.A., Cort J.R., Goldsmith-Fischman S., Kornhaber G.J., RA Xiao R., Shastry R., Acton T.B., Honig B., Montelione G.T., RA Kennedy M.A.; RT "Solution NMR structure of the iron-sulfur cluster assembly protein U RT (IscU) with zinc bound at the active site."; RL J. Mol. Biol. 344:567-583(2004). CC -!- FUNCTION: A scaffold on which IscS assembles Fe-S clusters. CC Subsequently gives the nascent cluster to other proteins. It is CC likely that Fe-S cluster coordination is flexible as the role of CC this complex is to build and then hand off Fe-S clusters (By CC similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15522305}; CC Note=Binds 1 Zn(2+) ion; this is probably a substitute for Fe-S CC centers. {ECO:0000269|PubMed:15522305}; CC -!- SUBUNIT: Forms a heterotetramer with IscS; each subunit of the CC IscS dimer contacts an IscU monomer (By similarity). Upon CC overexpression can be isolated a monomer, dimers and other CC oligomers. {ECO:0000250, ECO:0000269|PubMed:15522305}. CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22034.1; -; Genomic_DNA. DR RefSeq; NP_438538.2; NC_000907.1. DR PDB; 1Q48; NMR; -; A=1-126. DR PDB; 1R9P; NMR; -; A=1-126. DR PDBsum; 1Q48; -. DR PDBsum; 1R9P; -. DR ProteinModelPortal; Q57074; -. DR SMR; Q57074; 1-126. DR STRING; 71421.HI0377; -. DR PRIDE; Q57074; -. DR EnsemblBacteria; AAC22034; AAC22034; HI_0377. DR GeneID; 949477; -. DR KEGG; hin:HI0377; -. DR PATRIC; 20189299; VBIHaeInf48452_0395. DR eggNOG; ENOG4107XTC; Bacteria. DR eggNOG; COG0822; LUCA. DR KO; K04488; -. DR OMA; VMDHFTN; -. DR OrthoDB; EOG6GFGQT; -. DR EvolutionaryTrace; Q57074; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0036455; F:iron-sulfur transferase activity; IBA:GO_Central. DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central. DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central. DR InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU. DR InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N. DR Pfam; PF01592; NifU_N; 1. DR TIGRFAMs; TIGR01999; iscU; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Reference proteome; KW Zinc. FT CHAIN 1 126 Iron-sulfur cluster assembly scaffold FT protein IscU. FT /FTId=PRO_0000166187. FT METAL 37 37 Zinc. FT METAL 63 63 Zinc. FT METAL 105 105 Zinc. FT METAL 106 106 Zinc. FT STRAND 3 5 {ECO:0000244|PDB:1Q48}. FT TURN 14 16 {ECO:0000244|PDB:1Q48}. FT STRAND 21 24 {ECO:0000244|PDB:1Q48}. FT STRAND 27 33 {ECO:0000244|PDB:1Q48}. FT TURN 35 37 {ECO:0000244|PDB:1Q48}. FT STRAND 40 47 {ECO:0000244|PDB:1Q48}. FT STRAND 49 59 {ECO:0000244|PDB:1Q48}. FT TURN 64 66 {ECO:0000244|PDB:1Q48}. FT HELIX 67 77 {ECO:0000244|PDB:1Q48}. FT HELIX 82 85 {ECO:0000244|PDB:1Q48}. FT HELIX 90 97 {ECO:0000244|PDB:1Q48}. FT HELIX 105 123 {ECO:0000244|PDB:1Q48}. SQ SEQUENCE 126 AA; 13399 MW; 9918E1334646E67B CRC64; MAYSEKVIDH YENPRNVGSL DKKDSNVGTG MVGAPACGDV MQLQIKVDDN GIIEDAKFKT YGCGSAIASS SLITEWVKGK SLEEAGAIKN SQIAEELELP PVKVHCSILA EDAIKAAIAD YKAKQG // ID ISPF_HAEIN Reviewed; 158 AA. AC P44815; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; DE Short=MECDP-synthase; DE Short=MECPP-synthase; DE Short=MECPS; DE EC=4.6.1.12; GN Name=ispF; OrderedLocusNames=HI_0671; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COBALT IONS, AND RP SUBUNIT. RX PubMed=12211023; DOI=10.1002/prot.10182; RA Lehmann C., Lim K., Toedt J., Krajewski W., Howard A., Eisenstein E., RA Herzberg O.; RT "Structure of 2C-methyl-D-erythrol-2,4-cyclodiphosphate synthase from RT Haemophilus influenzae: activation by conformational transition."; RL Proteins 49:135-138(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2-158 IN COMPLEX WITH RP SUBSTRATE ANALOGS AND MANGANESE IONS, COFACTOR, AND SUBUNIT. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate CC (IPP) and dimethylallyl diphosphate (DMAPP), two major building CC blocks of isoprenoid compounds. Catalyzes the conversion of 4- CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to CC 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a CC corresponding release of cytidine 5-monophosphate (CMP) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C- CC methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate CC + CMP. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000269|PubMed:16021622}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000269|PubMed:16021622}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 4/6. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12211023, CC ECO:0000269|PubMed:16021622}. CC -!- SIMILARITY: Belongs to the IspF 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; L42023; AAC22331.1; -; Genomic_DNA. DR PIR; F64156; F64156. DR RefSeq; NP_438831.1; NC_000907.1. DR RefSeq; WP_005687916.1; NC_000907.1. DR PDB; 1JN1; X-ray; 2.90 A; A/B/C=1-158. DR PDB; 1VH8; X-ray; 2.35 A; A/B/C/D/E/F=2-158. DR PDB; 1VHA; X-ray; 2.35 A; A/B/C/D/E/F=2-158. DR PDB; 5ESV; X-ray; 3.10 A; E/F/G=2-13, E/F/G=38-158. DR PDB; 5ESZ; X-ray; 4.19 A; C/G=2-14, C/G=38-158. DR PDBsum; 1JN1; -. DR PDBsum; 1VH8; -. DR PDBsum; 1VHA; -. DR PDBsum; 5ESV; -. DR PDBsum; 5ESZ; -. DR ProteinModelPortal; P44815; -. DR SMR; P44815; 1-157. DR STRING; 71421.HI0671; -. DR EnsemblBacteria; AAC22331; AAC22331; HI_0671. DR GeneID; 950633; -. DR KEGG; hin:HI0671; -. DR PATRIC; 20189959; VBIHaeInf48452_0701. DR eggNOG; ENOG4108UH8; Bacteria. DR eggNOG; COG0245; LUCA. DR KO; K01770; -. DR OMA; IRIGNGY; -. DR OrthoDB; EOG6J48RZ; -. DR PhylomeDB; P44815; -. DR BRENDA; 4.6.1.12; 2529. DR UniPathway; UPA00056; UER00095. DR EvolutionaryTrace; P44815; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.50; -; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. DR TIGRFAMs; TIGR00151; ispF; 1. DR PROSITE; PS01350; ISPF; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isoprene biosynthesis; Lyase; KW Manganese; Metal-binding; Reference proteome. FT CHAIN 1 158 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT /FTId=PRO_0000189472. FT REGION 9 11 Substrate binding. {ECO:0000250}. FT REGION 35 36 Substrate binding. {ECO:0000250}. FT REGION 39 47 Substrate binding. {ECO:0000250}. FT REGION 57 59 Substrate binding. {ECO:0000250}. FT REGION 62 66 Substrate binding. {ECO:0000250}. FT REGION 101 107 Substrate binding. {ECO:0000250}. FT REGION 132 136 Substrate binding. {ECO:0000250}. FT REGION 140 143 Substrate binding. FT METAL 9 9 Divalent metal cation. FT METAL 11 11 Divalent metal cation. FT METAL 43 43 Divalent metal cation. FT BINDING 66 66 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 140 140 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 143 143 Substrate. {ECO:0000250}. FT SITE 35 35 Transition state stabilizer. FT {ECO:0000250}. FT SITE 134 134 Transition state stabilizer. FT {ECO:0000250}. FT STRAND 2 12 {ECO:0000244|PDB:1VH8}. FT STRAND 14 21 {ECO:0000244|PDB:1VH8}. FT STRAND 24 32 {ECO:0000244|PDB:1VH8}. FT HELIX 40 52 {ECO:0000244|PDB:1VH8}. FT HELIX 58 60 {ECO:0000244|PDB:1VH8}. FT HELIX 64 67 {ECO:0000244|PDB:1JN1}. FT STRAND 68 70 {ECO:0000244|PDB:1JN1}. FT HELIX 74 87 {ECO:0000244|PDB:1VH8}. FT STRAND 90 100 {ECO:0000244|PDB:1VH8}. FT STRAND 102 104 {ECO:0000244|PDB:1JN1}. FT HELIX 107 120 {ECO:0000244|PDB:1VH8}. FT HELIX 125 127 {ECO:0000244|PDB:1VH8}. FT STRAND 128 133 {ECO:0000244|PDB:1VH8}. FT HELIX 139 142 {ECO:0000244|PDB:1VH8}. FT STRAND 145 157 {ECO:0000244|PDB:1VH8}. SQ SEQUENCE 158 AA; 17194 MW; DC34BF347DEC2EFF CRC64; MIRIGHGFDV HAFGEDRPLI IGGVEVPYHT GFIAHSDGDV ALHALTDAIL GAAALGDIGK LFPDTDMQYK NADSRGLLRE AFRQVQEKGY KIGNVDITII AQAPKMRPHI DAMRAKIAED LQCDIEQVNV KATTTEKLGF TGRQEGIACE AVALLIRQ // ID ISCX_HAEIN Reviewed; 64 AA. AC P44668; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=Protein IscX; GN Name=iscX; OrderedLocusNames=HI_0371; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May function as iron donor in the assembly of iron- CC sulfur clusters. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the IscX 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; L42023; AAC22029.1; -; Genomic_DNA. DR PIR; B64150; B64150. DR RefSeq; NP_438532.1; NC_000907.1. DR RefSeq; WP_005656371.1; NC_000907.1. DR ProteinModelPortal; P44668; -. DR SMR; P44668; 1-62. DR STRING; 71421.HI0371; -. DR EnsemblBacteria; AAC22029; AAC22029; HI_0371. DR GeneID; 949472; -. DR KEGG; hin:HI0371; -. DR PATRIC; 20189287; VBIHaeInf48452_0389. DR eggNOG; ENOG4105WVQ; Bacteria. DR eggNOG; COG2975; LUCA. DR OMA; AIQQAWI; -. DR OrthoDB; EOG6ZD6DN; -. DR PhylomeDB; P44668; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR Gene3D; 1.10.10.600; -; 1. DR InterPro; IPR007479; ISC_FeS_clus_asmbl_IscsX. DR Pfam; PF04384; Fe-S_assembly; 1. DR PIRSF; PIRSF039003; IscX; 1. DR SUPFAM; SSF140319; SSF140319; 1. DR TIGRFAMs; TIGR03412; iscX_yfhJ; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 64 Protein IscX. FT /FTId=PRO_0000211857. SQ SEQUENCE 64 AA; 7712 MW; A242087BEDFA3F6A CRC64; MKWTDAQLIA EELYDRNPDL DPKTVRFTDL HKWICELENF DDDPNKSNES ILEAILLKWL DEFE // ID ISPB_HAEIN Reviewed; 329 AA. AC P44916; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Octaprenyl-diphosphate synthase; DE EC=2.5.1.90; DE AltName: Full=All-trans-octaprenyl-diphosphate synthase; DE AltName: Full=Octaprenyl pyrophosphate synthase; DE Short=OPP synthase; GN Name=ispB; OrderedLocusNames=HI_0881; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Supplies octaprenyl diphosphate, the precursor for the CC side chain of the isoprenoid quinones ubiquinone and menaquinone. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + 5 isopentenyl CC diphosphate = 5 diphosphate + all-trans-octaprenyl diphosphate. 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 -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22540.1; -; Genomic_DNA. DR PIR; I64160; I64160. DR RefSeq; NP_439042.1; NC_000907.1. DR RefSeq; WP_005693233.1; NC_000907.1. DR ProteinModelPortal; P44916; -. DR STRING; 71421.HI0881; -. DR EnsemblBacteria; AAC22540; AAC22540; HI_0881. DR GeneID; 949563; -. DR KEGG; hin:HI0881; -. DR PATRIC; 20190419; VBIHaeInf48452_0923. DR eggNOG; ENOG4105EAH; Bacteria. DR eggNOG; COG0142; LUCA. DR KO; K02523; -. DR OMA; LIIAMQR; -. DR OrthoDB; EOG6TN43W; -. DR PhylomeDB; P44916; -. DR BRENDA; 2.5.1.90; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1 329 Octaprenyl-diphosphate synthase. FT /FTId=PRO_0000124006. FT METAL 90 90 Magnesium 1. {ECO:0000250}. FT METAL 90 90 Magnesium 2. {ECO:0000250}. FT METAL 94 94 Magnesium 1. {ECO:0000250}. FT METAL 94 94 Magnesium 2. {ECO:0000250}. FT METAL 217 217 Magnesium 3. {ECO:0000250}. FT BINDING 51 51 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 54 54 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 83 83 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 99 99 Polyprenyl diphosphate. {ECO:0000250}. FT BINDING 100 100 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 176 176 Polyprenyl diphosphate. {ECO:0000250}. FT BINDING 177 177 Polyprenyl diphosphate. {ECO:0000250}. FT BINDING 214 214 Polyprenyl diphosphate. {ECO:0000250}. SQ SEQUENCE 329 AA; 35912 MW; 65DBC4CCDAD72E04 CRC64; MKKQDLMSID EIQKLADPDM QKVNQNILAQ LNSDVPLIGQ LGFYIVQGGG KRIRPLIAVL AARSLGFEGS NSITCATFVE FIHTASLLHD DVVDESDMRR GRATANAEFG NAASVLVGDF IYTRAFQLVA QLESLKILSI MADATNVLAE GEVQQLMNVN DPETSEANYM RVIYSKTARL FEVAGQAAAI VAGGTEAQEK ALQDYGRYLG TAFQLVDDVL DYSANTQALG KNVGDDLAEG KPTLPLLHAM RHGNAQQAAL IREAIEQGGK REAIDEVLAI MTEHKSLDYA MNRAKEEAQK AVDAIEILPE SEYKQALISL AYLSVDRNY // ID ISPH_HAEIN Reviewed; 314 AA. AC P44976; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; Synonyms=lytB; GN OrderedLocusNames=HI_1007; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate CC (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [3Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00191}; CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3- CC methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22668.1; -; Genomic_DNA. DR RefSeq; NP_439168.1; NC_000907.1. DR RefSeq; WP_010869105.1; NC_000907.1. DR STRING; 71421.HI1007; -. DR EnsemblBacteria; AAC22668; AAC22668; HI_1007. DR GeneID; 950001; -. DR KEGG; hin:HI1007; -. DR PATRIC; 20190675; VBIHaeInf48452_1050. DR eggNOG; ENOG4105C48; Bacteria. DR eggNOG; COG0761; LUCA. DR KO; K03527; -. DR OMA; DDLTFMT; -. DR OrthoDB; EOG6HF624; -. DR PhylomeDB; P44976; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 3Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 314 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase. FT /FTId=PRO_0000128824. FT REGION 225 227 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 12 12 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 96 96 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 197 197 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 41 41 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 74 74 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 167 167 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 269 269 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. SQ SEQUENCE 314 AA; 34468 MW; 44860D110E9F9EBC CRC64; MKIILANPRG FCAGVDRAIS IVELALEIHG APIYVRHEVV HNRFVVNGLR ERGAIFVEEL SEVPDGAIVI FSAHGVSQAV RQEAKDRNLK VFDATCPLVT KVHMQVARAS RKGTKAILIG HKGHPEVEGT MGQYSNEDGG IFLIEKVEDI ARLPMQENDN LTFMTQTTLS LDDTAETIAA LKEKYPAIQG PHKNDICYAT TNRQEAVREL AKLSDLVLVV GSKNSSNSNR LAELASRMGV KSQLLDEPAD IQADWFNDVK TIGITAGASA PEELGQSIIS RLKRFGANSI EELQGLEGNM FFEVPKELRI KEVN // ID K1PF_HAEIN Reviewed; 313 AA. AC P44330; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=1-phosphofructokinase; DE EC=2.7.1.56; DE AltName: Full=Fructose 1-phosphate kinase; GN Name=fruK; OrderedLocusNames=HI_0447; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 1-phosphate = ADP + D- CC fructose 1,6-bisphosphate. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB 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; L42023; AAC22106.1; -; Genomic_DNA. DR PIR; A64069; A64069. DR RefSeq; NP_438608.1; NC_000907.1. DR RefSeq; WP_005693714.1; NC_000907.1. DR ProteinModelPortal; P44330; -. DR STRING; 71421.HI0447; -. DR EnsemblBacteria; AAC22106; AAC22106; HI_0447. DR GeneID; 949542; -. DR KEGG; hin:HI0447; -. DR PATRIC; 20189449; VBIHaeInf48452_0467. DR eggNOG; ENOG4105DE4; Bacteria. DR eggNOG; COG1105; LUCA. DR KO; K00882; -. DR OMA; EVNTVET; -. DR OrthoDB; EOG61KBKF; -. DR PhylomeDB; P44330; -. DR Proteomes; UP000000579; 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; IPR022463; 1-PFruKinase. 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 TIGRFAMs; TIGR03168; 1-PFK; 1. DR TIGRFAMs; TIGR03828; pfkB; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 313 1-phosphofructokinase. FT /FTId=PRO_0000080079. FT NP_BIND 186 189 ATP. {ECO:0000255}. FT ACT_SITE 255 255 {ECO:0000255}. SQ SEQUENCE 313 AA; 33522 MW; 72FE0D6A1C240A55 CRC64; MASVVTITLN AAYDLVGRLN RIQLGEVNTV ETLGLFPAGK GINVAKVLKD LGVNVAVGGF LGKDNSADFE QMFNQHGLED KFHRVDGKTR INVKITETEA DVTDLNFLGY QISPQVWQQF VTDSLAYCLN YDIVAVCGSL PRGVSPELFA DWLNQLHQAG VKVVLDSSNA ALTAGLKAKP WLVKPNHREL EAWVGHPLNS LEEIIAAAQQ LKAEGIENVI ISMGAKGSLW INNEGVLKAE PAQCENVVST VGAGDSMVAG LIYGFEKGLS KTETLAFATA VSAFAVSQSN VGVSDLSLLD PILEKVQITM IEG // ID ISPD_HAEIN Reviewed; 225 AA. AC O05029; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; DE EC=2.7.7.60; DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase; DE AltName: Full=MEP cytidylyltransferase; DE Short=MCT; GN Name=ispD; OrderedLocusNames=HI_0672; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C- CC methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4- CC phosphate (MEP). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate = CC diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 2/6. CC -!- SIMILARITY: Belongs to the IspD 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; L42023; AAC22332.1; -; Genomic_DNA. DR PIR; G64156; G64156. DR RefSeq; NP_438832.1; NC_000907.1. DR RefSeq; WP_005655267.1; NC_000907.1. DR ProteinModelPortal; O05029; -. DR STRING; 71421.HI0672; -. DR EnsemblBacteria; AAC22332; AAC22332; HI_0672. DR GeneID; 950888; -. DR KEGG; hin:HI0672; -. DR PATRIC; 20189961; VBIHaeInf48452_0702. DR eggNOG; ENOG4105CE5; Bacteria. DR eggNOG; COG1211; LUCA. DR KO; K00991; -. DR OMA; QAYTPQM; -. DR OrthoDB; EOG6J48RZ; -. DR PhylomeDB; O05029; -. DR UniPathway; UPA00056; UER00093. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00108; IspD; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR018294; ISPD_synthase_CS. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00453; ispD; 1. DR PROSITE; PS01295; ISPD; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 225 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. FT /FTId=PRO_0000075579. FT SITE 17 17 Transition state stabilizer. FT {ECO:0000250}. FT SITE 24 24 Transition state stabilizer. FT {ECO:0000250}. FT SITE 150 150 Positions MEP for the nucleophilic FT attack. {ECO:0000250}. FT SITE 206 206 Positions MEP for the nucleophilic FT attack. {ECO:0000250}. SQ SEQUENCE 225 AA; 24548 MW; 2155A297B44CD8C9 CRC64; MARSIIAVLP AAGVGSRMQA DKPKQYLTLL GKTLLEHTLD VMLSYPAVSK IILAVSKDDP YISTLSLDPK IQLVEGGTTR AESVLNGLNA IAEKNAWVLV HDAARPCLQH ADIDKLLAIE DKQGAILAIP VTDTIKRADN QQCIVKTEDR SQLWQAMTPQ FFPVDILRDA LSTGIQQGAN ITDEASAIEL AGFRPHLVAG RSDNLKVTRP EDLALAEFYL TRNKL // ID ISPE_HAEIN Reviewed; 313 AA. AC P45271; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; DE Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061}; DE EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061}; DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061}; GN Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; GN OrderedLocusNames=HI_1608; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy CC group of 4-diphosphocytidyl-2C-methyl-D-erythritol. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D- CC erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl- CC D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000255|HAMAP- CC Rule:MF_00061}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00061}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23252.1; -; Genomic_DNA. DR PIR; A64173; A64173. DR RefSeq; NP_439750.1; NC_000907.1. DR RefSeq; WP_010869257.1; NC_000907.1. DR ProteinModelPortal; P45271; -. DR SMR; P45271; 23-296. DR STRING; 71421.HI1608; -. DR EnsemblBacteria; AAC23252; AAC23252; HI_1608. DR GeneID; 950459; -. DR KEGG; hin:HI1608; -. DR PATRIC; 20191947; VBIHaeInf48452_1681. DR eggNOG; ENOG4105CTR; Bacteria. DR eggNOG; COG1947; LUCA. DR KO; K00919; -. DR OMA; RWPSPAK; -. DR OrthoDB; EOG62VNQ2; -. DR PhylomeDB; P45271; -. DR UniPathway; UPA00056; UER00094. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00061; IspE; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR004424; IspE. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR20861:SF2; PTHR20861:SF2; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF010376; IspE; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00154; ispE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 313 4-diphosphocytidyl-2-C-methyl-D- FT erythritol kinase. FT /FTId=PRO_0000189223. FT NP_BIND 113 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 29 29 {ECO:0000255|HAMAP-Rule:MF_00061}. FT ACT_SITE 155 155 {ECO:0000255|HAMAP-Rule:MF_00061}. SQ SEQUENCE 313 AA; 34658 MW; 7A84BAACA196821B CRC64; MKSHQFSTAL CQNTTESNGQ PLRFPSPAKL NLFLYINGKF PNGYHELQTL FQFLDFGDWL DISIREQDNQ IVLTPEIPNL KTENNLIYRA AKLLQEKANI QLGANIHLDK ILPMGGGVGG GSSNAATALV SLNYLWQANL SIDELAKLGL TLGADVPIFV HGHAAFAEGV GEKITYCEPA EKWFVILKPD DSISTAVIFQ DPNLPRNTPK KSLAQLLSEP YKNDCEKVVI NHYSNVEKAL NWLLQYAPAR LTGTGACVFA EFDHEAEAQA VFRQKPEAFF GFVAKGLNVS PLHAMLKQLS STHTHRQSKP EVL // ID KDGL_HAEIN Reviewed; 118 AA. AC P44424; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Diacylglycerol kinase; DE Short=DAGK; DE EC=2.7.1.107; DE AltName: Full=Diglyceride kinase; DE Short=DGK; GN Name=dgkA; OrderedLocusNames=HI_0335; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Recycling of diacylglycerol produced during the turnover CC of membrane phospholipid. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2- CC diacyl-sn-glycerol 3-phosphate. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial diacylglycerol 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; L42023; AAC21997.1; -; Genomic_DNA. DR PIR; E64062; E64062. DR RefSeq; NP_438499.1; NC_000907.1. DR RefSeq; WP_005694338.1; NC_000907.1. DR STRING; 71421.HI0335; -. DR EnsemblBacteria; AAC21997; AAC21997; HI_0335. DR GeneID; 949443; -. DR KEGG; hin:HI0335; -. DR PATRIC; 20189213; VBIHaeInf48452_0352. DR eggNOG; ENOG41080IJ; Bacteria. DR eggNOG; COG0818; LUCA. DR KO; K00901; -. DR OMA; RFWRATI; -. DR OrthoDB; EOG60W7XM; -. DR PhylomeDB; P44424; -. DR Proteomes; UP000000579; 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:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR000829; Diacylglycerol_kinase_prok. DR Pfam; PF01219; DAGK_prokar; 1. DR PROSITE; PS01069; DAGK_PROKAR; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Lipid biosynthesis; Lipid metabolism; Membrane; KW Nucleotide-binding; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 118 Diacylglycerol kinase. FT /FTId=PRO_0000195263. FT TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TOPO_DOM 50 54 Periplasmic. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TOPO_DOM 76 97 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. SQ SEQUENCE 118 AA; 13025 MW; 649175CBAB159FAA CRC64; MYKTTGLTHL INSTKYSLQG LKSAFKNETA FRHECFLACI LIPLTFFLGE TKIEIILMIS SVLLVMALEL LNSAVETVVD RIGTERHELS GRAKDQGSAS VFIALCIVGI VWGGILFF // ID KDKA_HAEIN Reviewed; 241 AA. AC O86224; Q9F438; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=3-deoxy-D-manno-octulosonic acid kinase; DE Short=Kdo kinase; DE EC=2.7.1.166; GN Name=kdkA; OrderedLocusNames=HI_0260.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, RP SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, GENE NAME, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10531340; DOI=10.1074/jbc.274.44.31391; RA White K.A., Lin S., Cotter R.J., Raetz C.R.H.; RT "A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy- RT D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo RT phosphorylation in bacterial virulence."; RL J. Biol. Chem. 274:31391-31400(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd, and I69 / Serotype B; RX PubMed=10952982; DOI=10.1074/jbc.M005204200; RA Brabetz W., Mueller-Loennies S., Brade H.; RT "3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and Kdo RT kinase (KdkA) of Haemophilus influenzae are both required to RT complement a waaA knockout mutation of Escherichia coli."; RL J. Biol. Chem. 275:34954-34962(2000). RN [3] RP FUNCTION, SUBSTRATE SPECIFICITY, PH DEPENDENCE, AND SUBCELLULAR RP LOCATION. RC STRAIN=722; RX PubMed=9195966; DOI=10.1074/jbc.272.26.16555; RA White K.A., Kaltashov I.A., Cotter R.J., Raetz C.R.; RT "A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase RT and a Kdo kinase in extracts of Haemophilus influenzae."; RL J. Biol. Chem. 272:16555-16563(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [5] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of the 3- CC deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at CC the 4-OH position. To a lesser extent, can use GTP instead of ATP CC as substrate. {ECO:0000269|PubMed:10531340, CC ECO:0000269|PubMed:10952982, ECO:0000269|PubMed:9195966}. CC -!- CATALYTIC ACTIVITY: Alpha-Kdo-(2->6)-lipid IV(A) + ATP = 4-O- CC phospho-alpha-Kdo-(2->6)-lipid IV(A) + ADP. CC {ECO:0000269|PubMed:10531340}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11.6 uM for Kdo-lipid IV(A) {ECO:0000269|PubMed:10531340}; CC Vmax=73625 nmol/min/mg enzyme {ECO:0000269|PubMed:10531340}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:9195966}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:10531340, ECO:0000305|PubMed:9195966}; CC Peripheral membrane protein {ECO:0000305|PubMed:10531340, CC ECO:0000305|PubMed:9195966}; Cytoplasmic side CC {ECO:0000305|PubMed:10531340, ECO:0000305|PubMed:9195966}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP 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; AY043284; AAK92207.1; -; Genomic_DNA. DR EMBL; AJ277816; CAC07180.1; -; Genomic_DNA. DR EMBL; AJ277817; CAC07181.1; -; Genomic_DNA. DR EMBL; L42023; AAC21931.1; -; Genomic_DNA. DR RefSeq; NP_438429.1; NC_000907.1. DR RefSeq; WP_005694044.1; NC_000907.1. DR STRING; 71421.HI0260.1; -. DR EnsemblBacteria; AAC21931; AAC21931; HI_0260.1. DR GeneID; 950779; -. DR KEGG; hin:HI0260.1; -. DR PATRIC; 20189047; VBIHaeInf48452_0275. DR eggNOG; ENOG4108W7E; Bacteria. DR eggNOG; COG0515; LUCA. DR KO; K11211; -. DR OMA; CHTDLNA; -. DR OrthoDB; EOG615VH4; -. DR BioCyc; MetaCyc:MONOMER-15507; -. DR BRENDA; 2.7.1.166; 2529. DR UniPathway; UPA00958; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00521; KDO_kinase; 1. DR InterPro; IPR022826; KDO_kinase. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR010440; LipoPS_kinase. DR Pfam; PF06293; Kdo; 1. DR SUPFAM; SSF56112; SSF56112; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 241 3-deoxy-D-manno-octulosonic acid kinase. FT /FTId=PRO_0000194313. FT ACT_SITE 171 171 {ECO:0000255}. FT VARIANT 46 46 I -> T (in strain: I69). FT VARIANT 85 85 E -> D (in strain: I69). FT VARIANT 151 153 TWM -> IWR (in strain: I69). FT VARIANT 200 201 SA -> LG (in strain: I69). SQ SEQUENCE 241 AA; 28569 MW; 897A905BBA4BED09 CRC64; MHQFQQDNQY FIFNFDRTFE QATEFFQAEF WQKQERVIGS AKGRGITYFL QTEDWFGVNC ALRHYYRGGL WGKLNKDRYR FSALETTRSF AEFHLLQRLY EAGLPVPKPI AARIQKGKLG ICYQADILTE KIENAQDLTA LLQTQTLPKE TWMQIGRLIR KLHDLQICHT DLNAHNILLQ QTEQGQKCWL LDFDKCGEKS ADFWKVQNLN RLKRSFEKEV GRMNIQFTEQ NWADLTSAYH Q // ID KDSA_HAEIN Reviewed; 284 AA. AC P45251; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 109. DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase; DE EC=2.5.1.55; DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase; DE AltName: Full=KDO-8-phosphate synthase; DE Short=KDO 8-P synthase; DE Short=KDOPS; DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase; GN Name=kdsA; OrderedLocusNames=HI_1557; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + D-arabinose 5-phosphate CC + H(2)O = 3-deoxy-D-manno-octulosonate 8-phosphate + phosphate. CC -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5- CC phosphate: step 2/3. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the KdsA 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; L42023; AAC23206.1; -; Genomic_DNA. DR PIR; G64129; G64129. DR RefSeq; NP_439706.1; NC_000907.1. DR RefSeq; WP_005693586.1; NC_000907.1. DR PDB; 1O60; X-ray; 1.80 A; A/B/C/D=1-284. DR PDBsum; 1O60; -. DR ProteinModelPortal; P45251; -. DR SMR; P45251; 2-282. DR STRING; 71421.HI1557; -. DR EnsemblBacteria; AAC23206; AAC23206; HI_1557. DR GeneID; 950417; -. DR KEGG; hin:HI1557; -. DR PATRIC; 20191839; VBIHaeInf48452_1628. DR eggNOG; ENOG4105CXR; Bacteria. DR eggNOG; COG2877; LUCA. DR KO; K01627; -. DR OMA; FRGIPTM; -. DR OrthoDB; EOG680X4R; -. DR PhylomeDB; P45251; -. DR BRENDA; 2.5.1.55; 2529. DR UniPathway; UPA00030; -. DR UniPathway; UPA00357; UER00474. DR EvolutionaryTrace; P45251; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00056; KDO8P_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006218; DAHP1/KDSA. DR InterPro; IPR006269; KDO8P_synthase. DR Pfam; PF00793; DAHP_synth_1; 1. DR TIGRFAMs; TIGR01362; KDO8P_synth; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 284 2-dehydro-3-deoxyphosphooctonate FT aldolase. FT /FTId=PRO_0000187131. FT STRAND 6 8 {ECO:0000244|PDB:1O60}. FT STRAND 11 13 {ECO:0000244|PDB:1O60}. FT STRAND 20 27 {ECO:0000244|PDB:1O60}. FT HELIX 31 48 {ECO:0000244|PDB:1O60}. FT STRAND 52 58 {ECO:0000244|PDB:1O60}. FT HELIX 74 88 {ECO:0000244|PDB:1O60}. FT STRAND 91 95 {ECO:0000244|PDB:1O60}. FT HELIX 99 101 {ECO:0000244|PDB:1O60}. FT HELIX 102 106 {ECO:0000244|PDB:1O60}. FT STRAND 110 114 {ECO:0000244|PDB:1O60}. FT HELIX 116 118 {ECO:0000244|PDB:1O60}. FT HELIX 122 130 {ECO:0000244|PDB:1O60}. FT STRAND 134 138 {ECO:0000244|PDB:1O60}. FT HELIX 145 147 {ECO:0000244|PDB:1O60}. FT HELIX 148 157 {ECO:0000244|PDB:1O60}. FT STRAND 163 167 {ECO:0000244|PDB:1O60}. FT HELIX 183 190 {ECO:0000244|PDB:1O60}. FT STRAND 196 199 {ECO:0000244|PDB:1O60}. FT HELIX 200 203 {ECO:0000244|PDB:1O60}. FT HELIX 221 231 {ECO:0000244|PDB:1O60}. FT STRAND 234 243 {ECO:0000244|PDB:1O60}. FT HELIX 244 246 {ECO:0000244|PDB:1O60}. FT HELIX 257 259 {ECO:0000244|PDB:1O60}. FT HELIX 260 276 {ECO:0000244|PDB:1O60}. SQ SEQUENCE 284 AA; 30921 MW; 7A3D2076A9B011B0 CRC64; MQNKIVKIGN IDVANDKPFV LFGGMNVLES RDMAMQVCEA YVKVTEKLGV PYVFKASFDK ANRSSIHSYR GPGMEEGLKI FQELKDTFGV KIITDVHEIY QCQPVADVVD IIQLPAFLAR QTDLVEAMAK TGAVINVKKP QFLSPSQMGN IVEKIEECGN DKIILCDRGT NFGYDNLIVD MLGFSVMKKA SKGSPVIFDV THSLQCRDPF GAASSGRRAQ VTELARSGLA VGIAGLFLEA HPNPNQAKCD GPSALPLSAL EGFVSQMKAI DDLVKSFPEL DTSI // ID KDSB_HAEIN Reviewed; 254 AA. AC P44490; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 117. DE RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase; DE EC=2.7.7.38; DE AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase; DE Short=CKS; DE Short=CMP-KDO synthase; GN Name=kdsB; OrderedLocusNames=HI_0058; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for CC incorporation into bacterial lipopolysaccharide in Gram-negative CC bacteria. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CTP + 3-deoxy-D-manno-octulosonate = CC diphosphate + CMP-3-deoxy-D-manno-octulosonate. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno- CC octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from CC 3-deoxy-D-manno-octulosonate and CTP: step 1/1. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the KdsB 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; L42023; AAC21736.1; -; Genomic_DNA. DR PIR; G64045; G64045. DR RefSeq; NP_438231.1; NC_000907.1. DR RefSeq; WP_005693864.1; NC_000907.1. DR PDB; 1VH3; X-ray; 2.70 A; A/B/C=2-254. DR PDB; 1VIC; X-ray; 1.80 A; A/B=2-254. DR PDB; 3DUV; X-ray; 2.30 A; A/B=1-254. DR PDBsum; 1VH3; -. DR PDBsum; 1VIC; -. DR PDBsum; 3DUV; -. DR ProteinModelPortal; P44490; -. DR SMR; P44490; 2-254. DR STRING; 71421.HI0058; -. DR EnsemblBacteria; AAC21736; AAC21736; HI_0058. DR GeneID; 950957; -. DR KEGG; hin:HI0058; -. DR PATRIC; 20188569; VBIHaeInf48452_0058. DR eggNOG; ENOG4105CET; Bacteria. DR eggNOG; COG1212; LUCA. DR KO; K00979; -. DR OMA; NSGTERC; -. DR OrthoDB; EOG6KT2SK; -. DR PhylomeDB; P44490; -. DR BRENDA; 2.7.7.38; 2529. DR UniPathway; UPA00030; -. DR UniPathway; UPA00358; UER00476. DR EvolutionaryTrace; P44490; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IBA:GO_Central. DR GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00057; CMP_KDO_synth; 1. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR004528; KdsB. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR21485:SF4; PTHR21485:SF4; 1. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00466; kdsB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; KW Lipopolysaccharide biosynthesis; Nucleotidyltransferase; KW Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 254 3-deoxy-manno-octulosonate FT cytidylyltransferase. FT /FTId=PRO_0000188506. FT STRAND 4 8 {ECO:0000244|PDB:1VIC}. FT STRAND 14 16 {ECO:0000244|PDB:1VIC}. FT HELIX 19 21 {ECO:0000244|PDB:1VIC}. FT STRAND 25 27 {ECO:0000244|PDB:1VH3}. FT HELIX 29 39 {ECO:0000244|PDB:1VIC}. FT STRAND 43 50 {ECO:0000244|PDB:1VIC}. FT HELIX 52 60 {ECO:0000244|PDB:1VIC}. FT STRAND 64 67 {ECO:0000244|PDB:1VIC}. FT HELIX 75 85 {ECO:0000244|PDB:1VIC}. FT STRAND 93 96 {ECO:0000244|PDB:1VIC}. FT HELIX 106 119 {ECO:0000244|PDB:1VIC}. FT STRAND 122 129 {ECO:0000244|PDB:1VIC}. FT HELIX 133 136 {ECO:0000244|PDB:1VIC}. FT STRAND 143 146 {ECO:0000244|PDB:1VIC}. FT STRAND 150 158 {ECO:0000244|PDB:1VIC}. FT HELIX 164 167 {ECO:0000244|PDB:1VIC}. FT HELIX 173 175 {ECO:0000244|PDB:1VIC}. FT STRAND 183 192 {ECO:0000244|PDB:1VIC}. FT HELIX 193 201 {ECO:0000244|PDB:1VIC}. FT HELIX 206 211 {ECO:0000244|PDB:1VIC}. FT HELIX 216 220 {ECO:0000244|PDB:1VIC}. FT STRAND 225 229 {ECO:0000244|PDB:1VIC}. FT HELIX 241 253 {ECO:0000244|PDB:1VIC}. SQ SEQUENCE 254 AA; 28255 MW; 2FAC2BB15BD961A2 CRC64; MSFTVIIPAR FASSRLPGKP LADIKGKPMI QHVFEKALQS GASRVIIATD NENVADVAKS FGAEVCMTSV NHNSGTERLA EVVEKLAIPD NEIIVNIQGD EPLIPPVIVR QVADNLAKFN VNMASLAVKI HDAEELFNPN AVKVLTDKDG YVLYFSRSVI PYDRDQFMNL QDVQKVQLSD AYLRHIGIYA YRAGFIKQYV QWAPTQLENL EKLEQLRVLY NGERIHVELA KEVPAVGVDT AEDLEKVRAI LAAN // ID KCY1_HAEIN Reviewed; 231 AA. AC P43892; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Cytidylate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CK 1 {ECO:0000255|HAMAP-Rule:MF_00238}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238}; DE AltName: Full=Cytidine monophosphate kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CMP kinase 1 {ECO:0000255|HAMAP-Rule:MF_00238}; GN Name=cmk1 {ECO:0000255|HAMAP-Rule:MF_00238}; Synonyms=cmkA; GN OrderedLocusNames=HI_1219; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22872.1; -; Genomic_DNA. DR PIR; I64110; I64110. DR RefSeq; NP_439375.2; NC_000907.1. DR ProteinModelPortal; P43892; -. DR SMR; P43892; 2-217. DR STRING; 71421.HI1219; -. DR EnsemblBacteria; AAC22872; AAC22872; HI_1219. DR GeneID; 950461; -. DR KEGG; hin:HI1219; -. DR PATRIC; 20191117; VBIHaeInf48452_1271. DR eggNOG; ENOG4105CAT; Bacteria. DR eggNOG; COG0283; LUCA. DR KO; K00945; -. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR Proteomes; UP000000579; 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 1 231 Cytidylate kinase 1. FT /FTId=PRO_0000131921. FT NP_BIND 7 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 231 AA; 25500 MW; 3DD5694F323C98D3 CRC64; MIITVDGPSG AGKGTLCYAL AEKLGYALLD SGAIYRVTAL AALQRKTDLT NETDLAELAR HLDIQFIPQN GEVSILLAGM DVSRLIRTQE VADAASKVAV FQKVRSALLQ LQQDFAKNDG LIADGRDMGT VVFPNAQVKL FLDASAEERA KRRYKQLQNK GINGNFAQIL AEIKERDFRD RNREVAPLKP ADDALLLDST TLSIDEVIDQ ALAYIQRXGI SFRFNCLFKE E // ID KEFX_HAEIN Reviewed; 618 AA. AC P44933; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 112. DE RecName: Full=Glutathione-regulated potassium-efflux system protein; DE AltName: Full=K(+)/H(+) antiporter; GN Name=kefBC; OrderedLocusNames=HI_0911; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transport system that facilitate potassium-efflux, CC possibly by potassium-proton antiport. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 CC (CPA2) transporter (TC 2.A.37) family. {ECO:0000305}. 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; L42023; AAC22568.1; -; Genomic_DNA. DR PIR; A64102; A64102. DR RefSeq; NP_439071.1; NC_000907.1. DR RefSeq; WP_010869086.1; NC_000907.1. DR ProteinModelPortal; P44933; -. DR STRING; 71421.HI0911; -. DR DNASU; 950431; -. DR EnsemblBacteria; AAC22568; AAC22568; HI_0911. DR GeneID; 950431; -. DR KEGG; hin:HI0911; -. DR PATRIC; 20190477; VBIHaeInf48452_0952. DR eggNOG; ENOG4105CKD; Bacteria. DR eggNOG; COG0475; LUCA. DR eggNOG; COG1226; LUCA. DR KO; K11747; -. DR OMA; MSHGGEF; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P44933; -. DR Proteomes; UP000000579; 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:0015299; F:solute:proton antiporter activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006153; Cation/H_exchanger. DR InterPro; IPR004771; K/H_exchanger. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003148; RCK_N. DR Pfam; PF00999; Na_H_Exchanger; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00932; 2a37; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Antiport; Cell inner membrane; Cell membrane; Complete proteome; KW Ion transport; Membrane; Potassium; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 618 Glutathione-regulated potassium-efflux FT system protein. FT /FTId=PRO_0000196614. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. FT TRANSMEM 298 318 Helical. {ECO:0000255}. FT TRANSMEM 336 356 Helical. {ECO:0000255}. FT TRANSMEM 362 382 Helical. {ECO:0000255}. FT DOMAIN 411 533 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. SQ SEQUENCE 618 AA; 68077 MW; 2F9AED8FCCE6B37A CRC64; MSQLANPELM KVVILLASSV TIVPLFKRLG LGSVLGYLVA GCLIGPSVFG IVQEPTAVVH LAELGVVMFL FIIGLEMYPE RLWAMRKAIF GRGLLQVGLC GCLLTFSGIY LLGLTKEVSF IAGMGFTLSS TAIVMQSLEE RGLTSTSKGQ RVISTLIFED IAIVPLLASV AFLAPHSKEA TPHTDWVSIG IALSAVVGLI VTGKWLMNPL FRLISKARIR EMMTAGALLV VLGAALAMEI GGLSMAMGAF VAGVMMSESA FRHQLEADIE PFRGLLLGLF FMGVGMSLDL HLVFNHWILL LGIVFLYILG KASAVYIIAR ITRLDHREAI GRMSLMAHGG EFAFVLFSAA ATAEVISNEE QATFTAAVII SMLFSPIIAQ IARKLIQRTE PKHLDQLDEN DLDTIVDLED NVLVIGFGRF SQIVCQTLLI RGISVSVIDR NIENIRAAAK FGFKVYYGDG IRLDVLRAAG IEKAKCVVLG INDTQRIEHI VSQMKEAYPN LPILTRTYDR KTTVSLIKQD VDFIVRETFE SAITLSRATL MKLGIDKIEA EEIIKEVRTL DQERLNEEVL HGFSNEIVKK YWTPRPFIKP HLDTKALNKE TEEILSEKIE EEISNDHS // ID KDSC_HAEIN Reviewed; 180 AA. AC P45314; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC; DE EC=3.1.3.45; DE AltName: Full=KDO 8-P phosphatase; GN OrderedLocusNames=HI_1679; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION AS A KDO 8-P PHOSPHATASE, AND COFACTOR. RX PubMed=12639950; DOI=10.1074/jbc.M301983200; RA Wu J., Woodard R.W.; RT "Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate RT phosphatase."; RL J. Biol. Chem. 278:18117-18123(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH DIVALENT RP METALS, SUBUNIT, AND METAL-BINDING. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11835514; DOI=10.1002/prot.10057; RA Parsons J.F., Lim K., Tempczyk A., Krajewski W., Eisenstein E., RA Herzberg O.; RT "From structure to function: YrbI from Haemophilus influenzae (HI1679) RT is a phosphatase."; RL Proteins 46:393-404(2002). CC -!- FUNCTION: Involved in the biosynthesis of lipopolysaccharides CC (LPSs), but is not essential. Catalyzes the hydrolysis of 3-deoxy- CC D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno- CC octulosonate (KDO) and inorganic phosphate. CC {ECO:0000269|PubMed:12639950}. CC -!- CATALYTIC ACTIVITY: 3-deoxy-D-manno-octulosonate 8-phosphate + CC H(2)O = 3-deoxy-D-manno-octulosonate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000305|PubMed:12639950}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11835514}. CC -!- MISCELLANEOUS: Cobalt was used in the crystallography experiment CC but magnesium is likely to be the physiological metal. CC -!- SIMILARITY: Belongs to the KdsC 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; L42023; AAC23325.1; -; Genomic_DNA. DR PIR; G64174; G64174. DR RefSeq; NP_439821.1; NC_000907.1. DR RefSeq; WP_005665007.1; NC_000907.1. DR PDB; 1J8D; X-ray; 2.30 A; A/B/C/D=1-180. DR PDB; 1K1E; X-ray; 1.67 A; A/B/C/D/E/F/G/H/I/J/K/L=1-180. DR PDB; 4HGP; X-ray; 1.80 A; A=1-180. DR PDBsum; 1J8D; -. DR PDBsum; 1K1E; -. DR PDBsum; 4HGP; -. DR ProteinModelPortal; P45314; -. DR SMR; P45314; 1-180. DR STRING; 71421.HI1679; -. DR EnsemblBacteria; AAC23325; AAC23325; HI_1679. DR GeneID; 950506; -. DR KEGG; hin:HI1679; -. DR PATRIC; 20192109; VBIHaeInf48452_1758. DR eggNOG; ENOG4108Z4R; Bacteria. DR eggNOG; COG1778; LUCA. DR KO; K03270; -. DR OMA; FDENFHE; -. DR OrthoDB; EOG62C9JR; -. DR PhylomeDB; P45314; -. DR EvolutionaryTrace; P45314; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0019143; F:3-deoxy-manno-octulosonate-8-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IBA:GO_Central. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR010023; KDO_8-P_phosphatase. DR Pfam; PF08282; Hydrolase_3; 1. DR PIRSF; PIRSF006118; KDO8-P_Ptase; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01670; KdsC-phosphatas; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 180 3-deoxy-D-manno-octulosonate 8-phosphate FT phosphatase KdsC. FT /FTId=PRO_0000201703. FT REGION 14 16 Substrate binding. {ECO:0000250}. FT REGION 37 41 Substrate binding. {ECO:0000250}. FT REGION 58 59 Substrate binding. {ECO:0000250}. FT METAL 14 14 Magnesium. {ECO:0000305}. FT METAL 16 16 Magnesium. {ECO:0000305}. FT METAL 107 107 Magnesium. {ECO:0000305}. FT BINDING 16 16 Substrate. {ECO:0000250}. FT BINDING 60 60 Substrate. {ECO:0000250}. FT BINDING 68 68 Substrate. {ECO:0000250}. FT BINDING 84 84 Substrate. {ECO:0000250}. FT BINDING 174 174 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT HELIX 5 7 {ECO:0000244|PDB:1K1E}. FT STRAND 10 14 {ECO:0000244|PDB:1K1E}. FT TURN 16 18 {ECO:0000244|PDB:1K1E}. FT STRAND 22 27 {ECO:0000244|PDB:1K1E}. FT STRAND 30 37 {ECO:0000244|PDB:1K1E}. FT HELIX 38 49 {ECO:0000244|PDB:1K1E}. FT STRAND 53 59 {ECO:0000244|PDB:1K1E}. FT HELIX 63 72 {ECO:0000244|PDB:1K1E}. FT STRAND 76 80 {ECO:0000244|PDB:1K1E}. FT HELIX 84 95 {ECO:0000244|PDB:1K1E}. FT HELIX 99 101 {ECO:0000244|PDB:1K1E}. FT STRAND 102 106 {ECO:0000244|PDB:1K1E}. FT HELIX 109 111 {ECO:0000244|PDB:1K1E}. FT HELIX 112 117 {ECO:0000244|PDB:1K1E}. FT STRAND 118 123 {ECO:0000244|PDB:1K1E}. FT HELIX 129 132 {ECO:0000244|PDB:1K1E}. FT STRAND 135 138 {ECO:0000244|PDB:1K1E}. FT TURN 143 146 {ECO:0000244|PDB:1K1E}. FT HELIX 147 158 {ECO:0000244|PDB:1K1E}. FT HELIX 163 166 {ECO:0000244|PDB:1K1E}. FT HELIX 168 174 {ECO:0000244|PDB:1K1E}. FT HELIX 175 177 {ECO:0000244|PDB:1K1E}. SQ SEQUENCE 180 AA; 19432 MW; 23CD435E4E83A095 CRC64; MQQKLENIKF VITDVDGVLT DGQLHYDANG EAIKSFHVRD GLGIKMLMDA DIQVAVLSGR DSPILRRRIA DLGIKLFFLG KLEKETACFD LMKQAGVTAE QTAYIGDDSV DLPAFAACGT SFAVADAPIY VKNAVDHVLS THGGKGAFRE MSDMILQAQG KSSVFDTAQG FLKSVKSMGQ // ID KAD_HAEIN Reviewed; 214 AA. AC P24323; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 116. 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=HI_0349; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1956282; DOI=10.1111/j.1365-2958.1991.tb01874.x; RA Maskell D.J., Szabo M.J., Butler P.D., Williams A.E., Moxon E.R.; RT "Molecular analysis of a complex locus from Haemophilus influenzae RT involved in phase-variable lipopolysaccharide biosynthesis."; RL Mol. Microbiol. 5:1013-1022(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 (By similarity). It may be linked to the biosynthesis of CC lipopolysaccharide surface molecules, which are important for the CC pathogenesis of H.influenzae. {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. 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. {ECO:0000255|HAMAP- CC 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; X57315; CAA40570.1; -; Genomic_DNA. DR EMBL; L42023; AAC22010.1; -; Genomic_DNA. DR PIR; I64062; I64062. DR RefSeq; NP_438513.1; NC_000907.1. DR RefSeq; WP_005649108.1; NC_000907.1. DR ProteinModelPortal; P24323; -. DR SMR; P24323; 1-214. DR STRING; 71421.HI0349; -. DR EnsemblBacteria; AAC22010; AAC22010; HI_0349. DR GeneID; 949455; -. DR KEGG; hin:HI0349; -. DR PATRIC; 20189245; VBIHaeInf48452_0368. DR eggNOG; ENOG4105CC8; Bacteria. DR eggNOG; COG0563; LUCA. DR KO; K00939; -. DR OMA; RTPEQVI; -. DR OrthoDB; EOG679TH4; -. DR PhylomeDB; P24323; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000579; 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:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23359; PTHR23359; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01351; adk; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 214 Adenylate kinase. FT /FTId=PRO_0000158776. FT NP_BIND 10 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 57 59 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 85 88 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT NP_BIND 132 133 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT REGION 30 59 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00235}. FT REGION 122 159 LID. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 31 31 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 36 36 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 92 92 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 123 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 156 156 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 167 167 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}. FT BINDING 200 200 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00235}. FT CONFLICT 78 78 T -> A (in Ref. 1; CAA40570). FT {ECO:0000305}. SQ SEQUENCE 214 AA; 23508 MW; B83B630EE9E1AACF CRC64; MKIILLGAPG AGKGTQAQFI MNKFGIPQIS TGDMFRAAIK AGTELGKQAK ALMDEGKLVP DELTVALVKD RIAQADCTNG FLLDGFPRTI PQADALKDSG VKIDFVLEFD VPDEVIVERM SGRRVHQASG RSYHIVYNPP KVEGKDDVTG EDLIIRADDK PETVLDRLAV YHKQTSPLID YYQAEAKAGN TQYFRLDGTQ KVEEVSQELD KILG // ID KDGK_HAEIN Reviewed; 314 AA. AC P44482; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=2-dehydro-3-deoxygluconokinase; DE EC=2.7.1.45; DE AltName: Full=2-keto-3-deoxygluconokinase; DE AltName: Full=3-deoxy-2-oxo-D-gluconate kinase; DE AltName: Full=KDG kinase; GN Name=kdgK; OrderedLocusNames=HI_0049; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate CC (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2- CC dehydro-3-deoxy-6-phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D- CC gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate CC from 2-dehydro-3-deoxy-D-gluconate: step 1/2. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB 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; L42023; AAC21727.1; -; Genomic_DNA. DR PIR; C64045; C64045. DR RefSeq; NP_438222.1; NC_000907.1. DR RefSeq; WP_005693872.1; NC_000907.1. DR ProteinModelPortal; P44482; -. DR STRING; 71421.HI0049; -. DR EnsemblBacteria; AAC21727; AAC21727; HI_0049. DR GeneID; 950949; -. DR KEGG; hin:HI0049; -. DR PATRIC; 20188551; VBIHaeInf48452_0049. DR eggNOG; ENOG4107SS6; Bacteria. DR eggNOG; COG0524; LUCA. DR KO; K00874; -. DR OMA; DDEQLIW; -. DR OrthoDB; EOG6NGVTW; -. DR PhylomeDB; P44482; -. DR UniPathway; UPA00856; UER00828. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase 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 Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 314 2-dehydro-3-deoxygluconokinase. FT /FTId=PRO_0000080087. FT NP_BIND 168 170 ATP. {ECO:0000250}. FT NP_BIND 228 234 ATP. {ECO:0000250}. FT NP_BIND 260 263 ATP. {ECO:0000250}. FT REGION 102 104 Substrate binding. {ECO:0000250}. FT ACT_SITE 263 263 Proton acceptor. {ECO:0000250}. FT BINDING 88 88 Substrate. {ECO:0000250}. FT BINDING 170 170 Substrate. {ECO:0000250}. FT BINDING 197 197 ATP. {ECO:0000250}. FT BINDING 263 263 Substrate. {ECO:0000250}. FT BINDING 287 287 ATP. {ECO:0000250}. SQ SEQUENCE 314 AA; 35462 MW; 24CA631C8B0485F9 CRC64; MKKIAFIGEC MIELNGKPFA EMWQSYGGDT LNSATYLSRV SSSKEIQVHY VSALGTDNLS KQMLKYWQAD GIQTNWVLQD EQHQPGLYLI QLDAQGERTF LYWRNQSAAR YMVQHPDFAK VIAELQQVDV IYLSGISLAI LPKNDRTFLI EQLSSLAKKG TEIVFDSNYR PKLWDSLEEA QDCYLQLLPS VNIALVTFDD EQALWKDKTS RDTLERLHKI GIPKVIVKCG KNGAIFSDRY LSQYGQVIPE PILNVVDTTS AGDSFNAGFL NGYLRNKSLE ICCQQGNRIA GIVIQHKGAI IDKVAISHLQ SEFN // ID KGUA_HAEIN Reviewed; 208 AA. AC P44310; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8; DE AltName: Full=GMP kinase; GN Name=gmk; OrderedLocusNames=HI_1743; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23390.1; -; Genomic_DNA. DR PIR; H64139; H64139. DR RefSeq; NP_439887.1; NC_000907.1. DR RefSeq; WP_005693898.1; NC_000907.1. DR ProteinModelPortal; P44310; -. DR SMR; P44310; 2-207. DR STRING; 71421.HI1743; -. DR EnsemblBacteria; AAC23390; AAC23390; HI_1743. DR GeneID; 950885; -. DR KEGG; hin:HI1743; -. DR PATRIC; 20192257; VBIHaeInf48452_1826. DR eggNOG; ENOG4108UHA; Bacteria. DR eggNOG; COG0194; LUCA. DR KO; K00942; -. DR OMA; DYCVIND; -. DR OrthoDB; EOG6CP410; -. DR PhylomeDB; P44310; -. DR Proteomes; UP000000579; 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; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; 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 1 208 Guanylate kinase. FT /FTId=PRO_0000170545. FT DOMAIN 4 185 Guanylate kinase-like. FT NP_BIND 11 18 ATP. {ECO:0000250}. SQ SEQUENCE 208 AA; 23419 MW; 82E3F92253B96E16 CRC64; MSQGNLYILS APSGAGKSSL ISALLASDSS TQKMVSVSHT TRAPRPGEVE GVHYYFVSKE EFESLIEQDL FLEYAKVFGG NYYGTSLPAI EENLAKGIDV FLDIDWQGAQ QIRKKVPSVK SIFILPPSLP ELERRLIGRG QDSEEVIAER MSKAMSEISH YDEYDYVIVN DDFEKTLKDL QSILQSERLT KDYQQKQNAM LIQQLLAK // ID KCY2_HAEIN Reviewed; 222 AA. AC P43893; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Cytidylate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CK 2 {ECO:0000255|HAMAP-Rule:MF_00238}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238}; DE AltName: Full=Cytidine monophosphate kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CMP kinase 2 {ECO:0000255|HAMAP-Rule:MF_00238}; GN Name=cmk2 {ECO:0000255|HAMAP-Rule:MF_00238}; Synonyms=cmkB; GN OrderedLocusNames=HI_1646; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC23293.1; 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; L42023; AAC23293.1; ALT_INIT; Genomic_DNA. DR PIR; H64134; H64134. DR RefSeq; NP_439788.1; NC_000907.1. DR RefSeq; WP_010869265.1; NC_000907.1. DR ProteinModelPortal; P43893; -. DR SMR; P43893; 2-205. DR STRING; 71421.HI1646m; -. DR EnsemblBacteria; AAC23293; AAC23293; HI_1646. DR GeneID; 950485; -. DR KEGG; hin:HI1646m; -. DR PATRIC; 20192037; VBIHaeInf48452_1722. DR eggNOG; ENOG4105CAT; Bacteria. DR eggNOG; COG0283; LUCA. DR KO; K00945; -. DR OMA; AKFYLTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR PhylomeDB; P43893; -. DR Proteomes; UP000000579; 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 1 222 Cytidylate kinase 2. FT /FTId=PRO_0000131922. FT NP_BIND 7 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 222 AA; 24368 MW; 1F9B12FE434D16F0 CRC64; MIITVDGPSG AGKGTLCYAL AEKLGYALLD SGAIYRVTAL AALQRKTDLT NETDLAELAR HLDIQFIPQN GEVNIFLAGM DVSRLIRTQE VADAASKVAV FQKVRSALLQ LQQDFAKNDG LIADGRDMGT VVFPNAQVKL FLDASAEERA KRRYKQLQNK GINGNFAQIL AEIKERDFRD RNREVAPLKP ADDAFYYSLN SSIISCAFFT ISSEPTNSGT RS // ID KHSE_HAEIN Reviewed; 314 AA. AC P44504; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384}; DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00384}; DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384}; DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384}; GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; GN OrderedLocusNames=HI_0088; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L- CC homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00384}. CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00384}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00384}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21766.1; -; Genomic_DNA. DR PIR; I64047; I64047. DR RefSeq; NP_438261.1; NC_000907.1. DR RefSeq; WP_005654296.1; NC_000907.1. DR ProteinModelPortal; P44504; -. DR STRING; 71421.HI0088; -. DR DNASU; 950993; -. DR EnsemblBacteria; AAC21766; AAC21766; HI_0088. DR GeneID; 950993; -. DR KEGG; hin:HI0088; -. DR PATRIC; 20188639; VBIHaeInf48452_0089. DR eggNOG; ENOG4105D5I; Bacteria. DR eggNOG; COG0083; LUCA. DR KO; K00872; -. DR OMA; FVHICKV; -. DR OrthoDB; EOG6DG2WK; -. DR PhylomeDB; P44504; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00384; Homoser_kinase; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR000870; Homoserine_kinase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF000676; Homoser_kin; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00191; thrB; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Reference proteome; KW Threonine biosynthesis; Transferase. FT CHAIN 1 314 Homoserine kinase. FT /FTId=PRO_0000156574. FT NP_BIND 96 106 ATP. {ECO:0000255|HAMAP-Rule:MF_00384}. SQ SEQUENCE 314 AA; 34310 MW; E9C0EABD7866294D CRC64; MLRIYAPASS ANISVGFDTL GAAISPIDGS LLGDVVQIES ISTGFELESA GYFVRKLPKE PQKNIVYQAY VLFSEQLKLR GANVKPLRLT LEKNMPIGSG LGSSACSIVA ALVALNQFHN EPFSKMELLE MMGELEGRIS GSIHYDNVAP CYLGGVQFMV QSLGNICQKL PFFDNWYWVL AYPGIEVSTA EARAILPKSY TRQNVIAHGR HLGGFVHACH THQENLAAIM MKDVIAEPYR ESLLPNFAEV KQATRDLGAL ATGISGSGPT IFSIAPDLQT AIKLSSYLES HYLQNNEGFV HVCKVDNEGT REIK // ID KDTA_HAEIN Reviewed; 427 AA. AC P44806; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase; DE Short=Kdo transferase; DE EC=2.4.99.12 {ECO:0000269|PubMed:10952982, ECO:0000269|PubMed:9195966}; DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase; DE AltName: Full=Monofunctional Kdo transferase; GN Name=waaA; Synonyms=kdtA; OrderedLocusNames=HI_0652; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd, and I69 / Serotype B; RX PubMed=10952982; DOI=10.1074/jbc.M005204200; RA Brabetz W., Mueller-Loennies S., Brade H.; RT "3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and Kdo RT kinase (KdkA) of Haemophilus influenzae are both required to RT complement a waaA knockout mutation of Escherichia coli."; RL J. Biol. Chem. 275:34954-34962(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, PH DEPENDENCE, AND SUBCELLULAR LOCATION. RC STRAIN=722; RX PubMed=9195966; DOI=10.1074/jbc.272.26.16555; RA White K.A., Kaltashov I.A., Cotter R.J., Raetz C.R.; RT "A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase RT and a Kdo kinase in extracts of Haemophilus influenzae."; RL J. Biol. Chem. 272:16555-16563(1997). RN [4] RP DOMAIN. RX PubMed=20394418; DOI=10.1021/bi100343e; RA Chung H.S., Raetz C.R.; RT "Interchangeable domains in the Kdo transferases of Escherichia coli RT and Haemophilus influenzae."; RL Biochemistry 49:4126-4137(2010). CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. CC Catalyzes the transfer of a single 3-deoxy-D-manno-octulosonate CC (Kdo) residue from CMP-Kdo to lipid IV(A), the CC tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Is CC strictly monofunctional, i.e. is capable of adding only a single CC Kdo residue to the acceptor lipid. {ECO:0000269|PubMed:10952982, CC ECO:0000269|PubMed:9195966}. CC -!- CATALYTIC ACTIVITY: Lipid IV(A) + CMP-beta-Kdo = alpha-Kdo-(2->6)- CC lipid IV(A) + CMP. {ECO:0000269|PubMed:10952982, CC ECO:0000269|PubMed:9195966}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:9195966}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:9195966}; Single-pass membrane protein CC {ECO:0000305|PubMed:9195966}; Cytoplasmic side CC {ECO:0000305|PubMed:9195966}. CC -!- DOMAIN: The N-terminal half of KdtA, especially the first 30 amino CC acid residues, is responsible for determining the number of Kdo CC residues that are transferred to lipid IVA. CC {ECO:0000269|PubMed:20394418}. CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 30 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; AJ277814; CAC07178.1; -; Genomic_DNA. DR EMBL; AJ277815; CAC07179.1; -; Genomic_DNA. DR EMBL; L42023; AAC22311.1; -; Genomic_DNA. DR PIR; F64084; F64084. DR RefSeq; NP_438812.1; NC_000907.1. DR RefSeq; WP_005694491.1; NC_000907.1. DR ProteinModelPortal; P44806; -. DR STRING; 71421.HI0652; -. DR CAZy; GT30; Glycosyltransferase Family 30. DR EnsemblBacteria; AAC22311; AAC22311; HI_0652. DR GeneID; 949683; -. DR KEGG; hin:HI0652; -. DR PATRIC; 20189919; VBIHaeInf48452_0681. DR eggNOG; ENOG4105D8A; Bacteria. DR eggNOG; COG1519; LUCA. DR KO; K02527; -. DR OMA; KHGGHNP; -. DR OrthoDB; EOG6H7FNN; -. DR PhylomeDB; P44806; -. DR BRENDA; 2.4.99.12; 2529. DR UniPathway; UPA00958; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IBA:GO_Central. DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR007507; Glycos_transf_N. DR Pfam; PF00534; Glycos_transf_1; 1. DR Pfam; PF04413; Glycos_transf_N; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 427 3-deoxy-D-manno-octulosonic acid FT transferase. FT /FTId=PRO_0000080289. FT TRANSMEM 4 24 Helical; Signal-anchor. {ECO:0000255}. FT REGION 270 271 CMP-Kdo binding. {ECO:0000250}. FT REGION 311 313 CMP-Kdo binding. {ECO:0000250}. FT REGION 337 340 CMP-Kdo binding. {ECO:0000250}. FT ACT_SITE 62 62 Proton acceptor. {ECO:0000250}. FT SITE 132 132 Transition state stabilizer. FT {ECO:0000250}. FT SITE 210 210 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 427 AA; 48743 MW; 2B007E5B47EDD17D CRC64; MWRFFYTSLL LICQPLILCF IGLLSVKSPR YRQRLAERYG FYGNASCPPP QGIFIHAASV GEVIAATPLV RQLQQDYPHL SITFTTFTPT GSERVKATFG DSVFHYYLPL DLPFSIHRFI NFVQPKLCIV METELWPNLI HQLFLRNIPF VIANARLSAR SAHRYGKIKA HLQTMWSQIS LIAAQDNISG KRYATLGYPK EKLNITGNIK YDLNTNDELL RKIDSLRTLW KQDRPIWIAA STHNGEDEII LKSHRALLAK YPNLLLLLVP RHPERFNVVA DLLKKEKFQF IRRSTNELPN ENTQVILGDS MGELMLMYGI SDIAFVGGSL VKHGGHNPLE PLAFKMPVIT GKHTFNFPEI FRMLVEVQGV LEVNSTADAL ERAVEALLNS KESRERLGNA GYEVLMENRG ALQRLLDLLK PYLERNV // ID KITH_HAEIN Reviewed; 193 AA. AC P44309; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. 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=HI_0529; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22186.1; -; Genomic_DNA. DR PIR; G64074; G64074. DR RefSeq; NP_438687.2; NC_000907.1. DR ProteinModelPortal; P44309; -. DR STRING; 71421.HI0529; -. DR EnsemblBacteria; AAC22186; AAC22186; HI_0529. DR GeneID; 949592; -. DR KEGG; hin:HI0529; -. DR PATRIC; 20189611; VBIHaeInf48452_0548. DR eggNOG; ENOG4107104; Bacteria. DR eggNOG; COG1435; LUCA. DR KO; K00857; -. DR OMA; FFEYGAM; -. DR OrthoDB; EOG69D3J2; -. DR Proteomes; UP000000579; 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 Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00124; Thymidine_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001267; Thymidine_kinase. DR InterPro; IPR020633; Thymidine_kinase_CS. DR PANTHER; PTHR11441; PTHR11441; 1. DR Pfam; PF00265; TK; 1. DR PIRSF; PIRSF035805; TK_cell; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1. PE 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 1 193 Thymidine kinase. FT /FTId=PRO_0000174979. FT NP_BIND 9 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT NP_BIND 87 90 ATP. {ECO:0000255|HAMAP-Rule:MF_00124}. FT ACT_SITE 88 88 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00124}. FT METAL 145 145 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 147 147 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 182 182 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. FT METAL 185 185 Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}. SQ SEQUENCE 193 AA; 22177 MW; 0967391437EAF6B3 CRC64; MAKLYFYYST MNAGKSTTLL QSSYNYRERD MNTLVYTAAI DDRFGVGKVT SRIGISQDAF LFRSETNLFD EINEHLKKEK VHCVLVDEAQ FLSKQQVYQL SDVVDKLKIP VLCYGLRTDF QAELFEGSKY LLAWADQLEE LKTICYCGRK ANFVLRLNDQ GEVIKEGAQI QIGGNDSYLS VCRLHYKEKC GQI // ID LDHD_HAEIN Reviewed; 564 AA. AC P45295; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=D-lactate dehydrogenase; DE EC=1.1.1.28; GN Name=dld; OrderedLocusNames=HI_1649; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: First component of the membrane-bound D-lactate oxidase, CC which is believed to play an important role in the energization of CC the active transport of a variety of sugars and amino acids. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00718}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23296.1; -; Genomic_DNA. DR PIR; I64134; I64134. DR RefSeq; NP_439791.1; NC_000907.1. DR RefSeq; WP_005694374.1; NC_000907.1. DR ProteinModelPortal; P45295; -. DR SMR; P45295; 4-562. DR STRING; 71421.HI1649; -. DR EnsemblBacteria; AAC23296; AAC23296; HI_1649. DR GeneID; 950490; -. DR KEGG; hin:HI1649; -. DR PATRIC; 20192043; VBIHaeInf48452_1725. DR eggNOG; ENOG4105CXG; Bacteria. DR eggNOG; COG0277; LUCA. DR KO; K03777; -. DR OMA; RDRYEHH; -. DR OrthoDB; EOG6Z3KJX; -. DR PhylomeDB; P45295; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006089; P:lactate metabolic process; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR Gene3D; 3.30.1370.20; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.30.70.610; -; 2. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016172; D-lactate_DH_C-sub1. DR InterPro; IPR016173; D-lactate_DH_C-sub2. DR InterPro; IPR012256; D_lactate_DH. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR015409; Lactate_DH_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF09330; Lact-deh-memb; 1. DR PIRSF; PIRSF000101; D-lactate_dh; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 564 D-lactate dehydrogenase. FT /FTId=PRO_0000084389. FT DOMAIN 36 207 FAD-binding PCMH-type. FT {ECO:0000255|PROSITE-ProRule:PRU00718}. SQ SEQUENCE 564 AA; 64126 MW; D1211B2D3D5C6418 CRC64; MSVQQLISRL TDIVGSRYII TDPTKTEAYR SGYRFGTGNA LAVVRPATLL EFWNIVKVCV EHDVIVINQA ANTGLTGGST PDGNDYDRDI VVINTMRIDG IQLINNASQV ICLPGSTLNE LENQLKPFGR EPHSVIGSSC IGASVIGGIC NNSGGALVQR GPAYTEMALY AQLNEKGELE LKNHLGIDLG ETPEEILTNL QEKRYQVKDI RQDCGHGHDH YYCNYVRQVD EGSPARFNAD PARHYEASGC AGKLAVFAVR LDTFPLEKET AVFYIGTNQT SVLSDIRRHM LVNFEVLPIS GEYIHRDAFD IAAKYGKDTF WVIKKFGTHW LPKLFSLKSN VDRIGKKFFF LPQHLSDKFM QTVSKFIPEH LPQSLWDYRN KYEHHLIIKM GGKGIQEARE YLESYIADGS KGGYFECNAI ETQAAMLHRF AVASAAIRYR AIHEKEVEEI VALDVALRRN DQDWFEVLPP EIDNRIISKL YYGHFMCHVF HQDYIVKKGY DYEELEYEML KLLDKRGAQY PAEHNVGHLY EAKPTLRKFY KELDPTNSFN PGIGKTTRKK YWAE // ID KPRS_HAEIN Reviewed; 315 AA. AC P44328; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. 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=HI_1609; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23253.1; -; Genomic_DNA. DR PIR; C64132; C64132. DR RefSeq; NP_439751.1; NC_000907.1. DR RefSeq; WP_005647284.1; NC_000907.1. DR ProteinModelPortal; P44328; -. DR SMR; P44328; 4-310. DR STRING; 71421.HI1609; -. DR PRIDE; P44328; -. DR EnsemblBacteria; AAC23253; AAC23253; HI_1609. DR GeneID; 950463; -. DR KEGG; hin:HI1609; -. DR PATRIC; 20191949; VBIHaeInf48452_1682. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR KO; K00948; -. DR OMA; HENVRGQ; -. DR OrthoDB; EOG6Z99XQ; -. DR PhylomeDB; P44328; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.2020; -; 2. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 315 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141142. FT NP_BIND 37 39 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 96 99 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 195 197 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 222 229 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 309 311 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 129 129 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 140 140 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 144 144 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 105 105 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 131 131 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 136 136 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 171 171 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 315 AA; 34170 MW; 90001487D72DE63E CRC64; MPDIKLFAGN ATPELAKRIS ERLYISLGDA TVARFSDGEI QVQINENVRG ADVFIIQSTC APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADLLSIV GIDRVLTCDL HAEQIQGFFD VPVDNVFGSP VLIHDILKKS DLKNPIVVSP DIGGVVRARA VAKLLNDTDM AIIDKRRPRA NVAQVMHIIG DVADRDCILV DDMIDTGGTL CKAAEALKER GAKRVFAYAT HAVFSGAAAK NLASDAIDEV VVTDTIPLSE EMKAIGKVRV LTLSSMLAEA IRRISNEESI SAMFN // ID KPYK_HAEIN Reviewed; 478 AA. AC P43924; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 107. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pykA; OrderedLocusNames=HI_1573; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Allosterically activated by AMP and by several CC sugar phosphates. Belongs to type II PK (By similarity). 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; L42023; AAC23216.1; -; Genomic_DNA. DR PIR; C64130; C64130. DR RefSeq; NP_439719.1; NC_000907.1. DR RefSeq; WP_010869247.1; NC_000907.1. DR ProteinModelPortal; P43924; -. DR STRING; 71421.HI1573; -. DR EnsemblBacteria; AAC23216; AAC23216; HI_1573. DR GeneID; 950433; -. DR KEGG; hin:HI1573; -. DR PATRIC; 20191875; VBIHaeInf48452_1645. DR eggNOG; ENOG4105CA9; Bacteria. DR eggNOG; COG0469; LUCA. DR KO; K00873; -. DR OMA; TPRDMEI; -. DR OrthoDB; EOG6GBMB0; -. DR PhylomeDB; P43924; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000579; 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; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 2. DR SUPFAM; SSF52935; SSF52935; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 478 Pyruvate kinase. FT /FTId=PRO_0000112075. FT METAL 38 38 Potassium. {ECO:0000250}. FT METAL 40 40 Potassium. {ECO:0000250}. FT METAL 70 70 Potassium. {ECO:0000250}. FT METAL 225 225 Magnesium. {ECO:0000250}. FT METAL 252 252 Magnesium. {ECO:0000250}. FT BINDING 36 36 Substrate. {ECO:0000250}. FT BINDING 251 251 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 252 252 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 284 284 Substrate. {ECO:0000250}. FT SITE 223 223 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 478 AA; 51055 MW; FF803EC3E3BD6216 CRC64; MSRRLRRTKI VCTMGPSTDR DNNLEKIIAA GANVVRMNFS HGTPDDHIGR AERVRSIAKK LGKTVAILGD LQGPKIRVST FKDGKIFLNV GDKFILDAEL PKGEGTQESV GLDYKTLPQD VVPGDILLLD DGRVQLKVLS TDGAKVFTEV TVGGPLSNNK GINKLGGGLS ADALTEKDKA DIITAARIGV DFLAVSFPRS SADLNYAREL AQQAGLNAKI VAKVERAETV ANDEAMDDII LASDVIMVAR GDLGVEIGDP ELVGVQKKLI RRSRQLNRAV ITATQMMESM ISNPMPTRAE VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMASVCLG AEKMPSINVS RHRMDKEFET IEESVAMSAM YAANHMKGVA AIVTLSSTGR TPLLMSRISS GLPIFALSRN QETLNLCALY RGVTPIYHGE ESRTEAGAKA APQSLKEKGY LSTGDLVLVT QGGQGATQTN VCRTLIVE // ID LEP4_HAEIN Reviewed; 230 AA. AC P44620; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative type 4 prepilin-like proteins leader peptide-processing enzyme; DE EC=3.4.23.43; GN Name=hofD; Synonyms=hopD; OrderedLocusNames=HI_0296; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cleaves type-4 fimbrial leader sequence and methylates CC the N-terminal (generally Phe) residue. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Typically cleaves a -Gly-|-Phe- bond to CC release an N-terminal, basic peptide of 5-8 residues from type IV CC prepilin, and then N-methylates the new N-terminal amino group, CC the methyl donor being S-adenosyl-L-methionine. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase A24 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; L42023; AAC21960.1; -; Genomic_DNA. DR PIR; C64060; C64060. DR RefSeq; NP_438463.1; NC_000907.1. DR RefSeq; WP_005694370.1; NC_000907.1. DR STRING; 71421.HI0296; -. DR EnsemblBacteria; AAC21960; AAC21960; HI_0296. DR GeneID; 950669; -. DR KEGG; hin:HI0296; -. DR PATRIC; 20189131; VBIHaeInf48452_0312. DR eggNOG; COG1989; LUCA. DR KO; K02506; -. DR OMA; LDWHYQL; -. DR OrthoDB; EOG69D3BR; -. DR PhylomeDB; P44620; -. DR Proteomes; UP000000579; 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:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF01478; Peptidase_A24; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; S-adenosyl-L-methionine; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 230 Putative type 4 prepilin-like proteins FT leader peptide-processing enzyme. FT /FTId=PRO_0000192633. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 181 201 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. SQ SEQUENCE 230 AA; 26789 MW; CD12ABE9B74818D0 CRC64; MIYFTMFLLG GILGIALWFY LSGFITRLQQ NIYAIYVELF PQNRSPFQPH FASIQQKKCG HILRYFFSIG VGFIFLQIAF KDSIFTVWIG LTLIILWTIS YLDWHYQLIS TTPCLWLLTL GLFGADNNFS LLTLSESIKS AASFFIVFYV IYWLAKFYYG KEAFGRGDYW LAMALGSFIH LETLPHFLLL ASVLGICFSL IHRKKKEFLP FAPFMNLSAV IIYFVKYYGY // ID KTHY_HAEIN Reviewed; 210 AA. AC P44719; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 17-FEB-2016, entry version 100. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=HI_0456; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. 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; L42023; AAC22114.1; -; Genomic_DNA. DR RefSeq; NP_438617.2; NC_000907.1. DR ProteinModelPortal; P44719; -. DR SMR; P44719; 2-206. DR STRING; 71421.HI0456; -. DR EnsemblBacteria; AAC22114; AAC22114; HI_0456. DR GeneID; 949547; -. DR KEGG; hin:HI0456; -. DR PATRIC; 20189467; VBIHaeInf48452_0476. DR eggNOG; ENOG4108ZMD; Bacteria. DR eggNOG; COG0125; LUCA. DR KO; K00943; -. DR OMA; GGIDIAE; -. DR OrthoDB; EOG64JFSH; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central. DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central. DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central. DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central. DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central. DR GO; GO:0046939; P:nucleotide phosphorylation; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 210 Thymidylate kinase. FT /FTId=PRO_0000155281. FT NP_BIND 10 17 ATP. {ECO:0000255}. SQ SEQUENCE 210 AA; 23693 MW; C577F00602A0F204 CRC64; MKGKFIVIEG LEGAGKSSAH QSVVRVLHEL GIQDVVFTRE PGGTPLAEKL RHLIKHETEE PVTDKAELLM LYAARIQLVE NVIKPALMQG KWVVGDRHDM SSQAYQGGGR QLDPHFMLTL KETVLGNFEP DLTIYLDIDP SVGLARARGR GELDRIEQMD LDFFHRTRAR YLELVKDNPK AVVINAEQSI ELVQADIESA VKNWWKSNEK // ID LAPB_HAEIN Reviewed; 396 AA. AC P44130; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000255|HAMAP-Rule:MF_00994}; GN Name=lapB {ECO:0000255|HAMAP-Rule:MF_00994}; GN OrderedLocusNames=HI_1223; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Modulates cellular lipopolysaccharide (LPS) levels by CC regulating LpxC, which is involved in lipid A biosynthesis. May CC act by modulating the proteolytic activity of FtsH towards LpxC. CC May also coordinate assembly of proteins involved in LPS synthesis CC at the plasma membrane. {ECO:0000255|HAMAP-Rule:MF_00994}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00994}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00994}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00994}. CC -!- SIMILARITY: Belongs to the LapB family. {ECO:0000255|HAMAP- CC Rule:MF_00994}. CC -!- SIMILARITY: Contains 4 TPR repeats. {ECO:0000255|HAMAP- CC Rule:MF_00994}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22876.1; -; Genomic_DNA. DR PIR; D64022; D64022. DR RefSeq; NP_439379.1; NC_000907.1. DR RefSeq; WP_005694286.1; NC_000907.1. DR ProteinModelPortal; P44130; -. DR STRING; 71421.HI1223; -. DR EnsemblBacteria; AAC22876; AAC22876; HI_1223. DR GeneID; 950168; -. DR KEGG; hin:HI1223; -. DR PATRIC; 20191125; VBIHaeInf48452_1275. DR eggNOG; ENOG4105CFV; Bacteria. DR eggNOG; COG2956; LUCA. DR KO; K19804; -. DR OMA; RYRCAAC; -. DR OrthoDB; EOG68SVV7; -. DR PhylomeDB; P44130; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:InterPro. DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.25.40.10; -; 1. DR HAMAP; MF_00994; LPS_assembly_LapB; 1. DR InterPro; IPR030865; LapB. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Iron; Membrane; KW Metal-binding; Reference proteome; Repeat; TPR repeat; Transmembrane; KW Transmembrane helix. FT CHAIN 1 396 Lipopolysaccharide assembly protein B. FT /FTId=PRO_0000013831. FT TRANSMEM 1 20 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00994}. FT TOPO_DOM 21 396 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00994}. FT REPEAT 35 68 TPR 1. {ECO:0000255|HAMAP-Rule:MF_00994}. FT REPEAT 77 109 TPR 2. {ECO:0000255|HAMAP-Rule:MF_00994}. FT REPEAT 149 182 TPR 3. {ECO:0000255|HAMAP-Rule:MF_00994}. FT REPEAT 221 254 TPR 4. {ECO:0000255|HAMAP-Rule:MF_00994}. FT METAL 364 364 Iron. {ECO:0000255|HAMAP-Rule:MF_00994}. FT METAL 367 367 Iron. {ECO:0000255|HAMAP-Rule:MF_00994}. FT METAL 378 378 Iron. {ECO:0000255|HAMAP-Rule:MF_00994}. FT METAL 381 381 Iron. {ECO:0000255|HAMAP-Rule:MF_00994}. SQ SEQUENCE 396 AA; 45627 MW; E743D4A56B34334F CRC64; MIELLFLLLP IAAAYGWYMG RRSAKKDQDD ISNKLSRDYV TGVNFLLSNQ TDKAVDLFLD MLQKQEIENE IESHSQFEAE LTLGNLFRSR GEVDRALRIH QALDLSPNYT FEQKLLAKQQ LARDFMVVGF FDRAENLYIL LVDEPEFAEN ALQQLLVIYQ KTKEWKKAVN IAEKLAKIKP QENNIELAQC YCEYSQSLEP ESAVEKRSVL QKALSVSPTC VRASLLLANL AMLDGQYQQA VKILENVLEQ NPDYTGEILL PLKHCYEELN QLDNFELFLI RAGQIINNDE VELALAKLIE EKDGKSAAQA KLYQQLTKKP STLIFHRFMQ YQIDDAEDGR GKESLILLHK MVGERIKQTS PYRCTNCGYQ IHKLLWNCPS CRQWESIKPV SNQEHN // ID LEP_HAEIN Reviewed; 349 AA. AC P44454; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Signal peptidase I; DE Short=SPase I; DE EC=3.4.21.89; DE AltName: Full=Leader peptidase I; GN Name=lepB; OrderedLocusNames=HI_0015; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or CC leader sequences from secreted and periplasmic proteins. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S26 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; L42023; AAC21693.1; -; Genomic_DNA. DR PIR; H64042; H64042. DR RefSeq; NP_438188.1; NC_000907.1. DR RefSeq; WP_005693886.1; NC_000907.1. DR ProteinModelPortal; P44454; -. DR STRING; 71421.HI0015; -. DR MEROPS; S26.001; -. DR EnsemblBacteria; AAC21693; AAC21693; HI_0015. DR GeneID; 950912; -. DR KEGG; hin:HI0015; -. DR PATRIC; 20188481; VBIHaeInf48452_0015. DR eggNOG; ENOG4105C3F; Bacteria. DR eggNOG; COG0681; LUCA. DR KO; K03100; -. DR OMA; FKWAPAR; -. DR OrthoDB; EOG6KDKTM; -. DR PhylomeDB; P44454; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central. DR Gene3D; 2.10.109.10; -; 2. DR Gene3D; 2.170.230.10; -; 1. DR InterPro; IPR000223; Pept_S26A_signal_pept_1. DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS. DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS. DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR019533; Peptidase_S26. DR InterPro; IPR019766; Peptidase_S26A_all-beta_subdom. DR PANTHER; PTHR12383; PTHR12383; 3. DR Pfam; PF00717; Peptidase_S24; 1. DR Pfam; PF10502; Peptidase_S26; 1. DR PRINTS; PR00727; LEADERPTASE. DR SUPFAM; SSF51306; SSF51306; 2. DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1. DR PROSITE; PS00501; SPASE_I_1; 1. DR PROSITE; PS00760; SPASE_I_2; 1. DR PROSITE; PS00761; SPASE_I_3; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 349 Signal peptidase I. FT /FTId=PRO_0000109507. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TOPO_DOM 46 80 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TOPO_DOM 102 349 Periplasmic. {ECO:0000255}. FT ACT_SITE 115 115 {ECO:0000250}. FT ACT_SITE 196 196 {ECO:0000250}. SQ SEQUENCE 349 AA; 39734 MW; 8BAF091DCDF92F60 CRC64; MSNLFFVILL AVGFGVWKVL DYFQLPNTFS ILLLILTALS GVLWCYHRFV VLPKRHRQVA RAEQRSGKTL SEEEKAKIEP ISEASEFLSS LFPVLAVVFL VRSFLFEPFQ IPSGSMESTL RVGDFLVVNK YAYGVKDPIF QNTIIAGEKP QRGDVIVFKA PQQALIRTGL GATRAAFAEN LALSSKDNMS GVDYIKRIVG KGGDRVIFDV EQKTLKVVYG KEGKPCEIDC ETKAFEYTQN PTNPAFPNEL ELTEKGDVTH NVLISEYRRY SDLEFFPQEG MQTAEWLVPE GQYFVMGDHR DHSDDSRFWG FVPEKNIVGK ATYIWMSLEK EANEWPTGFR FERFFTAIK // ID LEU3_HAEIN Reviewed; 358 AA. AC P43860; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=3-isopropylmalate dehydrogenase; DE EC=1.1.1.85; DE AltName: Full=3-IPM-DH; DE AltName: Full=Beta-IPM dehydrogenase; DE Short=IMDH; GN Name=leuB; OrderedLocusNames=HI_0987; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- CC oxopentanoate. The product decarboxylates to 4-methyl-2 CC oxopentanoate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22648.1; -; Genomic_DNA. DR PIR; F64106; F64106. DR RefSeq; NP_439150.1; NC_000907.1. DR RefSeq; WP_005693328.1; NC_000907.1. DR ProteinModelPortal; P43860; -. DR SMR; P43860; 2-358. DR STRING; 71421.HI0987; -. DR PRIDE; P43860; -. DR EnsemblBacteria; AAC22648; AAC22648; HI_0987. DR GeneID; 949989; -. DR KEGG; hin:HI0987; -. DR PATRIC; 20190635; VBIHaeInf48452_1030. DR eggNOG; ENOG4105C0C; Bacteria. DR eggNOG; COG0473; LUCA. DR KO; K00052; -. DR OMA; KVGFDMA; -. DR OrthoDB; EOG65N1BN; -. DR PhylomeDB; P43860; -. DR UniPathway; UPA00048; UER00072. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.718.10; -; 1. DR HAMAP; MF_01033; LeuB_type1; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR004429; Isopropylmalate_DH. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR00169; leuB; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; KW Manganese; Metal-binding; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 358 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000083698. FT NP_BIND 77 90 NAD. {ECO:0000250}. FT NP_BIND 284 296 NAD. {ECO:0000250}. FT METAL 226 226 Magnesium or manganese. {ECO:0000250}. FT METAL 250 250 Magnesium or manganese. {ECO:0000250}. FT METAL 254 254 Magnesium or manganese. {ECO:0000250}. FT BINDING 98 98 Substrate. {ECO:0000250}. FT BINDING 108 108 Substrate. {ECO:0000250}. FT BINDING 137 137 Substrate. {ECO:0000250}. FT BINDING 226 226 Substrate. {ECO:0000250}. FT SITE 144 144 Important for catalysis. {ECO:0000250}. FT SITE 194 194 Important for catalysis. {ECO:0000250}. SQ SEQUENCE 358 AA; 38808 MW; 35727EEC16A32CB6 CRC64; MQSYNIAVLA GDGIGPEVMA EAIKVLNRVQ EKFGFKLNFN EFFVGGAAIE HCGYPLPAET LKGCDQADAI LFGSVGGPKW TNLPPDQQPE RGALLPLRKH FKLFCNLRPA TLYKGLEKFC PLRADIAAKG FDMVVVRELT GGIYFGQPKG REGDGVQTKA FDTEVYYKYE IERIARAAFE AAMKRNKKVT SVDKANVLQS SILWRETVTE MAKDYPEVTL EHIYIDNATM QLIKSPESFD VLLCSNIFGD IISDEAAMIT GSMGMLPSAS LNEEGFGLYE PAGGSAPDIA GKGIANPIAQ ILSAAMMLRY SFNLNEAADA IESAVQKVLA SGHRTADLAD DSTPVSTAEM GTLITQAI // ID LICC_HAEIN Reviewed; 233 AA. AC P14183; O05076; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 95. DE RecName: Full=Protein LicC; GN Name=licC; OrderedLocusNames=HI_1539; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=2479481; DOI=10.1016/0092-8674(89)90011-1; RA Weiser J.N., Love J.M., Moxon E.R.; RT "The molecular mechanism of phase variation of H. influenzae RT lipopolysaccharide."; RL Cell 59:657-665(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- MISCELLANEOUS: Lipopolysaccharide (LPS) is a glycolipid that is a CC necessary component and antigenic determinant of the outer CC membrane and has been shown to be an important factor in the host- CC parasite interaction in a number of Gram-negative species. CC -!- MISCELLANEOUS: H.influenzae is able to display an extensive CC repertoire of different surface configurations through variability CC of its LPS oligosaccharide. CC -!- MISCELLANEOUS: LicC is critical for the expression of the 6A2- CC specific epitope. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27280; AAA24973.1; -; Genomic_DNA. DR EMBL; L42023; AAC23189.1; -; Genomic_DNA. DR PIR; C33465; C33465. DR PIR; D64128; D64128. DR RefSeq; NP_439688.1; NC_000907.1. DR RefSeq; WP_005693563.1; NC_000907.1. DR ProteinModelPortal; P14183; -. DR STRING; 71421.HI1539; -. DR EnsemblBacteria; AAC23189; AAC23189; HI_1539. DR GeneID; 950402; -. DR KEGG; hin:HI1539; -. DR PATRIC; 20191803; VBIHaeInf48452_1610. DR eggNOG; COG4750; LUCA. DR OMA; LNIYTEQ; -. DR OrthoDB; EOG63Z7D4; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR017189; CTP-phospocholine_CTT. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF12804; NTP_transf_3; 1. DR PIRSF; PIRSF037382; CCT_LicC; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 233 Protein LicC. FT /FTId=PRO_0000084418. FT CONFLICT 118 118 K -> R (in Ref. 1; AAA24973). FT {ECO:0000305}. FT CONFLICT 142 142 I -> M (in Ref. 1; AAA24973). FT {ECO:0000305}. FT CONFLICT 145 145 D -> E (in Ref. 1; AAA24973). FT {ECO:0000305}. FT CONFLICT 157 159 ISF -> VSY (in Ref. 1; AAA24973). FT {ECO:0000305}. FT CONFLICT 163 163 Q -> R (in Ref. 1; AAA24973). FT {ECO:0000305}. FT CONFLICT 198 233 KLNIYTEQLNSDDIFEMDNLDDYHHILQKLTPNKEK -> N FT (in Ref. 1; AAA24973). {ECO:0000305}. SQ SEQUENCE 233 AA; 27319 MW; 5123FBF35AC29E55 CRC64; MNAIILAAGL GSRFKDITQS THKSLLDIHG TPNLERTLTF LRQANIDNIV IVTGYLHEQF EYLKKKYDCT LIYNEKYREY NSIYSFSLAQ DFFNDCYVID ADVVLNRNIF LTKPSHSKYF TVIRSKTHNE WLPILNSNGQ VIRIDIGSLN QPSLSGISFW TTQDCNIILT LLKEYTSEVR LKNPKLYWDT IPMEYIEKLN IYTEQLNSDD IFEMDNLDDY HHILQKLTPN KEK // ID LCFH_HAEIN Reviewed; 607 AA. AC P44446; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative long-chain-fatty-acid--CoA ligase; DE EC=6.2.1.3; DE AltName: Full=Long-chain acyl-CoA synthetase; DE Short=LACS; GN OrderedLocusNames=HI_0002; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP + CC diphosphate + an acyl-CoA. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; L42023; AAC21681.1; -; Genomic_DNA. DR PIR; H64041; H64041. DR RefSeq; NP_438175.1; NC_000907.1. DR RefSeq; WP_005693896.1; NC_000907.1. DR ProteinModelPortal; P44446; -. DR STRING; 71421.HI0002; -. DR EnsemblBacteria; AAC21681; AAC21681; HI_0002. DR GeneID; 950897; -. DR KEGG; hin:HI0002; -. DR PATRIC; 20188455; VBIHaeInf48452_0002. DR eggNOG; ENOG4108IQE; Bacteria. DR eggNOG; COG1022; LUCA. DR KO; K01897; -. DR OMA; GVQKQFR; -. DR OrthoDB; EOG64FKGZ; -. DR PhylomeDB; P44446; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; KW Lipid metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 607 Putative long-chain-fatty-acid--CoA FT ligase. FT /FTId=PRO_0000193123. SQ SEQUENCE 607 AA; 69694 MW; 111A5AA7A545D674 CRC64; MKIKNRVNMN LDLHFVHRIQ QQAKTRTNMT ALRYKEHGLW RDISWKNFQE QLNQLSRALL AHNIDVQDKI AIFAHNMERW TIVDIATLQI RAITVPIYAT NTAQQAEFIL NHADVKILFV GDQEQYDQTL EIAHHCPKLQ KIVAMKSTIQ LQQDPLSCTW ESFIKTGSNA QQDELTQRLN QKQLSDLFTI IYTSGTTGEP KGVMLDYANL AHQLETHDLS LNVTDQDISL SFLPFSHIFE RAWAAYILHR GAILCYLEDT NQVRSALTEI RPTLMCAVPR FYEKIYAAVL DKVQKAPKLR QIMFHWAISV GQKYFDLRAN NKAIPFLLKK QFALADKLVL SKLRQLLGGR IKMMPCGGAK LEPAIGLFFH AIGINIKLGY GMTETTATVS CWHDFQFNPN SIGTLMPKAE VKIGENNEIL VRGGMVMKGY YKKPEETAQA FTEDGFLKTG DAGEFDEQGN LFITDRIKEL MKTSNGKYIA PQYIESKIGK DKFIEQIAII ADAKKYVSAL IVPCFDSLEE YAKQLNIKYH DRLELLKNSD ILKMFEHRIN AVQKELAHFE QVKKFTLLSQ AFSIKLGEIT PTLKLRRKVI LERYRKQIEA MYHSQEA // ID LEU1_HAEIN Reviewed; 515 AA. AC P43861; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=2-isopropylmalate synthase; DE EC=2.3.3.13; DE AltName: Full=Alpha-IPM synthase; DE AltName: Full=Alpha-isopropylmalate synthase; GN Name=leuA; OrderedLocusNames=HI_0986; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7768823; RA Karudapuram S., Zhao X., Barcak G.J.; RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a RT gene required for chromosomal but not plasmid DNA transformation."; RL J. Bacteriol. 177:3235-3240(1995). CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = CC (2S)-2-isopropylmalate + CoA. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 1/4. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. LeuA type 1 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22647.1; 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; L42023; AAC22647.1; ALT_INIT; Genomic_DNA. DR EMBL; U18657; AAA70115.1; -; Genomic_DNA. DR PIR; E64106; E64106. DR RefSeq; NP_439149.2; NC_000907.1. DR RefSeq; WP_005693326.1; NC_000907.1. DR ProteinModelPortal; P43861; -. DR STRING; 71421.HI0986; -. DR EnsemblBacteria; AAC22647; AAC22647; HI_0986. DR GeneID; 949987; -. DR KEGG; hin:HI0986; -. DR PATRIC; 20190633; VBIHaeInf48452_1029. DR eggNOG; ENOG4105CYQ; Bacteria. DR eggNOG; COG0119; LUCA. DR KO; K01649; -. DR OMA; MAIKTRQ; -. DR OrthoDB; EOG6CGCF3; -. DR PhylomeDB; P43861; -. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01025; LeuA_type1; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005671; LeuA_bact_synth. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR00973; leuA_bact; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 515 2-isopropylmalate synthase. FT /FTId=PRO_0000140355. SQ SEQUENCE 515 AA; 56081 MW; 4521713EEE974792 CRC64; MTDRVIIFDT TLRDGEQALK ASLTVKEKLQ IALALERLGV DVMEVGFPVS SQGDFESVQT IARHIKNARV AALSRAVDKD IDAAYEALKV AEAFRIHTFI ASSALHVEAK LKRSFDDVVG MAVAAVKRAR NYTDDVEFSC EDAGRTGIDN ICRIVEAAIN AGATTVNIPD TVGFCLPNEY GNIIAQVRNC VPNIDKAVIS VHCHNDLGMA TANSLTAVQN GARQIECTIN GIGERAGNTS LEEVVMAMKV RQDFMGVDTH INTQEIHRVS QMVSQLCNMP IQPNKAIVGS NAFAHSSGIH QDGMLKNKNT YEILSPETIG LKKEKLNLTA RSGRAAVKGH MADMGYNEQD YDLDKLYDEF LKLADKKGQV FDYDLEALAF IDMQQGDEDR LVLDKLSAHS TKEYPATAFV QLKLDGEKLS TSSIGGNGPV DAVYNAILNL TGLEIKMSHY NLTAKGEGAE ALGQVDIVVE HKGRKFHGVG LATDIVESSA LALVHAINAI YRAHKVADIK NHKHH // ID LIC2A_HAEIN Reviewed; 302 AA. AC Q03974; Q48209; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Lipooligosaccharide biosynthesis protein lex-1; DE EC=2.-.-.-; GN Name=lex1; Synonyms=lic2A; OrderedLocusNames=HI_0550; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DL42 / Serotype B; RX PubMed=1956289; DOI=10.1111/j.1365-2958.1991.tb01884.x; RA Cope L.D., Yogev R., Mertsola J., Latimer J.L., Hanson M.S., RA McCracken G.H. Jr., Hansen E.J.; RT "Molecular cloning of a gene involved in lipooligosaccharide RT biosynthesis and virulence expression by Haemophilus influenzae type RT B."; RL Mol. Microbiol. 5:1113-1124(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=7523834; DOI=10.1111/j.1365-2958.1993.tb01257.x; RA High N.J., Deadman M.E., Moxon E.R.; RT "The role of a repetitive DNA motif (5'-CAAT-3') in the variable RT expression of the Haemophilus influenzae lipopolysaccharide epitope RT alpha Gal(1-4)beta Gal."; RL Mol. Microbiol. 9:1275-1282(1993). RN [4] RP MUTAGENESIS OF THE SINQ REPEATS, AND EXTENT OF VARIATION IN REPEAT RP NUMBERS. RC STRAIN=26 strains, and RM 7004 / Serotype B; RX PubMed=8861214; DOI=10.1111/j.1365-2958.1996.tb02498.x; RA High N.J., Jennings M.P., Moxon E.R.; RT "Tandem repeats of the tetramer 5'-CAAT-3' present in lic2A are RT required for phase variation but not lipopolysaccharide biosynthesis RT in Haemophilus influenzae."; RL Mol. Microbiol. 20:165-174(1996). CC -!- FUNCTION: Involved in extracellular lipooligosaccharide (LOS) CC biosynthesis and virulence expression. Involved in the synthesis CC of the oligosaccharide moiety of the LOS molecule by adding CC GalNAc. CC -!- DOMAIN: Between 2 and 7 copies of the SINQ repeats are to be found CC in different strains; these are thought to serve to generate CC phase-variable expression of this gene. The (SINQ)n peptide may CC form a random coiled structure that permits appropriate CC interactions between the N- and C-terminal domains of the protein. CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family. CC {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator. 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; L42023; AAC22208.1; -; Genomic_DNA. DR EMBL; X56903; CAA40221.1; -; Genomic_DNA. DR EMBL; L19441; AAA65534.1; -; Genomic_DNA. DR PIR; A64077; A64077. DR RefSeq; NP_438708.1; NC_000907.1. DR RefSeq; WP_005694147.1; NC_000907.1. DR STRING; 71421.HI0550; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR EnsemblBacteria; AAC22208; AAC22208; HI_0550. DR GeneID; 949673; -. DR KEGG; hin:HI0550; -. DR PATRIC; 20189655; VBIHaeInf48452_0570. DR eggNOG; ENOG4105W1T; Bacteria. DR eggNOG; COG3306; LUCA. DR KO; K07270; -. DR OMA; KEIVRFM; -. DR OrthoDB; EOG6R5C54; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Reference proteome; Repeat; KW Transferase; Virulence. FT CHAIN 1 302 Lipooligosaccharide biosynthesis protein FT lex-1. FT /FTId=PRO_0000216233. FT REPEAT 42 45 1. {ECO:0000269|PubMed:8861214}. FT REPEAT 46 49 2. {ECO:0000269|PubMed:8861214}. FT REPEAT 50 53 3. {ECO:0000269|PubMed:8861214}. FT REPEAT 54 57 4. {ECO:0000269|PubMed:8861214}. FT REPEAT 58 61 5. {ECO:0000269|PubMed:8861214}. FT REPEAT 62 65 6. {ECO:0000269|PubMed:8861214}. FT REPEAT 66 69 7. {ECO:0000269|PubMed:8861214}. FT REGION 42 69 7 X 4 AA tandem repeats of S-I-N-Q. FT VARIANT 29 29 K -> N (in strain: DL42 and RM 7004). FT VARIANT 63 70 Missing (in strain: RM 7004). FT VARIANT 67 70 Missing (in strain: DL42). FT VARIANT 106 106 F -> L (in strain: DL42 and RM 7004). FT VARIANT 151 151 Q -> R (in strain: DL42 and RM 7004). FT VARIANT 256 256 S -> P (in strain: RM 7004). FT VARIANT 274 274 N -> D (in strain: RM 7004). FT MUTAGEN 41 71 Missing: Reduces the rate of phase FT variation of the LOS, but does not FT abolish it. {ECO:0000269|PubMed:8861214}. SQ SEQUENCE 302 AA; 35490 MW; BFC204F9B3372D2C CRC64; MSAIENIVIS MENATERRKH ITKQFESKKL SFSFFNAYTY QSINQSINQS INQSINQSIN QSINQSINQS NSILHNIEES RILTKGEKGC LISHFLLWNK CVNENFEYLK IFEDDVILGE NAEVFLNQNE WLKTRFDFND IFIIRLETFL QPVKLEKQTK IPPFNSRNFD ILKSTHWGTA GYIISQGAAK YVIEYLKNIP SDEIVAVDEL IFNKLVDVDN YIVYQLNPAI CIQELQANQS KSVLTSGLEK ERQKRSKIRK KKTLKQRLTR IKENIIRALN RKKWKEQQRI KEMQGKEIVR FM // ID LEXA_HAEIN Reviewed; 207 AA. AC P44858; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 116. DE RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015}; DE EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015}; GN Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015}; GN OrderedLocusNames=HI_0749; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Represses a number of genes involved in the response to CC DNA damage (SOS response), including recA and lexA. In the CC presence of single-stranded DNA, RecA interacts with LexA causing CC an autocatalytic cleavage which disrupts the DNA-binding part of CC LexA, leading to derepression of the SOS regulon and eventually CC DNA repair. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor CC LexA. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SIMILARITY: Belongs to the peptidase S24 family. CC {ECO:0000255|HAMAP-Rule:MF_00015}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22408.1; 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; L42023; AAC22408.1; ALT_INIT; Genomic_DNA. DR PIR; E64090; E64090. DR RefSeq; NP_438908.2; NC_000907.1. DR RefSeq; WP_010869048.1; NC_000907.1. DR ProteinModelPortal; P44858; -. DR SMR; P44858; 2-203. DR STRING; 71421.HI0749; -. DR MEROPS; S24.001; -. DR EnsemblBacteria; AAC22408; AAC22408; HI_0749. DR GeneID; 949794; -. DR KEGG; hin:HI0749; -. DR PATRIC; 20190141; VBIHaeInf48452_0786. DR eggNOG; ENOG4105DS7; Bacteria. DR eggNOG; COG1974; LUCA. DR KO; K01356; -. DR OMA; GVNDHLK; -. DR OrthoDB; EOG6JHRHJ; -. DR PhylomeDB; P44858; -. DR Proteomes; UP000000579; Chromosome. DR CollecTF; EXPREG_00000ab0; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR HAMAP; MF_00015; LexA; 1. DR InterPro; IPR006200; LexA. DR InterPro; IPR006199; LexA_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01726; LexA_DNA_bind; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR TIGRFAMs; TIGR00498; lexA; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Hydrolase; Reference proteome; KW Repressor; SOS response; Transcription; Transcription regulation. FT CHAIN 1 207 LexA repressor. FT /FTId=PRO_0000170042. FT DNA_BIND 28 48 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00015}. FT ACT_SITE 123 123 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT ACT_SITE 160 160 For autocatalytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00015}. FT SITE 88 89 Cleavage; by autolysis. FT {ECO:0000255|HAMAP-Rule:MF_00015}. SQ SEQUENCE 207 AA; 23105 MW; 8E4F611D8AD5D4D7 CRC64; MRPLTARQQE VLDLLKRHLE TTGMPPTRAE ISRELGFKSA NAAEEHLKAL SRKGAIEIIP GASRGIRILD NSSNDEFDGL PLVGRVRAGE PILAEQHIEA TYRVDADMFK PQADFLLKVY GLSMKNVGIL DGDLLAVHST KDVRNGQIVV ARIEDEVTVK RLEKKGSIIY LHAENEEFDP IVVNLEEQKN FEIEGIAVGI IRNNAWM // ID LICD_HAEIN Reviewed; 265 AA. AC P14184; P71393; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Lipopolysaccharide cholinephosphotransferase LicD; DE EC=2.7.8.-; GN Name=licD; OrderedLocusNames=HI_1540; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=2479481; DOI=10.1016/0092-8674(89)90011-1; RA Weiser J.N., Love J.M., Moxon E.R.; RT "The molecular mechanism of phase variation of H. influenzae RT lipopolysaccharide."; RL Cell 59:657-665(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP FUNCTION. RX PubMed=10632893; DOI=10.1046/j.1365-2958.2000.01707.x; RA Lysenko E., Richards J.C., Cox A.D., Stewart A., Martin A., Kapoor M., RA Weiser J.N.; RT "The position of phosphorylcholine on the lipopolysaccharide of RT Haemophilus influenzae affects binding and sensitivity to C-reactive RT protein-mediated killing."; RL Mol. Microbiol. 35:234-245(2000). CC -!- FUNCTION: Transfers phosphorylcholine (ChoP) from choline CC diphosphonucleoside to the lipopolysaccharide (LPS). CC {ECO:0000269|PubMed:10632893}. CC -!- MISCELLANEOUS: Lipopolysaccharide (LPS) is a glycolipid that is a CC necessary component and antigenic determinant of the outer CC membrane and has been shown to be an important factor in the host- CC parasite interaction in a number of Gram-negative species. CC -!- MISCELLANEOUS: H.influenzae is able to display an extensive CC repertoire of different surface configurations through variability CC of its LPS oligosaccharide. CC -!- MISCELLANEOUS: LicD is required for the expression of the 12D9- CC specific epitope. CC -!- SIMILARITY: Belongs to the LicD transferase 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; M27280; AAA24974.1; -; Genomic_DNA. DR EMBL; L42023; AAC23190.1; -; Genomic_DNA. DR PIR; D33465; D33465. DR PIR; E64128; E64128. DR RefSeq; NP_439689.1; NC_000907.1. DR RefSeq; WP_005693564.1; NC_000907.1. DR STRING; 71421.HI1540; -. DR EnsemblBacteria; AAC23190; AAC23190; HI_1540. DR GeneID; 950403; -. DR KEGG; hin:HI1540; -. DR PATRIC; 20191805; VBIHaeInf48452_1611. DR eggNOG; ENOG4105KPE; Bacteria. DR eggNOG; COG3475; LUCA. DR KO; K07271; -. DR OMA; IYDGVPN; -. DR OrthoDB; EOG6M0T3V; -. DR PhylomeDB; P14184; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007074; LicD_fam. DR Pfam; PF04991; LicD; 1. PE 3: Inferred from homology; KW Complete proteome; Lipopolysaccharide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 265 Lipopolysaccharide FT cholinephosphotransferase LicD. FT /FTId=PRO_0000204725. FT CONFLICT 27 30 YKIS -> HQIH (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 77 77 H -> Y (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 80 80 M -> I (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 83 83 A -> V (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 90 90 Y -> K (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 106 116 DAKGRKSPMFM -> EIAGKKSAMFI (in Ref. 1; FT AAA24974). {ECO:0000305}. FT CONFLICT 127 127 E -> D (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 132 134 YPL -> CSF (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 138 146 HRRIKLRFS -> YRRTHRRFY (in Ref. 1; FT AAA24974). {ECO:0000305}. FT CONFLICT 154 154 R -> K (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 160 161 VQ -> LW (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 171 172 FL -> LI (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 181 181 A -> E (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 186 186 K -> T (in Ref. 1; AAA24974). FT {ECO:0000305}. FT CONFLICT 202 202 Y -> YDDY (in Ref. 1). {ECO:0000305}. SQ SEQUENCE 265 AA; 31873 MW; D59EE2BA4D6D49A4 CRC64; MKKLTLREQQ LVCLNILDYF HALCERYKIS YSLGGGTLIG AIRHKGFIPW DDDIDVYMHR DEYQRFVDVW FQETHEHYNM ETAEDILAQY TGEMAKIFDC RTQITDAKGR KSPMFMDIFI YDGVPNEPKI IYPLMKKHRR IKLRFSSCKK RWLRAKENTV QKAILNKLSH FLFSKMQKNL AQFQIKYPIK QCDYIGLVLS DYGGWQKSYM PKEYFNHVIY KEFEGRQFQV MNGYHEHLTQ YYGDYMKLPP EEDQKPHHIQ EAYIL // ID LIPA_HAEIN Reviewed; 320 AA. AC P44463; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000255|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000255|HAMAP-Rule:MF_00206}; GN OrderedLocusNames=HI_0026; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur CC atoms into the C-6 and C-8 positions of the octanoyl moiety bound CC to the lipoyl domains of lipoate-dependent enzymes, thereby CC converting the octanoylated domains into lipoylated derivatives. CC {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur- CC (sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] CC ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 CC L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] CC ferredoxin. {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00206}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000255|HAMAP-Rule:MF_00206}; CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl CC synthase family. {ECO:0000255|HAMAP-Rule:MF_00206}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21704.1; -; Genomic_DNA. DR PIR; G64043; G64043. DR RefSeq; NP_438199.1; NC_000907.1. DR RefSeq; WP_005652627.1; NC_000907.1. DR ProteinModelPortal; P44463; -. DR STRING; 71421.HI0026; -. DR EnsemblBacteria; AAC21704; AAC21704; HI_0026. DR GeneID; 950923; -. DR KEGG; hin:HI0026; -. DR PATRIC; 20188503; VBIHaeInf48452_0026. DR eggNOG; ENOG4105C0G; Bacteria. DR eggNOG; COG0320; LUCA. DR KO; K03644; -. DR OMA; NVCTRSC; -. DR OrthoDB; EOG6038ZS; -. DR PhylomeDB; P44463; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016992; F:lipoate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009107; P:lipoate biosynthetic process; IBA:GO_Central. DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00206; Lipoyl_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR031691; LIAS_N. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR10949; PTHR10949; 1. DR Pfam; PF16881; LIAS_N; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF005963; Lipoyl_synth; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00510; lipA; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 320 Lipoyl synthase. FT /FTId=PRO_0000102320. FT METAL 67 67 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 72 72 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 78 78 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 93 93 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 97 97 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. FT METAL 100 100 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00206}. SQ SEQUENCE 320 AA; 36197 MW; 7D4C4136925450C6 CRC64; MSTPFKMERG VKYRDAAKTS IIPVKNIDPN QDLLKKPEWM KIKLPASSAK IESIKNGMRR HGLHSVCEEA SCPNLHECFN HGTATFMILG AICTRRCPFC DVAHGKPLPP DPEEPQKLAE TIQDMKLKYV VITSVDRDDL PDRGAGHFSE CVKAVRELNP NIKIEILVPD FRGRITQALE KLKDNPPDVF NHNLENVPRL YKEIRPGADY EWSLKLLREF KEIFPNIPTK SGLMVGLGET NEEILQVMQD LRDNGVTMLT LGQYLQPSRH HLPVARYVPP TEFDEFRDKA NEMGFEHAAC GPFVRSSYHA DLQASGGLVK // ID LIPB_HAEIN Reviewed; 212 AA. AC P44464; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 17-FEB-2016, entry version 111. DE RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013}; DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013}; DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013}; GN Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; GN OrderedLocusNames=HI_0027; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate CC although octanoyl-ACP is likely to be the physiological substrate. CC {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. CC {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}. CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of CC octanoic 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:0000255|HAMAP-Rule:MF_00013}. CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP- CC Rule:MF_00013}. 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; L42023; AAC21705.1; -; Genomic_DNA. DR PIR; H64043; H64043. DR RefSeq; NP_438200.1; NC_000907.1. DR RefSeq; WP_010868920.1; NC_000907.1. DR ProteinModelPortal; P44464; -. DR STRING; 71421.HI0027; -. DR EnsemblBacteria; AAC21705; AAC21705; HI_0027. DR GeneID; 950925; -. DR KEGG; hin:HI0027; -. DR PATRIC; 20188505; VBIHaeInf48452_0027. DR eggNOG; ENOG4108BDP; Bacteria. DR eggNOG; COG0321; LUCA. DR KO; K03801; -. DR OMA; AYNIDSA; -. DR OrthoDB; EOG6XM7G6; -. DR PhylomeDB; P44464; -. DR UniPathway; UPA00538; UER00592. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC. DR GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro. DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro. DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central. DR HAMAP; MF_00013; LipB; 1. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR000544; Octanoyltransferase. DR InterPro; IPR020605; Octanoyltransferase_CS. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR PIRSF; PIRSF016262; LPLase; 1. DR TIGRFAMs; TIGR00214; lipB; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. DR PROSITE; PS01313; LIPB; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 212 Octanoyltransferase. FT /FTId=PRO_0000062841. FT DOMAIN 31 209 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT REGION 70 77 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT REGION 138 140 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT REGION 151 153 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00013}. FT ACT_SITE 169 169 Acyl-thioester intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00013}. FT SITE 135 135 Lowers pKa of active site Cys. FT {ECO:0000255|HAMAP-Rule:MF_00013}. SQ SEQUENCE 212 AA; 24058 MW; 06A56778EA6A6F0C CRC64; MNNSLIVRQL GLQDYQEIWH KMQDFTDTRN AETQDEIWLV QHYPVFTQGQ AGKPEHLLQR SEIPVVQSVR GGQITYHAPG QQVMYVLIDI KRHKNLNVRQ LVTALEQTVV KTLAEYGIES YPKPDAPGVY VDGKKICSLG LRIRRGCSFH GLALNINMDL NPFHYINPCG YAGLEMCQLA DFVNQDKADC DNVSAKLIKH FANLLGYNIT TL // ID LLDD_HAEIN Reviewed; 381 AA. AC P46454; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01559}; DE EC=1.1.-.- {ECO:0000255|HAMAP-Rule:MF_01559}; GN Name=lldD {ECO:0000255|HAMAP-Rule:MF_01559}; GN OrderedLocusNames=HI_1739.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Is CC coupled to the respiratory chain. {ECO:0000255|HAMAP- CC Rule:MF_01559}. CC -!- CATALYTIC ACTIVITY: (S)-lactate + an oxidized electron acceptor = CC pyruvate + a reduced electron acceptor. {ECO:0000255|HAMAP- CC Rule:MF_01559}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01559}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01559}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01559}. CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01559}. CC -!- SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain. CC {ECO:0000255|HAMAP-Rule:MF_01559}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23385.1; -; Genomic_DNA. DR PIR; T09429; T09429. DR RefSeq; NP_439882.1; NC_000907.1. DR RefSeq; WP_005693904.1; NC_000907.1. DR ProteinModelPortal; P46454; -. DR STRING; 71421.HI1739.1; -. DR EnsemblBacteria; AAC23385; AAC23385; HI_1739.1. DR GeneID; 950543; -. DR KEGG; hin:HI1739.1; -. DR PATRIC; 20192247; VBIHaeInf48452_1821. DR eggNOG; ENOG4105DMF; Bacteria. DR eggNOG; COG1304; LUCA. DR KO; K00101; -. DR OMA; AWIKEQW; -. DR OrthoDB; EOG6HMXBG; -. DR PhylomeDB; P46454; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004457; F:lactate dehydrogenase activity; IEA:InterPro. DR GO; GO:0019516; P:lactate oxidation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01559; L_lact_dehydr; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR InterPro; IPR020920; LldD. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein; KW FMN; Membrane; Oxidoreductase; Reference proteome. FT CHAIN 1 381 L-lactate dehydrogenase. FT /FTId=PRO_0000206339. FT DOMAIN 1 380 FMN hydroxy acid dehydrogenase. FT {ECO:0000255|HAMAP-Rule:MF_01559}. FT NP_BIND 306 330 FMN. {ECO:0000255|HAMAP-Rule:MF_01559}. FT ACT_SITE 275 275 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01559}. FT BINDING 24 24 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01559}. FT BINDING 106 106 FMN. {ECO:0000255|HAMAP-Rule:MF_01559}. FT BINDING 127 127 FMN. {ECO:0000255|HAMAP-Rule:MF_01559}. FT BINDING 129 129 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01559}. FT BINDING 155 155 FMN. {ECO:0000255|HAMAP-Rule:MF_01559}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01559}. FT BINDING 251 251 FMN. {ECO:0000255|HAMAP-Rule:MF_01559}. FT BINDING 278 278 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01559}. SQ SEQUENCE 381 AA; 41965 MW; E1BC62B0A1A6482D CRC64; MIISSASDYR EAARRRVPPF MFHYADGGSY AEQTLARNVS DLENIALRQR VLKDMSELDT SIELFGEKLS MPTILAPVGA CGMYARRGEV QAAQAADNKG VPFTLSTVSI CPIEEVAPAI KRPMWFQLYV LKDRGFMKNA LERAKAAGCS TLVFTVDMPT PGARYRDMHS GMSGPYKEIR RVLQGFTHPF WAYDVGIKGK PHTLGNVSTY MGRQIGLDDY IGWLTENFDP SISWKDLEWI REFWEGPMVI KGILDPEDAK DAVRFGADGI VVSNHGGRQL DGVLSSARAL PPIADAVKGD IKIIADSGIR NGLDIVRMLA LGADATMLGR AFVYALGAEG RQGVENMLDI FKKEMHVAMT LTSNRTIADI KPEALVDLSK L // ID LAPA_HAEIN Reviewed; 97 AA. AC P44129; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=Probable lipopolysaccharide assembly protein A {ECO:0000255|HAMAP-Rule:MF_01948}; GN Name=lapA {ECO:0000255|HAMAP-Rule:MF_01948}; GN OrderedLocusNames=HI_1222; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). CC {ECO:0000255|HAMAP-Rule:MF_01948}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01948}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01948}. CC -!- SIMILARITY: Belongs to the LapA family. {ECO:0000255|HAMAP- CC Rule:MF_01948}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22875.1; -; Genomic_DNA. DR PIR; C64022; C64022. DR RefSeq; NP_439378.1; NC_000907.1. DR RefSeq; WP_005650128.1; NC_000907.1. DR STRING; 71421.HI1222; -. DR EnsemblBacteria; AAC22875; AAC22875; HI_1222. DR GeneID; 950617; -. DR KEGG; hin:HI1222; -. DR PATRIC; 20191123; VBIHaeInf48452_1274. DR eggNOG; ENOG4105Q4A; Bacteria. DR eggNOG; COG3771; LUCA. DR KO; K08992; -. DR OMA; QGDYRIS; -. DR OrthoDB; EOG6VB700; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:InterPro. DR HAMAP; MF_01948; LPS_assembly_LapA; 1. DR InterPro; IPR032906; LapA. DR InterPro; IPR010445; LapA_dom. DR Pfam; PF06305; DUF1049; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Coiled coil; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 97 Probable lipopolysaccharide assembly FT protein A. FT /FTId=PRO_0000168888. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01948}. FT TRANSMEM 46 66 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01948}. FT COILED 67 95 {ECO:0000255|HAMAP-Rule:MF_01948}. SQ SEQUENCE 97 AA; 10915 MW; 506D6A897A597872 CRC64; MIKYILGIVI FIAIVLVAIT IGANNDQIIT FNYIVAESQF QLSSLVAILF GLGLILGWLI TAFFYIKLKL KNMALARQVK RQTLQINELT TTRDKVV // ID LOLD_HAEIN Reviewed; 227 AA. AC P45247; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=Lipoprotein-releasing system ATP-binding protein LolD {ECO:0000255|HAMAP-Rule:MF_01708}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01708}; GN Name=lolD {ECO:0000255|HAMAP-Rule:MF_01708}; GN OrderedLocusNames=HI_1549; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex LolCDE involved in CC the translocation of mature outer membrane-directed lipoproteins, CC from the inner membrane to the periplasmic chaperone, LolA. CC Responsible for the formation of the LolA-lipoprotein complex in CC an ATP-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01708}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (LolD) and two transmembrane proteins (LolC and LolE). CC {ECO:0000255|HAMAP-Rule:MF_01708}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01708}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Lipoprotein translocase (TC 3.A.1.125) family. {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01708}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23199.1; -; Genomic_DNA. DR PIR; A64129; A64129. DR RefSeq; NP_439698.1; NC_000907.1. DR RefSeq; WP_005693575.1; NC_000907.1. DR ProteinModelPortal; P45247; -. DR STRING; 71421.HI1549; -. DR EnsemblBacteria; AAC23199; AAC23199; HI_1549. DR GeneID; 950413; -. DR KEGG; hin:HI1549; -. DR PATRIC; 20191823; VBIHaeInf48452_1620. DR eggNOG; ENOG4105CQU; Bacteria. DR eggNOG; COG1136; LUCA. DR KO; K09810; -. DR OMA; KPRLAHK; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45247; -. DR Proteomes; UP000000579; 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:0042954; F:lipoprotein transporter 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; IPR015854; ABC_transpr_LolD. DR InterPro; IPR011924; LolD_lipo_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02211; LolD_lipo_ex; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51244; LOLD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 227 Lipoprotein-releasing system ATP-binding FT protein LolD. FT /FTId=PRO_0000092439. FT DOMAIN 6 227 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01708}. FT NP_BIND 42 49 ATP. {ECO:0000255|HAMAP-Rule:MF_01708}. SQ SEQUENCE 227 AA; 24974 MW; 7896B77DA3C4AB7E CRC64; MNNYLLKCEN INKFYQEGEN QTQVLKGVSF SMEPAELVAI VGSSGSGKST LLHTLGGLDQ PSSGEVFING QSLQKASANE LAALRNRYLG FVYQFHHLMA DFTALENVMM PMLIGHQNKT EAKDRAEKML SAVGLSHRIT HRPSALSGGE RQRVAIARAL VNNPSLVLAD EPTGNLDHKT TESIFELIQQ LNQEQNIAFL LVTHDMGLAE KLSRRLVMQD GLLKEGA // ID LOLE_HAEIN Reviewed; 416 AA. AC P44250; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Lipoprotein-releasing system transmembrane protein LolC; GN Name=lolE; OrderedLocusNames=HI_1548; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of an ATP-dependent transport system LolCDE CC responsible for the release of lipoproteins targeted to the outer CC membrane from the inner membrane. Such a release is dependent of CC the sorting-signal (absence of an Asp at position 2 of the mature CC lipoprotein) and of LolA (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC LolC/E 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; L42023; AAC23198.1; -; Genomic_DNA. DR PIR; H64035; H64035. DR RefSeq; NP_439697.1; NC_000907.1. DR RefSeq; WP_010869243.1; NC_000907.1. DR STRING; 71421.HI1548; -. DR EnsemblBacteria; AAC23198; AAC23198; HI_1548. DR GeneID; 950412; -. DR KEGG; hin:HI1548; -. DR PATRIC; 20191821; VBIHaeInf48452_1619. DR eggNOG; ENOG4105D60; Bacteria. DR eggNOG; COG4591; LUCA. DR KO; K09808; -. DR OMA; IKRIFIW; -. DR OrthoDB; EOG68SVTW; -. DR PhylomeDB; P44250; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. 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:0042954; F:lipoprotein transporter activity; IEA:InterPro. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR011926; LolC/E_gammaproteobact. DR InterPro; IPR011925; LolCE_TM. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. DR TIGRFAMs; TIGR02212; lolCE; 1. DR TIGRFAMs; TIGR02213; lolE_release; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 416 Lipoprotein-releasing system FT transmembrane protein LolC. FT /FTId=PRO_0000201819. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 276 296 Helical. {ECO:0000255}. FT TRANSMEM 334 354 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. SQ SEQUENCE 416 AA; 46229 MW; F9578BB3BC9DFC5B CRC64; MNTPFFISWR YQRGKQKNPL VALIAKFSAI GIALGVAVLI VGLSAMNGFE RELNQRILAV VPHAEILSAP NATEPTIHHW QNLEKRLQQN PQIKGISPFV SFTALVENGS KLKVVQVKGV EKQAEDKVSS IGNFVQEQGW NKFEKEGGLV LGSGIAKELD VKVGDWITLL ISQQNGDEQF AQPTREPVQV TSILRLDGQL DYSYALLPLA QAQTFLTYQP DQITGVELKL DDPFSARNLD LSMLNDYPQM LYMQNWISKF GYMYRDIQLI RTVMYIAMVL VIGVACFNIV STLIMAVKDK QGDIAIMRTL GANNAFIKRI FIWYGLQAGM KGCLIGIVLG IILALNLTTF IQGIEWVIGK KLLSGDVYFV DFLPSELHWL DVLMVLVAAL ALSLMASLYP ASRAAKLQPA QVLSSH // ID LONH_HAEIN Reviewed; 601 AA. AC P43865; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Putative Lon protease homolog; DE EC=3.4.21.-; DE AltName: Full=ATP-dependent protease La homolog; GN OrderedLocusNames=HI_1324; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- DOMAIN: Lacks the ATP-binding domain. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. 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; L42023; AAC22971.1; -; Genomic_DNA. DR PIR; F64116; F64116. DR RefSeq; NP_439475.1; NC_000907.1. DR RefSeq; WP_005694449.1; NC_000907.1. DR ProteinModelPortal; P43865; -. DR STRING; 71421.HI1324; -. DR MEROPS; S16.A10; -. DR EnsemblBacteria; AAC22971; AAC22971; HI_1324. DR GeneID; 950250; -. DR KEGG; hin:HI1324; -. DR PATRIC; 20191331; VBIHaeInf48452_1376. DR eggNOG; ENOG4105DAN; Bacteria. DR eggNOG; COG1067; LUCA. DR KO; K04770; -. DR OMA; GFFTICQ; -. DR OrthoDB; EOG63RGMZ; -. DR PhylomeDB; P43865; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central. DR GO; GO:0070361; F:mitochondrial light strand promoter anti-sense binding; IBA:GO_Central. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR008268; Peptidase_S16_AS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF05362; Lon_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. DR PROSITE; PS01046; LON_SER; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome; KW Serine protease. FT CHAIN 1 601 Putative Lon protease homolog. FT /FTId=PRO_0000076149. FT DOMAIN 363 560 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT ACT_SITE 455 455 {ECO:0000255|PROSITE-ProRule:PRU10087}. FT ACT_SITE 498 498 {ECO:0000255|PROSITE-ProRule:PRU10087}. SQ SEQUENCE 601 AA; 67570 MW; 14B8DB4941DF49F5 CRC64; MVNFSRKRPA VSSLFSQQQA IEQSLNWQAL QPDLVIQDFP LEPVNFWALQ PNATQGIDLF LRHPTRSLLM MKVGEPVEYA ELLQNFISQN HHKVRSIFGV NYVIEQGDSF SFPHVYTEPA KSLDDNFASQ GEALSALYCD QFQLFGSFRI HPRSQDIQLV PGLVHKANGG VLILSAATLL SQFDLWGRLK QILQTQTFDW YSAHPFKNLP CDIPSYALNL KVIVLGNRTE LATLAELEEN LYSFADYAEI ESYISVAEVE EQKTWAGYVQ QMAQEQNIEL DFLALNKLYQ LLVRESENRF LINASPLKLK EILQDASTFT EKTALSAVDF EGIFQQKLAQ YGFLKEQTYA DILNEQVYVE TQGEIVGQIN GLSVIEYPGT PVCFGEPSRI SCIVQFGDGE VIDVERKNEL AGNIHGKGMM IAQACLSNIL DLPSQLPFSA SLVFEQSYGE IDGDSASLAI FCVLVSALAD LPLPQHIAIT GSIDQFGLVH SVGGVNDKIE GFFTICQRRG LTGKQGVIIP MTTIQQLSLS DDVKSAVKNG EFFIYPVEDI YQACELLFGR DLLDENKDYT EKTESLSRLI QRRIEGRADS ERKSFWHFFR S // ID LPTF_HAEIN Reviewed; 372 AA. AC P45333; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Lipopolysaccharide export system permease protein LptF; GN Name=lptF; OrderedLocusNames=HI_1704; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in CC the translocation of lipopolysaccharide (LPS) from the inner CC membrane to the outer membrane. {ECO:0000250}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. The LptBFG transporter is composed of two ATP- CC binding proteins (LptB) and two transmembrane proteins (LptF and CC LptG) (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LptF/LptG 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; L42023; AAC23350.1; -; Genomic_DNA. DR PIR; A64176; A64176. DR RefSeq; NP_439846.1; NC_000907.1. DR RefSeq; WP_010869275.1; NC_000907.1. DR STRING; 71421.HI1704; -. DR EnsemblBacteria; AAC23350; AAC23350; HI_1704. DR GeneID; 949709; -. DR KEGG; hin:HI1704; -. DR PATRIC; 20192159; VBIHaeInf48452_1783. DR eggNOG; ENOG4108M8S; Bacteria. DR eggNOG; COG0795; LUCA. DR KO; K07091; -. DR OMA; LGLWWVH; -. DR OrthoDB; EOG6TR0CJ; -. DR PhylomeDB; P45333; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030922; LptF. DR InterPro; IPR005495; LptG/LptF_permease. DR Pfam; PF03739; YjgP_YjgQ; 1. DR TIGRFAMs; TIGR04407; LptF_YjgP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 372 Lipopolysaccharide export system permease FT protein LptF. FT /FTId=PRO_0000169775. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. SQ SEQUENCE 372 AA; 41337 MW; 3BEFE2417366FB38 CRC64; MILIRYLIKE VFKSQIAILL ILLLIFFSQQ FVRVLGAAAN GNVPADLVFS LLGLGMPTMA QLMLPLCLFI AILLTFGRLY AESEITVMRA CGVGQRILVK VALIMSLLTA GIAAYNALWL SPWAIQKQVN MVEDAKANPT VGVLSSGQFI STNNNNVVLF IDKIKDNQIR NVYLFQMTPQ KQTKPSVITA EKGELIALPN GDQVLNLKNT KRVEGTSALP DFRITHFDEY HAYLGYQSAE NTNDEVAELT LSQLIDLDSS SAKAELHWRI TLILAVPLMA LIAVPLSRVN PRQGRFAKIL PALLLYLIYF LLQSSFKSAG SAGKLEAELL MPLVNIGFFL LAVVLNSWDS EIMYKFRYLF SKKGSAKDDK YP // ID LPTG_HAEIN Reviewed; 358 AA. AC P45332; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Lipopolysaccharide export system permease protein LptG; GN Name=lptG; OrderedLocusNames=HI_1703; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in CC the translocation of lipopolysaccharide (LPS) from the inner CC membrane to the outer membrane. {ECO:0000250}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. The LptBFG transporter is composed of two ATP- CC binding proteins (LptB) and two transmembrane proteins (LptF and CC LptG) (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LptF/LptG 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; L42023; AAC23349.1; -; Genomic_DNA. DR PIR; I64175; I64175. DR RefSeq; NP_439845.1; NC_000907.1. DR RefSeq; WP_005694193.1; NC_000907.1. DR STRING; 71421.HI1703; -. DR DNASU; 950522; -. DR EnsemblBacteria; AAC23349; AAC23349; HI_1703. DR GeneID; 950522; -. DR KEGG; hin:HI1703; -. DR PATRIC; 20192157; VBIHaeInf48452_1782. DR eggNOG; ENOG4108K5H; Bacteria. DR eggNOG; COG0795; LUCA. DR KO; K11720; -. DR OMA; FAYLHAR; -. DR OrthoDB; EOG6J1D9D; -. DR PhylomeDB; P45332; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030923; LptG. DR InterPro; IPR005495; LptG/LptF_permease. DR Pfam; PF03739; YjgP_YjgQ; 1. DR TIGRFAMs; TIGR04408; LptG_lptG; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 358 Lipopolysaccharide export system permease FT protein LptG. FT /FTId=PRO_0000169778. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 276 296 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. FT TRANSMEM 332 352 Helical. {ECO:0000255}. SQ SEQUENCE 358 AA; 39963 MW; 6299124856964549 CRC64; MINTLDRYIG KSILGAIFAT LMTLVGLSAI IKFVEQFRSV GKGTYDIWQA VIFTGLTIPK DIETFFPMAA LLGALIALGN LASRSELVIM QSAGFSRFKI GIAVMKTALP LVVFTMIIGE WGIPQTEQFA RDTRAKALSG GSILSIKNGV WAKDGHHFVF VRRVTDDTKL DDIYIYTFDQ QHNLIKLKHA NQASYSEDEA KWTLRQVNHS TIMKDEIITT NHLSETWETS LTPDKLGAVS LRPTSLSISG LYHYISFLRE TGQDVSRFEL TFWRKIFQPV SVGVMMLLAL SFIFGSLRSV TAGARIVTGI CVGFLFYVVN EILGQTSVVY GIPAIFGALI PSLLFIVMIW WLLSRKRD // ID LCFA_HAEIN Reviewed; 562 AA. AC P46450; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Long-chain-fatty-acid--CoA ligase; DE EC=6.2.1.3; DE AltName: Full=Long-chain acyl-CoA synthetase; GN Name=fadD; OrderedLocusNames=HI_0390.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Catalyzes the esterification, concomitant with CC transport, of exogenous long-chain fatty acids into metabolically CC active CoA thioesters for subsequent degradation or incorporation CC into phospholipids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP + CC diphosphate + an acyl-CoA. CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane CC protein {ECO:0000305}. Note=Partially membrane-associated. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme 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; L42023; AAC22049.1; -; Genomic_DNA. DR RefSeq; NP_438551.1; NC_000907.1. DR RefSeq; WP_005693780.1; NC_000907.1. DR ProteinModelPortal; P46450; -. DR STRING; 71421.HI0390.1; -. DR PRIDE; P46450; -. DR EnsemblBacteria; AAC22049; AAC22049; HI_0390.1. DR GeneID; 950680; -. DR KEGG; hin:HI0390.1; -. DR PATRIC; 20189329; VBIHaeInf48452_0408. DR eggNOG; ENOG4105CEY; Bacteria. DR eggNOG; COG0318; LUCA. DR KO; K01897; -. DR OMA; PHAVTFR; -. DR OrthoDB; EOG6MH5BV; -. DR PhylomeDB; P46450; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; KW Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome. FT CHAIN 1 562 Long-chain-fatty-acid--CoA ligase. FT /FTId=PRO_0000193131. SQ SEQUENCE 562 AA; 63479 MW; 74BE7C8E9D711F12 CRC64; MEKIWFQNYP KGSEKFLDTS KYESILDMFD KAVREHPDRP AYINMGQVLT FRKLEERSRA FAAYLQNEFK LQRGDRVALM MPNLLQYPIA LFGILRAGLI AVNVNPLYTP RELELQLQDS GAVAIVVVSN FASTLEKVVF NTNVKHVILT RMGDQLSFGK RTLVNFVVKY VKKLVPKYKL PHAVTFREVL SIGKYRQYVR PEISREDLAF LQYTGGTTGV AKGAMLTHGN IITNVFQAKW IAEPFIGDHS RTRSAILALP LYHVFALTVN CLLFLELGVT AILITNPRDI EGFVKELKKY RFEAITGVNT LFNALLNNEN FKEVDFSALK LSVGGGMAIQ QSVATRWHEL TGCNIIEGYG MTECSPLIAA CPINVVKHNG TIGVPVPNTD IKIIKDDGSD AKIGEAGELW VKGDQVMRGY WQRPEATSEV LKDGWMATGD IVIMDESYSL RIVDRKKDII LVSGFNVYPN EIEDVVMLNY KVSEAVAIGV PHAVSGETIK IFVVKKDDSL TRDELRNHCR QYLTGYKVPK EIEFRDELPK TNVGKILRRV LRDEEIAKRP KH // ID LEUC_HAEIN Reviewed; 469 AA. AC P44968; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 114. DE RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000255|HAMAP-Rule:MF_01026}; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01026}; DE AltName: Full=Alpha-IPM isomerase {ECO:0000255|HAMAP-Rule:MF_01026}; DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01026}; DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01026}; GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01026}; GN OrderedLocusNames=HI_0988; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01026}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01026}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01026}. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000255|HAMAP- CC Rule:MF_01026}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01026}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22649.1; -; Genomic_DNA. DR PIR; F64163; F64163. DR RefSeq; NP_439151.1; NC_000907.1. DR RefSeq; WP_005693329.1; NC_000907.1. DR STRING; 71421.HI0988; -. DR DNASU; 950815; -. DR EnsemblBacteria; AAC22649; AAC22649; HI_0988. DR GeneID; 950815; -. DR KEGG; hin:HI0988; -. DR PATRIC; 20190637; VBIHaeInf48452_1031. DR eggNOG; ENOG4105CQI; Bacteria. DR eggNOG; COG0065; LUCA. DR KO; K01703; -. DR OMA; CNMSIEM; -. DR OrthoDB; EOG600DP5; -. DR PhylomeDB; P44968; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 3. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01026; LeuC_type1; 1. DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR PANTHER; PTHR11670; PTHR11670; 2. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR00170; leuC; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 469 3-isopropylmalate dehydratase large FT subunit. FT /FTId=PRO_0000076751. FT METAL 347 347 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. FT METAL 408 408 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. FT METAL 411 411 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01026}. SQ SEQUENCE 469 AA; 50874 MW; AAE53B9CE18848A2 CRC64; MAKTLYEKLF DSHIVYEAEG ETPILYINRH LIHEVTSPQA FDGLRVANRQ VRQVNKTFGT MDHSISTQVR DVNKLEGQAK IQVLELDKNT KATGIKLFDI TTKEQGIVHV MGPEQGLTLP GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ ARAKSMKIEV RGKVASGITA KDIILAIIGK TTMAGGTGHV VEFCGEAIQD LSMEGRMTVC NMAIEMGAKA GLIAPDETTF AYLKDRPHAP KGKDWEDAVA YWKTLKSDDD AQFDTVVTLE AKDIAPQVTW GTNPGQVISV NETIPNPQEM ADPVQRASAE KALHYIGLEA GTNLKDIKVD QVFIGSCTNS RIEDLRAAAA VMKGRKKADN VKRILVVPGS GLVKEQAEKE GLDKIFIAAG AEWRNPGCSM CLGMNDDRLG EWERCASTSN RNFEGRQGRN GRTHLVSPAM AAAAGVFGKF VDIRDVTLN // ID LEUD_HAEIN Reviewed; 200 AA. AC P44438; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=3-isopropylmalate dehydratase small subunit; DE EC=4.2.1.33; DE AltName: Full=Alpha-IPM isomerase; DE Short=IPMI; DE AltName: Full=Isopropylmalate isomerase; GN Name=leuD; OrderedLocusNames=HI_0989; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate CC and 3-isopropylmalate, via the formation of 2-isopropylmaleate. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 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; L42023; AAC22650.1; -; Genomic_DNA. DR PIR; G64106; G64106. DR RefSeq; NP_439152.1; NC_000907.1. DR RefSeq; WP_005693330.1; NC_000907.1. DR ProteinModelPortal; P44438; -. DR STRING; 71421.HI0989; -. DR EnsemblBacteria; AAC22650; AAC22650; HI_0989. DR GeneID; 949559; -. DR KEGG; hin:HI0989; -. DR PATRIC; 20190639; VBIHaeInf48452_1032. DR eggNOG; ENOG4105MQS; Bacteria. DR eggNOG; COG0066; LUCA. DR KO; K01704; -. DR OMA; AFTTHTG; -. DR OrthoDB; EOG661HCP; -. DR PhylomeDB; P44438; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01031; LeuD_type1; 1. DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00171; leuD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 200 3-isopropylmalate dehydratase small FT subunit. FT /FTId=PRO_0000141824. SQ SEQUENCE 200 AA; 22812 MW; 7B2093C1F77D7E59 CRC64; MAGFKQLSGL VVPLDAANVD TDAIIPKQFL QAITRIGFGK HLFHEWRYLD VEGTKPNPEF VLNYPQYQGA TILLARKNLG CGSSREHAPW ALADYGFKVM IAPSFADIFY NNSLNNHMLP IRLSEEEVEE IFQWVWANEG KQIHVDLEAM TVTVGDKVYT FELDEFRRHC LLNGLDNIGL TLQHEDKISA YEKNIPAFLR // ID LICA1_HAEIN Reviewed; 267 AA. AC P71392; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Protein LicA; GN Name=licA; OrderedLocusNames=HI_1537; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Mediates phase variation of the LPS epitopes. Phase CC variation of H.influenza LPS epitopes expressed by LicA is CC determined by a translational switch (By similarity). CC {ECO:0000250}. CC -!- MISCELLANEOUS: Lipopolysaccharide (LPS) is a glycolipid that is a CC necessary component and antigenic determinant of the outer CC membrane and has been shown to be an important factor in the host- CC parasite interaction in a number of Gram-negative species. CC -!- MISCELLANEOUS: H.influenzae is able to display an extensive CC repertoire of different surface configurations through variability CC of its LPS oligosaccharide. CC -!- SIMILARITY: Belongs to the peptidase S49 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; L42023; AAC23187.1; -; Genomic_DNA. DR PIR; B64128; B64128. DR RefSeq; NP_439686.1; NC_000907.1. DR RefSeq; WP_010869239.1; NC_000907.1. DR ProteinModelPortal; P71392; -. DR STRING; 71421.HI1537; -. DR DNASU; 950399; -. DR EnsemblBacteria; AAC23187; AAC23187; HI_1537. DR GeneID; 950399; -. DR KEGG; hin:HI1537; -. DR PATRIC; 20191799; VBIHaeInf48452_1608. DR eggNOG; ENOG4108KN0; Bacteria. DR eggNOG; ENOG410XXJR; LUCA. DR OMA; PEDRIHA; -. DR OrthoDB; EOG6SZ1HM; -. DR PhylomeDB; P71392; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR011009; Kinase-like_dom. DR SUPFAM; SSF56112; SSF56112; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 267 Protein LicA. FT /FTId=PRO_0000171451. SQ SEQUENCE 267 AA; 31395 MW; BA4866B07E87E1DD CRC64; MTNQNVLLNI SGVKFVLRIP NAVNLSLINR EYEAFNNAQA YRAGLNVETP VLDAKSGVKL TRYLENSNTL SQIQLNEQSC LSQVVNNLYR LHNSEFVFRN VFSVFDEFRQ YFSLLENKSA FYQADSRMDK LSAVFWQFEE INKEVILRPC HNDLVPENML LQDDRLFFID WEYSGLNDPL FDIATIIEEA HLSKEAADFL LETYCNQTNK YHKTEFQIAH KRLKIHRFCQ NVLWFLWTKV KEEHGENFGD YALKRLDAAF KLLEELP // ID LPXL_HAEIN Reviewed; 311 AA. AC P45239; Q48045; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 13-APR-2016, entry version 102. DE RecName: Full=Lipid A biosynthesis lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942}; DE EC=2.3.1.241 {ECO:0000255|HAMAP-Rule:MF_01942}; DE AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942}; GN Name=lpxL {ECO:0000255|HAMAP-Rule:MF_01942}; Synonyms=htrB, waaM; GN OrderedLocusNames=HI_1527; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi 2019; RX PubMed=7592970; DOI=10.1074/jbc.270.45.27151; RA Lee N.-G., Sunshine M.G., Engstrom J.J., Gibson B.W., Apicella M.A.; RT "Mutation of the htrB locus of Haemophilus influenzae nontypable RT strain 2019 is associated with modifications of lipid A and RT phosphorylation of the lipo-oligosaccharide."; RL J. Biol. Chem. 270:27151-27159(1995). CC -!- FUNCTION: Catalyzes the transfer of laurate from lauroyl-acyl CC carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)- CC (lauroyl)-lipid IV(A). {ECO:0000255|HAMAP-Rule:MF_01942}. CC -!- CATALYTIC ACTIVITY: A dodecanoyl-[acyl-carrier protein] + alpha- CC Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) = (Kdo)(2)-(dodecanoyl)- CC lipid IV(A) + a holo-[acyl-carrier protein]. {ECO:0000255|HAMAP- CC Rule:MF_01942}. CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; CC KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid CC IV(A): step 3/4. {ECO:0000255|HAMAP-Rule:MF_01942}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01942}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01942}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01942}. CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. CC {ECO:0000255|HAMAP-Rule:MF_01942}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23173.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23173.1; ALT_INIT; Genomic_DNA. DR EMBL; U17642; AAC43515.1; -; Genomic_DNA. DR PIR; D64127; D64127. DR RefSeq; NP_439676.2; NC_000907.1. DR RefSeq; WP_005693550.1; NC_000907.1. DR ProteinModelPortal; P45239; -. DR STRING; 71421.HI1527; -. DR EnsemblBacteria; AAC23173; AAC23173; HI_1527. DR GeneID; 950389; -. DR KEGG; hin:HI1527; -. DR PATRIC; 20191779; VBIHaeInf48452_1598. DR eggNOG; ENOG4105D1S; Bacteria. DR eggNOG; COG1560; LUCA. DR KO; K02517; -. DR OMA; ILCLPYP; -. DR OrthoDB; EOG657J8B; -. DR PhylomeDB; P45239; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00360; UER00485. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0008913; F:lauroyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1. DR InterPro; IPR004960; LipA_acyltrans. DR InterPro; IPR011920; Lipid_A_LpxL_LpxP. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. DR TIGRFAMs; TIGR02207; lipid_A_htrB; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Lipopolysaccharide biosynthesis; Membrane; KW Reference proteome; Stress response; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 311 Lipid A biosynthesis lauroyltransferase. FT /FTId=PRO_0000201776. FT TRANSMEM 19 39 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01942}. FT MOTIF 134 139 HXXXXD motif. {ECO:0000255|HAMAP- FT Rule:MF_01942}. FT CONFLICT 57 57 E -> K (in Ref. 2; AAC43515). FT {ECO:0000305}. FT CONFLICT 81 81 V -> T (in Ref. 2; AAC43515). FT {ECO:0000305}. FT CONFLICT 270 270 T -> V (in Ref. 2; AAC43515). FT {ECO:0000305}. FT CONFLICT 274 274 A -> V (in Ref. 2; AAC43515). FT {ECO:0000305}. FT CONFLICT 287 290 DITI -> GISQ (in Ref. 2; AAC43515). FT {ECO:0000305}. FT CONFLICT 305 305 K -> N (in Ref. 2; AAC43515). FT {ECO:0000305}. SQ SEQUENCE 311 AA; 36152 MW; F4250F7B1B5B6845 CRC64; MKNEKLPQFQ PHFLAPKYWL FWLGVAIWRS ILCLPYPILR HIGHGFGWLF SHLKVGERRA AIARRNLELC FPDMPENERE VILQENLRSV GMAIIETGMA WFWSDSRIKK WSKVEGLHYL KENQKDGIVL VGVHFLTLEL GARIIGLHHP GIGVYRPNDN PLLDWLQTQG RLRSNKDMLD RKDLRGMIKA LRHEETIWYA PDHDYGRKNA VFVPFFAVPD TCTTTGSYYL LKSSQNSKVI PFAPLRNKDG SGYTVSISAP VDFTDLQDET AIAARMNQIV EKEIMKDITI YMWLHRRFKT RPDEKTPSLY D // ID LEPA_HAEIN Reviewed; 598 AA. AC P43729; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 119. DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071}; DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN OrderedLocusNames=HI_0016; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for accurate and efficient protein synthesis CC under certain stress conditions. May act as a fidelity factor of CC the translation reaction, by catalyzing a one-codon backward CC translocation of tRNAs on improperly translocated ribosomes. Back- CC translocation proceeds from a post-translocation (POST) complex to CC a pre-translocation (PRE) complex, thus giving elongation factor G CC a second chance to translocate the tRNAs correctly. Binds to CC ribosomes in a GTP-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00071}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00071}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21694.1; -; Genomic_DNA. DR PIR; I64042; I64042. DR RefSeq; NP_438189.1; NC_000907.1. DR RefSeq; WP_005649880.1; NC_000907.1. DR ProteinModelPortal; P43729; -. DR SMR; P43729; 1-555. DR STRING; 71421.HI0016; -. DR EnsemblBacteria; AAC21694; AAC21694; HI_0016. DR GeneID; 950909; -. DR KEGG; hin:HI0016; -. DR PATRIC; 20188483; VBIHaeInf48452_0016. DR eggNOG; ENOG4105C4S; Bacteria. DR eggNOG; COG0481; LUCA. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR PhylomeDB; P43729; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; 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; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; 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 inner membrane; Cell membrane; Complete proteome; GTP-binding; KW Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 598 Elongation factor 4. FT /FTId=PRO_0000176280. FT DOMAIN 2 184 tr-type G. FT NP_BIND 14 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. FT NP_BIND 131 134 GTP. {ECO:0000255|HAMAP-Rule:MF_00071}. SQ SEQUENCE 598 AA; 66333 MW; FDDB1AC3516BF11E CRC64; MKNIRNFSII AHIDHGKSTL SDRLIQTCGG LSDREMEAQV LDSMDLERER GITIKAQSVT LNYKAKDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAI EMDLEVVPIL NKIDLPAADP ERVAEEIEDI VGIDAMEAVR CSAKTGVGIE DVLEEIVAKI PAPEGDPNAP LQALIIDSWF DNYLGVVSLV RIKNGVLRKG DKIKVMSTGQ TYNVDRLGIF TPKQEDTTVL ECGEVGWVVC AIKDILGAPV GDTLTHQHNS ATEVLPGFKK VKPQVYAGLF PVSSDDYEAF RDALGKLSLN DASLFYEPET STALGFGFRC GFLGLLHMEI IQERLEREYD LDLITTAPTV IYEVEMTNGE VVYVDSPAKL PPLNNIAEIR EPIAECNMLV PQEYLGNVIT LCVEKRGVQT NMVYHGNQIA LTYEIPMGEV VLDFFDRLKS TSRGYASLDY GFKRFQAADM VRVDIMINSE RVDALALIVH KDNSQYRGRE LVEKMRELIP RQQFDIAIQA AIGNHIIARS TVKQLRKNVL AKCYGGDVSR KKKLLQKQKE GKKRMKSLGN VEVPQEAFLA ILHVGKDK // ID LICB_HAEIN Reviewed; 292 AA. AC P14182; O05075; Q57357; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 83. DE RecName: Full=Protein LicB; GN Name=licB; OrderedLocusNames=HI_1538; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=2479481; DOI=10.1016/0092-8674(89)90011-1; RA Weiser J.N., Love J.M., Moxon E.R.; RT "The molecular mechanism of phase variation of H. influenzae RT lipopolysaccharide."; RL Cell 59:657-665(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- MISCELLANEOUS: Lipopolysaccharide (LPS) is a glycolipid that is a CC necessary component and antigenic determinant of the outer CC membrane and has been shown to be an important factor in the host- CC parasite interaction in a number of Gram-negative species. CC -!- MISCELLANEOUS: H.influenzae is able to display an extensive CC repertoire of different surface configurations through variability CC of its LPS oligosaccharide. CC -!- SIMILARITY: Contains 2 EamA domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M27280; AAA24972.1; -; Genomic_DNA. DR EMBL; L42023; AAC23188.1; -; Genomic_DNA. DR PIR; B33465; B33465. DR RefSeq; NP_439687.1; NC_000907.1. DR RefSeq; WP_005672105.1; NC_000907.1. DR STRING; 71421.HI1538; -. DR TCDB; 2.A.7.18.1; the drug/metabolite transporter (dmt) superfamily. DR EnsemblBacteria; AAC23188; AAC23188; HI_1538. DR GeneID; 950400; -. DR KEGG; hin:HI1538; -. DR PATRIC; 20191801; VBIHaeInf48452_1609. DR eggNOG; ENOG4106MCE; Bacteria. DR eggNOG; COG0697; LUCA. DR OMA; ANFNTSG; -. DR OrthoDB; EOG6R87KT; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 4: Predicted; KW Complete proteome; Reference proteome; Repeat. FT CHAIN 1 292 Protein LicB. FT /FTId=PRO_0000084417. FT DOMAIN 70 139 EamA 1. FT DOMAIN 160 286 EamA 2. FT CONFLICT 251 251 S -> L (in Ref. 1; AAA24972). FT {ECO:0000305}. FT CONFLICT 282 292 IVTLYYKGEQK -> TLHFITKGNKNECNHFSSRIRQSF FT (in Ref. 1; AAA24972). {ECO:0000305}. SQ SEQUENCE 292 AA; 32449 MW; 43359398135F7B94 CRC64; MRGYLFGILS AVFWALSGLL YNELPLSEYT ALGKVISLLF LIDFCSLLVI GITLWRKSAV DFQGVFWQPA LSGILGGPIG MSAYLLSIHY LTIYYAAPLS SLFPVFAALM SYWILKEKIT KTAQFGFALA IISSSLLAIE VGQEITFNTI GFIFLIICIL GWSSEIVISS YTMRSLSGLQ VYFLRLCGST IGYLLILFIL SLKNFSLDIL SFNYVQIAGV IIFGALSYCC YYQAIYLLKP IKAMALNITY SVWAIGLGYL LYKQPIKPIT LLLTLLLSAG VIVTLYYKGE QK // ID LOLA_HAEIN Reviewed; 205 AA. AC P45263; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Outer-membrane lipoprotein carrier protein; DE Flags: Precursor; GN Name=lolA; Synonyms=lplA; OrderedLocusNames=HI_1591; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Participates in the translocation of lipoproteins from CC the inner membrane to the outer membrane. Only forms a complex CC with a lipoprotein if the residue after the N-terminal Cys is not CC an aspartate (The Asp acts as a targeting signal to indicate that CC the lipoprotein should stay in the inner membrane) (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LolA 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; L42023; AAC23239.1; -; Genomic_DNA. DR PIR; G64172; G64172. DR RefSeq; NP_439736.1; NC_000907.1. DR RefSeq; WP_005693608.1; NC_000907.1. DR ProteinModelPortal; P45263; -. DR STRING; 71421.HI1591; -. DR EnsemblBacteria; AAC23239; AAC23239; HI_1591. DR GeneID; 950452; -. DR KEGG; hin:HI1591; -. DR PATRIC; 20191915; VBIHaeInf48452_1665. DR eggNOG; ENOG4107Y7W; Bacteria. DR eggNOG; COG2834; LUCA. DR KO; K03634; -. DR OMA; NDKSHWH; -. DR OrthoDB; EOG6677VP; -. DR PhylomeDB; P45263; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0042954; F:lipoprotein transporter activity; IEA:InterPro. DR HAMAP; MF_00240; LolA; 1. DR InterPro; IPR029046; LolA/LolB/LppX. DR InterPro; IPR004564; OM_lipoprot_carrier_LolA-like. DR InterPro; IPR018323; OM_lipoprot_carrier_LolA_Pbac. DR Pfam; PF03548; LolA; 1. DR SUPFAM; SSF89392; SSF89392; 1. DR TIGRFAMs; TIGR00547; lolA; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Periplasm; Protein transport; KW Reference proteome; Signal; Transport. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 205 Outer-membrane lipoprotein carrier FT protein. FT /FTId=PRO_0000018260. SQ SEQUENCE 205 AA; 23104 MW; 4E650B6D1831787E CRC64; MKKTTLKFAA LTLLGLSNLA LADAASELQM RLAKVDVLSA EFVQTVTSGS GKNVQQGSGK LQIKRPNLFR METKTPQETQ IISDGKTLWF YDPFVQQVTA QWVKNAVNNT PFVLLTSNDK SHWHQYTVTQ QSDTFVLKPT LSTSNIKQFD IRVDANGILR NFSTTEKDGQ TNLYVLRNIT NQTLSDSLFQ FKPEKGVEVD DQRKK // ID LPTA_HAEIN Reviewed; 172 AA. AC P45074; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Lipopolysaccharide export system protein LptA {ECO:0000255|HAMAP-Rule:MF_01914}; DE Flags: Precursor; GN Name=lptA {ECO:0000255|HAMAP-Rule:MF_01914}; GN OrderedLocusNames=HI_1149; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). CC Required for the translocation of LPS from the inner membrane to CC the outer membrane. May form a bridge between the inner membrane CC and the outer membrane, via interactions with LptC and LptD, CC thereby facilitating LPS transfer across the periplasm. CC {ECO:0000255|HAMAP-Rule:MF_01914}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. {ECO:0000255|HAMAP-Rule:MF_01914}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01914}. CC -!- SIMILARITY: Belongs to the LptA family. {ECO:0000255|HAMAP- CC Rule:MF_01914}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22804.1; 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; L42023; AAC22804.1; ALT_INIT; Genomic_DNA. DR PIR; A64168; A64168. DR RefSeq; NP_439307.1; NC_000907.1. DR RefSeq; WP_005693464.1; NC_000907.1. DR ProteinModelPortal; P45074; -. DR SMR; P45074; 24-161. DR STRING; 71421.HI1149m; -. DR EnsemblBacteria; AAC22804; AAC22804; HI_1149. DR GeneID; 950113; -. DR KEGG; hin:HI1149m; -. DR PATRIC; 20190973; VBIHaeInf48452_1199. DR eggNOG; ENOG4105WI0; Bacteria. DR eggNOG; COG1934; LUCA. DR KO; K09774; -. DR OMA; NGQKKSN; -. DR OrthoDB; EOG6KQ6FT; -. DR PhylomeDB; P45074; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01914; LPS_assembly_LptA; 1. DR InterPro; IPR014340; LptA. DR InterPro; IPR005653; OstA-like_N. DR Pfam; PF03968; OstA; 1. DR TIGRFAMs; TIGR03002; outer_YhbN_LptA; 1. PE 1: Evidence at protein level; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255|HAMAP-Rule:MF_01914}. FT CHAIN 24 172 Lipopolysaccharide export system protein FT LptA. FT /FTId=PRO_0000013915. SQ SEQUENCE 172 AA; 18700 MW; 2877F89B3D7F351E CRC64; MKLVSNKILF LATMVLASSS AFALKDDVNQ PINIVSDNQS LDMEKSVVTF TDNVVITQGS IVIKANKVVI TRPAEKSGKK ETVEAFGTPV TFHQQLDNGK PVDGKANKVH YDLGNEFLTL TNNAELKQLD SKINGSVITY DVKKQQLKAN GNGKSRVTTV LIPSQLQQAK GK // ID LPTB_HAEIN Reviewed; 241 AA. AC P45073; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 105. DE RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB; DE EC=3.6.3.-; GN Name=lptB; OrderedLocusNames=HI_1148; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in CC the translocation of lipopolysaccharide (LPS) from the inner CC membrane to the outer membrane. Probably responsible for energy CC coupling to the transport system (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. The LptBFG transporter is composed of two ATP- CC binding proteins (LptB) and two transmembrane proteins (LptF and CC LptG) (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Outer CC membrane lipopolysaccharide export (TC 1.B.42) family. 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; L42023; AAC22803.1; -; Genomic_DNA. DR PIR; I64167; I64167. DR RefSeq; NP_439306.1; NC_000907.1. DR RefSeq; WP_005647567.1; NC_000907.1. DR ProteinModelPortal; P45073; -. DR STRING; 71421.HI1148; -. DR EnsemblBacteria; AAC22803; AAC22803; HI_1148. DR GeneID; 950112; -. DR KEGG; hin:HI1148; -. DR PATRIC; 20190971; VBIHaeInf48452_1198. DR eggNOG; ENOG4108IUZ; Bacteria. DR eggNOG; COG1137; LUCA. DR KO; K06861; -. DR OMA; YYLGDNF; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; P45073; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; 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:0055085; P:transmembrane transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR032823; BCA_ABC_TP_C. DR InterPro; IPR030921; LPS_export_LptB. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF12399; BCA_ABC_TP_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04406; LPS_export_lptB; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Cytoplasm; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 241 Lipopolysaccharide export system ATP- FT binding protein LptB. FT /FTId=PRO_0000093182. FT DOMAIN 4 237 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 241 AA; 26814 MW; 7C46F4DE42CBB321 CRC64; MSILTAENLA KSYKSRKVVS DVSLTVNSNE IVGLLGPNGA GKTTTFYMVV GLVRQDQGKI VIDGEDISLL PMHNRAQRGI GYLPQEASIF RRLTVYENLM AVLEIRKDLT PQQRREKADE LIEEFNISHI RDNLGQALSG GERRRVEIAR ALAANPKFIL LDEPFAGVDP ISVSDIKKII TDLRNRGLGV LITDHNVRET LDVCERAYIV GAGKIIATGT PEQVMNDEQV KRVYLGEQFK L // ID LPXB_HAEIN Reviewed; 390 AA. AC P45011; P94807; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 96. DE RecName: Full=Lipid-A-disaccharide synthase; DE EC=2.4.1.182; GN Name=lpxB; OrderedLocusNames=HI_1060; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8917090; DOI=10.1016/0378-1119(96)00139-4; RA Servos S., Khan S., Maskell D.; RT "Cloning and expression of genes encoding lipid A biosynthesis from RT Haemophilus influenzae type b."; RL Gene 175:137-141(1996). CC -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3- CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a CC precursor of lipid A, a phosphorylated glycolipid that anchors the CC lipopolysaccharide to the outer membrane of the cell. CC -!- CATALYTIC ACTIVITY: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosamine + 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosaminyl 1-phosphate = UDP + 2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis((3R)- CC 3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 5/6. CC -!- SIMILARITY: Belongs to the LpxB 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; L42023; AAC22715.1; -; Genomic_DNA. DR EMBL; X87416; CAA60866.1; -; Genomic_DNA. DR RefSeq; NP_439218.1; NC_000907.1. DR RefSeq; WP_010869121.1; NC_000907.1. DR ProteinModelPortal; P45011; -. DR STRING; 71421.HI1060; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR EnsemblBacteria; AAC22715; AAC22715; HI_1060. DR GeneID; 950031; -. DR KEGG; hin:HI1060; -. DR PATRIC; 20190783; VBIHaeInf48452_1104. DR eggNOG; ENOG4105D0V; Bacteria. DR eggNOG; COG0763; LUCA. DR KO; K00748; -. DR OMA; YIAPQEW; -. DR OrthoDB; EOG6FBWZR; -. DR PhylomeDB; P45011; -. DR UniPathway; UPA00359; UER00481. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central. DR HAMAP; MF_00392; LpxB; 1. DR InterPro; IPR003835; Glyco_trans_19. DR Pfam; PF02684; LpxB; 1. DR TIGRFAMs; TIGR00215; lpxB; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1 390 Lipid-A-disaccharide synthase. FT /FTId=PRO_0000190168. FT CONFLICT 342 342 V -> A (in Ref. 3; CAA60866). FT {ECO:0000305}. FT CONFLICT 350 350 A -> S (in Ref. 3; CAA60866). FT {ECO:0000305}. FT CONFLICT 387 388 KE -> TK (in Ref. 3; CAA60866). FT {ECO:0000305}. SQ SEQUENCE 390 AA; 43637 MW; 690BEC98ECFEECCD CRC64; MNKTNPTIAL VAGEVSGDIL GAGLIRQLKA HYPNARFIGI AGPRMLAEGC ETLVDMEELS VMGLAEILKH LPRLLKIRKN VIQTMLQEKP DVYIGIDAPD FNLDVELKLK ANGIKTIHYV SPSVWAWRQN RIHKIAKATH QVLAFLPFEK AFYDKFNVPC RFIGHTMADA IPLKPNRAEA CQTLQIDPAQ RYLAILVGSR GSEVEFLAEP FLKTALLLKE QFPDLQFLVP LVNEKRRIQF ETIKAKITPN LDLHLIDGNA RQAMIAADAT LLASGTAALE AMLCKSPMVV GYRMKPLTYF LAKRLVKTDY ISLPNLLANE MLVPEMIQEE CTPELLAEKL SVYLSDDESA VKNRHVLIQH FTDLHQKIQC NADKQAAQAV IDLLEGKENV // ID LRP_HAEIN Reviewed; 166 AA. AC P45265; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Leucine-responsive regulatory protein; GN Name=lrp; OrderedLocusNames=HI_1596; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Mediates a global response to leucine. Exogenous leucine CC affects the expression of a number of different operons; lrp CC mediates this effect for at least some of these operons (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH asnC-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00319}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23241.1; -; Genomic_DNA. DR PIR; H64131; H64131. DR RefSeq; NP_439738.2; NC_000907.1. DR ProteinModelPortal; P45265; -. DR SMR; P45265; 14-166. DR STRING; 71421.HI1596; -. DR EnsemblBacteria; AAC23241; AAC23241; HI_1596. DR GeneID; 950361; -. DR KEGG; hin:HI1596; -. DR PATRIC; 20191923; VBIHaeInf48452_1669. DR eggNOG; ENOG4105EW9; Bacteria. DR eggNOG; COG1522; LUCA. DR KO; K03719; -. DR OMA; LVFVEIK; -. DR OrthoDB; EOG6F29D2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 166 Leucine-responsive regulatory protein. FT /FTId=PRO_0000111731. FT DOMAIN 16 91 HTH asnC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. FT DNA_BIND 35 54 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. SQ SEQUENCE 166 AA; 18910 MW; 22C0F1B78B110CEB CRC64; MSKEIKKMEK KRNKALDAID IKILNELQRN GKISNIDLSK KVGLSPTPCL ERVKRLEKQG VIMGYRALLN PELLDAPLLV IVEITLVRGK PDVFEEFNAA IQALEEIQEC HLVSGDFDYL LKTRVADMAE YRKLLGTTLL RLPGVNDTRT YVVMEEVKQT NFLVLK // ID LNT_HAEIN Reviewed; 522 AA. AC P44626; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Apolipoprotein N-acyltransferase; DE Short=ALP N-acyltransferase; DE EC=2.3.1.-; DE AltName: Full=Copper homeostasis protein CutE homolog; GN Name=lnt; Synonyms=cutE; OrderedLocusNames=HI_0302; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins. CC {ECO:0000250}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl CC transfer). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- CC acyltransferase subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CN hydrolase 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; L42023; AAC21967.1; -; Genomic_DNA. DR PIR; H64060; H64060. DR RefSeq; NP_438469.2; NC_000907.1. DR ProteinModelPortal; P44626; -. DR STRING; 71421.HI0302; -. DR EnsemblBacteria; AAC21967; AAC21967; HI_0302. DR GeneID; 949425; -. DR KEGG; hin:HI0302; -. DR PATRIC; 20189145; VBIHaeInf48452_0319. DR eggNOG; ENOG4105CE8; Bacteria. DR eggNOG; COG0815; LUCA. DR KO; K03820; -. DR OMA; IPQSMKW; -. DR OrthoDB; EOG6VTJXM; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.60.110.10; -; 1. DR HAMAP; MF_01148; Lnt; 1. DR InterPro; IPR004563; Apolipo_AcylTrfase. DR InterPro; IPR003010; C-N_Hydrolase. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR TIGRFAMs; TIGR00546; lnt; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 522 Apolipoprotein N-acyltransferase. FT /FTId=PRO_0000178068. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 495 515 Helical. {ECO:0000255}. FT DOMAIN 231 517 CN hydrolase. SQ SEQUENCE 522 AA; 58553 MW; 8D327E5C50053C8F CRC64; MKNLNRILLS IKFMNKYFTY LIAIISGLLG VFAFSPFDYW PLAYVSLLGL LYVAKNPKKS TALLSTFLWA MGFFCFGVSW LNVSIHQFGG ASLGVSYFLV GLLAAYLALY PMLFTYLVHH FKVQSAVIFA VIWTLTEFLR GWIFTGFPWL QFGYTQIDSP FYGIAPIFGV TGLTFFTVWA SAVIFNLVSS LFKTKNLKLV LANALLLIIV GGLSAYSSRI HFVKSVEDKA ISVTLAQGNI EQNLKWDPNY FYSTLAIYQK LITENLGKTD LIILPESALP TLENAITPFF EGLERAAKET KTEIMVGTVF QDTKSGKLLN SIMTAGNPDF PYQPNTQNRY NKHHLVPFGE YVPLESILRP LNSVFNLPMS AFQSGEAVQP SLIAKKRAFS PAICYEIIFG EQVRQNLKQD TDYLLTLSND AWFGDSIGPW QHLQMARMRA LELGKPLIRA TNTGISVFVD AQGKVLAQAP QFIETTLTYK IAPAEGKTPY SVLGNMPLYA LSLLFLLLHS MMAFIRRKMN IL // ID LOLB_HAEIN Reviewed; 209 AA. AC P45270; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Outer-membrane lipoprotein LolB; DE Flags: Precursor; GN Name=lolB; Synonyms=hemM; OrderedLocusNames=HI_1607; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a critical role in the incorporation of CC lipoproteins in the outer membrane after they are released by the CC LolA protein. {ECO:0000250}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LolB family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to be involved in delta- CC aminolevulinic acid biosynthesis. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23251.1; -; Genomic_DNA. DR PIR; I64172; I64172. DR RefSeq; NP_439749.1; NC_000907.1. DR RefSeq; WP_005693620.1; NC_000907.1. DR ProteinModelPortal; P45270; -. DR STRING; 71421.HI1607; -. DR EnsemblBacteria; AAC23251; AAC23251; HI_1607. DR GeneID; 950296; -. DR KEGG; hin:HI1607; -. DR PATRIC; 20191945; VBIHaeInf48452_1680. DR eggNOG; ENOG4105C1U; Bacteria. DR eggNOG; COG3017; LUCA. DR KO; K02494; -. DR OMA; FSSRFEW; -. DR OrthoDB; EOG6R5C6M; -. DR PhylomeDB; P45270; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008565; F:protein transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00233; LolB; 1. DR InterPro; IPR029046; LolA/LolB/LppX. DR InterPro; IPR004565; OM_lipoprot_LolB. DR Pfam; PF03550; LolB; 1. DR SUPFAM; SSF89392; SSF89392; 1. DR TIGRFAMs; TIGR00548; lolB; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Chaperone; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Protein transport; Reference proteome; Signal; KW Transport. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 209 Outer-membrane lipoprotein LolB. FT /FTId=PRO_0000018300. FT LIPID 22 22 N-palmitoyl cysteine. {ECO:0000255}. FT LIPID 22 22 S-diacylglycerol cysteine. {ECO:0000255}. SQ SEQUENCE 209 AA; 24193 MW; 0555F02F13E852A1 CRC64; MNNMKTFKFF TALFATAILT ACTLDMERPT NVQYIDKTDA IWQQHLQKIQ KIQSYQAKGQ IGYISPTERF SSRFEWQYQN PKSYTLKLYS LISKSTLWIQ MHQSGMTISD NNGNQQSAAN SKLLLQEIIG MDVPLEHLAY WLKGQPAMNA DYQVGTNHLL GAFTYHVDGS QWTADYLTYH SNNSMPENIL LKNDSTKQTL KIRVDEWIY // ID LOLC_HAEIN Reviewed; 393 AA. AC P44252; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Lipoprotein-releasing system transmembrane protein LolC; GN Name=lolC; OrderedLocusNames=HI_1555; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of an ATP-dependent transport system LolCDE CC responsible for the release of lipoproteins targeted to the outer CC membrane from the inner membrane. Such a release is dependent of CC the sorting-signal (absence of an Asp at position 2 of the mature CC lipoprotein) and of LolA (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC LolC/E 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; L42023; AAC23204.1; -; Genomic_DNA. DR PIR; A64036; A64036. DR RefSeq; NP_439704.1; NC_000907.1. DR RefSeq; WP_005654778.1; NC_000907.1. DR STRING; 71421.HI1555; -. DR EnsemblBacteria; AAC23204; AAC23204; HI_1555. DR GeneID; 949639; -. DR KEGG; hin:HI1555; -. DR PATRIC; 20191835; VBIHaeInf48452_1626. DR eggNOG; ENOG4105D60; Bacteria. DR eggNOG; COG4591; LUCA. DR KO; K09808; -. DR OMA; YVKHVTF; -. DR OrthoDB; EOG68SVTW; -. DR PhylomeDB; P44252; -. DR Proteomes; UP000000579; 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:0042954; F:lipoprotein transporter activity; IEA:InterPro. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR011925; LolCE_TM. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. DR TIGRFAMs; TIGR02212; lolCE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 393 Lipoprotein-releasing system FT transmembrane protein LolC. FT /FTId=PRO_0000201813. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 262 282 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 356 376 Helical. {ECO:0000255}. SQ SEQUENCE 393 AA; 43579 MW; 7ABEC4E335D57F34 CRC64; MNFPISLYIA LRYWRAKSAD RFGRLVTNLA SLGIVLGVMA LIIVLSVMNG LEGYQKQQVL SSIPHAIVSE EQPISTEKTL ENLPHFVQKA VPINTTNVIY QTAKGVSAGQ IIGIQSFSDD PLVESFDQTK FNEILPRGEF KLVIGDQLAQ KLGVNIGDKI RLMITENSQY TPFGRVPMQR LFTVSDIYYG YGEASGYEAF ANITDIGRLM RIQPQQAQGY RLFLNDPFQI TELPQHFPTQ KITDWRVQKG EFFQAVRMEK NMMGLLISLI IVVAISNIVT SLSLMVVDKQ GEIAILQTQG LTKSQVRSVF IYQGLLVGFV GTLLGAILGV LATLNLTDIV SAVNPQGVFL PTELSFVQMI FVIGFSLLLS LLSTLYPAYR AAKVEPAAAL RYE // ID LON_HAEIN Reviewed; 803 AA. AC P43864; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 120. 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}; Synonyms=lon-A; GN OrderedLocusNames=HI_0462; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22121.1; -; Genomic_DNA. DR PIR; A64070; A64070. DR RefSeq; NP_438623.1; NC_000907.1. DR RefSeq; WP_005693703.1; NC_000907.1. DR ProteinModelPortal; P43864; -. DR SMR; P43864; 9-111, 491-584, 594-781. DR STRING; 71421.HI0462; -. DR MEROPS; S16.001; -. DR EnsemblBacteria; AAC22121; AAC22121; HI_0462. DR GeneID; 949549; -. DR KEGG; hin:HI0462; -. DR PATRIC; 20189479; VBIHaeInf48452_0482. DR eggNOG; ENOG4105C6P; Bacteria. DR eggNOG; COG0466; LUCA. DR KO; K01338; -. DR OMA; YLLGMME; -. DR OrthoDB; EOG6XHC23; -. DR PhylomeDB; P43864; -. DR Proteomes; UP000000579; 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 1 803 Lon protease. FT /FTId=PRO_0000076136. FT DOMAIN 9 200 Lon N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU01123}. FT DOMAIN 592 773 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT NP_BIND 356 363 ATP. {ECO:0000255|HAMAP-Rule:MF_01973}. FT ACT_SITE 679 679 {ECO:0000255|HAMAP-Rule:MF_01973}. FT ACT_SITE 722 722 {ECO:0000255|HAMAP-Rule:MF_01973}. SQ SEQUENCE 803 AA; 89347 MW; 9E590852611EEA5B CRC64; MAKNTQRTMP VLPLRDVVVF PYMVMPLFVG RAKSINALEE AMNDDKQILL VSQREADLEE PTPEDLFDVG TIANIIQLLK LPDDTVKVLV EGQNRAKINS LEDGEKCFSA QITPIETTYG DEKELVVAKS AVLSEFENYL TLNKKVPTDI LNALQRIDDV DRLADTMAAH LPVSIRHKQN ALELANVQER LEYLLGMMES EADILQVEKR IRGRVKKQME KSQRNYYLNE QIKAIRKEMD GGENEDTIDE VEQLHQKVEA AGMPADVRDK VENELQKLKM MSAMSSEATV IRSYIEWMIQ VPWHQRSKVK KDIVKAQQVL DTDHYGLDRV KERILEYLAV QARLNKVKGP ILCLVGPPGV GKTSLGQSIA NATGRKYVRM ALGGVRDEAE IRGHRKTYIG ALPGKLIQKM AKVGVKNPLF LLDEIDKMAS DMRGDPASAL LEVLDPEQNT TFNDHYLEVD YDLSDVMFVA TSNSMNIPGP LLDRMEVIRL SGYTEDEKLN IAMRHLLAKQ IERNGLKKGE LTVEESAILD IIRYYTREAG VRGLEREISK ICRKAVKNLL VNPKLKSITV NSDNLHDYLG VKRFEFGKAD TQNRIGEVTG LAWTEVGGDL LTIETASVVG KGKLSFTGSL GDVMKESIQA AMTVVRARAD KLGINAEFHE KRDIHIHVPD GATPKDGPSA GIAMCTALIS CLTGNPVRAD VAMTGEISLR GKVLPIGGLK EKLLAAHRGG IKTVLIPKEN VKDLEEIPEN VKQNLAIHAV ETIDEVLGFA LENPPEGIEF VKVEAKPKAP RRKVTSKSER AVN // ID LPXA_HAEIN Reviewed; 262 AA. AC P43887; P94806; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387}; DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387}; GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387}; GN OrderedLocusNames=HI_1061; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8917090; DOI=10.1016/0378-1119(96)00139-4; RA Servos S., Khan S., Maskell D.; RT "Cloning and expression of genes encoding lipid A biosynthesis from RT Haemophilus influenzae type b."; RL Gene 175:137-141(1996). CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a CC phosphorylated glycolipid that anchors the lipopolysaccharide to CC the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- CATALYTIC ACTIVITY: (R)-3-hydroxytetradecanoyl-[acyl-carrier- CC protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier- CC protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D- CC glucosamine. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP- CC Rule:MF_00387}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC LpxA subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22716.1; -; Genomic_DNA. DR EMBL; X87416; CAA60865.1; -; Genomic_DNA. DR PIR; F64180; F64180. DR RefSeq; NP_439219.1; NC_000907.1. DR RefSeq; WP_005651701.1; NC_000907.1. DR ProteinModelPortal; P43887; -. DR SMR; P43887; 1-262. DR STRING; 71421.HI1061; -. DR EnsemblBacteria; AAC22716; AAC22716; HI_1061. DR GeneID; 950038; -. DR KEGG; hin:HI1061; -. DR PATRIC; 20190785; VBIHaeInf48452_1105. DR eggNOG; ENOG4105DAF; Bacteria. DR eggNOG; COG1043; LUCA. DR KO; K00677; -. DR OMA; VQDRSET; -. DR OrthoDB; EOG6F81P1; -. DR PhylomeDB; P43887; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.1180.10; -; 1. DR HAMAP; MF_00387; LpxA; 1. DR InterPro; IPR029098; Acetyltransf_C. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR010137; Lipid_A_LpxA. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF13720; Acetyltransf_11; 1. DR Pfam; PF00132; Hexapep; 2. DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat; KW Transferase. FT CHAIN 1 262 Acyl-[acyl-carrier-protein]--UDP-N- FT acetylglucosamine O-acyltransferase. FT /FTId=PRO_0000188051. FT CONFLICT 108 108 V -> I (in Ref. 2; CAA60865). FT {ECO:0000305}. SQ SEQUENCE 262 AA; 28741 MW; B525D0D1BC8AC7CF CRC64; MIHPSAKIHP TALIEEGAVI GEDVFIGPFC IIEGTVEIKA RTVLKSHVVV RGDTVIGEDN EIYQFTSIGE VNQDLKYKGE ATKTIIGNSN KIREHVTIHR GTIQGCGVTA IGNNNLLMIN VHVAHDCQIK NNCILANNAT LAGHVELDDF VIVGGMSAIH QFVIVGAHVM LGGGSMVSQD VPPYVMAQGN HARPFGVNLE GLKRRGFDKP TMHVIRNIYK MLYRSGKTLE EVLPEIEQIA ETDSAISFFV EFFKRSTRGI IR // ID LPXM_HAEIN Reviewed; 318 AA. AC P44567; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Lipid A biosynthesis myristoyltransferase {ECO:0000255|HAMAP-Rule:MF_01944}; DE EC=2.3.1.243 {ECO:0000255|HAMAP-Rule:MF_01944}; DE AltName: Full=Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase {ECO:0000255|HAMAP-Rule:MF_01944}; GN Name=lpxM {ECO:0000255|HAMAP-Rule:MF_01944}; Synonyms=msbB; GN OrderedLocusNames=HI_0199; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of myristate from myristoyl-acyl CC carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form CC Kdo(2)-lipid A. {ECO:0000255|HAMAP-Rule:MF_01944}. CC -!- CATALYTIC ACTIVITY: A tetradecanoyl-[acyl-carrier protein] + CC (Kdo)(2)-(dodecanoyl)-lipid IV(A) = Kdo(2)-lipid A + a holo-[acyl- CC carrier protein]. {ECO:0000255|HAMAP-Rule:MF_01944}. CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; CC KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid CC IV(A): step 4/4. {ECO:0000255|HAMAP-Rule:MF_01944}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01944}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01944}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01944}. CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01944}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21868.1; -; Genomic_DNA. DR PIR; I64053; I64053. DR RefSeq; NP_438368.1; NC_000907.1. DR RefSeq; WP_005694093.1; NC_000907.1. DR STRING; 71421.HI0199; -. DR EnsemblBacteria; AAC21868; AAC21868; HI_0199. DR GeneID; 951108; -. DR KEGG; hin:HI0199; -. DR PATRIC; 20188895; VBIHaeInf48452_0204. DR eggNOG; ENOG4105NWR; Bacteria. DR eggNOG; COG1560; LUCA. DR KO; K02560; -. DR OMA; QYVWILQ; -. DR OrthoDB; EOG657J8B; -. DR PhylomeDB; P44567; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00360; UER00486. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0019107; F:myristoyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01944; Lipid_A_LpxM; 1. DR InterPro; IPR004960; LipA_acyltrans. DR InterPro; IPR011921; Lipid_A_MsbB. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. DR TIGRFAMs; TIGR02208; lipid_A_msbB; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Lipopolysaccharide biosynthesis; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 318 Lipid A biosynthesis FT myristoyltransferase. FT /FTId=PRO_0000201778. FT TRANSMEM 27 47 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01944}. FT MOTIF 145 150 HXXXXD motif. {ECO:0000255|HAMAP- FT Rule:MF_01944}. SQ SEQUENCE 318 AA; 36883 MW; DE59952D78719445 CRC64; MSDNQQNLRL TARVGYEAHF SWSYLKPQYW GIWLGIFFLL LLAFVPFRLR DKLTGKLGIW IGHKAKKQRT RAQTNLQYCF PHWTEQQREQ VIDKMFAVVA QVMFGIGEIA IRSKKHLQKR SEFIGLEHIE QAKAEGKNII LMVPHGWAID ASGIILHTQG MPMTSMYNPH RNPLVDWLWT ITRQRFGGKM HARQNGIKPF LSHVRKGEMG YYLPDEDFGA EQSVFVDFFG TYKATLPGLN KMAKLSKAVV IPMFPRYNAE TGKYEMEIHP AMNLSDDPEQ SARAMNEEIE SFVTPAPEQY VWILQLLRTR KDGEDLYD // ID LSG1_HAEIN Reviewed; 401 AA. AC P71399; Q48210; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 16-MAR-2016, entry version 91. DE RecName: Full=Lsg locus putative protein 1; GN OrderedLocusNames=HI_1700; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polysaccharide synthase family. CC HI_0867/HI_1700 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23346.1; 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; M94855; AAA24978.1; -; Genomic_DNA. DR EMBL; L42023; AAC23346.1; ALT_INIT; Genomic_DNA. DR PIR; H64175; H64175. DR RefSeq; NP_439842.2; NC_000907.1. DR RefSeq; WP_005694190.1; NC_000907.1. DR STRING; 71421.HI1700; -. DR EnsemblBacteria; AAC23346; AAC23346; HI_1700. DR GeneID; 950658; -. DR KEGG; hin:HI1700; -. DR PATRIC; 20192151; VBIHaeInf48452_1779. DR eggNOG; ENOG4108MY6; Bacteria. DR eggNOG; COG2244; LUCA. DR OMA; CWIAQSE; -. DR OrthoDB; EOG6GFGNX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 401 Lsg locus putative protein 1. FT /FTId=PRO_0000166456. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. FT TRANSMEM 282 302 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 352 372 Helical. {ECO:0000255}. FT TRANSMEM 374 394 Helical. {ECO:0000255}. FT CONFLICT 249 249 V -> I (in Ref. 1; AAA24978). FT {ECO:0000305}. FT CONFLICT 276 276 V -> I (in Ref. 1; AAA24978). FT {ECO:0000305}. FT CONFLICT 358 358 I -> V (in Ref. 1; AAA24978). FT {ECO:0000305}. SQ SEQUENCE 401 AA; 45945 MW; FE2E7B02747B0874 CRC64; MKVFKDSVIY LVGELSSKLV PFLLLPYLSR KLGVEGYGSL SYYQTFLSLF LIVVSLTQEG AISRYFYFYG KRSLNLVVNT GYAYTTIIGS IILIGCWIAQ SEILFYAALS SIFQSFLNVQ LSVRQCQKKA WSYAFIQFSL TVTGAVFTVA LLEYYQNDLV EKRILAILLS NLVVWFFSYF LYRKSTTSKK YQFKHYQSAL FYILGFGLPL ILHYASFFLK GQLDRIFIYH KFSETDLGLY AMGAQLALVV SIAIQALNKA IIPYFYEALK QKKLVVQQLH KWALFSFLLI PIPALIMWII PEDVLVWILG SQFVGTKYYF ILFLISTTLS IPYLILVNYL FYYGKNKLIS QCSVLSTIIY VASLVALTFT EIKYIPYAGI IGSLSIIPIL YFMTSKVSKT L // ID LUXS_HAEIN Reviewed; 167 AA. AC P44007; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 112. DE RecName: Full=S-ribosylhomocysteine lyase; DE EC=4.4.1.21; DE AltName: Full=AI-2 synthesis protein; DE AltName: Full=Autoinducer-2 production protein LuxS; GN Name=luxS; OrderedLocusNames=HI_0491; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=11435117; DOI=10.1016/S0969-2126(01)00613-X; RA Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y., RA Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E., RA Sauder J.M., Buchanan S.G.; RT "A structural genomics approach to the study of quorum sensing: RT crystal structures of three LuxS orthologs."; RL Structure 9:527-537(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Chen C.C.H., Parsons J.F., Lim K., Lehmann C., Tempczyk A., RA Eisenstein E., Herzberg O.; RT "Crystal structure of autoinducer-2 production protein (luxS) from RT Haemophilus influenzae -- a case of twinned crystal."; RL Submitted (JUL-2001) to the PDB data bank. CC -!- FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which CC is secreted by bacteria and is used to communicate both the cell CC density and the metabolic potential of the environment. The CC regulation of gene expression in response to changes in cell CC density is called quorum sensing. Catalyzes the transformation of CC S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5- CC dihydroxy-2,3-pentadione (DPD). CC -!- CATALYTIC ACTIVITY: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L- CC homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 1 Fe cation per subunit.; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the LuxS 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; L42023; AAC22149.1; -; Genomic_DNA. DR PIR; G64008; G64008. DR RefSeq; NP_438651.1; NC_000907.1. DR RefSeq; WP_005693682.1; NC_000907.1. DR PDB; 1J6W; X-ray; 2.10 A; A/B=2-167. DR PDB; 1JOE; X-ray; 2.40 A; A/B/C/D=1-167. DR PDBsum; 1J6W; -. DR PDBsum; 1JOE; -. DR ProteinModelPortal; P44007; -. DR SMR; P44007; 3-163. DR STRING; 71421.HI0491; -. DR EnsemblBacteria; AAC22149; AAC22149; HI_0491. DR GeneID; 950775; -. DR KEGG; hin:HI0491; -. DR PATRIC; 20189535; VBIHaeInf48452_0510. DR eggNOG; ENOG4106762; Bacteria. DR eggNOG; COG1854; LUCA. DR KO; K07173; -. DR OMA; AGFMREH; -. DR OrthoDB; EOG68WRBM; -. DR PhylomeDB; P44007; -. DR BRENDA; 4.4.1.21; 2529. DR EvolutionaryTrace; P44007; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0043768; F:S-ribosylhomocysteine lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.80; -; 1. DR HAMAP; MF_00091; LuxS; 1. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR003815; S-ribosylhomocysteinase. DR Pfam; PF02664; LuxS; 1. DR PIRSF; PIRSF006160; AI2; 1. DR PRINTS; PR01487; LUXSPROTEIN. DR ProDom; PD013172; S-ribosylhomocysteinase; 1. DR SUPFAM; SSF63411; SSF63411; 1. PE 1: Evidence at protein level; KW 3D-structure; Autoinducer synthesis; Complete proteome; Iron; Lyase; KW Metal-binding; Quorum sensing; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 167 S-ribosylhomocysteine lyase. FT /FTId=PRO_0000172227. FT METAL 54 54 Iron. FT METAL 58 58 Iron. FT METAL 128 128 Iron. FT HELIX 5 8 {ECO:0000244|PDB:1J6W}. FT HELIX 11 13 {ECO:0000244|PDB:1J6W}. FT STRAND 16 26 {ECO:0000244|PDB:1J6W}. FT STRAND 32 39 {ECO:0000244|PDB:1J6W}. FT TURN 43 45 {ECO:0000244|PDB:1J6W}. FT HELIX 50 68 {ECO:0000244|PDB:1J6W}. FT STRAND 73 80 {ECO:0000244|PDB:1J6W}. FT STRAND 84 93 {ECO:0000244|PDB:1J6W}. FT HELIX 97 112 {ECO:0000244|PDB:1J6W}. FT HELIX 117 119 {ECO:0000244|PDB:1J6W}. FT TURN 125 127 {ECO:0000244|PDB:1J6W}. FT TURN 129 132 {ECO:0000244|PDB:1J6W}. FT HELIX 136 149 {ECO:0000244|PDB:1J6W}. FT STRAND 152 154 {ECO:0000244|PDB:1J6W}. FT HELIX 156 159 {ECO:0000244|PDB:1J6W}. SQ SEQUENCE 167 AA; 18527 MW; A8116FE96BA5F817 CRC64; MPLLDSFKVD HTKMNAPAVR IAKTMLTPKG DNITVFDLRF CIPNKEILSP KGIHTLEHLF AGFMRDHLNG DSIEIIDISP MGCRTGFYMS LIGTPNEQKV SEAWLASMQD VLGVQDQASI PELNIYQCGS YTEHSLEDAH EIAKNVIARG IGVNKNEDLS LDNSLLK // ID LGT_HAEIN Reviewed; 268 AA. AC P44930; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Prolipoprotein diacylglyceryl transferase; DE EC=2.4.99.-; GN Name=lgt; OrderedLocusNames=HI_0904; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC22563.1; -; Genomic_DNA. DR PIR; F64101; F64101. DR RefSeq; NP_439064.1; NC_000907.1. DR RefSeq; WP_005693254.1; NC_000907.1. DR STRING; 71421.HI0904; -. DR EnsemblBacteria; AAC22563; AAC22563; HI_0904. DR GeneID; 950017; -. DR KEGG; hin:HI0904; -. DR PATRIC; 20190463; VBIHaeInf48452_0945. DR eggNOG; ENOG4105C3B; Bacteria. DR eggNOG; COG0682; LUCA. DR KO; K13292; -. DR OMA; AHRTKRH; -. DR OrthoDB; EOG6MH5CQ; -. DR PhylomeDB; P44930; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro. DR HAMAP; MF_01147; Lgt; 1. DR InterPro; IPR001640; Prolipoprot_diAcglycer_Trfase. DR Pfam; PF01790; LGT; 1. DR TIGRFAMs; TIGR00544; lgt; 1. DR PROSITE; PS01311; LGT; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 268 Prolipoprotein diacylglyceryl FT transferase. FT /FTId=PRO_0000172610. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. SQ SEQUENCE 268 AA; 30570 MW; 1E50858E4F7E5606 CRC64; MNSNYLLLPH FDPSIFTLGD SNIGLRWYGL MYLLGFVFAR WLAVRRANRP NSGWTVDQVD SLLFNGFMGV FIGGRVGDVF FYNLDHFLQE PLYLFRVWEG GMSFHGGLIG VIVAMIWTSY SQKRNFWQTA DFVAPLIPFG LGLGRIGNFI NLELWGRETN VPWAMIFPND PLLLPRHPSQ LYEAFLEGLV LFTILNIFIK KPRPMASVAG LFLIGYGVFR FIVEYVREPE VENFFGIITR GQALCLPMII GGAFIMAWAY SRKSAVIK // ID LGUL_HAEIN Reviewed; 135 AA. AC P44638; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Lactoylglutathione lyase; DE EC=4.4.1.5; DE AltName: Full=Aldoketomutase; DE AltName: Full=Glyoxalase I; DE Short=Glx I; DE AltName: Full=Ketone-aldehyde mutase; DE AltName: Full=Methylglyoxalase; DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase; GN Name=gloA; OrderedLocusNames=HI_0323; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from CC methylglyoxal and glutathione, to S-lactoylglutathione. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione + CC methylglyoxal. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; CC Note=Binds 1 nickel ion per subunit. In the homodimer, two nickel CC ions are bound between subunits. {ECO:0000250}; CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal CC degradation; (R)-lactate from methylglyoxal: step 1/2. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glyoxalase 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; L42023; AAC21986.1; -; Genomic_DNA. DR PIR; I64147; I64147. DR RefSeq; NP_438488.1; NC_000907.1. DR RefSeq; WP_005688980.1; NC_000907.1. DR ProteinModelPortal; P44638; -. DR SMR; P44638; 1-125. DR STRING; 71421.HI0323; -. DR EnsemblBacteria; AAC21986; AAC21986; HI_0323. DR GeneID; 949438; -. DR KEGG; hin:HI0323; -. DR PATRIC; 20189187; VBIHaeInf48452_0340. DR eggNOG; ENOG4108UYE; Bacteria. DR eggNOG; COG0346; LUCA. DR KO; K01759; -. DR OMA; THNWDTP; -. DR OrthoDB; EOG6DVJXX; -. DR PhylomeDB; P44638; -. DR UniPathway; UPA00619; UER00675. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.180.10; -; 1. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom. DR InterPro; IPR004361; Glyoxalase_1. DR InterPro; IPR018146; Glyoxalase_1_CS. DR Pfam; PF00903; Glyoxalase; 1. DR SUPFAM; SSF54593; SSF54593; 1. DR TIGRFAMs; TIGR00068; glyox_I; 1. DR PROSITE; PS00934; GLYOXALASE_I_1; 1. DR PROSITE; PS00935; GLYOXALASE_I_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Lyase; Metal-binding; Nickel; Reference proteome. FT CHAIN 1 135 Lactoylglutathione lyase. FT /FTId=PRO_0000168093. FT ACT_SITE 122 122 Proton donor/acceptor. {ECO:0000250}. FT METAL 5 5 Nickel; via tele nitrogen; shared with FT dimeric partner. {ECO:0000250}. FT METAL 56 56 Nickel; shared with dimeric partner. FT {ECO:0000250}. FT METAL 74 74 Nickel; via tele nitrogen. {ECO:0000250}. FT METAL 122 122 Nickel. {ECO:0000250}. FT BINDING 9 9 Substrate; shared with dimeric partner. FT {ECO:0000250}. FT BINDING 60 60 Substrate; shared with dimeric partner. FT {ECO:0000250}. FT BINDING 74 74 Substrate. {ECO:0000250}. SQ SEQUENCE 135 AA; 14893 MW; B6DF5FFCD9669E80 CRC64; MQILHTMLRV GDLDRSIKFY QDVLGMRLLR TSENPEYKYT LAFLGYEDGE SAAEIELTYN WGVDKYEHGT AYGHIAIGVD DIYATCEAVR ASGGNVTREA GPVKGGSTVI AFVEDPDGYK IEFIENKSTK SGLGN // ID LPPB_HAEIN Reviewed; 405 AA. AC P44833; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 106. DE RecName: Full=Outer membrane antigenic lipoprotein B; DE Flags: Precursor; GN Name=lppB; OrderedLocusNames=HI_0706; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May be a virulence determinant. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. CC -!- SIMILARITY: Belongs to the E.coli NlpD/Haemophilus LppB family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 LysM domain. {ECO:0000255|PROSITE- CC ProRule:PRU01118}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22363.1; -; Genomic_DNA. DR PIR; F64087; F64087. DR RefSeq; NP_438864.1; NC_000907.1. DR RefSeq; WP_005694590.1; NC_000907.1. DR ProteinModelPortal; P44833; -. DR STRING; 71421.HI0706; -. DR EnsemblBacteria; AAC22363; AAC22363; HI_0706. DR GeneID; 949731; -. DR KEGG; hin:HI0706; -. DR PATRIC; 20190029; VBIHaeInf48452_0736. DR eggNOG; ENOG4108K5P; Bacteria. DR eggNOG; COG0739; LUCA. DR KO; K06194; -. DR OMA; QDIAKMG; -. DR OrthoDB; EOG61ZTBJ; -. DR PhylomeDB; P44833; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M23; 1. DR SMART; SM00257; LysM; 1. DR SUPFAM; SSF51261; SSF51261; 1. DR PROSITE; PS51782; LYSM; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal; Virulence. FT SIGNAL 1 17 {ECO:0000305}. FT CHAIN 18 405 Outer membrane antigenic lipoprotein B. FT /FTId=PRO_0000018034. FT DOMAIN 145 189 LysM. {ECO:0000255|PROSITE- FT ProRule:PRU01118}. FT LIPID 18 18 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 18 18 S-diacylglycerol cysteine. {ECO:0000305}. SQ SEQUENCE 405 AA; 42505 MW; 4134FB6B93EFE57F CRC64; MKKSFLLLPL SLVVLSACTS NFPAPISDAD GNFSPSVIQS VNGSNVGGAW QPEIQKNSLP TTGNMVTPQQ NFQPINQQPT MPTAPAQPAF QPSPKTVVSA PTVQTKTVTK TVADCVDGQH INIPRNPNTN APDYSKISKG SYKGNTYKVN KGDTMFLIAY LAGIDVKELA ALNNLSEPYN LSLGQVLKIS NCDIKTVTTT VSVKQPAVTA STATPVKPAV TYTPGANGTQ IGSDGTIIGP IKSEAGTSPS VPVATSSTQV TSSVNNANST PINSNVVAPI ASNVVWQWPT SGNIIQGFSS TDGGNKGIDI SGSRGQAVKA AAAGRIVYAG NALRGYGNLI IIKHNDDFLS AYAHNDKILV ADQQEVKAGQ DIAKMGSSGT NTVKLHFEIR YKGKSVDPVR YLPRH // ID LPXK_HAEIN Reviewed; 332 AA. AC P44491; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409}; DE EC=2.7.1.130 {ECO:0000255|HAMAP-Rule:MF_00409}; DE AltName: Full=Lipid A 4'-kinase {ECO:0000255|HAMAP-Rule:MF_00409}; GN Name=lpxK {ECO:0000255|HAMAP-Rule:MF_00409}; GN OrderedLocusNames=HI_0059; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position CC of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1- CC P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). CC {ECO:0000255|HAMAP-Rule:MF_00409}. CC -!- CATALYTIC ACTIVITY: ATP + (2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl)-(1->6)-(2-N,3-O- CC bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl phosphate) = CC ADP + (2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-4-O-phospho-beta- CC D-glucosaminyl)-(1->6)-(2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosaminyl phosphate). {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000255|HAMAP- CC Rule:MF_00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21737.1; -; Genomic_DNA. DR PIR; G64141; G64141. DR RefSeq; NP_438232.1; NC_000907.1. DR RefSeq; WP_005693863.1; NC_000907.1. DR ProteinModelPortal; P44491; -. DR STRING; 71421.HI0059; -. DR EnsemblBacteria; AAC21737; AAC21737; HI_0059. DR GeneID; 950959; -. DR KEGG; hin:HI0059; -. DR PATRIC; 20188571; VBIHaeInf48452_0059. DR eggNOG; ENOG4105CHD; Bacteria. DR eggNOG; COG1663; LUCA. DR KO; K00912; -. DR OMA; PTVIYLI; -. DR OrthoDB; EOG60GRWT; -. DR PhylomeDB; P44491; -. DR UniPathway; UPA00359; UER00482. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IBA:GO_Central. DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00409; LpxK; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003758; Tetraacyldisaccharide_4-kinase. DR Pfam; PF02606; LpxK; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00682; lpxK; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 332 Tetraacyldisaccharide 4'-kinase. FT /FTId=PRO_0000190929. FT NP_BIND 53 60 ATP. {ECO:0000255|HAMAP-Rule:MF_00409}. SQ SEQUENCE 332 AA; 37607 MW; D34D58BF0D480DC7 CRC64; MPFWYSNSKL IWLLSPFSLL FWLISQLRRA LFSLGLKSSY RAPKPVIIVG NLSVGGNGKT PVVVWLMEEL KKRGLRVGVI SRGYGSKSKT YPLFVTKNTN PIEGGDEPVL IAKRTNAPVV ISPNRQQAIE LLLSQAECDI IISDDGLQHY QLQRDLEIVV MDAERALGNG FVLPAGPLRE LPSRLKSVDF VITNGGKNQY SDAVMRLVPH FAINLKTNEK RQLNEFQSGV AIAGIGNPQR FFTMLEKLGI QLKQTQAFQD HQHFEASQLE KLAENQPLFM TEKDAVKCQS FAKDNWWYVP VDAEIIEAEK QRENLPHFWA KIDKLVEQYR NG // ID LSPA_HAEIN Reviewed; 171 AA. AC P44975; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 105. 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; OrderedLocusNames=HI_1006; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC22667.1; -; Genomic_DNA. DR PIR; H64107; H64107. DR RefSeq; NP_439167.1; NC_000907.1. DR RefSeq; WP_005651632.1; NC_000907.1. DR STRING; 71421.HI1006; -. DR EnsemblBacteria; AAC22667; AAC22667; HI_1006. DR GeneID; 949998; -. DR KEGG; hin:HI1006; -. DR PATRIC; 20190673; VBIHaeInf48452_1049. DR eggNOG; ENOG4105M02; Bacteria. DR eggNOG; COG0597; LUCA. DR KO; K03101; -. DR OMA; DFASKQW; -. DR OrthoDB; EOG6PGKBM; -. DR PhylomeDB; P44975; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000000579; 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; IPR020846; MFS_dom. DR InterPro; IPR001872; Peptidase_A8. DR PANTHER; PTHR33695:SF1; PTHR33695:SF1; 1. DR Pfam; PF01252; Peptidase_A8; 1. DR PRINTS; PR00781; LIPOSIGPTASE. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00077; lspA; 1. DR PROSITE; PS00855; SPASE_II; 1. PE 3: Inferred from homology; KW Aspartyl protease; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Protease; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 171 Lipoprotein signal peptidase. FT /FTId=PRO_0000178783. FT TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TOPO_DOM 29 63 Periplasmic. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TOPO_DOM 85 98 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TOPO_DOM 120 132 Periplasmic. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TOPO_DOM 154 171 Cytoplasmic. {ECO:0000255}. FT ACT_SITE 111 111 {ECO:0000250}. FT ACT_SITE 138 138 {ECO:0000250}. SQ SEQUENCE 171 AA; 19363 MW; D3DE4D74A173B3ED CRC64; MSKKSGLSFL WLSAVAFVID LLTKYIVVQK FDLYESVNVL PVFNLTYVRN YGAAFSFLAD HSGWQQYFFI LLALAISGML VYFLAKNNAE QKIQNSAYAL IIGGALANMV DRAYNGFVVD FFDFYWDIYH YPVFNIADIA ICIGAGLLVL DAFKSEKKKV QDKQVEKCGQ K // ID LPTC_HAEIN Reviewed; 209 AA. AC P45075; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Lipopolysaccharide export system protein LptC {ECO:0000255|HAMAP-Rule:MF_01915}; GN Name=lptC {ECO:0000255|HAMAP-Rule:MF_01915}; GN OrderedLocusNames=HI_1150; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). CC Required for the translocation of LPS from the inner membrane to CC the outer membrane. Facilitates the transfer of LPS from the inner CC membrane to the periplasmic protein LptA. Could be a docking site CC for LptA. {ECO:0000255|HAMAP-Rule:MF_01915}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. Interacts with LptA and the LptBFG transporter CC complex. {ECO:0000255|HAMAP-Rule:MF_01915}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01915}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01915}. CC -!- SIMILARITY: Belongs to the LptC family. {ECO:0000255|HAMAP- CC Rule:MF_01915}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22805.1; -; Genomic_DNA. DR PIR; B64168; B64168. DR RefSeq; NP_439308.2; NC_000907.1. DR STRING; 71421.HI1150; -. DR EnsemblBacteria; AAC22805; AAC22805; HI_1150. DR GeneID; 950694; -. DR KEGG; hin:HI1150; -. DR PATRIC; 20190975; VBIHaeInf48452_1200. DR eggNOG; ENOG4108P1K; Bacteria. DR eggNOG; COG3117; LUCA. DR KO; K11719; -. DR OMA; WFTQPVM; -. DR OrthoDB; EOG6W7212; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015221; F:lipopolysaccharide transmembrane transporter activity; IEA:InterPro. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01915; LPS_assembly_LptC; 1. DR InterPro; IPR010664; LipoPS_assembly_LptC-rel. DR InterPro; IPR026265; LptC. DR Pfam; PF06835; LptC; 1. DR PIRSF; PIRSF028513; LptC; 1. DR TIGRFAMs; TIGR04409; LptC_YrbK; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 209 Lipopolysaccharide export system protein FT LptC. FT /FTId=PRO_0000169474. FT TRANSMEM 7 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01915}. SQ SEQUENCE 209 AA; 23819 MW; 589EE98DB0C91133 CRC64; MIEIKMNIRW NVILGVIALC ALAWFYSLNQ ETADLSELVK KPDSPDYVGY KMETTVFSPD GKKQYLALSD KIEHYTVNEQ TLFTAPLVYL YPTTSNEKEK EKNANQNVDF FSTQSWKLSA NQARLTKDQI LYLEGNVVAQ NLTSDSRLQR IETESAVVNL KTQDITSETQ VKIKGKNFSS TGLKLVGNLR QQVATLKEQV KTYYEVSKQ // ID LPXH_HAEIN Reviewed; 237 AA. AC P44046; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000255|HAMAP-Rule:MF_00575}; DE EC=3.6.1.54 {ECO:0000255|HAMAP-Rule:MF_00575}; DE AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000255|HAMAP-Rule:MF_00575}; GN Name=lpxH {ECO:0000255|HAMAP-Rule:MF_00575}; GN OrderedLocusNames=HI_0735; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the hydrolysis of the pyrophosphate bond of CC UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1- CC phosphate (lipid X) and UMP. {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- CATALYTIC ACTIVITY: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)- CC alpha-D-glucosamine + H(2)O = 2-N,3-O-bis((3R)-3- CC hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + UMP. CC {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 4/6. {ECO:0000255|HAMAP- CC Rule:MF_00575}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00575}. CC -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000255|HAMAP- CC Rule:MF_00575}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22394.1; -; Genomic_DNA. DR PIR; A64013; A64013. DR RefSeq; NP_438894.1; NC_000907.1. DR RefSeq; WP_005693139.1; NC_000907.1. DR ProteinModelPortal; P44046; -. DR STRING; 71421.HI0735; -. DR DNASU; 950740; -. DR EnsemblBacteria; AAC22394; AAC22394; HI_0735. DR GeneID; 950740; -. DR KEGG; hin:HI0735; -. DR PATRIC; 20190107; VBIHaeInf48452_0769. DR eggNOG; ENOG4105F10; Bacteria. DR eggNOG; COG2908; LUCA. DR KO; K03269; -. DR OMA; FMHGNRD; -. DR OrthoDB; EOG6FNHR2; -. DR PhylomeDB; P44046; -. DR UniPathway; UPA00359; UER00480. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 2. DR HAMAP; MF_00575; LpxH; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 2. DR TIGRFAMs; TIGR01854; lipid_A_lpxH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome. FT CHAIN 1 237 UDP-2,3-diacylglucosamine hydrolase. FT /FTId=PRO_0000214112. SQ SEQUENCE 237 AA; 27786 MW; 7218733241F395B7 CRC64; MKHSYFISDL HLSETQPELT ALFVDFMQNL APQAERLYIL GDLFDFWIGD DEQSALIQQV KDLIKFVSDQ GVQCYFQHGN RDFLIGERFS KETGAQLLPD YQLITLYDKK ILLCHGDTLC IDDEAYQQFR RRVHQKWLQR LFLCLPLKVR VIIAEKIRAK SNQDKQAKSQ EIMDVNQAFT AEKVQEFGVN LLIHGHTHRE AIHQQEEFTR IVLGDWRKNY ASILKMDESG EFGFIKD // ID LSG4_HAEIN Reviewed; 257 AA. AC P71398; Q48213; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Lsg locus putative protein 4; DE EC=2.-.-.-; GN OrderedLocusNames=HI_1697; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 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; L42023; AAC23343.1; -; Genomic_DNA. DR EMBL; M94855; AAA24981.1; -; Genomic_DNA. DR PIR; E64175; E64175. DR RefSeq; NP_439839.1; NC_000907.1. DR RefSeq; WP_005694186.1; NC_000907.1. DR STRING; 71421.HI1697; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR DNASU; 950869; -. DR EnsemblBacteria; AAC23343; AAC23343; HI_1697. DR GeneID; 950869; -. DR KEGG; hin:HI1697; -. DR PATRIC; 20192145; VBIHaeInf48452_1776. DR eggNOG; ENOG41068D6; Bacteria. DR eggNOG; COG3306; LUCA. DR KO; K07270; -. DR OMA; KGEIGCT; -. DR OrthoDB; EOG6ND0HN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 257 Lsg locus putative protein 4. FT /FTId=PRO_0000216241. FT CONFLICT 17 17 E -> K (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 30 30 V -> I (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 46 46 A -> S (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 102 102 S -> L (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 127 127 K -> N (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 130 130 D -> N (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 134 134 F -> T (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 153 153 D -> N (in Ref. 1; AAA24981). FT {ECO:0000305}. FT CONFLICT 214 214 I -> M (in Ref. 1; AAA24981). FT {ECO:0000305}. SQ SEQUENCE 257 AA; 29864 MW; D1ECDE47763EE059 CRC64; MLKKYLISLD KDIQRRELFF SQKNTEDFQV FSAINTMQKD WDELAAIFNI EQFKAHYFRN VTKGEIGCTL SHLSVYQKIV EDNDIAEDSY ALVCEDDALF HSDFQQNLTA LLSEKLEAEI ILLGQSKIND FNDFDLEINY PTTFSFLCKK TGDVNYAFPY KSYFAGTVGY LIKKSAARRF IQQISQNKPF WLADDFLLFE QNFNIRNKVV RPLIVIENPV LISNLESVRG SLSNNLLKKL MKYPLKKIFA IKKNLAN // ID LPOA_HAEIN Reviewed; 575 AA. AC P45299; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Penicillin-binding protein activator LpoA; DE Short=PBP activator LpoA; DE Flags: Precursor; GN Name=lpoA; OrderedLocusNames=HI_1655; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 256-573, AND DISULFIDE BOND. RX PubMed=18412262; DOI=10.1002/prot.22033; RA Vijayalakshmi J., Akerley B.J., Saper M.A.; RT "Structure of YraM, a protein essential for growth of Haemophilus RT influenzae."; RL Proteins 73:204-217(2008). CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential CC for the function of penicillin-binding protein 1A (PBP1a). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with PBP1a. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid- CC anchor {ECO:0000250}; Periplasmic side {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LpoA 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; L42023; AAC23299.1; -; Genomic_DNA. DR PIR; B64174; B64174. DR RefSeq; NP_439797.1; NC_000907.1. DR RefSeq; WP_005694381.1; NC_000907.1. DR PDB; 3CKM; X-ray; 1.35 A; A=256-573. DR PDB; 4P29; X-ray; 1.95 A; A/B=33-253. DR PDBsum; 3CKM; -. DR PDBsum; 4P29; -. DR ProteinModelPortal; P45299; -. DR SMR; P45299; 257-573. DR STRING; 71421.HI1655; -. DR EnsemblBacteria; AAC23299; AAC23299; HI_1655. DR GeneID; 950219; -. DR KEGG; hin:HI1655; -. DR PATRIC; 20192059; VBIHaeInf48452_1733. DR eggNOG; ENOG4105E1C; Bacteria. DR eggNOG; COG3107; LUCA. DR KO; K07121; -. DR OMA; FCETPWL; -. DR OrthoDB; EOG66MQQ3; -. DR PhylomeDB; P45299; -. DR EvolutionaryTrace; P45299; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_01890; LpoA; 1. DR InterPro; IPR007443; LpoA. DR InterPro; IPR028082; Peripla_BP_I. DR Pfam; PF04348; LppC; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Cell shape; Complete proteome; KW Disulfide bond; Lipoprotein; Membrane; Palmitate; KW Peptidoglycan synthesis; Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 575 Penicillin-binding protein activator FT LpoA. FT /FTId=PRO_0000169453. FT LIPID 26 26 N-palmitoyl cysteine. {ECO:0000255}. FT LIPID 26 26 S-diacylglycerol cysteine. {ECO:0000255}. FT DISULFID 356 554 {ECO:0000269|PubMed:18412262}. FT HELIX 34 39 {ECO:0000244|PDB:4P29}. FT HELIX 46 51 {ECO:0000244|PDB:4P29}. FT HELIX 53 55 {ECO:0000244|PDB:4P29}. FT HELIX 59 75 {ECO:0000244|PDB:4P29}. FT HELIX 79 87 {ECO:0000244|PDB:4P29}. FT HELIX 94 110 {ECO:0000244|PDB:4P29}. FT HELIX 114 122 {ECO:0000244|PDB:4P29}. FT HELIX 126 128 {ECO:0000244|PDB:4P29}. FT HELIX 131 147 {ECO:0000244|PDB:4P29}. FT HELIX 151 164 {ECO:0000244|PDB:4P29}. FT HELIX 168 184 {ECO:0000244|PDB:4P29}. FT HELIX 187 192 {ECO:0000244|PDB:4P29}. FT HELIX 199 214 {ECO:0000244|PDB:4P29}. FT HELIX 218 231 {ECO:0000244|PDB:4P29}. FT HELIX 236 239 {ECO:0000244|PDB:4P29}. FT HELIX 243 247 {ECO:0000244|PDB:4P29}. FT STRAND 259 263 {ECO:0000244|PDB:3CKM}. FT HELIX 270 284 {ECO:0000244|PDB:3CKM}. FT STRAND 291 295 {ECO:0000244|PDB:3CKM}. FT TURN 296 298 {ECO:0000244|PDB:3CKM}. FT HELIX 301 310 {ECO:0000244|PDB:3CKM}. FT STRAND 315 317 {ECO:0000244|PDB:3CKM}. FT HELIX 322 330 {ECO:0000244|PDB:3CKM}. FT HELIX 332 335 {ECO:0000244|PDB:3CKM}. FT STRAND 339 343 {ECO:0000244|PDB:3CKM}. FT STRAND 355 357 {ECO:0000244|PDB:3CKM}. FT HELIX 362 375 {ECO:0000244|PDB:3CKM}. FT STRAND 382 388 {ECO:0000244|PDB:3CKM}. FT HELIX 389 406 {ECO:0000244|PDB:3CKM}. FT STRAND 411 417 {ECO:0000244|PDB:3CKM}. FT HELIX 420 427 {ECO:0000244|PDB:3CKM}. FT STRAND 434 437 {ECO:0000244|PDB:3CKM}. FT HELIX 441 451 {ECO:0000244|PDB:3CKM}. FT TURN 452 454 {ECO:0000244|PDB:3CKM}. FT STRAND 459 462 {ECO:0000244|PDB:3CKM}. FT HELIX 464 466 {ECO:0000244|PDB:3CKM}. FT HELIX 469 472 {ECO:0000244|PDB:3CKM}. FT HELIX 475 480 {ECO:0000244|PDB:3CKM}. FT TURN 481 483 {ECO:0000244|PDB:3CKM}. FT STRAND 485 488 {ECO:0000244|PDB:3CKM}. FT HELIX 490 493 {ECO:0000244|PDB:3CKM}. FT HELIX 498 506 {ECO:0000244|PDB:3CKM}. FT TURN 507 509 {ECO:0000244|PDB:3CKM}. FT HELIX 511 528 {ECO:0000244|PDB:3CKM}. FT HELIX 530 535 {ECO:0000244|PDB:3CKM}. FT STRAND 541 543 {ECO:0000244|PDB:3CKM}. FT STRAND 546 550 {ECO:0000244|PDB:3CKM}. FT STRAND 555 559 {ECO:0000244|PDB:3CKM}. FT STRAND 561 566 {ECO:0000244|PDB:3CKM}. FT STRAND 569 572 {ECO:0000244|PDB:3CKM}. SQ SEQUENCE 575 AA; 63437 MW; 3FCF093B22C56326 CRC64; MSILLQGERF KKRLMPILLS MALAGCSNLL GSNFTQTLQK DANASSEFYI NKLGQTQELE DQQTYKLLAA RVLIRENKVE QSAALLRELG ELNDAQKLDR ALIEARISAA KNANEVAQNQ LRALDLNKLS PSQKSRYYET LAIVAENRKD MIEAVKARIE MDKNLTDVQR HQDNIDKTWA LLRSANTGVI NNASDEGNAA LGGWLTLIKA YNDYIRQPVQ LSQALQSWKN AYPNHAAATL FPKELLTLLN FQQTNVSQIG LLLPLSGDGQ ILGTTIQSGF NDAKGNSTIP VQVFDTSMNS VQDIIAQAKQ AGIKTLVGPL LKQNLDVILA DPAQIQGMDV LALNATPNSR AIPQLCYYGL SPEDEAESAA NKMWNDGVRN PLVAMPQNDL GQRVGNAFNV RWQQLAGTDA NIRYYNLPAD VTYFVQENNS NTTALYAVAS PTELAEMKGY LTNIVPNLAI YASSRASASA TNTNTDFIAQ MNGVQFSDIP FFKDTNSPQY QKLAKSTGGE YQLMRLYAMG ADAWLLINQF NELRQVPGYR LSGLTGILSA DTNCNVERDM TWYQYQDGAI VPVAN // ID LPTD_HAEIN Reviewed; 782 AA. AC P44846; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=LPS-assembly protein LptD {ECO:0000255|HAMAP-Rule:MF_01411}; DE Flags: Precursor; GN Name=lptD {ECO:0000255|HAMAP-Rule:MF_01411}; Synonyms=imp, ostA; GN OrderedLocusNames=HI_0730; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Together with LptE, is involved in the assembly of CC lipopolysaccharide (LPS) at the surface of the outer membrane. CC {ECO:0000255|HAMAP-Rule:MF_01411}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. Interacts with LptE and LptA. CC {ECO:0000255|HAMAP-Rule:MF_01411}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01411}. CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP- CC Rule:MF_01411}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22389.1; -; Genomic_DNA. DR PIR; G64157; G64157. DR RefSeq; NP_438889.1; NC_000907.1. DR RefSeq; WP_010869043.1; NC_000907.1. DR ProteinModelPortal; P44846; -. DR STRING; 71421.HI0730; -. DR EnsemblBacteria; AAC22389; AAC22389; HI_0730. DR GeneID; 949761; -. DR KEGG; hin:HI0730; -. DR PATRIC; 20190097; VBIHaeInf48452_0764. DR eggNOG; ENOG4105E7H; Bacteria. DR eggNOG; COG1452; LUCA. DR KO; K04744; -. DR OMA; DYSHLDW; -. DR OrthoDB; EOG6SZ1CP; -. DR PhylomeDB; P44846; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro. DR GO; GO:0010033; P:response to organic substance; IEA:InterPro. DR HAMAP; MF_01411; LPS_assembly_LptD; 1. DR InterPro; IPR020889; LipoPS_assembly_LptD. DR InterPro; IPR005653; OstA-like_N. DR InterPro; IPR007543; OstA_C. DR Pfam; PF03968; OstA; 1. DR Pfam; PF04453; OstA_C; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal. FT SIGNAL 1 23 {ECO:0000255|HAMAP-Rule:MF_01411}. FT CHAIN 24 782 LPS-assembly protein LptD. FT /FTId=PRO_0000020281. SQ SEQUENCE 782 AA; 90084 MW; E73C8A5786B02D1B CRC64; MNKKHTLISL AILTALYSQQ SLADLHEQCL MGVPKFSGEV VTGDVNALPV YIEADNAEIN QPNDATYQGN VDLKQGNRHL LAQSVQVKQS GNQSTPLRMA YVRNGFDYKD NQINMLGKDA EFNLDSHDGN LTNSEYEFVG RQGRGKADNI TLHNNYRVMK NATFTSCLHG DNAWAVDASE IRQYVKEEYA EMWHARFKIH GVPVFYTPYL QLPIGDRRRS GLLIPSAGTS SQDGLWYAQP IYWNIAPNYD LTFTPKYMSR RGWQANGEFR YLTSIGEGKV AGEYLGKVRY SEYASDNRKR HLFYWNHNSS FLQNWRLNIN YTRVSDKRYF NDFDSIYGRS TDGYANQYAR IAYYQPNYNF SLSAHQFQIF DDIVNIGPYR AVPQLDFNYH KYDLANGWLN FKLHSQAVRF DNDSKLMPTA WRFHAEPSLN SLMSNKYGSL NIETKLYATR YEQKKGSGKN AEDVQKTVNR VIPQFKVDLQ SVLARDITFL KEYTQTFEPH VQYLYRPYRN QSNIGSTLNN DYLGFGYDSA LVQQDYYSLF RDRRYSGLDR ISSANQVTLG GTTRFYDIAG EERFNLSAGQ IYYLSNSRID ENPANKTPTS SSAWALESNW KISNKWYWRG SYQFDTHTNS TSLANTSLEY NPEKNNLIQL NYRYANQEYI DQNLGKSANA YQQDIQQVGL VVGWEIANNW AVVGRYYQDL ALQKPVEQYL GVQYNSCCWA ASVGVKRNVT NHQNQTRNEI VYDNSIGITL ELRGLGSNDH QSGIQEMLEK GKLPYIRAFS LD // ID LPTE_HAEIN Reviewed; 167 AA. AC Q57457; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 2. DT 11-NOV-2015, entry version 90. DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000255|HAMAP-Rule:MF_01186}; DE Flags: Precursor; GN Name=lptE {ECO:0000255|HAMAP-Rule:MF_01186}; GN OrderedLocusNames=HI_0922; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Together with LptD, is involved in the assembly of CC lipopolysaccharide (LPS) at the surface of the outer membrane. CC Required for the proper assembly of LptD. Binds LPS and may serve CC as the LPS recognition site at the outer membrane. CC {ECO:0000255|HAMAP-Rule:MF_01186}. CC -!- SUBUNIT: Component of the lipopolysaccharide transport and CC assembly complex. Interacts with LptD. {ECO:0000255|HAMAP- CC Rule:MF_01186}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01186}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01186}. CC -!- SIMILARITY: Belongs to the LptE lipoprotein family. CC {ECO:0000255|HAMAP-Rule:MF_01186}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22582.1; -; Genomic_DNA. DR PIR; I64102; I64102. DR RefSeq; NP_439082.2; NC_000907.1. DR RefSeq; WP_005659127.1; NC_000907.1. DR ProteinModelPortal; Q57457; -. DR STRING; 71421.HI0922; -. DR EnsemblBacteria; AAC22582; AAC22582; HI_0922. DR GeneID; 950738; -. DR KEGG; hin:HI0922; -. DR PATRIC; 20190499; VBIHaeInf48452_0963. DR eggNOG; COG2980; LUCA. DR KO; K03643; -. DR OMA; RKLLTVH; -. DR OrthoDB; EOG67DPND; -. DR PhylomeDB; Q57457; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01186; LPS_assembly_LptE; 1. DR InterPro; IPR007485; LPS_assembly_LptE. DR Pfam; PF04390; LptE; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|HAMAP-Rule:MF_01186}. FT CHAIN 20 167 LPS-assembly lipoprotein LptE. FT /FTId=PRO_0000018186. FT LIPID 20 20 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_01186}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_01186}. SQ SEQUENCE 167 AA; 19270 MW; 38482542AA46651E CRC64; MINSIKTLLL IATLAILSAC GWHFQQSVTM PSEWRTLALE SDDSYNDFTV IMRRKLQENQ VNVVNLEQNI PILRINKQIT SDQVASIFKH GREAEKLLML EVEATFRLAN GESYPINAKV NRTFFDNARA ALAKSEEREV IWNDMREQVA RQLIVKIIAL QNQIKRK // ID LYXK_HAEIN Reviewed; 485 AA. AC P44991; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Probable L-xylulose kinase; DE Short=L-xylulokinase; DE EC=2.7.1.53; GN Name=lyx; Synonyms=lyxK, sgbK; OrderedLocusNames=HI_1027; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-xylulose = ADP + L-xylulose 5- CC phosphate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FGGY 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; L42023; AAC22687.1; -; Genomic_DNA. DR PIR; H64164; H64164. DR RefSeq; NP_439187.1; NC_000907.1. DR RefSeq; WP_010869108.1; NC_000907.1. DR ProteinModelPortal; P44991; -. DR STRING; 71421.HI1027; -. DR EnsemblBacteria; AAC22687; AAC22687; HI_1027. DR GeneID; 949892; -. DR KEGG; hin:HI1027; -. DR PATRIC; 20190717; VBIHaeInf48452_1071. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00880; -. DR OMA; TWCVNAV; -. DR OrthoDB; EOG6KDKMT; -. DR PhylomeDB; P44991; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008744; F:L-xylulokinase activity; IEA:UniProtKB-EC. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 485 Probable L-xylulose kinase. FT /FTId=PRO_0000059561. SQ SEQUENCE 485 AA; 54965 MW; 8E63C56CB775A66D CRC64; MHYYLGIDCG GTFIKAAIFD QNGTLQSIAR RNIPIISEKP GYAERDMDEL WNLCAQVIQK TIRQSSILPQ QIKAIGISAQ GKGAFFLDKD NKPLGRAILS SDQRAYEIVQ CWQKENILQK FYPITLQTLW MGHPVSILRW IKENEPSRYE QIHTILMSHD YLRFCLTEKL YCEETNISES NFYNMREGKY DIQLAKLFGI TECIDKLPPI IKSNKIAGYV TSRAAEQSGL VEGIPVVGGL FDVVSTALCA DLKDDQHLNV VLGTWSVVSG VTHYIDDNQT IPFVYGKYPE KNKFIIHEAS PTSAGNLEWF VNQFNLPNYD DINHEIAKLK PASSSVLFAP FLYGSNAKLG MQAGFYGIQS HHTQIHLLQA IYEGVIFSLM SHLERMQVRF PNASTVRVTG GPAKSEVWMQ MLADISGMRL EIPNIEETGC LGAALMAMQA ESAVEISQIL NIDRKIFLPD KNQYSKYQHK YHRYLKFIEA LKNLD // ID MAO2_HAEIN Reviewed; 756 AA. AC P43837; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=NADP-dependent malic enzyme; DE Short=NADP-ME; DE EC=1.1.1.40; GN Name=maeB; OrderedLocusNames=HI_1245; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) + CC NADPH. CC -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000250}; CC -!- SIMILARITY: In the N-terminal section; belongs to the malic CC enzymes family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate CC acetyltransferase and 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; L42023; AAC22896.1; -; Genomic_DNA. DR PIR; F64112; F64112. DR RefSeq; NP_439401.1; NC_000907.1. DR RefSeq; WP_005694306.1; NC_000907.1. DR ProteinModelPortal; P43837; -. DR STRING; 71421.HI1245; -. DR PRIDE; P43837; -. DR EnsemblBacteria; AAC22896; AAC22896; HI_1245. DR GeneID; 949562; -. DR KEGG; hin:HI1245; -. DR PATRIC; 20191169; VBIHaeInf48452_1297. DR eggNOG; ENOG4105C6K; Bacteria. DR eggNOG; COG0280; LUCA. DR eggNOG; COG0281; LUCA. DR KO; K00029; -. DR OMA; DIMPDSP; -. DR OrthoDB; EOG6QCD9W; -. DR PhylomeDB; P43837; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro. DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR012188; ME_PTA. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR002505; PTA_PTB. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; Malic_M; 1. DR Pfam; PF01515; PTA_PTB; 1. DR PIRSF; PIRSF036684; ME_PTA; 1. DR SMART; SM01274; malic; 1. DR SMART; SM00919; Malic_M; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Multifunctional enzyme; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 756 NADP-dependent malic enzyme. FT /FTId=PRO_0000160243. FT NP_BIND 76 83 NADP. {ECO:0000250}. FT REGION 1 428 Malic enzyme. FT REGION 429 756 Phosphate acetyltransferase. FT ACT_SITE 94 94 Proton acceptor. {ECO:0000250}. FT METAL 136 136 Divalent metal cation. {ECO:0000250}. FT METAL 137 137 Divalent metal cation. {ECO:0000250}. FT BINDING 162 162 NAD. {ECO:0000250}. FT BINDING 288 288 NAD. {ECO:0000250}. SQ SEQUENCE 756 AA; 81880 MW; 8D303736F08B8E3B CRC64; MTEQLRQAAL DFHEFPIPGK IEVTPTKSLA TQRDLALAYS PGVAEPCLEI EKDPAASYKY TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGINVFDIE VNEHDPDKLV DIIASLEPTF GGVNLEDIKA PECFYIEQKL RERMNIPVFH DDQHGTAIIS AAAIINSLRI VGKKIEDVRL VASGAGAASI ACLNLLLSLG MKRENITVCD SKGVVYKGRD DKMDQTKKEY AIEDNGWRKL ADAIPNADIF LGCSAAGALT QDMVKSMAAH PIILALANPN PEITPPEAKA VRPDAIVCTG RSDYPNQVNN VLCFPFIFRG ALDVGATTIN EEMKRAAVYA IADLALEEQN EVVTSAYGGE GATFGADYVI PRPFDPRLIV RIAPAVAKAA MESGVATRPI QNWDAYVEKL TQFVYKTSLF MRPIFSQAKS AKQRIILAEG EENKALHATQ EVISMGLANP ILIGRRSVIE EKIKKLGLRL TAGVDFEIVD NEDNPRYEEC WKHYYELTKR KGITPAIAKR VVRSNTTVLA STLLSLGYAD ALVCGLFGSY GKHLASIRDI IGLKDGVKTA AALNSLVLPT GNVFLTDTHV NSNPTAEELA EITLMAAEEI HRFGIEPAVA LLSHSNFGSS DSLGAPKMRE VLQIVKERNP HLMIDGEMRG DLAMNEAHRK ELMPDSPLKG SANLLVFPDL SASRISYSLL RGTTTAITVG PILMGMNKSA HILNPGASVR RIINMIAYAA VKAQQE // ID LPXC_HAEIN Reviewed; 305 AA. AC P45070; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; DE Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; DE EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388}; DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388}; GN Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388}; Synonyms=envA; GN OrderedLocusNames=HI_1144; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and CC acetate, the committed step in lipid A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00388}. CC -!- CATALYTIC ACTIVITY: UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N- CC acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3- CC hydroxytetradecanoyl)-alpha-D-glucosamine + acetate. CC {ECO:0000255|HAMAP-Rule:MF_00388}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388}; CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid CC IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and CC UDP-N-acetyl-alpha-D-glucosamine: step 2/6. {ECO:0000255|HAMAP- CC Rule:MF_00388}. CC -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP- CC Rule:MF_00388}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22799.1; -; Genomic_DNA. DR PIR; A64186; A64186. DR RefSeq; NP_439302.1; NC_000907.1. DR RefSeq; WP_005693459.1; NC_000907.1. DR ProteinModelPortal; P45070; -. DR SMR; P45070; 1-294. DR STRING; 71421.HI1144; -. DR EnsemblBacteria; AAC22799; AAC22799; HI_1144. DR GeneID; 950276; -. DR KEGG; hin:HI1144; -. DR PATRIC; 20190963; VBIHaeInf48452_1194. DR eggNOG; ENOG4105C7C; Bacteria. DR eggNOG; COG0774; LUCA. DR KO; K02535; -. DR OMA; NSMLVKA; -. DR OrthoDB; EOG6PGK74; -. DR PhylomeDB; P45070; -. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1700.10; -; 1. DR Gene3D; 3.30.230.20; -; 1. DR HAMAP; MF_00388; LpxC; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR004463; UDP-acyl_GlcNac_deAcase. DR InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C. DR InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N. DR Pfam; PF03331; LpxC; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR TIGRFAMs; TIGR00325; lpxC; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 305 UDP-3-O-acyl-N-acetylglucosamine FT deacetylase. FT /FTId=PRO_0000191934. FT ACT_SITE 265 265 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00388}. FT METAL 79 79 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00388}. FT METAL 238 238 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00388}. FT METAL 242 242 Zinc. {ECO:0000255|HAMAP-Rule:MF_00388}. SQ SEQUENCE 305 AA; 34103 MW; 89D997A79471D2F0 CRC64; MIKQRTLKQS IKVTGVGLHS GEKVTLTLRP AMPNTGVVYY RTDLNPAVAF PADPNSVRDT MLCTALINEQ GVRISTVEHL NAALAGLGID NIIIEVDAPE IPIMDGSASP FIYLLLDAGI EEQNAAKKFI RIKQYVRVED GDKWAEFKPY NGFRLDFTID FDHPAIGKDV RNYEMNFSAQ AFVHQISRAR TFGFMKDIEY LQSQGLVLGG SLDNAIVLDD YRILNEDGLR FKDELVRHKM LDAIGDLYMA GYNIIGDFKA YKSGHGLNNK LLRAVLANQE AWEFVTFEDK AQVPQGYVAP VQVLI // ID LPXD_HAEIN Reviewed; 341 AA. AC P43888; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523}; DE EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_00523}; GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; GN OrderedLocusNames=HI_0915; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine CC using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the CC biosynthesis of lipid A, a phosphorylated glycolipid that anchors CC the lipopolysaccharide to the outer membrane of the cell. CC {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + CC UDP-3-O-acyl-alpha-D-glucosamine = UDP-2,3-diacyl-alpha-D- CC glucosamine + [acyl-carrier-protein]. {ECO:0000255|HAMAP- CC Rule:MF_00523}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC LpxD subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22573.1; -; Genomic_DNA. DR PIR; D64102; D64102. DR RefSeq; NP_439075.1; NC_000907.1. DR RefSeq; WP_005693262.1; NC_000907.1. DR ProteinModelPortal; P43888; -. DR STRING; 71421.HI0915; -. DR EnsemblBacteria; AAC22573; AAC22573; HI_0915. DR GeneID; 949919; -. DR KEGG; hin:HI0915; -. DR PATRIC; 20190485; VBIHaeInf48452_0956. DR eggNOG; ENOG4105D7M; Bacteria. DR eggNOG; COG1044; LUCA. DR KO; K02536; -. DR OMA; WANVTLY; -. DR OrthoDB; EOG6JB11D; -. DR PhylomeDB; P43888; -. DR UniPathway; UPA00973; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00523; LpxD; 1. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR007691; LpxD. DR InterPro; IPR011004; Trimer_LpxA-like. DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep. DR Pfam; PF00132; Hexapep; 3. DR Pfam; PF04613; LpxD; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 3. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Lipid A biosynthesis; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat; KW Transferase. FT CHAIN 1 341 UDP-3-O-acylglucosamine N- FT acyltransferase. FT /FTId=PRO_0000059677. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00523}. SQ SEQUENCE 341 AA; 36036 MW; 63CCA7EADFC64D19 CRC64; MQKSYSLQEL ATQIGATVRG NTDVVVENIA PLDKAQSNQL TFISNVKFRV LLKDSKAGIL IVSEEDVEHC SPESNLLIVK DPYVAYAILA QYMDSTPKAA QGIAKSAVIF DGVLLGENVS IGANAVIEEG VVLGDNVIIG ANCFVGKNTK IGSGTQLWAN VTVYHNVEIG ANCLIQSGTV IGSDGFGYAN DRGRWIKIPQ VGQVIIGNNV EIGANTCIDR GALDATIIED NVIIDNLCQI AHNVHIGTGT AVAGGVIMAG SLTVGRYCLI GGASVINGHM EICDKVTITG MGMVMRPITE PGVYSSGIPL QTNKEWRKTA ALTLGIDGIN KRLKALEKKI S // ID MATP_HAEIN Reviewed; 148 AA. AC P44161; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Macrodomain Ter protein {ECO:0000255|HAMAP-Rule:MF_01073}; GN Name=matP {ECO:0000255|HAMAP-Rule:MF_01073}; GN OrderedLocusNames=HI_1323; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for spatial organization of the terminus region CC of the chromosome (Ter macrodomain) during the cell cycle. CC Prevents early segregation of duplicated Ter macrodomains during CC cell division. Binds specifically to matS, which is a 13 bp CC signature motif repeated within the Ter macrodomain. CC {ECO:0000255|HAMAP-Rule:MF_01073}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01073}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01073}. CC -!- SIMILARITY: Belongs to the MatP family. {ECO:0000255|HAMAP- CC Rule:MF_01073}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22968.1; -; Genomic_DNA. DR PIR; H64025; H64025. DR RefSeq; NP_439474.1; NC_000907.1. DR RefSeq; WP_005628871.1; NC_000907.1. DR STRING; 71421.HI1323; -. DR EnsemblBacteria; AAC22968; AAC22968; HI_1323. DR GeneID; 950258; -. DR KEGG; hin:HI1323; -. DR PATRIC; 20191329; VBIHaeInf48452_1375. DR eggNOG; ENOG4108R9Q; Bacteria. DR eggNOG; COG3120; LUCA. DR KO; K09911; -. DR OMA; MSTLKQD; -. DR OrthoDB; EOG68DD08; -. DR PhylomeDB; P44161; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01073; MatP; 1. DR InterPro; IPR009390; MatP. DR Pfam; PF06303; MatP; 1. DR ProDom; PD033720; DUF1047; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 148 Macrodomain Ter protein. FT /FTId=PRO_0000070351. SQ SEQUENCE 148 AA; 17997 MW; F400CFE7A4958314 CRC64; MKYQKLENQE ANWKWIYLIR KHREGENITR YEERSLQEAK AQELLESQNY PEKIEEWIKN HLSPALPIKL DQAIRARRKR FFNGEKQHTK KKSIDLEYAV WLRLSKYSRK MKMTLSETIT YMIDERESKA QFENQMAAMK TSLKNLLK // ID MDAB_HAEIN Reviewed; 192 AA. AC P44803; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 75. DE RecName: Full=Modulator of drug activity B homolog; GN Name=mdaB; Synonyms=mda66; OrderedLocusNames=HI_0648; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli MadB and S.pombe SPAC5H10.05c. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22308.1; 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; L42023; AAC22308.1; ALT_INIT; Genomic_DNA. DR PIR; C64084; C64084. DR RefSeq; NP_438808.2; NC_000907.1. DR RefSeq; WP_005694496.1; NC_000907.1. DR ProteinModelPortal; P44803; -. DR SMR; P44803; 1-192. DR STRING; 71421.HI0648; -. DR EnsemblBacteria; AAC22308; AAC22308; HI_0648. DR GeneID; 949679; -. DR KEGG; hin:HI0648; -. DR PATRIC; 20189911; VBIHaeInf48452_0677. DR eggNOG; ENOG4105NF4; Bacteria. DR eggNOG; COG2249; LUCA. DR KO; K03923; -. DR OMA; PTFICND; -. DR OrthoDB; EOG6ZWJFM; -. DR PhylomeDB; P44803; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 192 Modulator of drug activity B homolog. FT /FTId=PRO_0000096315. SQ SEQUENCE 192 AA; 21876 MW; 3ACF977F06A4BF0F CRC64; MNILLLDGGK AFGHSHGELN HTLHKKAKEV LTALGHNVKE TVIDAGYDVE AEIEKFLWMD AVIWQMPSWW MHEPWTVKKY IDEVLTNGHG KLYHSDGRHS VNPTEGYGTG GLLQGKKHML SLTWNAPIEA FTREGDFFEG KGVDVLYMHF HKLNEFLGLT RLPTFLCNDV VKSPQVEQYL ADYQAHLEKV FG // ID MDH_HAEIN Reviewed; 311 AA. AC P44427; Q7WRT7; Q83V59; Q83V60; Q99Q89; Q99Q90; Q99QA9; Q9AMQ2; AC Q9AMQ3; Q9AMQ4; Q9AMQ5; Q9AMQ6; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 120. DE RecName: Full=Malate dehydrogenase; DE EC=1.1.1.37; GN Name=mdh; OrderedLocusNames=HI_1210; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195. RC STRAIN=1124, 1158, 1181, 1209, 375, 477, 667, 723, a1042, a6062, RC a6064, a6073, a7190, a7205, b1324, b6107, b7017, b7109, b7651, b7717, RC Beagan, c1271, c6132, c6134, c7424, c8032, d6137, Drm118, e6158, RC e6181, e6229, e7066, f6237, f6252, f7283, and f7290; RX PubMed=11136255; DOI=10.1073/pnas.98.1.182; RA Feil E.J., Holmes E.C., Bessen D.E., Chan M.-S., Day N.P.J., RA Enright M.C., Goldstein R., Hood D.W., Kalia A., Moore C.E., Zhou J., RA Spratt B.G.; RT "Recombination within natural populations of pathogenic bacteria: RT Short-term empirical estimates and long-term phylogenetic RT consequences."; RL Proc. Natl. Acad. Sci. U.S.A. 98:182-187(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195. RC STRAIN=1008, 1180, 1200, 1207, 1231, 1233, 1247, 1268, 162, 176, 285, RC 432, 486, and 981; RX PubMed=12797973; DOI=10.1016/S1567-1348(02)00152-1; RA Cody A.J., Field D., Feil E.J., Stringer S., Deadman M.E., RA Tsolaki A.G., Gratz B., Bouchet V., Goldstein R., Hood D.W., RA Moxon E.R.; RT "High rates of recombination in otitis media isolates of non-typeable RT Haemophilus influenzae."; RL Infect. Genet. Evol. 3:57-66(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195. RC STRAIN=767, 769, 773, 788, 794, 795, 796, and 800; RX PubMed=12843045; DOI=10.1128/JCM.41.7.3064-3069.2003; RA O'Neill J.M., St Geme J.W. III, Cutter D., Adderson E.E., Anyanwu J., RA Jacobs R.F., Schutze G.E.; RT "Invasive disease due to nontypeable Haemophilus influenzae among RT children in Arkansas."; RL J. Clin. Microbiol. 41:3064-3069(2003). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-195. RC STRAIN=BR134, BR229, BR355, BR48, and BRC1-13; RX PubMed=12800772; RA Platonov A.E., Mironov K.O., Iatsyshina S.B., Koroleva I.S., RA Platonova O.V., Gushchin A.E., Shipulin G.A.; RT "Multilocus sequence-typing for characterization of Moscow strains of RT Haemophilus influenzae type b."; RL Mol. Genet. Mikrobiol. Virusol. 2:21-25(2003). CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to CC oxaloacetate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22864.1; -; Genomic_DNA. DR EMBL; AF322740; AAK11394.1; -; Genomic_DNA. DR EMBL; AF322741; AAK11395.1; -; Genomic_DNA. DR EMBL; AF322742; AAK11396.1; -; Genomic_DNA. DR EMBL; AF322743; AAK11397.1; -; Genomic_DNA. DR EMBL; AF322744; AAK11398.1; -; Genomic_DNA. DR EMBL; AF322745; AAK11399.1; -; Genomic_DNA. DR EMBL; AF322746; AAK11400.1; -; Genomic_DNA. DR EMBL; AF322747; AAK11401.1; -; Genomic_DNA. DR EMBL; AF322748; AAK11402.1; -; Genomic_DNA. DR EMBL; AF322749; AAK11403.1; -; Genomic_DNA. DR EMBL; AF322750; AAK11404.1; -; Genomic_DNA. DR EMBL; AF322751; AAK11405.1; -; Genomic_DNA. DR EMBL; AF322752; AAK11406.1; -; Genomic_DNA. DR EMBL; AF322753; AAK11407.1; -; Genomic_DNA. DR EMBL; AF322754; AAK11408.1; -; Genomic_DNA. DR EMBL; AF322755; AAK11409.1; -; Genomic_DNA. DR EMBL; AF322756; AAK11410.1; -; Genomic_DNA. DR EMBL; AF322757; AAK11411.1; -; Genomic_DNA. DR EMBL; AF322758; AAK11412.1; -; Genomic_DNA. DR EMBL; AF322759; AAK11413.1; -; Genomic_DNA. DR EMBL; AF322760; AAK11414.1; -; Genomic_DNA. DR EMBL; AF322761; AAK11415.1; -; Genomic_DNA. DR EMBL; AF322762; AAK11416.1; -; Genomic_DNA. DR EMBL; AF322763; AAK11417.1; -; Genomic_DNA. DR EMBL; AF322764; AAK11418.1; -; Genomic_DNA. DR EMBL; AF322765; AAK11419.1; -; Genomic_DNA. DR EMBL; AF322766; AAK11420.1; -; Genomic_DNA. DR EMBL; AF322767; AAK11421.1; -; Genomic_DNA. DR EMBL; AF322768; AAK11422.1; -; Genomic_DNA. DR EMBL; AF322769; AAK11423.1; -; Genomic_DNA. DR EMBL; AF322770; AAK11424.1; -; Genomic_DNA. DR EMBL; AF322771; AAK11425.1; -; Genomic_DNA. DR EMBL; AF322772; AAK11426.1; -; Genomic_DNA. DR EMBL; AF322773; AAK11427.1; -; Genomic_DNA. DR EMBL; AF322774; AAK11428.1; -; Genomic_DNA. DR EMBL; AF322775; AAK11429.1; -; Genomic_DNA. DR EMBL; AF322776; AAK11430.1; -; Genomic_DNA. DR EMBL; AF536037; AAP19893.1; -; Genomic_DNA. DR EMBL; AF536038; AAP19894.1; -; Genomic_DNA. DR EMBL; AF536039; AAP19895.1; -; Genomic_DNA. DR EMBL; AF536040; AAP19896.1; -; Genomic_DNA. DR EMBL; AF536041; AAP19897.1; -; Genomic_DNA. DR EMBL; AF536042; AAP19898.1; -; Genomic_DNA. DR EMBL; AF536043; AAP19899.1; -; Genomic_DNA. DR EMBL; AF536044; AAP19900.1; -; Genomic_DNA. DR EMBL; AF536045; AAP19901.1; -; Genomic_DNA. DR EMBL; AF536046; AAP19902.1; -; Genomic_DNA. DR EMBL; AF536047; AAP19903.1; -; Genomic_DNA. DR EMBL; AF536048; AAP19904.1; -; Genomic_DNA. DR EMBL; AF536049; AAP19905.1; -; Genomic_DNA. DR EMBL; AF536050; AAP19906.1; -; Genomic_DNA. DR EMBL; AY245392; AAP74406.1; -; Genomic_DNA. DR EMBL; AY245393; AAP74407.1; -; Genomic_DNA. DR EMBL; AY245394; AAP74408.1; -; Genomic_DNA. DR EMBL; AY245395; AAP74409.1; -; Genomic_DNA. DR EMBL; AY245396; AAP74410.1; -; Genomic_DNA. DR EMBL; AY245397; AAP74411.1; -; Genomic_DNA. DR EMBL; AY245398; AAP74412.1; -; Genomic_DNA. DR EMBL; AY245399; AAP74413.1; -; Genomic_DNA. DR EMBL; AF525726; AAM91960.1; -; Genomic_DNA. DR EMBL; AF525727; AAM91961.1; -; Genomic_DNA. DR EMBL; AF525728; AAM91962.1; -; Genomic_DNA. DR EMBL; AF525729; AAM91963.1; -; Genomic_DNA. DR EMBL; AF525730; AAM91964.1; -; Genomic_DNA. DR PIR; C64110; C64110. DR RefSeq; NP_439366.1; NC_000907.1. DR RefSeq; WP_005694235.1; NC_000907.1. DR ProteinModelPortal; P44427; -. DR SMR; P44427; 1-310. DR STRING; 71421.HI1210; -. DR PRIDE; P44427; -. DR EnsemblBacteria; AAC22864; AAC22864; HI_1210. DR GeneID; 950148; -. DR KEGG; hin:HI1210; -. DR PATRIC; 20191099; VBIHaeInf48452_1262. DR eggNOG; ENOG4105C80; Bacteria. DR eggNOG; COG0039; LUCA. DR KO; K00024; -. DR OMA; VEVKGFA; -. DR OrthoDB; EOG6091FG; -. DR PhylomeDB; P44427; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR HAMAP; MF_01516; Malate_dehydrog_1; 1. DR InterPro; IPR001557; L-lactate/malate_DH. 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; IPR001252; Malate_DH_AS. DR InterPro; IPR010097; Malate_DH_type1. DR InterPro; IPR023958; Malate_DH_type1_bac. 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 SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1. DR PROSITE; PS00068; MDH; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 311 Malate dehydrogenase. FT /FTId=PRO_0000113306. FT NP_BIND 7 13 NAD. {ECO:0000250}. FT NP_BIND 117 119 NAD. {ECO:0000250}. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000250}. FT BINDING 34 34 NAD. {ECO:0000250}. FT BINDING 81 81 Substrate. {ECO:0000250}. FT BINDING 87 87 Substrate. {ECO:0000250}. FT BINDING 94 94 NAD. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000250}. FT BINDING 153 153 Substrate. {ECO:0000250}. FT BINDING 227 227 NAD. {ECO:0000250}. FT VARIANT 63 63 P -> L (in strain: 767 and 794). FT VARIANT 64 64 T -> I (in strain: 432). FT VARIANT 66 66 A -> T (in strain: 1124). FT VARIANT 107 108 VT -> TI (in strain: 773, 796 and 1231). FT VARIANT 107 107 V -> I (in strain: 162, 375, 723, 788, FT 800, 1008, 1124, 1158, 1180, 1181, 1207, FT 1233, 1247, a6062, e6158, e6229, e7066, FT f6237 and 1209). FT VARIANT 107 107 V -> T (in strain: a7205, BR355 and FT e6181). FT VARIANT 128 128 A -> V (in strain: c6132). FT VARIANT 135 135 A -> S (in strain: a7205). FT VARIANT 163 163 G -> D (in strain: f6252). FT VARIANT 193 193 K -> E (in strain: 176, 667, a7205, FT b7017, c1271, c6134, c7424 and c8032). SQ SEQUENCE 311 AA; 32543 MW; 1311441B90E4EA2C CRC64; MKVAVLGAAG GIGQALALLL KLQLPAGTDL SLYDIAPVTP GVAVDVSHIP TAVNVKGFSG EDPTPALEGA DVVLISAGVA RKPGMDRSDL FNINAGIVRG LIEKVAVTCP KACVGIITNP VNTTVAIAAE VLKKAGVYDK RKLFGVTTLD VLRSETFVAE LKGLNVSRTS VPVIGGHSGV TILPLLSQVQ YAKWNEDEIE PLTKRIQNAG TEVLNAKAGG GSATLSMAQA AARFARSLVK GLSGETVVEC TYVEGDGKYA RFFSQPVRLG KEGVEEILPI GPLSNFEQQA LENMLPTLRA DIELGEKFIN G // ID LST_HAEIN Reviewed; 304 AA. AC Q48211; O05084; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 20-JAN-2016, entry version 78. DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase; DE Short=Alpha 2,3-ST; DE Short=Beta-galactoside alpha-2,3-sialyltransferase; DE EC=2.4.99.-; DE AltName: Full=Lipooligosaccharide sialyltransferase; GN Name=lst; OrderedLocusNames=HI_1699; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfers sialic acid from the substrate CMP-sialic acid CC donor to the terminal beta-D-galactosyl-1,4-acetyl-beta-D- CC glucosamine on the lacto-N-neotetraose branch of the CC lipooligosaccharide. CC -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl- CC 1,4-acetyl-beta-D-glucosamine = CMP + alpha-N-acetylneuraminyl- CC 2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 52 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; M94855; AAA24979.1; -; Genomic_DNA. DR EMBL; L42023; AAC23345.1; -; Genomic_DNA. DR PIR; G64175; G64175. DR RefSeq; NP_439841.1; NC_000907.1. DR STRING; 71421.HI1699; -. DR CAZy; GT52; Glycosyltransferase Family 52. DR EnsemblBacteria; AAC23345; AAC23345; HI_1699. DR GeneID; 950520; -. DR KEGG; hin:HI1699; -. DR PATRIC; 20192149; VBIHaeInf48452_1778. DR eggNOG; ENOG4105P7J; Bacteria. DR eggNOG; ENOG4111XG2; LUCA. DR KO; K00785; -. DR OMA; CCTPLQV; -. DR OrthoDB; EOG6MD922; -. DR UniPathway; UPA00030; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR012477; Glyco_transf_52. DR Pfam; PF07922; Glyco_transf_52; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 304 CMP-N-acetylneuraminate-beta- FT galactosamide-alpha-2,3- FT sialyltransferase. FT /FTId=PRO_0000080571. FT CONFLICT 4 4 M -> I (in Ref. 1; AAA24979). FT {ECO:0000305}. FT CONFLICT 68 68 F -> S (in Ref. 1; AAA24979). FT {ECO:0000305}. FT CONFLICT 130 130 G -> D (in Ref. 1; AAA24979). FT {ECO:0000305}. FT CONFLICT 220 220 Y -> C (in Ref. 1; AAA24979). FT {ECO:0000305}. SQ SEQUENCE 304 AA; 35706 MW; B6D03890AC1CDD28 CRC64; MNLMLCCTPL QVLIARKIIE LHPNEQFFGV MFGGVWDKKR TLYASKLAEV CSDSMNIDTG KDLKGFDFLK LMRQLKNKIT HKGFDKVFLA NLNSLWLQTY LSHVSFKELY TFDDGSDNIF PHPNLLREPG TFKYKLIKAF IGDKYSVNKL FKKIKKHYTV YPNYKNIVSN IEPISLWDNQ IDCEIDGEVS FFIGQPLLNT KEENISLIKK LKDQIPFDYY FPHPAEDYRV DGVNYVESEL IFEDYVFKHL SNKKIIIYTF FSSVAFNLLS HPNVEIRFIR TSIPRWQFCY DSFPDLGLTI YKEI // ID MALQ_HAEIN Reviewed; 699 AA. AC P45176; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=4-alpha-glucanotransferase; DE EC=2.4.1.25; DE AltName: Full=Amylomaltase; DE AltName: Full=Disproportionating enzyme; DE Short=D-enzyme; GN Name=malQ; OrderedLocusNames=HI_1356; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan CC to a new position in an acceptor, which may be glucose or a CC (1->4)-alpha-D-glucan. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the disproportionating 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; L42023; AAC23003.1; -; Genomic_DNA. DR PIR; H64118; H64118. DR RefSeq; NP_439507.1; NC_000907.1. DR RefSeq; WP_005694004.1; NC_000907.1. DR ProteinModelPortal; P45176; -. DR STRING; 71421.HI1356; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR EnsemblBacteria; AAC23003; AAC23003; HI_1356. DR GeneID; 950287; -. DR KEGG; hin:HI1356; -. DR PATRIC; 20191397; VBIHaeInf48452_1409. DR eggNOG; ENOG4107RTM; Bacteria. DR eggNOG; COG1640; LUCA. DR KO; K00705; -. DR OMA; WASPYSS; -. DR OrthoDB; EOG6SR926; -. DR PhylomeDB; P45176; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.80; -; 2. DR InterPro; IPR003385; Glyco_hydro_77. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF02446; Glyco_hydro_77; 1. DR SUPFAM; SSF51445; SSF51445; 2. DR TIGRFAMs; TIGR00217; malQ; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Glycosyltransferase; Reference proteome; Transferase. FT CHAIN 1 699 4-alpha-glucanotransferase. FT /FTId=PRO_0000170126. SQ SEQUENCE 699 AA; 80252 MW; 80D6E1D51EC2E1E9 CRC64; MVSMQISDSL KQKAEKCGIA LSHYDIDGHL IFADEKTVST FVELLQPPPK AKGQFDDVLA AFENEPIDYR LNRLDLPPSA EYRYQLTDES NAILLEKILS NLSVLSLPPL PFGYYQLSIF SDTEQYRIRL LISPKTAFQP PVLENKKVWG VNVQLYSLRS EQNWGIGDFG DLAYLIEQSA KQGADYVGIN PLHLPYPAVP NWASPYSSSS RRWLNFLYLD IPDLPEFKRC RSVQNWFKRE DIQAKIAALR ESDCVDYSSI LALKLTALEP LFDFFQRSQS VEIVTRRKIF AEYLKNKGEP LLLQGLFNVL DLQEHADHQA EENTIGWLGW RKEWQHLSAA KRKALLKTHH EKIQFFAWLQ WLTEEQLSAL QNLCKQSGMK LGIYGDLAVN SSRGSADVWS DPDLYCVNAS IGAPPDPLGP VGQNWNLPPY NPTVLKARGF APFIDMLCAN MQYFGVLRID HVMGLFRLWW IPKGKTAADG AYVHYPFDEL MAILAIESVR NECLIIGEDL GTVPDEVRWK LNEFQIFSYF VLYFAQRNGE FPRISDYPRN AYATIGTHDV PSLQSFWHCR DLELFNQLGI LNGEVLKQKY DQRVMDKQAL LNSLHRDNYL PPHYEGDALS MAMHDYLNRM IHYYLAESNS RLIGVQLENL LSQEISFNLP STSNEYPNWC KKLAQPLAFI FSNEALKTFF VQINQGRNV // ID MENC_HAEIN Reviewed; 329 AA. AC P44961; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 20-JAN-2016, entry version 104. DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470}; DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470}; DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470}; DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470}; GN Name=menC {ECO:0000255|HAMAP-Rule:MF_00470}; GN OrderedLocusNames=HI_0969; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). CC {ECO:0000255|HAMAP-Rule:MF_00470}. CC -!- CATALYTIC ACTIVITY: (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4- CC diene-1-carboxylate = 2-succinylbenzoate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00470}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00470}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 4/7. {ECO:0000255|HAMAP-Rule:MF_00470}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00470}. CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing CC enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00470}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22626.1; 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; L42023; AAC22626.1; ALT_INIT; Genomic_DNA. DR PIR; C64105; C64105. DR RefSeq; NP_439130.2; NC_000907.1. DR ProteinModelPortal; P44961; -. DR SMR; P44961; 4-322. DR STRING; 71421.HI0969; -. DR EnsemblBacteria; AAC22626; AAC22626; HI_0969. DR GeneID; 949968; -. DR KEGG; hin:HI0969; -. DR PATRIC; 20190595; VBIHaeInf48452_1010. DR eggNOG; ENOG4105DNI; Bacteria. DR eggNOG; COG1441; LUCA. DR KO; K02549; -. DR OMA; YEANRDG; -. DR OrthoDB; EOG6VXFBR; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00165. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00470; MenC_1; 1. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR029017; Enolase_N-like. DR InterPro; IPR013342; Mandelate_racemase_C. DR InterPro; IPR001354; MR/MLE/MAL. DR InterPro; IPR010196; OSB_synthase_MenC1. DR InterPro; IPR010197; OSB_synthase_MenC_2. DR PANTHER; PTHR13794; PTHR13794; 1. DR PANTHER; PTHR13794:SF8; PTHR13794:SF8; 1. DR Pfam; PF13378; MR_MLE_C; 1. DR SMART; SM00922; MR_MLE; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Magnesium; Menaquinone biosynthesis; KW Metal-binding; Reference proteome. FT CHAIN 1 329 o-succinylbenzoate synthase. FT /FTId=PRO_0000171272. FT ACT_SITE 140 140 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00470}. FT ACT_SITE 242 242 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00470}. FT METAL 168 168 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00470}. FT METAL 197 197 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00470}. FT METAL 220 220 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00470}. SQ SEQUENCE 329 AA; 36970 MW; 26353A1B50D5FF60 CRC64; MAEKSFNLYR YSIPVDSQLI LRDRFLKRRE GLIVRVSCSR DGWGEIAPLP GFSEETLDQA QEQAIEWLTT WCNASCDAPR VPLDGTYPSV AFGISCAMDE MKGYLQAEGN YHTAPLCYGD PDELYAKLAS MEGEKVAKMK VGIYEANRDG LIADMFLEAI PDLQLRLDAN RHWSLEKALQ FAAKVKLQHR KRIQFLEEPC KTQALSREFA VQTDIAIAWD ESVREPNFCL EKEPHLSAVV IKPTLIGSIQ RCTELINQAH SLGLKAVISS SIESSLGLSQ LARIAQQYTP NVTPGLDTLD LMEYQVLRAW PSSDLPIVDL ESEFITKII // ID MENH_HAEIN Reviewed; 247 AA. AC P44611; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Putative 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01660}; DE Short=SHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01660}; DE EC=4.2.99.20 {ECO:0000255|HAMAP-Rule:MF_01660}; GN Name=menH {ECO:0000255|HAMAP-Rule:MF_01660}; GN OrderedLocusNames=HI_0282; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes a proton abstraction reaction that results in CC 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6- CC hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of CC 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). CC {ECO:0000255|HAMAP-Rule:MF_01660}. CC -!- CATALYTIC ACTIVITY: 5-enolpyruvoyl-6-hydroxy-2-succinylcyclohex-3- CC ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4- CC diene-1-carboxylate + pyruvate. {ECO:0000255|HAMAP-Rule:MF_01660}. CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 3/7. {ECO:0000255|HAMAP-Rule:MF_01660}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01660}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01660}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family. CC {ECO:0000255|HAMAP-Rule:MF_01660}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21945.1; -; Genomic_DNA. DR PIR; B64147; B64147. DR RefSeq; NP_438450.1; NC_000907.1. DR RefSeq; WP_005694025.1; NC_000907.1. DR ProteinModelPortal; P44611; -. DR STRING; 71421.HI0282; -. DR ESTHER; haein-yfbb; MenH_SHCHC. DR EnsemblBacteria; AAC21945; AAC21945; HI_0282. DR GeneID; 949409; -. DR KEGG; hin:HI0282; -. DR PATRIC; 20189103; VBIHaeInf48452_0298. DR eggNOG; ENOG4107J5P; Bacteria. DR eggNOG; COG0596; LUCA. DR KO; K08680; -. DR OMA; LNDWYQQ; -. DR OrthoDB; EOG689HPM; -. DR PhylomeDB; P44611; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00900. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IBA:GO_Central. DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central. DR GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR HAMAP; MF_01660; MenH; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR022485; SHCHC_synthase_MenH. DR Pfam; PF00561; Abhydrolase_1; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR03695; menH_SHCHC; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Menaquinone biosynthesis; KW Reference proteome. FT CHAIN 1 247 Putative 2-succinyl-6-hydroxy-2,4- FT cyclohexadiene-1-carboxylate synthase. FT /FTId=PRO_0000169175. SQ SEQUENCE 247 AA; 28342 MW; 59193CF43B0949CD CRC64; MINIIFLHGL LGTKNDWQKV IENLPHFNCI ALDLPFHGQA KDLEVTNFED SAEYLAQQIK SAVKNGPYFL VGYSLGGRIA LYYALQAQLE RSNLQGVILE GANLGLKTDE EKQARFQQDF AWAQRFMQES PEKVLNDWYQ QPVFSHLTTE ERLQLVEKRK SNCGKNIGKM LLATSLSKQP DFSEKVRLSS LPFFYFCGER DHKFQVLAKE NQIDLVTIPC AGHNSHLENS KYFSKKIENC ILKIVRP // ID MEPA_HAEIN Reviewed; 286 AA. AC P44566; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 98. DE RecName: Full=Penicillin-insensitive murein endopeptidase; DE EC=3.4.24.-; DE Flags: Precursor; GN Name=mepA; OrderedLocusNames=HI_0197; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the removal of murein from the sacculus. May CC also facilitate integration of nascent murein strands into the CC sacculus by cleaving the peptide bonds between neighboring strands CC in mature murein (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Splits the D-alanyl-gamma-meso-2,6-diamino- CC pimelyl peptide bond connecting neighboring peptidoglycan strands. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M74 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; L42023; AAC21866.1; -; Genomic_DNA. DR PIR; H64053; H64053. DR RefSeq; NP_438366.1; NC_000907.1. DR RefSeq; WP_005694094.1; NC_000907.1. DR ProteinModelPortal; P44566; -. DR STRING; 71421.HI0197; -. DR MEROPS; M74.001; -. DR EnsemblBacteria; AAC21866; AAC21866; HI_0197. DR GeneID; 951103; -. DR KEGG; hin:HI0197; -. DR PATRIC; 20188891; VBIHaeInf48452_0202. DR eggNOG; ENOG4105HPZ; Bacteria. DR eggNOG; COG3770; LUCA. DR KO; K07261; -. DR OMA; VRPWWGH; -. DR OrthoDB; EOG6F295X; -. DR PhylomeDB; P44566; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.30.1380.10; -; 1. DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom. DR InterPro; IPR005073; Peptidase_M74. DR Pfam; PF03411; Peptidase_M74; 1. DR PIRSF; PIRSF018455; MepA; 1. DR SUPFAM; SSF55166; SSF55166; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Periplasm; Protease; Reference proteome; Signal; Zinc. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 286 Penicillin-insensitive murein FT endopeptidase. FT /FTId=PRO_0000028521. FT METAL 117 117 Zinc 1. {ECO:0000250}. FT METAL 120 120 Zinc 1. {ECO:0000250}. FT METAL 127 127 Zinc 1. {ECO:0000250}. FT METAL 152 152 Zinc 2. {ECO:0000250}. FT METAL 218 218 Zinc 1. {ECO:0000250}. SQ SEQUENCE 286 AA; 31652 MW; 5D9EAF5FE0F86FD2 CRC64; MNKILLKTTI IFTALFSLNV VASPLDWQKV KRPIPSEDGK ASPIGSYTNG CIIGAQALPP KGEGYQVIRM NRNRYYGHPN MIQYLERLGQ RAKAAGLPTM LVGDIAMPGG GRFLTGHASH QMGLDADIWL RMGEMSDADA LNSDGKGLLV VDRKAQRVDE RVWNSNHATL IKLAAQDPNV TRIFVNPAIK VKLCQTAGND RGWLHKIRPW HGHNSHFHVR LTCPADASYC ENQAPVPAGD GCGDELYSWF EPPKPGTSVS KPKVTPPEPF LCQQILNSPN RREWLE // ID LYSO_HAEIN Reviewed; 195 AA. AC P44201; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative lysine exporter {ECO:0000250|UniProtKB:P75826}; GN OrderedLocusNames=HI_1452; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Mediates export of lysine. CC {ECO:0000250|UniProtKB:P75826}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000255}. CC -!- SIMILARITY: Belongs to the LysO 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; L42023; AAC23105.1; -; Genomic_DNA. DR PIR; D64030; D64030. DR RefSeq; NP_439603.1; NC_000907.1. DR RefSeq; WP_005693915.1; NC_000907.1. DR STRING; 71421.HI1452; -. DR EnsemblBacteria; AAC23105; AAC23105; HI_1452. DR GeneID; 950785; -. DR KEGG; hin:HI1452; -. DR PATRIC; 20191607; VBIHaeInf48452_1513. DR eggNOG; ENOG4105DWU; Bacteria. DR eggNOG; COG2431; LUCA. DR OMA; MKGSLIV; -. DR OrthoDB; EOG6N3CR6; -. DR PhylomeDB; P44201; -. DR Proteomes; UP000000579; 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:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR InterPro; IPR005642; LysO. DR Pfam; PF03956; DUF340; 1. DR ProDom; PD022789; DUF340_prk_mem; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 195 Putative lysine exporter. FT /FTId=PRO_0000168738. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 170 190 Helical. {ECO:0000255}. SQ SEQUENCE 195 AA; 21241 MW; 56155768F992102F CRC64; MEELLSAVII GIVLGWLCKD WLHFPNGSNL YVLITLIFFV GIQLRNNGIS LKEVLLNKQG LMMGAIFTLS SLIGGVISAF FLSMPITQGL AFSSGFGWYS LSSVVLTNAW GPMQGSIAFF NDLSREILSL FLIPLFMQHY RSTAIEITGA TALDCTLPII QKSGGIEVTP IAISFGMVTN LLPPLLLVFF SSFPI // ID MAP1_HAEIN Reviewed; 268 AA. AC P44421; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. 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=HI_1722; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23368.1; -; Genomic_DNA. DR PIR; C64138; C64138. DR RefSeq; NP_439863.1; NC_000907.1. DR RefSeq; WP_005694208.1; NC_000907.1. DR ProteinModelPortal; P44421; -. DR SMR; P44421; 2-262. DR STRING; 71421.HI1722; -. DR MEROPS; M24.001; -. DR EnsemblBacteria; AAC23368; AAC23368; HI_1722. DR GeneID; 950876; -. DR KEGG; hin:HI1722; -. DR PATRIC; 20192197; VBIHaeInf48452_1801. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR OMA; VIKDEYH; -. DR OrthoDB; EOG6MWNDS; -. DR PhylomeDB; P44421; -. DR Proteomes; UP000000579; 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 1 268 Methionine aminopeptidase. FT /FTId=PRO_0000148940. FT METAL 97 97 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 108 108 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 108 108 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 172 172 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT METAL 205 205 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 236 236 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT METAL 236 236 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01974}. FT BINDING 79 79 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. FT BINDING 179 179 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01974}. SQ SEQUENCE 268 AA; 29896 MW; C71DEA15BB5E732B CRC64; MAIPIRTEKE IVKLREACKL ASDVLVMIEP YVKAGVTTGE LDRICHEYMV NEQKVIPACL NYHGFPKATC ISINEVVCHG IPSDDKVLKN GDIVNIDVTV IKDGYFGDNS KMYIVGGETN IRSKKLVEAA QEALYVGIRT VKPDIRLNEI GKAVQKYTES QTFSVVREYC GHGVGTEFHC EPQVLHYYAD DGGVILKPGM VFTIEPMINA GKKEVRVMGD GWTVKTKDRS HSAQYEHQLI VTETGCEVMT IRDEEIAEGR ISRIMVNV // ID METJ_HAEIN Reviewed; 105 AA. AC P44618; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 11-NOV-2015, entry version 106. DE RecName: Full=Met repressor; DE AltName: Full=Met regulon regulatory protein MetJ; GN Name=metJ; OrderedLocusNames=HI_0294; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This regulatory protein, when combined with SAM (S- CC adenosylmethionine) represses the expression of the methionine CC regulon and of enzymes involved in SAM synthesis. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Does not bind DNA by a helix-turn-helix motif. CC -!- SIMILARITY: Belongs to the MetJ 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; L42023; AAC21958.1; -; Genomic_DNA. DR PIR; A64060; A64060. DR RefSeq; NP_438461.1; NC_000907.1. DR RefSeq; WP_005631186.1; NC_000907.1. DR ProteinModelPortal; P44618; -. DR SMR; P44618; 2-105. DR STRING; 71421.HI0294; -. DR EnsemblBacteria; AAC21958; AAC21958; HI_0294. DR GeneID; 949418; -. DR KEGG; hin:HI0294; -. DR PATRIC; 20189127; VBIHaeInf48452_0310. DR eggNOG; ENOG4105GGQ; Bacteria. DR eggNOG; COG3060; LUCA. DR KO; K03764; -. DR OMA; LRKERHD; -. DR OrthoDB; EOG6V1M74; -. DR PhylomeDB; P44618; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.140.10; -; 1. DR HAMAP; MF_00744; MetJ; 1. DR InterPro; IPR002084; Met_repressor_MetJ. DR InterPro; IPR023453; Met_repressor_MetJ_dom. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR Pfam; PF01340; MetJ; 1. DR ProDom; PD020365; Met_repressor_MetJ; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; DNA-binding; KW Methionine biosynthesis; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 105 Met repressor. FT /FTId=PRO_0000198401. SQ SEQUENCE 105 AA; 12111 MW; 5F5C5AFE09F4F876 CRC64; MANWDGKYIS PYAEHGKKSE QVKKITVSIP IKVLEILTNE RTRRQLKSLR HATNSELLCE AFLHAFTGQP LPTDADLMKE RNDEIPEDAK VLMRELGVDP ESWEY // ID MAZG_HAEIN Reviewed; 263 AA. AC P44723; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Nucleoside triphosphate pyrophosphohydrolase; DE Short=NTP-PPase; DE EC=3.6.1.8; GN Name=mazG; OrderedLocusNames=HI_0460; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the regulation of bacterial cell survival CC under conditions of nutritional stress. Regulates the MazE-MazF CC toxin-antitoxin (TA) module that mediates programmed cell death CC (PCD). This is achieved by lowering the cellular concentration of CC (p)ppGpp produced by RelA under amino acid starvation, thus CC protecting the cell from the toxicity of MazF. Reduction of CC (p)ppGpp can be achieved by direct degradation of (p)ppGpp or by CC degradation of NTPs, which are substrates for (p)ppGpp synthesis CC by RelA (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = AMP + diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nucleoside triphosphate CC pyrophosphohydrolase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22118.1; -; Genomic_DNA. DR PIR; H64069; H64069. DR RefSeq; NP_438621.1; NC_000907.1. DR RefSeq; WP_005693705.1; NC_000907.1. DR ProteinModelPortal; P44723; -. DR STRING; 71421.HI0460; -. DR EnsemblBacteria; AAC22118; AAC22118; HI_0460. DR GeneID; 949607; -. DR KEGG; hin:HI0460; -. DR PATRIC; 20189475; VBIHaeInf48452_0480. DR eggNOG; ENOG4105DXN; Bacteria. DR eggNOG; COG1694; LUCA. DR KO; K04765; -. DR OMA; AYRVQKK; -. DR OrthoDB; EOG67X1VS; -. DR PhylomeDB; P44723; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047693; F:ATP diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central. DR GO; GO:0046061; P:dATP catabolic process; IBA:GO_Central. DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central. DR GO; GO:0046076; P:dTTP catabolic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR GO; GO:0046047; P:TTP catabolic process; IBA:GO_Central. DR GO; GO:0046052; P:UTP catabolic process; IBA:GO_Central. DR InterPro; IPR004518; MazG_cat. DR InterPro; IPR011551; NTP_PyrPHydrolase_MazG. DR PANTHER; PTHR30522:SF0; PTHR30522:SF0; 1. DR Pfam; PF03819; MazG; 2. DR TIGRFAMs; TIGR00444; mazG; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 263 Nucleoside triphosphate FT pyrophosphohydrolase. FT /FTId=PRO_0000096250. FT NP_BIND 170 174 ATP 1. {ECO:0000250}. FT NP_BIND 191 194 ATP 1. {ECO:0000250}. FT NP_BIND 224 228 ATP 2. {ECO:0000250}. FT METAL 174 174 Magnesium. {ECO:0000250}. FT METAL 177 177 Magnesium. {ECO:0000250}. FT METAL 195 195 Magnesium. {ECO:0000250}. FT METAL 198 198 Magnesium. {ECO:0000250}. FT BINDING 177 177 ATP 1. {ECO:0000250}. FT BINDING 198 198 ATP 1. {ECO:0000250}. FT BINDING 255 255 ATP 2. {ECO:0000250}. SQ SEQUENCE 263 AA; 30520 MW; B397803562943121 CRC64; MRYSIQDFIQ LIAQLRNPNG GCPWDLKQNY ESMISCLTEE TYEVIEAIEK KDIPNLREEL GDLLLQVVFF SQLAREDKYF AFDDVLQDVA EKIVRRHPHV FGDAKAGDET EALSRWNEMK AKEKQGKSEE TSILDNVPRA LPSLTRAAKL QKRCSKVGFD WEEISPVFDK VREELEEVQA EINRTSIEQN KVEEEIGDLL FATVNLARHL KCDPEDALRK ANLKFERRFR AVEQAVQQQG KQVNNVPLIE LDLLWDEVKK QEN // ID MEND_HAEIN Reviewed; 568 AA. AC P44612; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659}; DE Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659}; DE EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659}; DE AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659}; GN Name=menD {ECO:0000255|HAMAP-Rule:MF_01659}; GN OrderedLocusNames=HI_0283; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent CC decarboxylation of 2-oxoglutarate and the subsequent addition of CC the resulting succinic semialdehyde-thiamine pyrophosphate anion CC to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3- CC cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000255|HAMAP- CC Rule:MF_01659}. CC -!- CATALYTIC ACTIVITY: Isochorismate + 2-oxoglutarate = 5- CC enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CC CO(2). {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01659}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01659}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 2/7. {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01659}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21946.1; -; Genomic_DNA. DR PIR; D64059; D64059. DR RefSeq; NP_438451.1; NC_000907.1. DR RefSeq; WP_010868971.1; NC_000907.1. DR ProteinModelPortal; P44612; -. DR STRING; 71421.HI0283; -. DR DNASU; 949474; -. DR EnsemblBacteria; AAC21946; AAC21946; HI_0283. DR GeneID; 949474; -. DR KEGG; hin:HI0283; -. DR PATRIC; 20189105; VBIHaeInf48452_0299. DR eggNOG; ENOG4105C4A; Bacteria. DR eggNOG; COG1165; LUCA. DR KO; K02551; -. DR OMA; IFRILPG; -. DR OrthoDB; EOG6NWBQW; -. DR PhylomeDB; P44612; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00164. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.970; -; 2. DR HAMAP; MF_01659; MenD; 1. DR InterPro; IPR004433; MenaQ_synth_MenD. DR InterPro; IPR032264; MenD_middle. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF16582; TPP_enzyme_M_2; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR PIRSF; PIRSF004983; MenD; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00173; menD; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Manganese; Menaquinone biosynthesis; KW Metal-binding; Reference proteome; Thiamine pyrophosphate; KW Transferase. FT CHAIN 1 568 2-succinyl-5-enolpyruvyl-6-hydroxy-3- FT cyclohexene-1-carboxylate synthase. FT /FTId=PRO_0000090830. SQ SEQUENCE 568 AA; 63097 MW; C0BE9A36E7EAAE4F CRC64; MSVSVFNRCW SKVILETLVR QGVSHLCIAP GSRSTPLTLE AVRLQNAGAV TCHTHFDERG LGFFALGIAK ATQSPVAIIV TSGTATANLY PAIIEARQTG VNLFVLTADR PPELWECGAN QAILQQNMFG QYPVANVNLP KPNADYSAQW LISLLEQAVF QQKQQGGVVH INVPFAEPLY DATDEEVNSH SWLQPLQRWL IQNKSWINVE AQQNEVLMHE NWDHWRTKRG VVVVGQLPAE QAMGINSWAS AMGWVLLTDI QSGVVPTTPY EDIWLANQTV REKLLQADIV IQFGARFISK RINQFLQAFK GEFWLVEQSG KALDPYHHSL TRFNAKVHHW LRAHPPLRQK PWLLEPLALS KFCATFIEQQ VGGNLTEASL ALRLPTLLPY NGVLFLGNSL LVRLVDALTQ LPESYPVYTN RGASGIDGLL ATAAGIGIGS NKPVVAVIGD TSTLYDLNSF ALFKNVTQPT LIFVINNNGG AIFDMLPVDE QVKDQFYRLP HNGDFSQIAA MFDLKYAHPY TWADLNSVVK QAYSRRKATL IEIKTNPSDG SSLYKRLIEQ ISHAVIGA // ID MENF_HAEIN Reviewed; 430 AA. AC P44613; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Isochorismate synthase MenF {ECO:0000255|HAMAP-Rule:MF_01935}; DE EC=5.4.4.2 {ECO:0000255|HAMAP-Rule:MF_01935}; DE AltName: Full=Isochorismate mutase {ECO:0000255|HAMAP-Rule:MF_01935}; GN Name=menF {ECO:0000255|HAMAP-Rule:MF_01935}; GN OrderedLocusNames=HI_0285; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of chorismate to isochorismate. CC {ECO:0000255|HAMAP-Rule:MF_01935}. CC -!- CATALYTIC ACTIVITY: Chorismate = isochorismate. CC {ECO:0000255|HAMAP-Rule:MF_01935}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01935}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 1/7. {ECO:0000255|HAMAP-Rule:MF_01935}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01935}. CC -!- SIMILARITY: Belongs to the isochorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01935}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21947.1; -; Genomic_DNA. DR PIR; E64059; E64059. DR RefSeq; NP_438452.1; NC_000907.1. DR RefSeq; WP_005694023.1; NC_000907.1. DR ProteinModelPortal; P44613; -. DR STRING; 71421.HI0285; -. DR EnsemblBacteria; AAC21947; AAC21947; HI_0285. DR GeneID; 949812; -. DR KEGG; hin:HI0285; -. DR PATRIC; 20189107; VBIHaeInf48452_0300. DR eggNOG; ENOG4105E4F; Bacteria. DR eggNOG; COG1169; LUCA. DR KO; K02552; -. DR OMA; YPQFYLH; -. DR OrthoDB; EOG6PGK1Z; -. DR PhylomeDB; P44613; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00163. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.120.10; -; 1. DR HAMAP; MF_01935; MenF_gammaproteo; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR015890; Chorismate_C. DR InterPro; IPR004561; IsoChor_synthase. DR Pfam; PF00425; Chorismate_bind; 1. DR SUPFAM; SSF56322; SSF56322; 1. DR TIGRFAMs; TIGR00543; isochor_syn; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Menaquinone biosynthesis; KW Metal-binding; Reference proteome. FT CHAIN 1 430 Isochorismate synthase MenF. FT /FTId=PRO_0000154148. FT ACT_SITE 187 187 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01935}. FT ACT_SITE 237 237 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01935}. FT METAL 281 281 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01935}. FT METAL 414 414 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01935}. SQ SEQUENCE 430 AA; 48466 MW; 3BA131F8B62A1B38 CRC64; MYLKQNLMSY LAQAIGELKS QIHAYLQQST NELVRFQVKL DKVDLLAWLK GQSAYPQFYL HFRDEEKALA ALGAVQSFSQ LNLAQEFIEE SGFPLVGGLQ FQGTAQFVLP KMLVEQDNKG TLVSFFVKNE QSANDTLAHL KTFENLTALS ALPKQIPLHT ELRANERTWC DWVNQALVEI KSGELTKIVL ANETTFHLKQ AINAYDFLAE SEKQNQGCYH FLWAENSHSV FVGSTPERLF AREYNLLLTE ALAGTASVSE SEEETQSQAN WLLNDEKNLK ENWLVVEDIS QNLRKQVESF DVSNVELKPL RKVQHLIRKI RANLTAHYAD VNILKAIHPT AAVSGLPQQQ AKMILSEIET FDRGWYAGTL GVMSDVCSEF CVAIRSAFIE GHRIRVFAGA GIVAGSQPLE EWKEIERKAA GLISLFAEEK // ID METI_HAEIN Reviewed; 213 AA. AC P46492; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=Probable D-methionine transport system permease protein MetI; GN Name=metI; OrderedLocusNames=HI_0620.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for D-methionine. Probably responsible for the translocation of CC the substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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 -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=179; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P46492; -. DR OMA; ACSTFAG; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0048473; P:D-methionine transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 213 Probable D-methionine transport system FT permease protein MetI. FT /FTId=PRO_0000060103. FT TRANSMEM 13 33 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 50 72 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 89 109 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 139 159 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 183 203 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 9 202 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 213 AA; 22935 MW; 2C3A3FCB04411C51 CRC64; MWGVVATATY ETVYISFAST LLAVLVGVPV GIWTFLTGKN EILQNNRTHF VLNTIINIGR SIPFIILLLI LLPVTRFIVG TVLGTTAAII PLSICAMPFV ARLTANALME IPNGLTEAAQ AMGATKWQIV RKFYLSEALP TLINGVTLTL VTLVGYSAMA GTQGGGGLGS LAINYGRIRN MPYVTWVATI IIVLFVMISQ KLGDTLAKKV DHR // ID METN_HAEIN Reviewed; 345 AA. AC P44785; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Methionine import ATP-binding protein MetN {ECO:0000255|HAMAP-Rule:MF_01719}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01719}; GN Name=metN {ECO:0000255|HAMAP-Rule:MF_01719}; GN OrderedLocusNames=HI_0621; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex MetNIQ involved in CC methionine import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01719}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MetN), two transmembrane proteins (MetI) and a solute-binding CC protein (MetQ). {ECO:0000255|HAMAP-Rule:MF_01719}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01719}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01719}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Methionine CC importer (TC 3.A.1.24) family. {ECO:0000255|HAMAP-Rule:MF_01719}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01719}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22280.1; -; Genomic_DNA. DR PIR; C64082; C64082. DR RefSeq; NP_438780.1; NC_000907.1. DR RefSeq; WP_010869021.1; NC_000907.1. DR ProteinModelPortal; P44785; -. DR STRING; 71421.HI0621; -. DR EnsemblBacteria; AAC22280; AAC22280; HI_0621. DR GeneID; 950557; -. DR KEGG; hin:HI0621; -. DR PATRIC; 20189827; VBIHaeInf48452_0646. DR eggNOG; ENOG4108JEI; Bacteria. DR eggNOG; COG1135; LUCA. DR KO; K02071; -. DR OMA; VITHEMK; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P44785; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0048474; F:D-methionine transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR026253; ABC_MetN. DR InterPro; IPR012692; ABC_MetN_proteobac. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR017908; ABC_transprt_methionine_MetN_C. DR InterPro; IPR018449; NIL_domain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR24220:SF455; PTHR24220:SF455; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF09383; NIL; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00930; NIL; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02314; ABC_MetN; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51264; METN; 1. PE 3: Inferred from homology; KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 345 Methionine import ATP-binding protein FT MetN. FT /FTId=PRO_0000092509. FT DOMAIN 2 241 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01719}. FT NP_BIND 38 45 ATP. {ECO:0000255|HAMAP-Rule:MF_01719}. SQ SEQUENCE 345 AA; 37880 MW; 7457118E8BEB79C2 CRC64; MIKLNNIXKI FELPXKKLTA LDNVSLNIEK GQICGVIGAS GAGKSTLIRC VNLLEKPTSG SVIVDGVELT KLSDRELVLA RRQIGMIFQH FNLLSSRTVF ENVALPLELE SESKAKIQEK ITALLDLVGL SEKRDAYPSN LSGGQKQRVA IARALASDPK VLLCDEATSA LDPATTQSIL KLLKEINRTL GITILLITHE MEVVKQICDQ VAVIDQGRLV EQGTVGEIFA NPKTELAQEF IRSTFHISLP DEYLENLTDT PKHSKAYPII KFEFTGRSVD APLLSQASKK FGVELSILTS QIDYAGGVKF GYTIAEVEGD EDAITQTKVY LMENNVRVEV LGYVQ // ID MGLA_HAEIN Reviewed; 506 AA. AC P44884; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Galactose/methyl galactoside import ATP-binding protein MglA {ECO:0000255|HAMAP-Rule:MF_01717}; DE EC=3.6.3.17 {ECO:0000255|HAMAP-Rule:MF_01717}; GN Name=mglA {ECO:0000255|HAMAP-Rule:MF_01717}; GN OrderedLocusNames=HI_0823; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex MglABC involved in CC galactose/methyl galactoside import. Responsible for energy CC coupling to the transport system. {ECO:0000255|HAMAP- CC Rule:MF_01717}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + monosaccharide(Out) = ADP + CC phosphate + monosaccharide(In). {ECO:0000255|HAMAP-Rule:MF_01717}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MglA), two transmembrane proteins (MglC) and a solute-binding CC protein (MglB). {ECO:0000255|HAMAP-Rule:MF_01717}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01717}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Galactose/methyl galactoside importer (TC 3.A.1.2.3) family. CC {ECO:0000255|HAMAP-Rule:MF_01717}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_01717}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22482.1; -; Genomic_DNA. DR PIR; H64096; H64096. DR RefSeq; NP_438983.1; NC_000907.1. DR RefSeq; WP_005652432.1; NC_000907.1. DR ProteinModelPortal; P44884; -. DR STRING; 71421.HI0823; -. DR DNASU; 949835; -. DR EnsemblBacteria; AAC22482; AAC22482; HI_0823. DR GeneID; 949835; -. DR KEGG; hin:HI0823; -. DR PATRIC; 20190301; VBIHaeInf48452_0864. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR KO; K10542; -. DR OMA; NTSQNEI; -. DR OrthoDB; EOG6QK4RR; -. DR PhylomeDB; P44884; -. DR Proteomes; UP000000579; 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:0005354; F:galactose transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015862; ABC_transpr_MglA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS51260; MGLA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Sugar transport; Transport. FT CHAIN 1 506 Galactose/methyl galactoside import ATP- FT binding protein MglA. FT /FTId=PRO_0000092515. FT DOMAIN 14 249 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_01717}. FT DOMAIN 260 506 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_01717}. FT NP_BIND 46 53 ATP. {ECO:0000255|HAMAP-Rule:MF_01717}. SQ SEQUENCE 506 AA; 56568 MW; E00C133D72941FD5 CRC64; MTAQTQCQDS QVLLTMTNVC KSFPGVKALD NANLTVRSHS VHALMGENGA GKSTLLKCLF GIYAKDEGEI LFLGEPVNFK TSKEALENGI SMVHQELNLV RQTSVMDNLW LGRYPLKGPF VDHAKMYRDT KAIFDELDID VDPKEKVAKL SVSQMQMIEI AKAFSYNAKI VIMDEPTSSL SEKEVEHLFK IIDKLKQRGC GIIYISHKMD EIFKICDEIT ILRDGKWINT VNVKESTMEQ IVGMMVGREL TQRFPEKTNV PKEVILQVEN LTAKNQPSIQ DVSFELRKGE ILGIAGLVGA KRTDIVEAIF GVRELIEGTI KLHGKTVKNH TALEAINNGF ALVTEERRST GIYSNLSIEF NSLISNMKSY LTPWKLLSTK KMKSDTQWVI DSMNVKTPSH RTTIGSLSGG NQQKVIIGRW LLTQPEILML DEPTRGIDIG AKFEIYQLIQ ELAKKDKGII MISSEMPELL GVTDRILVMS NGKLAGIVES AKTSQEEILQ LAAKYL // ID MIAB_HAEIN Reviewed; 474 AA. AC Q57163; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864}; DE EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864}; GN Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864}; GN OrderedLocusNames=HI_0019; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC (dimethylallyl)adenosine (i(6)A), leading to the formation of 2- CC methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 CC in tRNAs that read codons beginning with uridine. CC {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA + CC sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced CC electron acceptor = 2-methylthio-N(6)-dimethylallyladenine(37) in CC tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine CC + 5'-deoxyadenosine + electron acceptor. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01864}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01864}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01864}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21697.1; -; Genomic_DNA. DR PIR; D64140; D64140. DR RefSeq; NP_438192.1; NC_000907.1. DR RefSeq; WP_005649877.1; NC_000907.1. DR ProteinModelPortal; Q57163; -. DR STRING; 71421.HI0019; -. DR EnsemblBacteria; AAC21697; AAC21697; HI_0019. DR GeneID; 950916; -. DR KEGG; hin:HI0019; -. DR PATRIC; 20188489; VBIHaeInf48452_0019. DR eggNOG; ENOG4105CIW; Bacteria. DR eggNOG; COG0621; LUCA. DR KO; K06168; -. DR OMA; IPMDLIL; -. DR OrthoDB; EOG6P5ZD8; -. DR PhylomeDB; Q57163; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0035597; F:N6-isopentenyladenosine methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GOC. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR006463; MiaB_methiolase. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW Transferase; tRNA processing. FT CHAIN 1 474 tRNA-2-methylthio-N(6)- FT dimethylallyladenosine synthase. FT /FTId=PRO_0000141737. FT DOMAIN 3 120 MTTase N-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT DOMAIN 378 441 TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 12 12 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 49 49 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01864}. FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 161 161 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. FT METAL 164 164 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01864}. SQ SEQUENCE 474 AA; 53640 MW; A6ECDFBBAE16923D CRC64; MTQKLHIKTW GCQMNEYDSS KMADLLLSTH GLELTEAPEE ADVLLLNTCS IREKAQEKVF HQLGRWKELK KNNPNLVIGV GGCVASQEGE HIRHRAPYVD IIFGPQTLHR LPEMINQIRG GKSSVVDVSF PEIEKFDRLP EPRAEGPTAF VSIMEGCNKY CTFCVVPYTR GEEVSRPVDD VLFEIAQLAE QGVREVNLLG QNVNAYRGPT HDGQICSFAE LLRLVASIDG IDRLRFTTSH PIEFTDDIID VYRDTPELVS FLHLPVQAGS DRVLTMMKRA HTALEYKSII RKLRAVRPDI QISSDFIVGF PGETAEDFEQ TMNLIAQVNF DMSFSFVYSA RPGTPAADMP DDVTEDEKKQ RLYVLQERIN QQAAQFSRRM LGTEQRVLVE GPSKKDIMEL TGRTETNRIV NFQGSPEMIG KFVDVKITDV YTNSLRGEVV RTEDEMGLRI AQSPQEVMNR TRKEDELGVG RYHG // ID METF_HAEIN Reviewed; 292 AA. AC P45208; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=5,10-methylenetetrahydrofolate reductase; DE EC=1.5.1.20; GN Name=metF; OrderedLocusNames=HI_1444; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase 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; L42023; AAC23094.1; -; Genomic_DNA. DR PIR; H64123; H64123. DR RefSeq; NP_439596.1; NC_000907.1. DR RefSeq; WP_005652747.1; NC_000907.1. DR ProteinModelPortal; P45208; -. DR SMR; P45208; 3-292. DR STRING; 71421.HI1444; -. DR PRIDE; P45208; -. DR EnsemblBacteria; AAC23094; AAC23094; HI_1444. DR GeneID; 950344; -. DR KEGG; hin:HI1444; -. DR PATRIC; 20191593; VBIHaeInf48452_1506. DR eggNOG; ENOG4105SYT; Bacteria. DR eggNOG; COG0685; LUCA. DR KO; K00297; -. DR OMA; EMHPQAR; -. DR OrthoDB; EOG6D2KVW; -. DR PhylomeDB; P45208; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:InterPro. DR GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IBA:GO_Central. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.220; -; 1. DR InterPro; IPR029041; FAD-linked_oxidoreductase-like. DR InterPro; IPR003171; Mehydrof_redctse. DR InterPro; IPR004620; MTHF_reductase_bac. DR Pfam; PF02219; MTHFR; 1. DR SUPFAM; SSF51730; SSF51730; 1. DR TIGRFAMs; TIGR00676; fadh2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; KW Methionine biosynthesis; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 292 5,10-methylenetetrahydrofolate reductase. FT /FTId=PRO_0000190263. FT NP_BIND 26 31 NAD. {ECO:0000250}. FT NP_BIND 57 60 FAD. {ECO:0000250}. FT NP_BIND 57 58 NAD. {ECO:0000250}. FT NP_BIND 116 118 FAD. {ECO:0000250}. FT NP_BIND 129 130 FAD. {ECO:0000250}. FT NP_BIND 154 157 FAD. {ECO:0000250}. FT NP_BIND 163 170 FAD. {ECO:0000250}. FT ACT_SITE 26 26 Proton donor/acceptor. {ECO:0000250}. FT BINDING 86 86 FAD. {ECO:0000250}. FT BINDING 118 118 Substrate. {ECO:0000250}. FT BINDING 150 150 FAD. {ECO:0000250}. FT BINDING 181 181 Substrate. {ECO:0000250}. FT BINDING 217 217 Substrate. {ECO:0000250}. FT BINDING 273 273 Substrate. {ECO:0000250}. FT BINDING 277 277 Substrate. {ECO:0000250}. SQ SEQUENCE 292 AA; 33020 MW; C6DCC9BC80CFF9B4 CRC64; MSYAKEIDTL NQHIADFNKK INVSFEFFPP KNEKMETLLW DSIHRLKVLK PKFVSVTYGA NSGERDRTHG IVKAIKQETG LEAAPHLTGI DATPEELKQI ARDYWDSGIR RIVALRGDEP KGYAKKPFYA SDLVELLRSV ADFDISVAAY PEVHPEAKSA QADLINLKRK IDAGANHVIT QFFFDIENYL RFRDRCASIG IDTEIVPGIL PVTNFKQLQK MASFTNVKIP AWLVKAYDGL DNDPTTRNLV AASVAMDMVK ILSREGVNDF HFYTLNRSEL TYAICHMLGV RP // ID MENE_HAEIN Reviewed; 452 AA. AC P44565; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=2-succinylbenzoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00731}; DE EC=6.2.1.26 {ECO:0000255|HAMAP-Rule:MF_00731}; DE AltName: Full=o-succinylbenzoyl-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731}; DE Short=OSB-CoA synthetase {ECO:0000255|HAMAP-Rule:MF_00731}; GN Name=menE {ECO:0000255|HAMAP-Rule:MF_00731}; GN OrderedLocusNames=HI_0194; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl- CC CoA (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731}. CC -!- CATALYTIC ACTIVITY: ATP + 2-succinylbenzoate + CoA = AMP + CC diphosphate + 2-succinylbenzoyl-CoA. {ECO:0000255|HAMAP- CC Rule:MF_00731}. CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 5/7. {ECO:0000255|HAMAP-Rule:MF_00731}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00731}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme CC family. MenE subfamily. {ECO:0000255|HAMAP-Rule:MF_00731}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21863.1; -; Genomic_DNA. DR PIR; F64053; F64053. DR RefSeq; NP_438363.1; NC_000907.1. DR RefSeq; WP_005694098.1; NC_000907.1. DR ProteinModelPortal; P44565; -. DR STRING; 71421.HI0194; -. DR EnsemblBacteria; AAC21863; AAC21863; HI_0194. DR GeneID; 951106; -. DR KEGG; hin:HI0194; -. DR PATRIC; 20188885; VBIHaeInf48452_0199. DR eggNOG; ENOG4105CEY; Bacteria. DR eggNOG; COG0318; LUCA. DR KO; K01911; -. DR OMA; MASTICA; -. DR OrthoDB; EOG6WX4MJ; -. DR PhylomeDB; P44565; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00166. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00731; MenE; 1. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR010192; MenE. DR Pfam; PF00501; AMP-binding; 1. DR TIGRFAMs; TIGR01923; menE; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Menaquinone biosynthesis; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 452 2-succinylbenzoate--CoA ligase. FT /FTId=PRO_0000193177. SQ SEQUENCE 452 AA; 51394 MW; 3EFA6456AC6F7CBF CRC64; MYPWQDFAIQ PDFSDKIALR TTQGDMLTWI ELTTKINQTV AFLQKKGVNA ESAVAFVGKN SEKILFLYLA TIQLGAKVLG INPAFPQEKI AKLCEFYQID FCFYDKDLLN LQEIDVFTQK ADFFRPATMT LTSGSTGLPK AVVHNVQAHL DNAKGVCNLM KFDCNQSWLL SLPLYHVSGQ GIVWRWLYCG AQLHFPEDDF YASLLKTTHV SLVPTQLQRL LDYLQENPSI SFATRHILLG GAHIPTELTQ NMLKYGIETY SGYGMTEMAS TVFAKKSDRK QGVGQPLLGR EYCLVNDEIW LKGAGLAMGY WKDRQIVPLT NNQGWIQTKD KGIWQEGELV IIGRLDNMFI SGGENIQPEE IEQVIIQHSS VNQVFVLPQK NKEFGQRPVA LVDFNEPFSK SAVENLMFFL QDKLARFKQP IAYYPLPLML EKGIKISRKQ LADWLAKRDE IN // ID METE_HAEIN Reviewed; 756 AA. AC P45331; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; DE EC=2.1.1.14; DE AltName: Full=Cobalamin-independent methionine synthase; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme; GN Name=metE; OrderedLocusNames=HI_1702; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L- CC homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetE route): step CC 1/1. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine CC synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23348.1; -; Genomic_DNA. DR PIR; B64137; B64137. DR RefSeq; NP_439844.1; NC_000907.1. DR RefSeq; WP_005694192.1; NC_000907.1. DR ProteinModelPortal; P45331; -. DR STRING; 71421.HI1702; -. DR PRIDE; P45331; -. DR DNASU; 949942; -. DR EnsemblBacteria; AAC23348; AAC23348; HI_1702. DR GeneID; 949942; -. DR KEGG; hin:HI1702; -. DR PATRIC; 20192155; VBIHaeInf48452_1781. DR eggNOG; ENOG4105DSS; Bacteria. DR eggNOG; COG0620; LUCA. DR KO; K00549; -. DR OMA; RFGWVQS; -. DR OrthoDB; EOG6FFS3G; -. DR PhylomeDB; P45331; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central. DR HAMAP; MF_00172; Meth_synth; 1. DR InterPro; IPR013215; Cbl-indep_Met_Synth_N. DR InterPro; IPR006276; Cobalamin-indep_Met_synthase. DR InterPro; IPR002629; Met_Synth_C/arc. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW Repeat; Transferase; Zinc. FT CHAIN 1 756 5-methyltetrahydropteroyltriglutamate-- FT homocysteine methyltransferase. FT /FTId=PRO_0000098633. FT METAL 642 642 Zinc. {ECO:0000250}. FT METAL 644 644 Zinc. {ECO:0000250}. FT METAL 727 727 Zinc. {ECO:0000250}. SQ SEQUENCE 756 AA; 85239 MW; FD48C9033E51BDE8 CRC64; MTTSHILGFP RVGAKRELKF AQERYWRKEL AEQDLLDLAK ALREKNWKHQ AAANADFVAV GDFTFYDHIL DLQVATGAIP ARFGFDSQNL TLDQYFQLAR GNKDQFAIEM TKWFDTNYHY LVPEFQKSTA FKANPAHYVN QIREAKALGL NFKPVIVGPL TFLWLGKEKG EAFNRFDLLN QLVPVYVEIL NALVAEGAEW IQIDEPALAL DLPAEWVEAY KSVYTELSKV NAKLLLATYF GSVAEHAELL KALPVAGLHL DLVRAPEQLA AFEDYSKVLS AGVIEGRNIW RANLNKVLDV LEPLKAKLGE RLWIAPSCSL LHTPFDLEVE VQLKEKNTAL YSWLSFTLQK VEELNVLKQA LNNGRASVQA ALDASQVAAD ARATSKEIHR PEVAERLANL PKGADQRKSP FAERIVKQNA WLNLPLLPTT NIGSFPQTTE IRHARASFKK GELSLADYEA AMKKEIEYVV RRQEELDLDV LVHGEAERND MVEYFGELLD GFAFTKFGWV QSYGSRCVKP PVIYGDVTRP EPMTVRWSQY AQSLTNRVMK GMLTGPVTIL QWSFVRNDIP RSTVCKQIGV ALSDEVLDLE AAGIKVIQID EPAIREGLPL KRADWDAYLQ WAGEAFRLSS MGVQDDTQIH THMCYSEFND ILPAIAALDA DVITIETSRS DMELLTAFAD FKYPNDIGPG VYDIHSPRVP TATEVEHLLR KALNVIPKER LWVNPDCGLK TRGWTETIDQ LKVMVDVTKK LRAELA // ID METX_HAEIN Reviewed; 358 AA. AC P45131; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 123. DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296}; DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296}; DE AltName: Full=Homoserine O-trans-acetylase {ECO:0000255|HAMAP-Rule:MF_00296}; DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296}; DE Short=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296}; GN Name=metX {ECO:0000255|HAMAP-Rule:MF_00296}; Synonyms=met2; GN OrderedLocusNames=HI_1263; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND PROTEIN SEQUENCE OF RP 2-11. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL RP PROPERTIES, REACTION MECHANISM, AND SUBUNIT. RX PubMed=10913262; DOI=10.1021/bi000462p; RA Born T.L., Franklin M., Blanchard J.S.; RT "Enzyme-catalyzed acylation of homoserine: mechanistic RT characterization of the Haemophilus influenzae met2-encoded homoserine RT transacetylase."; RL Biochemistry 39:8556-8564(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), ACTIVE SITE, AND SUBUNIT. RX PubMed=16313180; DOI=10.1021/bi051951y; RA Mirza I.A., Nazi I., Korczynska M., Wright G.D., Berghuis A.M.; RT "Crystal structure of homoserine transacetylase from Haemophilus RT influenzae reveals a new family of alpha/beta-hydrolases."; RL Biochemistry 44:15768-15773(2005). CC -!- FUNCTION: Involved in the methionine biosynthesis. Catalyzes the CC transfer of the acetyl group from acetyl-CoA to the hydroxyl group CC of L-homoserine to yield O-acetyl-L-homoserine. CC {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:10913262}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-homoserine = CoA + O-acetyl-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00296, CC ECO:0000269|PubMed:10913262}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=90 uM for propionyl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=130 uM for crotonyl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=130 uM for L-homoserine (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=140 uM for acetyl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=210 uM for butyryl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=280 uM for glutaryl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=360 uM for succinyl-CoA (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC KM=1400 uM for 4-nitrophenyl acetate (at 25 degrees Celsius and CC pH 7.5) {ECO:0000269|PubMed:10913262}; CC KM=4700 uM for D-homoserine (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10913262}; CC Note=Kcat is 92 (sec-1) for acetyl-CoA and L-homoserin (at 25 CC degrees Celsius and pH 7.5).; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296, CC ECO:0000269|PubMed:10913262, ECO:0000269|PubMed:16313180}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}. CC -!- MASS SPECTROMETRY: Mass=39859; Method=Electrospray; Range=2-358; CC Evidence={ECO:0000269|PubMed:10913262}; CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi CC reaction mechanism. {ECO:0000305|PubMed:10913262}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. HTA family. CC {ECO:0000255|HAMAP-Rule:MF_00296}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22916.1; -; Genomic_DNA. DR PIR; D64113; D64113. DR RefSeq; NP_439418.1; NC_000907.1. DR RefSeq; WP_005694320.1; NC_000907.1. DR PDB; 2B61; X-ray; 1.65 A; A=1-358. DR PDBsum; 2B61; -. DR ProteinModelPortal; P45131; -. DR SMR; P45131; 2-358. DR STRING; 71421.HI1263; -. DR ESTHER; haein-metx; Homoserine_transacetylase. DR EnsemblBacteria; AAC22916; AAC22916; HI_1263. DR GeneID; 950208; -. DR KEGG; hin:HI1263; -. DR PATRIC; 20191207; VBIHaeInf48452_1315. DR eggNOG; ENOG4105DWV; Bacteria. DR eggNOG; COG2021; LUCA. DR KO; K00641; -. DR OMA; GSVGGMN; -. DR OrthoDB; EOG67T5J4; -. DR PhylomeDB; P45131; -. DR BRENDA; 2.3.1.31; 2529. DR UniPathway; UPA00051; UER00074. DR EvolutionaryTrace; P45131; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central. DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR HAMAP; MF_00296; Homoser_O_acetyltr; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR008220; Homoserine_AcTrfase. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Methionine biosynthesis; Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7542800}. FT CHAIN 2 358 Homoserine O-acetyltransferase. FT /FTId=PRO_0000155719. FT ACT_SITE 143 143 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00296}. FT ACT_SITE 304 304 {ECO:0000255|HAMAP-Rule:MF_00296}. FT ACT_SITE 337 337 {ECO:0000255|HAMAP-Rule:MF_00296}. FT STRAND 4 12 {ECO:0000244|PDB:2B61}. FT STRAND 24 33 {ECO:0000244|PDB:2B61}. FT STRAND 42 46 {ECO:0000244|PDB:2B61}. FT STRAND 58 60 {ECO:0000244|PDB:2B61}. FT HELIX 66 68 {ECO:0000244|PDB:2B61}. FT STRAND 73 76 {ECO:0000244|PDB:2B61}. FT TURN 77 79 {ECO:0000244|PDB:2B61}. FT STRAND 81 85 {ECO:0000244|PDB:2B61}. FT STRAND 91 95 {ECO:0000244|PDB:2B61}. FT TURN 102 104 {ECO:0000244|PDB:2B61}. FT STRAND 105 107 {ECO:0000244|PDB:2B61}. FT HELIX 109 111 {ECO:0000244|PDB:2B61}. FT HELIX 117 130 {ECO:0000244|PDB:2B61}. FT STRAND 136 142 {ECO:0000244|PDB:2B61}. FT HELIX 144 155 {ECO:0000244|PDB:2B61}. FT STRAND 159 167 {ECO:0000244|PDB:2B61}. FT HELIX 174 188 {ECO:0000244|PDB:2B61}. FT HELIX 194 196 {ECO:0000244|PDB:2B61}. FT HELIX 205 219 {ECO:0000244|PDB:2B61}. FT HELIX 222 228 {ECO:0000244|PDB:2B61}. FT TURN 229 231 {ECO:0000244|PDB:2B61}. FT HELIX 245 258 {ECO:0000244|PDB:2B61}. FT HELIX 263 275 {ECO:0000244|PDB:2B61}. FT TURN 278 281 {ECO:0000244|PDB:2B61}. FT HELIX 285 289 {ECO:0000244|PDB:2B61}. FT STRAND 294 301 {ECO:0000244|PDB:2B61}. FT STRAND 305 307 {ECO:0000244|PDB:2B61}. FT HELIX 309 321 {ECO:0000244|PDB:2B61}. FT STRAND 325 331 {ECO:0000244|PDB:2B61}. FT HELIX 336 338 {ECO:0000244|PDB:2B61}. FT HELIX 339 342 {ECO:0000244|PDB:2B61}. FT HELIX 344 356 {ECO:0000244|PDB:2B61}. SQ SEQUENCE 358 AA; 39990 MW; 2484D6BEAC761983 CRC64; MSVQNVVLFD TQPLTLMLGG KLSHINVAYQ TYGTLNAEKN NAVLICHALT GDAEPYFDDG RDGWWQNFMG AGLALDTDRY FFISSNVLGG CKGTTGPSSI NPQTGKPYGS QFPNIVVQDI VKVQKALLDH LGISHLKAII GGSFGGMQAN QWAIDYPDFM DNIVNLCSSI YFSAEAIGFN HVMRQAVIND PNFNGGDYYE GTPPDQGLSI ARMLGMLTYR TDLQLAKAFG RATKSDGSFW GDYFQVESYL SYQGKKFLER FDANSYLHLL RALDMYDPSL GYDNVKEALS RIKARYTLVS VTTDQLFKPI DLYKSKQLLE QSGVDLHFYE FPSDYGHDAF LVDYDQFEKR IRDGLAGN // ID MENA_HAEIN Reviewed; 308 AA. AC P44739; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=1,4-dihydroxy-2-naphthoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937}; DE Short=DHNA-octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01937}; DE EC=2.5.1.74 {ECO:0000255|HAMAP-Rule:MF_01937}; GN Name=menA {ECO:0000255|HAMAP-Rule:MF_01937}; GN OrderedLocusNames=HI_0509; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to CC demethylmenaquinone (DMK). {ECO:0000255|HAMAP-Rule:MF_01937}. CC -!- CATALYTIC ACTIVITY: An all-trans-polyprenyl diphosphate + 1,4- CC dihydroxy-2-naphthoate = a demethylmenaquinol + diphosphate + CC CO(2). {ECO:0000255|HAMAP-Rule:MF_01937}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis; CC menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_01937}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01937}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01937}. CC -!- SIMILARITY: Belongs to the MenA family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01937}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22167.1; -; Genomic_DNA. DR PIR; H64153; H64153. DR RefSeq; NP_438667.2; NC_000907.1. DR STRING; 71421.HI0509; -. DR EnsemblBacteria; AAC22167; AAC22167; HI_0509. DR GeneID; 949923; -. DR KEGG; hin:HI0509; -. DR PATRIC; 20189571; VBIHaeInf48452_0528. DR eggNOG; ENOG4105EIS; Bacteria. DR eggNOG; COG1575; LUCA. DR KO; K02548; -. DR OMA; TVGKKPY; -. DR OrthoDB; EOG6W7220; -. DR UniPathway; UPA00079; UER00168. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01937; MenA_1; 1. DR InterPro; IPR004657; MenA. DR InterPro; IPR000537; UbiA_prenyltransferase. DR InterPro; IPR026046; UBIAD1. DR Pfam; PF01040; UbiA; 1. DR PIRSF; PIRSF005355; UBIAD1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Menaquinone biosynthesis; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 308 1,4-dihydroxy-2-naphthoate FT octaprenyltransferase. FT /FTId=PRO_0000096415. FT TRANSMEM 22 42 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 47 67 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 101 121 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 129 149 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 153 173 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 186 206 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 235 255 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 256 276 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. FT TRANSMEM 286 306 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01937}. SQ SEQUENCE 308 AA; 33346 MW; 7A873AFC8071AF6B CRC64; MRSKKMINEK LKMWWETARP KTLPLALASI FTGSALGYWA NPQGFNGLVM VLCLLTTILL QVLSNFANDY GDHQKGSDTE ERIGPLRGIQ KGAISAKELK WGLILMVMAS FLSGSFLIGI AYENLSDLFA FAGLGILAIV AAITYTVGVK PYGYMGLGDI SVLVFFGLLG VGGTYYLQTH SIDSHIILPA IGSGLLASAV LNINNLRDIE QDAKAGKNTL AVRLGAYKGR VYHCILLSVA ALCYLAFAVA TAISWTNYLF VLAMPLLAKH AIFVYCSQQP SELRPILAQM SMISLLINIL FSLGLLIG // ID MENB_HAEIN Reviewed; 285 AA. AC P44960; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934}; DE Short=DHNA-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934}; DE EC=4.1.3.36 {ECO:0000255|HAMAP-Rule:MF_01934}; GN Name=menB {ECO:0000255|HAMAP-Rule:MF_01934}; GN OrderedLocusNames=HI_0968; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4- CC dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP- CC Rule:MF_01934}. CC -!- CATALYTIC ACTIVITY: 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4- CC dihydroxy-2-naphthoyl-CoA + H(2)O. {ECO:0000255|HAMAP- CC Rule:MF_01934}. CC -!- COFACTOR: CC Name=bicarbonate; Xref=ChEBI:CHEBI:17544; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01934}; CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step CC 6/7. {ECO:0000255|HAMAP-Rule:MF_01934}. CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01934}. CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. CC MenB subfamily. {ECO:0000255|HAMAP-Rule:MF_01934}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22625.1; -; Genomic_DNA. DR PIR; B64105; B64105. DR RefSeq; NP_439129.1; NC_000907.1. DR RefSeq; WP_005693314.1; NC_000907.1. DR ProteinModelPortal; P44960; -. DR SMR; P44960; 12-285. DR STRING; 71421.HI0968; -. DR EnsemblBacteria; AAC22625; AAC22625; HI_0968. DR GeneID; 949967; -. DR KEGG; hin:HI0968; -. DR PATRIC; 20190593; VBIHaeInf48452_1009. DR eggNOG; ENOG4108IPT; Bacteria. DR eggNOG; COG0447; LUCA. DR KO; K01661; -. DR OMA; SIKMLKF; -. DR OrthoDB; EOG6K9QJX; -. DR PhylomeDB; P44960; -. DR UniPathway; UPA00079; -. DR UniPathway; UPA01057; UER00167. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.12.10; -; 1. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_01934; MenB; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR014748; Crontonase_C. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR010198; DHNA-CoA_synthase_MenB. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR01929; menB; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Menaquinone biosynthesis; KW Reference proteome. FT CHAIN 1 285 1,4-dihydroxy-2-naphthoyl-CoA synthase. FT /FTId=PRO_0000109327. FT REGION 84 88 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT REGION 129 133 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT REGION 154 156 Bicarbonate binding. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 45 45 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 97 97 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 155 155 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 161 161 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 258 258 Substrate; shared with neighboring FT subunit. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT BINDING 273 273 Substrate; shared with neighboring FT subunit. {ECO:0000255|HAMAP- FT Rule:MF_01934}. FT SITE 97 97 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01934}. FT SITE 258 258 Important for catalysis. FT {ECO:0000255|HAMAP-Rule:MF_01934}. SQ SEQUENCE 285 AA; 31700 MW; 4A2F68CF0DCEC996 CRC64; MQNPKDDVLY APVEWIDHSE GYSDIRYHKS TDGIAKITIN RPEVRNAFRP QTVKEMMTAF SDARFDENIG VIVLTGEGEK AFCSGGDQKV RGDYGGYKDD SGVHHLNVLD FQRDIRSCPK PVVAMVAGYA IGGGHVLHML CDLTIAAENA IFGQTGPKVG SFDGGWGASY MARLVGQKKA REIWFLCRQY NAQEALDMGL VNTVVPYADL EKETVRWCRE MLRNSPIAIR CLKAALNADC DGQAGLQELA GNATMLFYMT EEGQEGRNAF NEKRAPDFSK FRRNP // ID METR_HAEIN Reviewed; 309 AA. AC P45349; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 106. DE RecName: Full=HTH-type transcriptional regulator MetR; GN Name=metR; OrderedLocusNames=HI_1739; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Control of the last step in methionine biosynthesis; CC MetR is a positive activator of the metA, metE and metH genes. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23383.1; -; Genomic_DNA. DR PIR; D64139; D64139. DR RefSeq; NP_439881.1; NC_000907.1. DR RefSeq; WP_005694223.1; NC_000907.1. DR ProteinModelPortal; P45349; -. DR STRING; 71421.HI1739; -. DR DNASU; 950886; -. DR EnsemblBacteria; AAC23383; AAC23383; HI_1739. DR GeneID; 950886; -. DR KEGG; hin:HI1739; -. DR PATRIC; 20192235; VBIHaeInf48452_1820. DR eggNOG; ENOG4105DZ2; Bacteria. DR eggNOG; ENOG410XQG7; LUCA. DR KO; K03576; -. DR OMA; ACEHLPF; -. DR OrthoDB; EOG64BQ3T; -. DR PhylomeDB; P45349; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Activator; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW DNA-binding; Methionine biosynthesis; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 309 HTH-type transcriptional regulator MetR. FT /FTId=PRO_0000105679. FT DOMAIN 6 63 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 23 42 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 309 AA; 35345 MW; A0C2F0277DE8B274 CRC64; MKPTFLEFRH LKTLLALKET GSVSLAAKRV YLTQSALSHQ IKLIEEQFGL PLFERKSNPL RFTSAGERLI RLANEVMPKV IDAERDLARV KHGDAGQLRI AVECHTCFDW LMPAMDEFRQ HWGLVELDIV SGFHTDPVGL LLSHRADWAI VSEIEHNDDV IFKPLFSYEM VGICSKNHSL AEKDIWEAED FIDETWVTYP VPDDMLDLWR KVLKSKGINP TRRTTELTIA MIQLVASRRG IATIPYWAAL PYLEKGYVVA RKVTKEGLYS NLYAAIRKED ESLSYLEDFY QTVKSQSFST LPGLSVLNL // ID MFD_HAEIN Reviewed; 1146 AA. AC P45128; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Transcription-repair-coupling factor {ECO:0000255|HAMAP-Rule:MF_00969}; DE Short=TRCF {ECO:0000255|HAMAP-Rule:MF_00969}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00969}; GN Name=mfd {ECO:0000255|HAMAP-Rule:MF_00969}; OrderedLocusNames=HI_1258; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent CC release of RNAP and its truncated transcript from the DNA, and CC recruitment of nucleotide excision repair machinery to the damaged CC site. {ECO:0000255|HAMAP-Rule:MF_00969}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family. CC {ECO:0000255|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase CC family. RecG subfamily. {ECO:0000255|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00969}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00969}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22905.1; -; Genomic_DNA. DR PIR; I64112; I64112. DR RefSeq; NP_439413.1; NC_000907.1. DR RefSeq; WP_005694314.1; NC_000907.1. DR ProteinModelPortal; P45128; -. DR STRING; 71421.HI1258; -. DR EnsemblBacteria; AAC22905; AAC22905; HI_1258. DR GeneID; 950181; -. DR KEGG; hin:HI1258; -. DR PATRIC; 20191197; VBIHaeInf48452_1310. DR eggNOG; ENOG4108JA2; Bacteria. DR eggNOG; COG1197; LUCA. DR KO; K03723; -. DR OMA; GTHKLIQ; -. DR OrthoDB; EOG6FNHKW; -. DR PhylomeDB; P45128; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00969; TRCF; 1. DR InterPro; IPR003711; CarD-like/TRCF_domain. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR004576; Mfd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005118; TRCF_C. DR Pfam; PF02559; CarD_CdnL_TRCF; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF03461; TRCF; 1. DR SMART; SM01058; CarD_TRCF; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00982; TRCF; 1. DR SUPFAM; SSF141259; SSF141259; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR TIGRFAMs; TIGR00580; mfd; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair; KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 1146 Transcription-repair-coupling factor. FT /FTId=PRO_0000102167. FT DOMAIN 617 778 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00969}. FT DOMAIN 800 953 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00969}. FT NP_BIND 630 637 ATP. {ECO:0000255|HAMAP-Rule:MF_00969}. FT MOTIF 731 734 DEEH box. SQ SEQUENCE 1146 AA; 130130 MW; 6E3052B431978475 CRC64; MKTAFFQPDI PTQPNDHKIL GNVLPGADAL AISEISEQNQ NLTVVVTPDT RSAVRLSRVL SELSSQDVCL FPDWETLPYD TFSPHQEIIS SRLSALFHLQ NAKKGIFLLP ISTLMQRLCP PQYLQHNVLL IKKGDRLVID KMRLQLEAAG YRAVEQVLEH GEYAVRGALL DLFPMGSAVP FRLDFFDDEI DSIRTFDVDT QRTLDEISSI NLLPAHEFPT DDKGIEFFRA QFRETFGEIR RDPEHIYQQI SKGTLISGIE YWQPLFFAEM ATLFDYLPEQ TLFVDMENNQ TQGERFYQDA KQRYEQRKVD PMRPLLSPEK LWLNVDEVNR RLKSYPRITF KAEKVRSSVR QKNLPVAALP EVTIQSQQKE PLGQLRQFIE HFKGNVLFSV ETEGRRETLL DLLSPLKLKP KQIQSLEQIE NEKFSLLVSS LEQGFIIEQS LPVAIIGEAN LLGKRIQQRS RDKRKTINPD TLVRNLAELK IGQPVVHLDH GVGRYGGLVT LDTGGIKAEY LLLNYANESK LYVPVTSLHL ISRYVGGSDE SAPLHKLGNE AWAKSRQKAA EKIRDVAAEL LDVYAQREAK KGFAFKYDRE EFQQFSATFP FEETYDQEMA INAVISDMCQ PKAMDRLVCG DVGFGKTEVA MRAAFLAVMN HKQVAVLVPT TLLAQQHYEN FKDRFANLPV NVEVLSRFKT AKEQKQILEN LAEGKVDILI GTHKLIQSDV KFNDLGLLII DEEHRFGVGQ KEKIKQLRAN IDILTLTATP IPRTLNMAMN GIRDLSIIST PPARRLSIKT FVRQNDDLVV REAILREILR GGQVYYLHND VASIENTAEK LTALVPEARV IVGHGQMRER ELERVMSDFY HQRYNVLVCS TIIETGIDVP TANTIIIERA DHFGLAQLHQ LRGRVGRSHH QAYAYLLTPP PKMMTKDAER RLDALENLDN LGAGFILATH DLEIRGAGEL LGNEQSGQIE SIGFSLYMEL LDAAVKALKE GREPSLEELT QQQADIELRV PALLPDDYLG DVNMRLSFYK RIAAAESKAE LDELKVELID RFGLLPDATK NLLQITELRL LVEPLNVVRI DAGTQGGFIE FSAKAQVNPD KFIQLIQKEP IVYRFDGPFK FKFMKDLSDN KVRLEFVVDL LRTIAA // ID MGLC_HAEIN Reviewed; 336 AA. AC P44885; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Galactoside transport system permease protein MglC; GN Name=mglC; OrderedLocusNames=HI_0824; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for galactoside. Probably responsible for the translocation of the CC substrate across the membrane (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. AraH/RbsC 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; L42023; AAC22483.1; -; Genomic_DNA. DR PIR; I64096; I64096. DR RefSeq; NP_438984.1; NC_000907.1. DR RefSeq; WP_005652434.1; NC_000907.1. DR STRING; 71421.HI0824; -. DR EnsemblBacteria; AAC22483; AAC22483; HI_0824. DR GeneID; 949838; -. DR KEGG; hin:HI0824; -. DR PATRIC; 20190303; VBIHaeInf48452_0865. DR eggNOG; ENOG4108HWV; Bacteria. DR eggNOG; COG4211; LUCA. DR KO; K10541; -. DR OMA; HLVFVYA; -. DR OrthoDB; EOG61P6T8; -. DR PhylomeDB; P44885; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR InterPro; IPR030158; MglC. DR PANTHER; PTHR32196:SF18; PTHR32196:SF18; 1. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 336 Galactoside transport system permease FT protein MglC. FT /FTId=PRO_0000060108. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 181 201 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. SQ SEQUENCE 336 AA; 35727 MW; F8B1474A9026B36B CRC64; MSALEKNKSF DLLKQNAIYF VLLILLGIII AQDPTFLNLV NFSNILTQSS VRLIIALGVA GLLITQGTDL SAGRQVGLAA VISATMLQSM ENINRVFPEM GQIPIPVVIL AVCAIGAVIG LVNGLVIAYL NVTPFIATMG TMIIIYGFNS LYYDAVGGSP IAGFSENFST FAQGFFRVGS FKLSYITIYA AIAALLVWIM WNKTRFGKNV FAIGGNPEAA KVSGVNVARN LVAIYMIAGM FYAFGGMLEA GRIGSATNNL GFMYELDAIA ACVVGGVSFA GGVGTVIGVI TGVIIFTVIN YGLTYIGVNP YWQYIIKGSI IILAVAIDSL KYAKKK // ID METB_HAEIN Reviewed; 369 AA. AC P44502; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 108. DE RecName: Full=Cystathionine gamma-synthase; DE Short=CGS; DE EC=2.5.1.48; DE AltName: Full=O-succinylhomoserine (thiol)-lyase; GN Name=metB; OrderedLocusNames=HI_0086; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of L-cystathionine from O- CC succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- CC replacement reaction. In the absence of thiol, catalyzes gamma- CC elimination to form 2-oxobutanoate, succinate and ammonia (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: O(4)-succinyl-L-homoserine + L-cysteine = L- CC cystathionine + succinate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21764.1; 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; L42023; AAC21764.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_438259.1; NC_000907.1. DR RefSeq; WP_005693832.1; NC_000907.1. DR ProteinModelPortal; P44502; -. DR STRING; 71421.HI0086; -. DR EnsemblBacteria; AAC21764; AAC21764; HI_0086. DR GeneID; 950982; -. DR KEGG; hin:HI0086; -. DR PATRIC; 20188627; VBIHaeInf48452_0087. DR eggNOG; ENOG4105C28; Bacteria. DR eggNOG; COG0626; LUCA. DR KO; K01739; -. DR OMA; SPIDCYL; -. DR OrthoDB; EOG67DPN3; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00868; CYS_MET_METAB_PP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Methionine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 369 Cystathionine gamma-synthase. FT /FTId=PRO_0000114757. FT MOD_RES 200 200 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 369 AA; 40371 MW; D76A8A03FEAF7A14 CRC64; MTQQYAIDTL LAQAGNRSDE RTGAVSAPIF LSTAYGHCGI GESTGFDYTR TKNPTRTVLE ETIAKLENGD RGFAFSSGMA AIQVLMTLFT APDEWIVSSD VYGGTYRLLD FSYKNNNSVK PVYVNTASAS AIEAAINPNT KAIFIETPSN PLMEECDVVE IAKLAKKHNL MLIVDNTFLT PVLSRPLDLG ADVVIHSGTK YIAGHNDALV GLIVAKGQEL CDRIAYIQNG AGAVLSPFDS WLTIRGMKTL SLRMKRHQEN AQAIAEFLKA QPQVESVLYP NKGGMLSFRL QDEAWVNTFL KSIKLITFAE SLGGTESFIT YPATQTHMDI PESERVARGI TNTLLRFSVG IEDVEDIKAD LLQAFANLK // ID METC_HAEIN Reviewed; 396 AA. AC P44527; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Cystathionine beta-lyase; DE Short=CBL; DE EC=4.4.1.8; DE AltName: Full=Beta-cystathionase; DE AltName: Full=Cysteine lyase; GN Name=metC; OrderedLocusNames=HI_0122; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: L-cystathionine + H(2)O = L-homocysteine + CC NH(3) + pyruvate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homocysteine from L-cystathionine: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes 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; L42023; AAC21796.1; -; Genomic_DNA. DR PIR; E64049; E64049. DR RefSeq; NP_438294.1; NC_000907.1. DR RefSeq; WP_005694414.1; NC_000907.1. DR ProteinModelPortal; P44527; -. DR SMR; P44527; 7-395. DR STRING; 71421.HI0122; -. DR EnsemblBacteria; AAC21796; AAC21796; HI_0122. DR GeneID; 951030; -. DR KEGG; hin:HI0122; -. DR PATRIC; 20188729; VBIHaeInf48452_0126. DR eggNOG; ENOG4105C28; Bacteria. DR eggNOG; COG0626; LUCA. DR KO; K01760; -. DR OMA; EQSYLMG; -. DR OrthoDB; EOG67DPN3; -. DR PhylomeDB; P44527; -. DR UniPathway; UPA00051; UER00078. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz. DR InterPro; IPR006233; Cys_b_lyase_bac. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1. DR PROSITE; PS00868; CYS_MET_METAB_PP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Lyase; KW Methionine biosynthesis; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 396 Cystathionine beta-lyase. FT /FTId=PRO_0000114770. FT MOD_RES 211 211 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 396 AA; 44345 MW; 5ABFD4A3C4F991EE CRC64; MQTKYDLSTM FIHSGRQKRF SQGSVNPVLQ RASSLLFDSI EDKKHATQRR AKGELFYGRR GTLTHFALQD LMCEMEGGAG CYLYPCGTAA VTNSILSFVK TGDHVLMSGA AYEPTQYFCN IVLKKMQIDI TYYDPLIGED IATLIQPNTK VLFLEAPSSI TMEIPDIPTI VKAARKVNPN IVIMIDNTWS AGVLFKALEH DIDISIQAGT KYLVGHSDIM IGTAVANART WDQLREHSYL MGQMVDADSA YTTARGIRTL GVRLKQHQES SIKVAKWLSE QPEVKTVYHP ALPSCPGHEF FLRDFSGSSG LFSFELTQRL TSEQVSKFMD HFQLFAMAYS WGGFESLILC NQPEEIAHIR PNIKRNLTGS LIRVHIGFEN VDELIADLKA GFERIA // ID METK_HAEIN Reviewed; 384 AA. AC P43762; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=S-adenosylmethionine synthase; DE Short=AdoMet synthase; DE EC=2.5.1.6; DE AltName: Full=MAT; DE AltName: Full=Methionine adenosyltransferase; GN Name=metK; OrderedLocusNames=HI_1172; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22825.1; -; Genomic_DNA. DR PIR; H64187; H64187. DR RefSeq; NP_439330.1; NC_000907.1. DR RefSeq; WP_010869144.1; NC_000907.1. DR ProteinModelPortal; P43762; -. DR SMR; P43762; 2-384. DR STRING; 71421.HI1172; -. DR EnsemblBacteria; AAC22825; AAC22825; HI_1172. DR GeneID; 950016; -. DR KEGG; hin:HI1172; -. DR PATRIC; 20191023; VBIHaeInf48452_1224. DR eggNOG; ENOG4105CPH; Bacteria. DR eggNOG; COG0192; LUCA. DR KO; K00789; -. DR OMA; DNFLAFD; -. DR OrthoDB; EOG68WR6M; -. DR PhylomeDB; P43762; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IBA:GO_Central. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00086; S_AdoMet_synth1; 1. DR InterPro; IPR022631; ADOMET_SYNTHASE_CS. DR InterPro; IPR022630; S-AdoMet_synt_C. DR InterPro; IPR022629; S-AdoMet_synt_central. DR InterPro; IPR022628; S-AdoMet_synt_N. DR InterPro; IPR002133; S-AdoMet_synthetase. DR InterPro; IPR022636; S-AdoMet_synthetase_sfam. DR PANTHER; PTHR11964; PTHR11964; 1. DR Pfam; PF02773; S-AdoMet_synt_C; 1. DR Pfam; PF02772; S-AdoMet_synt_M; 1. DR Pfam; PF00438; S-AdoMet_synt_N; 1. DR PIRSF; PIRSF000497; MAT; 1. DR SUPFAM; SSF55973; SSF55973; 3. DR TIGRFAMs; TIGR01034; metK; 1. DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1. DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cobalt; Complete proteome; Cytoplasm; Magnesium; KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 384 S-adenosylmethionine synthase. FT /FTId=PRO_0000174529. FT NP_BIND 260 267 ATP. {ECO:0000255}. FT METAL 17 17 Magnesium. {ECO:0000250}. FT METAL 43 43 Potassium. {ECO:0000250}. FT METAL 264 264 Potassium. {ECO:0000250}. FT METAL 272 272 Magnesium. {ECO:0000250}. SQ SEQUENCE 384 AA; 41974 MW; 3E4F873092C331B7 CRC64; MSSYLFTSES VSEGHPDKIA DQISDAVLDE ILKQDPKARV ACETYVKTGM ALVGGEITTS AWVDIENLTR KVICDIGYEH SEMGFDGHSC AVLNAIGKQS ADINQGVDRE NPLDQGAGDQ GIMFGYATNE TDVLMPAAIT YAHRLMEKQS EVRKSGKLAW LRPDAKSQVT LKYEDNKIVG VDAVVLSTQH SEEVSQKDLH EGVMEEIIKP VLPSEWLSKE TKFFINPTGR FVIGGPMGDC GLTGRKIIVD TYGGAARHGG GAFSGKEPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQLS YAIGVAEPTS IMVETFGTGK VANELLVSLV REFFDLRPYG LIKMLDLIQP IYRETAAYGH FGREQFPWEK VDRAEDLRIA AGLK // ID METQ_HAEIN Reviewed; 273 AA. AC P31728; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 105. DE RecName: Full=Probable D-methionine-binding lipoprotein MetQ; DE AltName: Full=28 kDa outer membrane protein; DE Flags: Precursor; GN Name=metQ; Synonyms=hlpA; OrderedLocusNames=HI_0620; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Serotype B; RX PubMed=1987077; RA Chanyangam M., Smith A.L., Moseley S.L., Kuehn M., Jenny P.; RT "Contribution of a 28-kilodalton membrane protein to the virulence of RT Haemophilus influenzae."; RL Infect. Immun. 59:600-608(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: This protein is a component of a D-methionine permease, CC a binding protein-dependent, ATP-driven transport system. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NlpA lipoprotein 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; M59804; AAA24939.1; -; Genomic_DNA. DR EMBL; L42023; AAC22279.1; -; Genomic_DNA. DR PIR; B64082; B64082. DR RefSeq; NP_438778.1; NC_000907.1. DR RefSeq; WP_005694548.1; NC_000907.1. DR ProteinModelPortal; P31728; -. DR STRING; 71421.HI0620; -. DR EnsemblBacteria; AAC22279; AAC22279; HI_0620. DR GeneID; 950676; -. DR KEGG; hin:HI0620; -. DR PATRIC; 20189823; VBIHaeInf48452_0644. DR eggNOG; ENOG4105D01; Bacteria. DR eggNOG; COG1464; LUCA. DR KO; K02073; -. DR OMA; QIWEVVT; -. DR OrthoDB; EOG6P073X; -. DR PhylomeDB; P31728; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR InterPro; IPR004872; Lipoprotein_NlpA. DR PANTHER; PTHR30429; PTHR30429; 1. DR Pfam; PF03180; Lipoprotein_9; 1. DR PIRSF; PIRSF002854; MetQ; 1. DR TIGRFAMs; TIGR00363; TIGR00363; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Amino-acid transport; Cell outer membrane; Complete proteome; KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal; KW Transport. FT SIGNAL 1 20 {ECO:0000305}. FT CHAIN 21 273 Probable D-methionine-binding lipoprotein FT MetQ. FT /FTId=PRO_0000019745. FT LIPID 21 21 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 21 21 S-diacylglycerol cysteine. {ECO:0000305}. FT CONFLICT 249 249 I -> V (in Ref. 1; AAA24939). FT {ECO:0000305}. SQ SEQUENCE 273 AA; 29828 MW; 429838A8AC7DD7D7 CRC64; MKLKQLFAIT AIASALVLTG CKEDKKPEAA AAPLKIKVGV MSGPEHQVAE IAAKVAKEKY GLDVQFVEFN DYALPNEAVS KGDLDANAMQ HKPYLDEDAK AKNLNNLVIV GNTFVYPLAG YSKKIKNVNE LQDGAKVVVP NDPTNRGRAL ILLEKQGLIK LKDANNLLST VLDIVENPKK LNITEVDTSV AARALDDVDL AVVNNTYAGQ VGLNAQDDGV FVEDKDSPYV NIIVSRTDNK DSKAVQDFIK SYQTEEVYQE AQKHFKDGVV KGW // ID MGSA_HAEIN Reviewed; 152 AA. AC P45120; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Methylglyoxal synthase; DE Short=MGS; DE EC=4.2.3.3; GN Name=mgsA; OrderedLocusNames=HI_1234; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Glycerone phosphate = methylglyoxal + CC phosphate. CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22887.1; -; Genomic_DNA. DR PIR; D64169; D64169. DR RefSeq; NP_439390.1; NC_000907.1. DR RefSeq; WP_010869160.1; NC_000907.1. DR STRING; 71421.HI1234; -. DR EnsemblBacteria; AAC22887; AAC22887; HI_1234. DR GeneID; 950176; -. DR KEGG; hin:HI1234; -. DR PATRIC; 20191147; VBIHaeInf48452_1286. DR eggNOG; ENOG4108Z5K; Bacteria. DR eggNOG; COG1803; LUCA. DR KO; K01734; -. DR OMA; EPQPHDP; -. DR OrthoDB; EOG644ZN1; -. DR PhylomeDB; P45120; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00549; Methylglyoxal_synth; 1. DR InterPro; IPR004363; Methylgl_synth. DR InterPro; IPR018148; Methylglyoxal_synth_AS. DR InterPro; IPR011607; MGS-like_dom. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF006614; Methylglyox_syn; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR TIGRFAMs; TIGR00160; MGSA; 1. DR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 152 Methylglyoxal synthase. FT /FTId=PRO_0000178631. FT ACT_SITE 71 71 {ECO:0000250}. SQ SEQUENCE 152 AA; 17065 MW; FC51303186402ABB CRC64; MQTTTRTLTQ HKRIALVAHD SCKKNLLNWT QKHKEALKPH ILYATGTTGH ILERETGLSI QSLLSGPMGG DQQLGGLIAE KKIDMMIFFW XPMNAAPHEP DVKALMRIAT VWNIPVAINQ SSADFLLTSV LFEQDVEIDV PDYEGYLKER LA // ID MIOC_HAEIN Reviewed; 146 AA. AC P44813; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=Protein MioC homolog; GN Name=mioC; OrderedLocusNames=HI_0669; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable electron transporter required for biotin CC synthase activity. {ECO:0000250}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the flavodoxin family. MioC subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22329.1; -; Genomic_DNA. DR PIR; C64085; C64085. DR RefSeq; NP_438829.1; NC_000907.1. DR RefSeq; WP_005694621.1; NC_000907.1. DR ProteinModelPortal; P44813; -. DR STRING; 71421.HI0669; -. DR EnsemblBacteria; AAC22329; AAC22329; HI_0669. DR GeneID; 949711; -. DR KEGG; hin:HI0669; -. DR PATRIC; 20189955; VBIHaeInf48452_0699. DR eggNOG; ENOG4105QTB; Bacteria. DR eggNOG; COG0716; LUCA. DR KO; K06205; -. DR OMA; FETTIHN; -. DR OrthoDB; EOG6MPWWD; -. DR PhylomeDB; P44813; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR001094; Flavdoxin-like. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR SUPFAM; SSF52218; SSF52218; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Flavoprotein; FMN; KW Reference proteome; Transport. FT CHAIN 1 146 Protein MioC homolog. FT /FTId=PRO_0000196574. FT DOMAIN 3 142 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. SQ SEQUENCE 146 AA; 16030 MW; 2A08A4E4133953EA CRC64; MHICILSGST LGGAEYVAEH LNDVLETQGF STALFHGPNL SDIENEKIWL VVTSTHGAGE LPDNLKPLFD ELANSQKDFS DVRFAVVGLG SSDYDTFCYA ADKVEQTLQA KSAVKICETL KIDVLNVDDQ ESYAEEWLPS FIEGLK // ID MOAE_HAEIN Reviewed; 150 AA. AC P45308; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Molybdopterin synthase catalytic subunit; DE EC=2.8.1.12; DE AltName: Full=MPT synthase subunit 2; DE AltName: Full=Molybdenum cofactor biosynthesis protein E; DE AltName: Full=Molybdopterin-converting factor large subunit; DE AltName: Full=Molybdopterin-converting factor subunit 2; GN Name=moaE; OrderedLocusNames=HI_1673; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts molybdopterin precursor Z into molybdopterin. CC This requires the incorporation of two sulfur atoms into precursor CC Z to generate a dithiolene group. The sulfur is provided by MoaD CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cyclic pyranopterin phosphate + 2 CC [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)- CC C(O)SH + H(2)O = molybdopterin + 2 [molybdopterin-synthase sulfur- CC carrier protein]. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. CC Also stable as homodimer. The enzyme changes between these two CC forms during catalysis (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MoaE 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; L42023; AAC23318.1; -; Genomic_DNA. DR PIR; H64135; H64135. DR RefSeq; NP_439815.1; NC_000907.1. DR RefSeq; WP_005694395.1; NC_000907.1. DR ProteinModelPortal; P45308; -. DR SMR; P45308; 3-150. DR STRING; 71421.HI1673; -. DR EnsemblBacteria; AAC23318; AAC23318; HI_1673. DR GeneID; 950861; -. DR KEGG; hin:HI1673; -. DR PATRIC; 20192097; VBIHaeInf48452_1752. DR eggNOG; ENOG4108ZAF; Bacteria. DR eggNOG; COG0314; LUCA. DR KO; K03635; -. DR OMA; RERWPLN; -. DR OrthoDB; EOG6KMBD9; -. DR PhylomeDB; P45308; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030366; F:molybdopterin synthase activity; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.90.1170.40; -; 1. DR InterPro; IPR003448; Mopterin_biosynth_MoaE. DR PANTHER; PTHR23404:SF2; PTHR23404:SF2; 1. DR Pfam; PF02391; MoaE; 1. DR SUPFAM; SSF54690; SSF54690; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 150 Molybdopterin synthase catalytic subunit. FT /FTId=PRO_0000163084. FT REGION 37 39 Substrate binding. {ECO:0000250}. FT REGION 103 104 Substrate binding. {ECO:0000250}. FT REGION 126 128 Substrate binding. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000250}. SQ SEQUENCE 150 AA; 17212 MW; 35149D46365F0185 CRC64; MTDIQIAVQE QPFDQNAVYQ WLSEQHSIGA TVIFVGKVRD LNLGDEVSSL YLEHYPAMTE KALNEIVAQA KVRWDIQRVS VIHRVGLLQT GDEIVLVGVS SAHRGDAYHA NEFIMDFLKS KAPFWKKEQT NQGERWIEAR ESDKEALEKW // ID MOBA_HAEIN Reviewed; 192 AA. AC P44899; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Molybdenum cofactor guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316}; DE Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316}; GN Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316}; Synonyms=mob; GN OrderedLocusNames=HI_0844; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo- CC MPT) cofactor (Moco or molybdenum cofactor) to form Mo- CC molybdopterin guanine dinucleotide (Mo-MGD) cofactor. CC {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate + CC guanylyl molybdenum cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00316}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition CC and specific binding, while the C-terminal domain determines the CC specific binding to the target protein. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22501.1; -; Genomic_DNA. DR PIR; A64098; A64098. DR RefSeq; NP_439004.1; NC_000907.1. DR RefSeq; WP_005693194.1; NC_000907.1. DR ProteinModelPortal; P44899; -. DR STRING; 71421.HI0844; -. DR EnsemblBacteria; AAC22501; AAC22501; HI_0844. DR GeneID; 950590; -. DR KEGG; hin:HI0844; -. DR PATRIC; 20190343; VBIHaeInf48452_0885. DR eggNOG; ENOG4105C6R; Bacteria. DR eggNOG; COG0746; LUCA. DR KO; K03752; -. DR OMA; DELPDFQ; -. DR OrthoDB; EOG6PKFG0; -. DR PhylomeDB; P44899; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00316; MobA; 1. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR013482; Molybde_CF_guanTrfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR02665; molyb_mobA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Molybdenum cofactor biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 192 Molybdenum cofactor guanylyltransferase. FT /FTId=PRO_0000134891. FT NP_BIND 10 12 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT METAL 99 99 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00316}. FT BINDING 23 23 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 51 51 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 69 69 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 99 99 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. SQ SEQUENCE 192 AA; 21754 MW; 804AC64948CD3AFD CRC64; MTITISAVIL AGGKARRMGG QDKGLQILGK QSLIEHIINR LQPQIHQISI NANRNQTEYA KFGFPVFSDE LPDFQGPLSG MLTALEKTKS DFILFTPCDT PFFPMNLLDK LKSAVKNDRT LIAYACDEER EHPVFCLMSV QLKEKLRHYL ASGERRLLQF MKENGGISVK FTQEEGNFEN FNTLDDLKKT VI // ID MOEA_HAEIN Reviewed; 404 AA. AC P45210; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Molybdopterin molybdenumtransferase; DE Short=MPT Mo-transferase; DE EC=2.10.1.1; GN Name=moeA; Synonyms=chlE; OrderedLocusNames=HI_1448; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the insertion of molybdate into adenylated CC molybdopterin with the concomitant release of AMP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate = CC molybdenum cofactor + AMP. 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 -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoeA 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; L42023; AAC23098.1; -; Genomic_DNA. DR PIR; B64124; B64124. DR RefSeq; NP_439600.1; NC_000907.1. DR RefSeq; WP_005693918.1; NC_000907.1. DR ProteinModelPortal; P45210; -. DR SMR; P45210; 1-403. DR STRING; 71421.HI1448; -. DR EnsemblBacteria; AAC23098; AAC23098; HI_1448. DR GeneID; 950719; -. DR KEGG; hin:HI1448; -. DR PATRIC; 20191601; VBIHaeInf48452_1510. DR eggNOG; ENOG4105CVM; Bacteria. DR eggNOG; COG0303; LUCA. DR KO; K03750; -. DR OMA; LAHDVHA; -. DR OrthoDB; EOG66MQMC; -. DR PhylomeDB; P45210; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IBA:GO_Central. DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central. DR Gene3D; 2.40.340.10; -; 1. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR InterPro; IPR005111; MoeA_C_domain_IV. DR InterPro; IPR005110; MoeA_linker/N. DR Pfam; PF00994; MoCF_biosynth; 1. DR Pfam; PF03454; MoeA_C; 1. DR Pfam; PF03453; MoeA_N; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR SUPFAM; SSF63867; SSF63867; 1. DR SUPFAM; SSF63882; SSF63882; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Molybdenum; KW Molybdenum cofactor biosynthesis; Reference proteome; Transferase. FT CHAIN 1 404 Molybdopterin molybdenumtransferase. FT /FTId=PRO_0000170990. SQ SEQUENCE 404 AA; 44310 MW; 5844F4B4DF123728 CRC64; MLTLDQARSK MLEQLPFPTQ TEYLNLQEAA NRICAEDIIS PINVPSFDNS AMDGYAVRLS DLQQSLTLSV AGKSFAGNPF QEEWPSKSAV RIMTGAMIPE GTDAVIMQEQ VTLNEDGTIT FSELPKPNQN IRRIGEDVKK GDVVLEQGAQ LTPVSLPLLA SLGIAEVKCY RQLKVGVLST GDELVEVGKP LQSGQIYDTN RFTVKLLLEK LHCEVIDLGL LPDNEAEFEK AFIAAQSQAD LVITSGGVSV GEADFTKAVL EKVGQVNFWK IAIKPGKPFA FGKLENAWFC GLPGNPVSAL VTFYQLVQPL IAKLQGQKQW KKPPHFSAIA TMNLKKAVGR LDFQRGFYYI NEQGQIEVQS VGFQGSHLFS AFVKSNCFIV LEQERGNVSA GETVTIEPFN HLLG // ID MIAA_HAEIN Reviewed; 311 AA. AC P44495; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; Synonyms=trpX; GN OrderedLocusNames=HI_0068; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the CC adenine at position 37 in tRNAs that read codons beginning with CC uridine, leading to the formation of N6-(dimethylallyl)adenosine CC (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + adenine(37) in CC tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. CC {ECO:0000255|HAMAP-Rule:MF_00185}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21746.1; -; Genomic_DNA. DR PIR; F64046; F64046. DR RefSeq; NP_438241.1; NC_000907.1. DR RefSeq; WP_005693854.1; NC_000907.1. DR ProteinModelPortal; P44495; -. DR SMR; P44495; 3-305. DR STRING; 71421.HI0068; -. DR EnsemblBacteria; AAC21746; AAC21746; HI_0068. DR GeneID; 950968; -. DR KEGG; hin:HI0068; -. DR PATRIC; 20188591; VBIHaeInf48452_0069. DR eggNOG; ENOG4105DKX; Bacteria. DR eggNOG; COG0324; LUCA. DR KO; K00791; -. DR OMA; HTRNYAK; -. DR OrthoDB; EOG661HB3; -. DR PhylomeDB; P44495; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR018022; IPP_trans. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase; tRNA processing. FT CHAIN 1 311 tRNA dimethylallyltransferase. FT /FTId=PRO_0000163924. FT NP_BIND 10 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 12 17 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00185}. FT REGION 35 38 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 159 163 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT REGION 240 245 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 101 101 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. FT SITE 123 123 Interaction with substrate tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00185}. SQ SEQUENCE 311 AA; 35204 MW; 4B5E3EEFE28DC637 CRC64; MKPTAIFLMG PTASGKTDLA IQLRSQLPVE VISVDSALIY KGMDIGTAKP SKEELALAPH RLIDILDPSE SYSAMNFRDD ALREMADITA QGKIPLLVGG TMLYYKALIE GLSPLPSADE NIRAELEQKA AQQGWAALHT ELAKIDPISA ARINPSDSQR INRALEVFYI TGKSLTELTE EKGEALPYDF VQFAIAPQDR HVLHERIEQR FHKMIELGFQ AEVEKLYARG DLNINLPSIR CVGYRQMWEY LQGDYAYEEM IFRGICATRQ LAKRQLTWLR GWKTPIQWLD SLQPQQAKET VLRHLDSYQK G // ID MLAA_HAEIN Reviewed; 250 AA. AC P44042; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Probable phospholipid-binding lipoprotein MlaA {ECO:0000250|UniProtKB:P76506}; DE Flags: Precursor; GN Name=mlaA {ECO:0000250|UniProtKB:P76506}; OrderedLocusNames=HI_0718; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Actively prevents phospholipid accumulation at the cell CC surface. Probably maintains lipid asymmetry in the outer membrane CC by retrograde trafficking of phospholipids from the outer membrane CC to the inner membrane. {ECO:0000250|UniProtKB:P76506}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000250|UniProtKB:P76506}; Lipid-anchor CC {ECO:0000250|UniProtKB:P76506, ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Belongs to the MlaA 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; L42023; AAC22375.1; -; Genomic_DNA. DR PIR; F64012; F64012. DR RefSeq; NP_438876.1; NC_000907.1. DR RefSeq; WP_005694634.1; NC_000907.1. DR STRING; 71421.HI0718; -. DR DNASU; 949738; -. DR EnsemblBacteria; AAC22375; AAC22375; HI_0718. DR GeneID; 949738; -. DR KEGG; hin:HI0718; -. DR PATRIC; 20190059; VBIHaeInf48452_0750. DR eggNOG; ENOG410903C; Bacteria. DR eggNOG; COG2853; LUCA. DR KO; K04754; -. DR OMA; GIHNIFR; -. DR OrthoDB; EOG6677N2; -. DR PhylomeDB; P44042; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007428; VacJ. DR PANTHER; PTHR30035; PTHR30035; 1. DR Pfam; PF04333; MlaA; 1. DR PRINTS; PR01805; VACJLIPOPROT. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 19 250 Probable phospholipid-binding lipoprotein FT MlaA. FT /FTId=PRO_0000018212. FT LIPID 19 19 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 250 AA; 28110 MW; 7DDEC4FC587091BB CRC64; MKTKTILTAL LSAIALTGCA NNNDTKQVSE RNDSLEDFNR TMWKFNYNVI DRYVLEPAAK GWNNYVPKPI SSGLAGIANN LDEPVSFINR LIEGEPKKAF VHFNRFWINT VFGLGGFIDF ASASKELRID NQRGFGETLG SYGVDAGTYI VLPIYNATTP RQLTGAVVDA AYMYPFWQWV GGPWALVKYG VQAVDARAKN LNNAELLRQA QDPYITFREA YYQNLQFKVN DGKLVESKES LPDDILKEID // ID MLAB_HAEIN Reviewed; 105 AA. AC Q57407; O05044; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Probable phospholipid ABC transporter-binding protein MlaB {ECO:0000250|UniProtKB:P64602}; GN Name=mlaB {ECO:0000250|UniProtKB:P64602}; OrderedLocusNames=HI_1083; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex MlaFEDB that CC actively prevents phospholipid accumulation at the cell surface. CC Probably maintains lipid asymmetry in the outer membrane by CC retrograde trafficking of phospholipids from the outer membrane to CC the inner membrane. {ECO:0000250|UniProtKB:P64602}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute- CC binding proteins (MlaB) and a periplamic solute-binding protein CC (MlaD). {ECO:0000250|UniProtKB:P64602}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P64602}. CC -!- SIMILARITY: Contains 1 STAS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22739.1; -; Genomic_DNA. DR PIR; A64166; A64166. DR RefSeq; NP_439240.1; NC_000907.1. DR RefSeq; WP_005693407.1; NC_000907.1. DR ProteinModelPortal; Q57407; -. DR STRING; 71421.HI1083; -. DR EnsemblBacteria; AAC22739; AAC22739; HI_1083. DR GeneID; 950057; -. DR KEGG; hin:HI1083; -. DR PATRIC; 20190831; VBIHaeInf48452_1128. DR eggNOG; COG3113; LUCA. DR KO; K07122; -. DR OMA; VWELSEV; -. DR OrthoDB; EOG6CK7R4; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.30.750.24; -; 1. DR InterPro; IPR002645; STAS_dom. DR Pfam; PF13466; STAS_2; 1. DR SUPFAM; SSF52091; SSF52091; 1. DR PROSITE; PS50801; STAS; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transport. FT CHAIN 1 105 Probable phospholipid ABC transporter- FT binding protein MlaB. FT /FTId=PRO_0000078001. FT DOMAIN 4 105 STAS. {ECO:0000255|PROSITE- FT ProRule:PRU00198}. SQ SEQUENCE 105 AA; 12105 MW; 0A629D39D79FDF6A CRC64; MLNWDLQKNN DKITLFLFGE LSRSTLLPMW QQRGVFLSAS TLDKTIVEWN LSDLQHIDSA GFAALCDFLR ECQKLNKTVR LVYPPKQLLT LADLFGLSDW IANFI // ID MLAD_HAEIN Reviewed; 167 AA. AC P45029; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Probable phospholipid ABC transporter-binding protein MlaD {ECO:0000250|UniProtKB:P64604}; GN Name=mlaD {ECO:0000250|UniProtKB:P64604}; OrderedLocusNames=HI_1085; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex MlaFEDB that CC actively prevents phospholipid accumulation at the cell surface. CC Probably maintains lipid asymmetry in the outer membrane by CC retrograde trafficking of phospholipids from the outer membrane to CC the inner membrane. {ECO:0000250|UniProtKB:P64604}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute- CC binding proteins (MlaB) and a periplamic solute-binding protein CC (MlaD). {ECO:0000250|UniProtKB:P64604}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P64604}; Single-pass type II membrane CC protein {ECO:0000250|UniProtKB:P64604}; Periplasmic side CC {ECO:0000250|UniProtKB:P64604}. CC -!- SIMILARITY: Belongs to the MlaD 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; L42023; AAC22741.1; -; Genomic_DNA. DR PIR; C64166; C64166. DR RefSeq; NP_439242.1; NC_000907.1. DR RefSeq; WP_005693409.1; NC_000907.1. DR STRING; 71421.HI1085; -. DR EnsemblBacteria; AAC22741; AAC22741; HI_1085. DR GeneID; 950060; -. DR KEGG; hin:HI1085; -. DR PATRIC; 20190835; VBIHaeInf48452_1130. DR eggNOG; ENOG4107PE3; Bacteria. DR eggNOG; COG1463; LUCA. DR KO; K02067; -. DR OMA; EQYIGLE; -. DR OrthoDB; EOG6F296G; -. DR PhylomeDB; P45029; -. DR Proteomes; UP000000579; 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:0015914; P:phospholipid transport; IEA:InterPro. DR InterPro; IPR030970; ABC_MlaD. DR InterPro; IPR003399; Mce/MlaD. DR Pfam; PF02470; MlaD; 1. DR TIGRFAMs; TIGR04430; OM_asym_MlaD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 167 Probable phospholipid ABC transporter- FT binding protein MlaD. FT /FTId=PRO_0000169464. FT TOPO_DOM 1 6 Cytoplasmic. FT {ECO:0000250|UniProtKB:P64604}. FT TRANSMEM 7 27 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 28 167 Periplasmic. FT {ECO:0000250|UniProtKB:P64604}. SQ SEQUENCE 167 AA; 18111 MW; 92A10F1B0FA72544 CRC64; MRQTIKYEFW VGLFLLLGIG ALVFLGLRVA NVQGFAETKS YTVTATFDNI GGLKVRAPLK IGGVVIGRVS AITLDEKSYL PKVSIAINQE YNEIPENSSL SIKTSGLLGE QYIALTMGFD DGDTAMLKNG SQIQDTTSAM VLEDLIGQFL YGSKKSDGNE KSESTEQ // ID MODA_HAEIN Reviewed; 254 AA. AC P45323; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Molybdate-binding periplasmic protein; DE Flags: Precursor; GN Name=modA; OrderedLocusNames=HI_1693; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 25-29. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Involved in the transport of molybdenum into the cell. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA 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; L42023; AAC23339.1; -; Genomic_DNA. DR EMBL; M94855; AAA24985.1; -; Genomic_DNA. DR PIR; A64175; A64175. DR PIR; S27583; S27583. DR RefSeq; NP_439835.1; NC_000907.1. DR RefSeq; WP_005694182.1; NC_000907.1. DR ProteinModelPortal; P45323; -. DR STRING; 71421.HI1693; -. DR EnsemblBacteria; AAC23339; AAC23339; HI_1693. DR GeneID; 950605; -. DR KEGG; hin:HI1693; -. DR PATRIC; 20192137; VBIHaeInf48452_1772. DR eggNOG; ENOG4108S6J; Bacteria. DR eggNOG; COG0725; LUCA. DR KO; K02020; -. DR OMA; LTHENLW; -. DR OrthoDB; EOG680X4N; -. DR PhylomeDB; P45323; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015412; F:molybdate transmembrane-transporting ATPase activity; IEA:InterPro. DR InterPro; IPR005950; Mo_ABC_perip-bd. DR PIRSF; PIRSF004846; ModA; 1. DR TIGRFAMs; TIGR01256; modA; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Molybdenum; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1 24 {ECO:0000269|PubMed:10675023}. FT CHAIN 25 254 Molybdate-binding periplasmic protein. FT /FTId=PRO_0000031828. FT CONFLICT 151 151 E -> A (in Ref. 2; AAA24985). FT {ECO:0000305}. FT CONFLICT 164 164 K -> Q (in Ref. 2; AAA24985). FT {ECO:0000305}. FT CONFLICT 170 170 G -> A (in Ref. 2; AAA24985). FT {ECO:0000305}. SQ SEQUENCE 254 AA; 27302 MW; 3292D9C1F8274285 CRC64; MKKLTKISTA LLIAGLGFSF AASAKVTVFA AASMTDALQQ VAKDYAKQNP KNEVVFSFAS SSTLAKQVEE GAPADIFVSA SNKWMKYLSE KDLTVKETEK VLVGNDLVLI APAKSAVNSV DIAKGEWINA LKDSYLSVGD PAHVPAGQYA EEALTKLNLW DKVKDRLARG KDVRGALALV ERAEAPYGIV YSTDAKVSQQ VKTVAVFPAD SHKPVVYPVS IVKGHDNADS RDFLKYLESD AAKKVLVGYG FSAK // ID MLAC_HAEIN Reviewed; 214 AA. AC P45028; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 92. DE RecName: Full=Probable phospholipid-binding protein MlaC {ECO:0000250|UniProtKB:P0ADV7}; DE Flags: Precursor; GN Name=mlaC {ECO:0000250|UniProtKB:P0ADV7}; OrderedLocusNames=HI_1084; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Actively prevents phospholipid accumulation at the cell CC surface. Probably maintains lipid asymmetry in the outer membrane CC by retrograde trafficking of phospholipids from the outer membrane CC to the inner membrane. May transfer phospholipid across the CC periplasmic space and deliver it to the MlaFEDB complex at the CC inner membrane. {ECO:0000250|UniProtKB:P0ADV7}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0ADV7}. CC -!- SIMILARITY: Belongs to the MlaC/ttg2D 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; L42023; AAC22740.1; -; Genomic_DNA. DR PIR; B64166; B64166. DR RefSeq; NP_439241.1; NC_000907.1. DR RefSeq; WP_005693408.1; NC_000907.1. DR ProteinModelPortal; P45028; -. DR STRING; 71421.HI1084; -. DR EnsemblBacteria; AAC22740; AAC22740; HI_1084. DR GeneID; 950058; -. DR KEGG; hin:HI1084; -. DR PATRIC; 20190833; VBIHaeInf48452_1129. DR eggNOG; ENOG4105E3I; Bacteria. DR eggNOG; COG2854; LUCA. DR KO; K07323; -. DR OMA; QSEWNGK; -. DR OrthoDB; EOG6X10ZT; -. DR PhylomeDB; P45028; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR Gene3D; 1.10.10.640; -; 2. DR Gene3D; 3.10.450.50; -; 2. DR InterPro; IPR008869; MlaC/ttg2D. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR023094; Tol_tolerance_alpha. DR Pfam; PF05494; MlaC; 1. DR PIRSF; PIRSF004649; MlaC; 1. PE 1: Evidence at protein level; KW Complete proteome; Periplasm; Reference proteome; Signal. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 214 Probable phospholipid-binding protein FT MlaC. FT /FTId=PRO_0000013917. SQ SEQUENCE 214 AA; 24510 MW; 5D209A3646FBEE75 CRC64; MNLIQLKKWF TILTFVLTAF LVTRTAIAET SPYVLMQQAA DKLFSDIQAN QSKIKQDPNY LRTIVRNDLL PYVNLEYAGS KVLGSYYKST SAEQREKFFK TFGELIEQKY AQALTNYSNQ KIQIESEKEL GDNNFINIRV NIIQANGVAP ILLYFKWRKG NKSGEWKVYD MVGAGVSMLE DTIKNWVGIL NKQGIDTLIT KMQQSASQPI IFNQ // ID MLAE_HAEIN Reviewed; 261 AA. AC P45030; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 107. DE RecName: Full=Probable phospholipid ABC transporter permease protein MlaE {ECO:0000250|UniProtKB:P64606}; GN Name=mlaE {ECO:0000250|UniProtKB:P64606}; OrderedLocusNames=HI_1086; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex MlaFEDB that CC actively prevents phospholipid accumulation at the cell surface. CC Probably maintains lipid asymmetry in the outer membrane by CC retrograde trafficking of phospholipids from the outer membrane to CC the inner membrane. {ECO:0000250|UniProtKB:P64606}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute- CC binding proteins (MlaB) and a periplamic solute-binding protein CC (MlaD). {ECO:0000250|UniProtKB:P64606}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P64606}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the MlaE permease 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; L42023; AAC22742.1; -; Genomic_DNA. DR PIR; D64166; D64166. DR RefSeq; NP_439243.1; NC_000907.1. DR RefSeq; WP_005693411.1; NC_000907.1. DR STRING; 71421.HI1086; -. DR EnsemblBacteria; AAC22742; AAC22742; HI_1086. DR GeneID; 950061; -. DR KEGG; hin:HI1086; -. DR PATRIC; 20190837; VBIHaeInf48452_1131. DR eggNOG; ENOG4105CY3; Bacteria. DR eggNOG; COG0767; LUCA. DR KO; K02066; -. DR OMA; YIMTELL; -. DR OrthoDB; EOG6RJV8Q; -. DR PhylomeDB; P45030; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central. DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central. DR InterPro; IPR003453; ABC_MlaE_Proteobac. DR InterPro; IPR030802; Permease_MalE. DR PANTHER; PTHR30188; PTHR30188; 1. DR Pfam; PF02405; MlaE; 1. DR TIGRFAMs; TIGR00056; TIGR00056; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 261 Probable phospholipid ABC transporter FT permease protein MlaE. FT /FTId=PRO_0000169469. FT TOPO_DOM 1 12 Cytoplasmic. FT {ECO:0000250|UniProtKB:P64606}. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TOPO_DOM 34 49 Periplasmic. FT {ECO:0000250|UniProtKB:P64606}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. FT TOPO_DOM 71 147 Cytoplasmic. FT {ECO:0000250|UniProtKB:P64606}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TOPO_DOM 169 198 Periplasmic. FT {ECO:0000250|UniProtKB:P64606}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TOPO_DOM 220 238 Cytoplasmic. FT {ECO:0000250|UniProtKB:P64606}. FT TRANSMEM 239 259 Helical. {ECO:0000255}. FT TOPO_DOM 260 261 Periplasmic. FT {ECO:0000250|UniProtKB:P64606}. SQ SEQUENCE 261 AA; 28015 MW; 4BC3695F247A6BF6 CRC64; MIVNFISALG KQVIDFFRAL GRAGFMLFGA LIGKPQIRKH FPLLVKQMHV LGVQSLLIIL LSGLFIGMVL GLQGYVVLID FSAETSLGQL VALSLLRELG PVVTALLFAG RAGSALTAEI GLMKATEQLS SLEMMAVDPL RRVIAPRFWA GVISMPVLSI LFIAIGIWGG SLVGVDWKGV DSGSFWSVMQ NSVSWSYDIL NGFIKAVFFA VAVTWIALFN GYDCMPTSEG ISQATTRTVV HASLVVLGLD FILTAIMFGA G // ID MLAF_HAEIN Reviewed; 264 AA. AC P45031; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Probable phospholipid import ATP-binding protein MlaF {ECO:0000250|UniProtKB:P63386}; DE EC=3.6.3.- {ECO:0000250|UniProtKB:P63386}; GN Name=mlaF {ECO:0000250|UniProtKB:P63386}; OrderedLocusNames=HI_1087; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the ABC transporter complex MlaFEDB that CC actively prevents phospholipid accumulation at the cell surface. CC Probably maintains lipid asymmetry in the outer membrane by CC retrograde trafficking of phospholipids from the outer membrane to CC the inner membrane. Probably responsible for energy coupling to CC the transport system. {ECO:0000250|UniProtKB:P63386}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute- CC binding proteins (MlaB) and a periplamic solute-binding protein CC (MlaD). {ECO:0000250|UniProtKB:P63386}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P63386}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P63386}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P63386}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. MlaF CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22743.1; -; Genomic_DNA. DR PIR; B64182; B64182. DR RefSeq; NP_439244.1; NC_000907.1. DR RefSeq; WP_005693412.1; NC_000907.1. DR ProteinModelPortal; P45031; -. DR STRING; 71421.HI1087; -. DR EnsemblBacteria; AAC22743; AAC22743; HI_1087. DR GeneID; 950090; -. DR KEGG; hin:HI1087; -. DR PATRIC; 20190839; VBIHaeInf48452_1132. DR eggNOG; ENOG4105DHJ; Bacteria. DR eggNOG; COG1127; LUCA. DR KO; K02065; -. DR OMA; QLIMFDE; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45031; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 264 Probable phospholipid import ATP-binding FT protein MlaF. FT /FTId=PRO_0000093174. FT DOMAIN 6 242 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 264 AA; 29395 MW; 0DB1F7DCE9853C25 CRC64; MNQNLIEVKN LTFKRGDRVI YDNLNLQVKK GKITAIMGPS GIGKTTLLKL IGGQLMPEQG EILFDGQDIC RLSNRELYEV RKRMGMLFQS GALFTDISTF DNVAFPIREH THLPENLIRQ IVLMKLEAVG LRGAAALMPS ELSGGMARRA ALARAIALDP DLIMFDEPFT GQDPISMGVI LSLIKRLNEA LNLTSIVVSH DVEEVLSIAD YAYIIADQKV IAEGTSEQLL QSQDLRVVQF LKGESDGPVR FKYPAQDYVK ELFE // ID MLTC_HAEIN Reviewed; 357 AA. AC P44049; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Membrane-bound lytic murein transglycosylase C {ECO:0000255|HAMAP-Rule:MF_01616}; DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_01616}; DE AltName: Full=Murein lyase C {ECO:0000255|HAMAP-Rule:MF_01616}; DE Flags: Precursor; GN Name=mltC {ECO:0000255|HAMAP-Rule:MF_01616}; GN OrderedLocusNames=HI_0761; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of CC muropeptides during cell elongation and/or cell division. CC {ECO:0000255|HAMAP-Rule:MF_01616}. CC -!- CATALYTIC ACTIVITY: Exolytic cleavage of the (1->4)-beta- CC glycosidic linkage between N-acetylmuramic acid (MurNAc) and N- CC acetylglucosamine (GlcNAc) residues in peptidoglycan, from either CC the reducing or the non-reducing ends of the peptidoglycan chains, CC with concomitant formation of a 1,6-anhydrobond in the MurNAc CC residue. {ECO:0000255|HAMAP-Rule:MF_01616}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP- CC Rule:MF_01616}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01616}. CC -!- SIMILARITY: Belongs to the transglycosylase Slt family. CC {ECO:0000255|HAMAP-Rule:MF_01616}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22420.1; -; Genomic_DNA. DR PIR; D64013; D64013. DR RefSeq; NP_438920.1; NC_000907.1. DR RefSeq; WP_005693158.1; NC_000907.1. DR ProteinModelPortal; P44049; -. DR STRING; 71421.HI0761; -. DR EnsemblBacteria; AAC22420; AAC22420; HI_0761. DR GeneID; 950821; -. DR KEGG; hin:HI0761; -. DR PATRIC; 20190169; VBIHaeInf48452_0800. DR eggNOG; ENOG4106S48; Bacteria. DR eggNOG; COG0741; LUCA. DR KO; K08306; -. DR OMA; AIMQIES; -. DR OrthoDB; EOG6Z0Q66; -. DR PhylomeDB; P44049; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-EC. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro. DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro. DR HAMAP; MF_01616; MltC; 1. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR023664; Murein_transglycosylaseC. DR InterPro; IPR024570; Murein_transglycosylaseC_N. DR InterPro; IPR000189; Transglyc_AS. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF11873; DUF3393; 1. DR Pfam; PF01464; SLT; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1. PE 3: Inferred from homology; KW Cell outer membrane; Cell wall biogenesis/degradation; KW Complete proteome; Lipoprotein; Lyase; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 15 {ECO:0000255|HAMAP-Rule:MF_01616}. FT CHAIN 16 357 Membrane-bound lytic murein FT transglycosylase C. FT /FTId=PRO_0000032790. FT LIPID 16 16 N-palmitoyl cysteine. {ECO:0000255|HAMAP- FT Rule:MF_01616}. FT LIPID 16 16 S-diacylglycerol cysteine. FT {ECO:0000255|HAMAP-Rule:MF_01616}. SQ SEQUENCE 357 AA; 40207 MW; 277DCF968E7248DD CRC64; MKKYLLLALL PFLYACSNSS NQGINYDEAF AKDTQGLDIL TGQFSHNIDR IWGVNELLVA SRKDYVKYTD SFYTRSHVSF DEGNIVIETQ QDLNRLHNAI VHTLLMGADA KGIDLFASGD VPISSRPFLL GQVVDHQGQH IANQVIASNF ATYLIQNKLQ TRRLQNGHTV QFVSVPMIAN HVEVRARKYL PLIRKAAQRY GIDESLILGI MQTESSFNPY AISYANAIGL MQVVPHTAGR DVFAMKGKGG QPSTRYLYDP ANNIDAGVSY LWILQNQYLD GITNPTSKRF AMISAYNSGA GAVLRVFDND KDTAIYKINQ MYPEQVYRIL TTVHPSSQAR NYLLKVDKAQ KKFRVRR // ID MNME_HAEIN Reviewed; 452 AA. AC P43730; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 17-FEB-2016, entry version 110. 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=HI_1002; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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=AAC22664.1; 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; L42023; AAC22664.1; ALT_INIT; Genomic_DNA. DR PIR; G64107; G64107. DR RefSeq; NP_439164.1; NC_000907.1. DR ProteinModelPortal; P43730; -. DR STRING; 71421.HI1002; -. DR EnsemblBacteria; AAC22664; AAC22664; HI_1002. DR GeneID; 949988; -. DR KEGG; hin:HI1002; -. DR PATRIC; 20190665; VBIHaeInf48452_1045. DR eggNOG; ENOG4105C1H; Bacteria. DR eggNOG; COG0486; LUCA. DR KO; K03650; -. DR OMA; FTPRYAY; -. DR OrthoDB; EOG6DC6K1; -. DR Proteomes; UP000000579; 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 1 452 tRNA modification GTPase MnmE. FT /FTId=PRO_0000188881. FT DOMAIN 214 375 TrmE-type G. FT NP_BIND 224 229 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 243 249 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT NP_BIND 268 271 GTP. {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 224 224 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 228 228 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 243 243 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 245 245 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT METAL 248 248 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT METAL 249 249 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00379}. FT BINDING 21 21 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 78 78 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 118 118 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. FT BINDING 452 452 Formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_00379}. SQ SEQUENCE 452 AA; 49232 MW; EC1362AF7778F8FF CRC64; MKETIVAQAT APGRGGIGIL RVSGPLATKV AQAILGKCPK PRMADYLPFK DADGTILDQG IALYFKSPNS FTGEDVLELQ GHGGQVVLDL LLKRILQIDG IRLARPGEFS EQAFLNDKLD LAQAEAIADL IDATSEQAVR SALKSLQGEF SKKVNELVDS VIYLRTYVEA SIDFPDEEID FLADGKIEAN LRGIINQLED VRSEAKQGSI LREGMKVVIA GRPNAGKSSL LNALAGREAA IVTDIAGTTR DVLREHIHID GMPLHIIDTA GLRDAIDEVE RIGISRAWTE IEQADRIILM LDSSDPESAD LSKVRSEFLA KLPSTLPVTI VRNKIDLNGE QASESEQGGY QMISLSAQTH DGVQLLREHL KQAMGFQTGM EGGFLARRRH LDALDKAAEH LQIGLVQLTE FHAGELLAEE LRLVQSYLSE ITGQFTSDDL LGNIFSSFCI GK // ID MOG_HAEIN Reviewed; 197 AA. AC P44645; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Molybdopterin adenylyltransferase; DE Short=MPT adenylyltransferase; DE EC=2.7.7.75; GN Name=mog; Synonyms=mogA; OrderedLocusNames=HI_0336; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of CC the biosynthesis of the molybdenum-cofactor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + molybdopterin = diphosphate + adenylyl- CC molybdopterin. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoaB/Mog 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; L42023; AAC21998.1; -; Genomic_DNA. DR PIR; D64148; D64148. DR RefSeq; NP_438500.1; NC_000907.1. DR RefSeq; WP_005647046.1; NC_000907.1. DR ProteinModelPortal; P44645; -. DR SMR; P44645; 3-192. DR STRING; 71421.HI0336; -. DR PRIDE; P44645; -. DR EnsemblBacteria; AAC21998; AAC21998; HI_0336. DR GeneID; 949444; -. DR KEGG; hin:HI0336; -. DR PATRIC; 20189215; VBIHaeInf48452_0353. DR eggNOG; ENOG4108RIR; Bacteria. DR eggNOG; COG0521; LUCA. DR KO; K03831; -. DR OMA; AAVPYCL; -. DR OrthoDB; EOG6SV58B; -. DR PhylomeDB; P44645; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR Pfam; PF00994; MoCF_biosynth; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 197 Molybdopterin adenylyltransferase. FT /FTId=PRO_0000170984. SQ SEQUENCE 197 AA; 21691 MW; 5F65A75C69DABD8F CRC64; MTALLKIGLV SVSDRASAGV YQDQGIPELQ AWLEQALVDP FHLETRLIPD EQPVIEQTLK ELVDEQGCHL VLTTGGTGPA KRDVTPDATL AVADREMPGF GEQMRQVSLH FVPTAILSRQ VGVIRKESLI LNLPGQPKAI KETLEGVKDK EGNVLVKGIF SAVPYCLQLI NGLYIDTKPE IIESFRPKSA RRENLEK // ID MSCL_HAEIN Reviewed; 128 AA. AC P44789; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Large-conductance mechanosensitive channel; GN Name=mscL; OrderedLocusNames=HI_0626; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Channel that opens in response to stretch forces in the CC membrane lipid bilayer. May participate in the regulation of CC osmotic pressure changes within the cell (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homopentamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MscL 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; L42023; AAC22286.1; -; Genomic_DNA. DR PIR; G64155; G64155. DR RefSeq; NP_438786.1; NC_000907.1. DR RefSeq; WP_005658680.1; NC_000907.1. DR ProteinModelPortal; P44789; -. DR STRING; 71421.HI0626; -. DR EnsemblBacteria; AAC22286; AAC22286; HI_0626. DR GeneID; 950793; -. DR KEGG; hin:HI0626; -. DR PATRIC; 20189847; VBIHaeInf48452_0652. DR eggNOG; ENOG4105M2E; Bacteria. DR eggNOG; COG1970; LUCA. DR KO; K03282; -. DR OMA; YGSFIQT; -. DR OrthoDB; EOG696C3G; -. DR PhylomeDB; P44789; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008381; F:mechanically-gated ion channel activity; IBA:GO_Central. DR GO; GO:0009992; P:cellular water homeostasis; IBA:GO_Central. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GOC. DR GO; GO:0006811; P:ion transport; IBA:GO_Central. DR HAMAP; MF_00115; MscL; 1. DR InterPro; IPR019823; Mechanosensitive_channel_CS. DR InterPro; IPR001185; MS_channel. DR Pfam; PF01741; MscL; 1. DR PRINTS; PR01264; MECHCHANNEL. DR SUPFAM; SSF81330; SSF81330; 1. DR TIGRFAMs; TIGR00220; mscL; 1. DR PROSITE; PS01327; MSCL; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion channel; KW Ion transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 128 Large-conductance mechanosensitive FT channel. FT /FTId=PRO_0000192444. FT TOPO_DOM 1 15 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 16 42 Helical. {ECO:0000250}. FT TOPO_DOM 43 74 Periplasmic. {ECO:0000250}. FT TRANSMEM 75 96 Helical. {ECO:0000250}. FT TOPO_DOM 97 128 Cytoplasmic. {ECO:0000250}. SQ SEQUENCE 128 AA; 14198 MW; BD3A68D27200E51A CRC64; MNFIKEFREF AMRGNVVDMA VGVIIGSAFG KIVSSLVSDI FTPVLGILTG GIDFKDMKFV LAQAQGDVPA VTLNYGLFIQ NVIDFIIIAF AIFMMIKVIN KVRKPEEKKT APKAETLLTE IRDLLKNK // ID MLTF_HAEIN Reviewed; 482 AA. AC P44587; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 11-MAY-2016, entry version 104. DE RecName: Full=Membrane-bound lytic murein transglycosylase F {ECO:0000255|HAMAP-Rule:MF_02016}; DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_02016}; DE AltName: Full=Murein lyase F {ECO:0000255|HAMAP-Rule:MF_02016}; DE Flags: Precursor; GN Name=mltF {ECO:0000255|HAMAP-Rule:MF_02016}; GN OrderedLocusNames=HI_0232; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Murein-degrading enzyme that degrades murein glycan CC strands and insoluble, high-molecular weight murein sacculi, with CC the concomitant formation of a 1,6-anhydromuramoyl product. Lytic CC transglycosylases (LTs) play an integral role in the metabolism of CC the peptidoglycan (PG) sacculus. Their lytic action creates space CC within the PG sacculus to allow for its expansion as well as for CC the insertion of various structures such as secretion systems and CC flagella. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- CATALYTIC ACTIVITY: Exolytic cleavage of the (1->4)-beta- CC glycosidic linkage between N-acetylmuramic acid (MurNAc) and N- CC acetylglucosamine (GlcNAc) residues in peptidoglycan, from either CC the reducing or the non-reducing ends of the peptidoglycan chains, CC with concomitant formation of a 1,6-anhydrobond in the MurNAc CC residue. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane CC protein. Note=Attached to the inner leaflet of the outer membrane. CC {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- DOMAIN: The N-terminal domain does not have lytic activity and CC probably modulates enzymatic activity. The C-terminal domain is CC the catalytic active domain. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial CC solute-binding protein 3 family. {ECO:0000255|HAMAP- CC Rule:MF_02016}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC transglycosylase Slt family. {ECO:0000255|HAMAP-Rule:MF_02016}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21901.1; 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; L42023; AAC21901.1; ALT_INIT; Genomic_DNA. DR PIR; H64145; H64145. DR RefSeq; NP_438404.1; NC_000907.1. DR RefSeq; WP_010868965.1; NC_000907.1. DR ProteinModelPortal; P44587; -. DR STRING; 71421.HI0232; -. DR EnsemblBacteria; AAC21901; AAC21901; HI_0232. DR GeneID; 951149; -. DR KEGG; hin:HI0232; -. DR PATRIC; 20188987; VBIHaeInf48452_0246. DR eggNOG; ENOG4105CHQ; Bacteria. DR eggNOG; COG4623; LUCA. DR KO; K18691; -. DR OMA; YYDILTW; -. DR OrthoDB; EOG62C9FB; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-EC. DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro. DR HAMAP; MF_02016; MltF; 1. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR023703; MltF. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR InterPro; IPR000189; Transglyc_AS. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR PANTHER; PTHR21666:SF215; PTHR21666:SF215; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR Pfam; PF01464; SLT; 1. DR SMART; SM00062; PBPb; 1. DR SUPFAM; SSF53955; SSF53955; 2. DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1. PE 3: Inferred from homology; KW Cell outer membrane; Cell wall biogenesis/degradation; KW Complete proteome; Lyase; Membrane; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255|HAMAP-Rule:MF_02016}. FT CHAIN 19 482 Membrane-bound lytic murein FT transglycosylase F. FT /FTId=PRO_0000196564. FT REGION 19 267 Non-LT domain. {ECO:0000255|HAMAP- FT Rule:MF_02016}. FT REGION 268 482 LT domain. {ECO:0000255|HAMAP- FT Rule:MF_02016}. FT ACT_SITE 312 312 {ECO:0000255|HAMAP-Rule:MF_02016}. SQ SEQUENCE 482 AA; 56106 MW; 47DB53FB3EB931B4 CRC64; MKGLFLRIIT ALALLFWAID MVFPWQFLRH TEENHYTAIQ ARGSLYVGTI NNQISYFINK DSERGFEYEL AKAFADTLGV ELEMKIFDNQ EQLFDELDKH NIDLAAAHLL YHPKNAERFQ IGPAYHSASW QLAYRKNENR PKNLGNVKKD IYISNNLALE ETLKELQKQY PQLIWKRNQA LTQEELLLQL AEGKIPYVIA NSIDIAAIQQ IKPELAIAFD ITDEANVHWY LPNNPYRDLQ TALLNFMNNA EETGLLDNLK EKYLGHISQF DYVDTRSYMN AIENTLPQFS PLFEKYKGEL DWRLLAAVAY QESHWNPDAT SPTGVRGIMM LTKNTAQHMK ISDRTDPEQS IKAGSEYLHW LISQLPESIE KEERIWFALV AYNIGLGHLI DARRLTQNLG GNPDNWFDVK KNLPLLAEKR YYSQLKYGYA RGYEAHQYVE NIRRYMNSIV NYHRVQENQT TNDNANNESA VKNLEEIKEN KD // ID MNMA_HAEIN Reviewed; 383 AA. AC P44551; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 16-MAR-2016, entry version 104. DE RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144}; DE EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144}; GN Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144}; Synonyms=trmU; GN OrderedLocusNames=HI_0174; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC21843.1; 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; L42023; AAC21843.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_438342.1; NC_000907.1. DR ProteinModelPortal; P44551; -. DR SMR; P44551; 25-383. DR STRING; 71421.HI0174; -. DR DNASU; 951080; -. DR EnsemblBacteria; AAC21843; AAC21843; HI_0174. DR GeneID; 951080; -. DR KEGG; hin:HI0174; -. DR PATRIC; 20188843; VBIHaeInf48452_0178. DR eggNOG; ENOG4105CCJ; Bacteria. DR eggNOG; COG0482; LUCA. DR KO; K00566; -. DR OMA; LHKINFA; -. DR OrthoDB; EOG6RZB5H; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central. DR Gene3D; 2.30.30.280; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1. DR InterPro; IPR023382; Adenine_a_hdrlase_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; tRNA-specific_2-thiouridylase. DR PANTHER; PTHR11933; PTHR11933; 1. DR TIGRFAMs; TIGR00420; trmU; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1 383 tRNA-specific 2-thiouridylase MnmA. FT /FTId=PRO_0000121636. FT NP_BIND 30 37 ATP. {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 116 118 Interaction with target base in tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 168 170 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT REGION 330 331 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT ACT_SITE 121 121 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT ACT_SITE 218 218 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT BINDING 56 56 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00144}. FT BINDING 146 146 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 147 147 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT SITE 363 363 Interaction with tRNA. FT {ECO:0000255|HAMAP-Rule:MF_00144}. FT DISULFID 121 218 Alternate. {ECO:0000255|HAMAP- FT Rule:MF_00144}. SQ SEQUENCE 383 AA; 42938 MW; 574371287ABCBA63 CRC64; MLISNTYNQH FPQLTQEQLA RNATKKVICG MSGGVDSSVS AFILQQQGYQ VEGLFMKNWE EDDDTDYCTA AADLADAQAV CDKLGIKLHK INFAAEYWDN VFEHFLTEYK AGRTPNPDIL CNKEIKFKAF LEYAAEDLGA DYIATGHYVR RAGDNENAKL LRGLDPNKDQ SYFLYTLSHK QVGQSLFPVG EIEKPIVRAI AEDLGLITAK KKDSTGICFI GERKFKDFLA RYLPAQPGNI RTVDDEIIGR HDGLMYHTLG QRKGLGIGGL KNAGDEAWYV VDKDVENNEL IVAQGHDHPR LFSKGLIASQ LHWVDREPIR ESLRCTVKTR YRQQDIPCVI EPIDDETIRV IFDEPQSAVT PGQSAVFYLG EVCLGGGIIA ERI // ID MNMG_HAEIN Reviewed; 629 AA. AC P44763; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 107. 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=HI_0582; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22240.1; -; Genomic_DNA. DR PIR; I64078; I64078. DR RefSeq; NP_438740.1; NC_000907.1. DR RefSeq; WP_005694554.1; NC_000907.1. DR ProteinModelPortal; P44763; -. DR SMR; P44763; 1-552. DR STRING; 71421.HI0582; -. DR EnsemblBacteria; AAC22240; AAC22240; HI_0582. DR GeneID; 950589; -. DR KEGG; hin:HI0582; -. DR PATRIC; 20189721; VBIHaeInf48452_0603. DR eggNOG; ENOG4107RE5; Bacteria. DR eggNOG; COG0445; LUCA. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR PhylomeDB; P44763; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00129; MnmG_GidA; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR026904; GidA-assoc_3. DR InterPro; IPR004416; MnmG. DR InterPro; IPR002218; MnmG-rel. DR InterPro; IPR020595; MnmG-rel_CS. DR Pfam; PF01134; GIDA; 1. DR Pfam; PF13932; GIDA_assoc; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR00136; gidA; 1. DR PROSITE; PS01280; GIDA_1; 1. DR PROSITE; PS01281; GIDA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; KW Reference proteome; tRNA processing. FT CHAIN 1 629 tRNA uridine 5-carboxymethylaminomethyl FT modification enzyme MnmG. FT /FTId=PRO_0000117109. FT NP_BIND 13 18 FAD. {ECO:0000255|HAMAP-Rule:MF_00129}. FT NP_BIND 273 287 NAD. {ECO:0000255|HAMAP-Rule:MF_00129}. SQ SEQUENCE 629 AA; 70104 MW; 03AAB4AC7A1E8C86 CRC64; MFYTETYDVI VIGGGHAGTE AALAPARMGF KTLLLTHNVD TLGQMSCNPA IGGIGKGHLV KEVDAMGGLM AHAADKAGIQ FRTLNSSKGP AVRATRAQSD RVLYRQAVRT ALENQPNLDI FQQEATDILI EQDRVTGVST KMGLTFRAKS VILTAGTFLA GKIHIGLENY EGGRAGDSAS VNLSHRLRDL GLRVDRLKTG TPPRIDARTI NFDILAKQHG DEVLPVFSFM GSVDDHPQQI PCYITHTNEQ THEVIRNNLD RSPMYTGVIE GIGPRYCPSI EDKVMRFADR NSHQIYLEPE GLTSNEVYPN GISTSLPFDV QMGIVNSMKG LENARIVKPG YAIEYDYFDP RDLKPTLETK SISGLFFAGQ INGTTGYEEA AAQGLLAGIN AGLYVQEKDA WYPRRDQSYT GVLVDDLCTL GTKEPYRVFT SRAEYRLLLR EDNADIRLTP IAHELGLIDE ARWARFNQKM ENIEQERQRL RSIWLHPRSE YLEEANKVLG SPLVREASGE DLLRRPEMTY DILTSLTPYK PAMEDKEAVE QVEIAIKYQG YIEHQQEEIE KQKRHENTAI PANFDYSKVS GLSNEVRAKL EQHRPVSIGQ ASRISGITPA AISIILVNLK KQGMLKRGE // ID MOAA_HAEIN Reviewed; 337 AA. AC P45311; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01225}; DE EC=4.1.99.18 {ECO:0000255|HAMAP-Rule:MF_01225}; DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01225}; GN Name=moaA {ECO:0000255|HAMAP-Rule:MF_01225}; GN OrderedLocusNames=HI_1676; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes, together with MoaC, the conversion of 5'-GTP CC to cyclic pyranopterin monophosphate (cPMP or molybdopterin CC precursor Z). {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- CATALYTIC ACTIVITY: GTP = cyclic pyranopterin phosphate + CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and CC the GTP-derived substrate. {ECO:0000255|HAMAP-Rule:MF_01225}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01225}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. CC {ECO:0000255|HAMAP-Rule:MF_01225}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23321.1; -; Genomic_DNA. DR PIR; B64136; B64136. DR RefSeq; NP_439818.1; NC_000907.1. DR RefSeq; WP_005694398.1; NC_000907.1. DR ProteinModelPortal; P45311; -. DR STRING; 71421.HI1676; -. DR EnsemblBacteria; AAC23321; AAC23321; HI_1676. DR GeneID; 950505; -. DR KEGG; hin:HI1676; -. DR PATRIC; 20192103; VBIHaeInf48452_1755. DR eggNOG; ENOG4105CM1; Bacteria. DR eggNOG; COG2896; LUCA. DR KO; K03639; -. DR OMA; GWIHQIR; -. DR OrthoDB; EOG64XXNN; -. DR PhylomeDB; P45311; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01225_B; MoaA_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR013483; MoaA. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR010505; Mob_synth_C. DR InterPro; IPR007197; rSAM. DR Pfam; PF06463; Mob_synth_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR02666; moaA; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase; KW Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 337 Cyclic pyranopterin monophosphate FT synthase. FT /FTId=PRO_0000152966. FT REGION 270 272 GTP binding. {ECO:0000255|HAMAP- FT Rule:MF_01225}. FT METAL 33 33 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 37 37 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 40 40 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 265 265 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 268 268 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 282 282 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 26 26 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 39 39 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 76 76 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 80 80 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01225}. FT BINDING 107 107 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 131 131 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 168 168 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 202 202 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01225}. SQ SEQUENCE 337 AA; 38305 MW; 1D47939FBBB2D0DE CRC64; MQSIPIKNVG ESRLVDPFQR QYYYLRLSIT DQCNFRCTYC LPDGYQPEAN KPSFLTLKEI THLAQAFAEM GTEKIRLTGG EPTLRKDFIS IAESITNIDG IRQLAVTTNG YRMAKDVADW KKAGITSINV SVDSLDPKMF HQITGINKFD DVMRGIDRAF EVGYNKVKVN SVLMKNLNDK EFEQFLAWVK DRPIQMRFIE LMQTGEMDSF FDKFHLSGQV LADKLLKNGW TLQHKSHTDG PAKVFTHPDY AGEIGLIMPY EKNFCASCNR LRVSAKGKLH LCLFGEEGIE LRDLLQSHEQ QGILQARIFA ALQGKREHHY LHIGDTGVRN HLASIGG // ID MOAD_HAEIN Reviewed; 81 AA. AC P45309; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Molybdopterin synthase sulfur carrier subunit; DE AltName: Full=MPT synthase subunit 1; DE AltName: Full=Molybdenum cofactor biosynthesis protein D; DE AltName: Full=Molybdopterin-converting factor small subunit; DE AltName: Full=Molybdopterin-converting factor subunit 1; DE AltName: Full=Sulfur carrier protein MoaD; GN Name=moaD; OrderedLocusNames=HI_1674; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in sulfur transfer in the conversion of CC molybdopterin precursor Z to molybdopterin. {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SUBUNIT: Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. CC Forms a stable heterotetrameric complex of 2 MoaD and 2 MoeB CC during adenylation of MoaD by MoeB. During catalysis MoaD shuttles CC between the two heterotetrameric complexes (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MoaD 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; L42023; AAC23319.1; -; Genomic_DNA. DR PIR; A59368; A59368. DR RefSeq; NP_439816.1; NC_000907.1. DR RefSeq; WP_005654167.1; NC_000907.1. DR ProteinModelPortal; P45309; -. DR SMR; P45309; 1-81. DR STRING; 71421.HI1674; -. DR EnsemblBacteria; AAC23319; AAC23319; HI_1674. DR GeneID; 950503; -. DR KEGG; hin:HI1674; -. DR PATRIC; 20192099; VBIHaeInf48452_1753. DR eggNOG; ENOG4105M00; Bacteria. DR eggNOG; COG1977; LUCA. DR KO; K03636; -. DR OMA; RELVACD; -. DR OrthoDB; EOG6KMBD9; -. DR PhylomeDB; P45309; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR010034; Mopterin_su_1. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR003749; ThiS/MoaD. DR Pfam; PF02597; ThiS; 1. DR SUPFAM; SSF54285; SSF54285; 1. DR TIGRFAMs; TIGR01682; moaD; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1 81 Molybdopterin synthase sulfur carrier FT subunit. FT /FTId=PRO_0000209132. FT MOD_RES 81 81 1-thioglycine; alternate. {ECO:0000250}. FT MOD_RES 81 81 Glycyl adenylate; alternate. FT {ECO:0000250}. SQ SEQUENCE 81 AA; 8826 MW; 35D1440F82456F22 CRC64; MLNVLFFAQT RELIGVDAIQ LEDDFATAEA VREHLAQKGD KWALALEKGK LLVAINQTLM PLESAVKNGD EIAFFPPVTG G // ID MRED_HAEIN Reviewed; 162 AA. AC P44476; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Rod shape-determining protein MreD; GN Name=mreD; OrderedLocusNames=HI_0039; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in formation of the rod shape of the cell. May CC also contribute to regulation of formation of penicillin-binding CC proteins (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MreD 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; L42023; AAC21717.1; -; Genomic_DNA. DR PIR; G64044; G64044. DR RefSeq; NP_438212.1; NC_000907.1. DR RefSeq; WP_005657800.1; NC_000907.1. DR STRING; 71421.HI0039; -. DR EnsemblBacteria; AAC21717; AAC21717; HI_0039. DR GeneID; 950936; -. DR KEGG; hin:HI0039; -. DR PATRIC; 20188529; VBIHaeInf48452_0039. DR eggNOG; COG2891; LUCA. DR KO; K03571; -. DR OMA; DLLRPSW; -. DR OrthoDB; EOG63JR9Q; -. DR PhylomeDB; P44476; -. DR Proteomes; UP000000579; 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR007227; Cell_shape_determining_MreD. DR InterPro; IPR026034; MreD_proteobac. DR Pfam; PF04093; MreD; 1. DR PIRSF; PIRSF018472; MreD_proteobac; 1. DR TIGRFAMs; TIGR03426; shape_MreD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cell shape; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 162 Rod shape-determining protein MreD. FT /FTId=PRO_0000062773. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. SQ SEQUENCE 162 AA; 18965 MW; 3985BA4EA37BAAE6 CRC64; MQTRFILQWF TILSFFVIAF VLELAPWPVG FQMLKPAWLV LVLLYWVLAI PNKVSIGWSF LLGLTWDLIL GSTLGVHALV LSTSMYIIAK NYLILRNLSL WFQSLLVVLF VFIIRLLIFL VEFSLHTAFF HWQAILGAFA SGLLWPWVFL LMRKIRRKVK LH // ID MODB_HAEIN Reviewed; 229 AA. AC P45322; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Molybdenum transport system permease protein ModB; GN Name=modB; OrderedLocusNames=HI_1692; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for molybdenum; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC23338.1; -; Genomic_DNA. DR PIR; A64137; A64137. DR RefSeq; NP_439834.1; NC_000907.1. DR RefSeq; WP_010869272.1; NC_000907.1. DR ProteinModelPortal; P45322; -. DR STRING; 71421.HI1692; -. DR EnsemblBacteria; AAC23338; AAC23338; HI_1692. DR GeneID; 949953; -. DR KEGG; hin:HI1692; -. DR PATRIC; 20192135; VBIHaeInf48452_1771. DR eggNOG; ENOG4105E0C; Bacteria. DR eggNOG; COG4149; LUCA. DR KO; K02018; -. DR OMA; TPGAEYQ; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45322; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015098; F:molybdate ion transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR011867; ModB_ABC. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR02141; modB_ABC; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Molybdenum; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 229 Molybdenum transport system permease FT protein ModB. FT /FTId=PRO_0000060113. FT TRANSMEM 12 32 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 45 65 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 83 103 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 132 152 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 196 216 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 6 214 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 229 AA; 24823 MW; 5F5441D9DB8C1A41 CRC64; MEISAINLSL SVAVSSMLWS LPLAIFVAWL LARKNFYGKS LITGVIHLPL VLPPVVIGYL LLVAMGRNGF IGKYLYQWFG LSFGFSWKGA VLSSAVVAFP LVVRAIRLSL ENIDIKLEQA AQTLGASAWR VFFTITLPLS LPGVLAGLVL GFARSLGEFG ATITFVSNIA GETQTIPLAM YSFIQTPGAE EQTARLCLFA IILSLISLLL SEWLSKRMQK KLGQGNVAD // ID MODD_HAEIN Reviewed; 281 AA. AC Q57278; O05066; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative pyrophosphorylase ModD; DE EC=2.4.2.-; GN Name=modD; OrderedLocusNames=HI_1473; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the NadC/ModD 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; L42023; AAC23121.1; -; Genomic_DNA. DR PIR; H64125; H64125. DR RefSeq; NP_439624.1; NC_000907.1. DR RefSeq; WP_005693490.1; NC_000907.1. DR ProteinModelPortal; Q57278; -. DR STRING; 71421.HI1473; -. DR PRIDE; Q57278; -. DR EnsemblBacteria; AAC23121; AAC23121; HI_1473. DR GeneID; 950721; -. DR KEGG; hin:HI1473; -. DR PATRIC; 20191661; VBIHaeInf48452_1540. DR eggNOG; ENOG4105D18; Bacteria. DR eggNOG; COG0157; LUCA. DR KO; K03813; -. DR OMA; VACTRKN; -. DR OrthoDB; EOG6W9XB3; -. DR PhylomeDB; Q57278; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1170.20; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006242; ModD. DR InterPro; IPR027277; NadC/ModD. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N. DR Pfam; PF01729; QRPTase_C; 1. DR Pfam; PF02749; QRPTase_N; 1. DR PIRSF; PIRSF006250; NadC_ModD; 1. DR SUPFAM; SSF51690; SSF51690; 1. DR TIGRFAMs; TIGR01334; modD; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 281 Putative pyrophosphorylase ModD. FT /FTId=PRO_0000155960. SQ SEQUENCE 281 AA; 31436 MW; 2CB8BF3681F2DC45 CRC64; MIYFSDKELD DLLLEDIYRG DLTTHALSIE NIPAKILFKR KNAGVVAGVS VAEKLLKKLD IQPHLYVKEG EWVESGALLI SAEGMSEQLH QAWKVVQLVL EWSCGVAQYT AEMIANAKSV NPTAVVACTR KSIPNTRKLA TNAVLAAGGH IHRQGVSETL LVFTNHRNLL SDPNDWTKIV DRLRQEAPEN KITLEADNYA QFEQMYMAEP DIIQLDKWLL EDVKKALDLL QSKQKDILLS VAGGVNKNNV SDYAKLGIRL FITSAPYYVP PEDIKVVIEK I // ID MODE_HAEIN Reviewed; 255 AA. AC P45324; Q9R7E9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-JAN-2016, entry version 112. DE RecName: Full=Transcriptional regulator ModE; GN Name=modE; OrderedLocusNames=HI_1694; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu K.Y., Young R., Spinola S., Apicella M.A.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP REVIEW. RX PubMed=9325422; DOI=10.1007/s002030050508; RA Grunden A.M., Shanmugam K.T.; RT "Molybdate transport and regulation in bacteria."; RL Arch. Microbiol. 168:345-354(1997). CC -!- FUNCTION: The ModE-Mo complex acts as a repressor of the modABC CC operon, involved in the transport of molybdate. Upon binding CC molybdate, the conformation of the protein changes, promoting CC dimerization of ModE-Mo. The protein dimer is then competent to CC bind a DNA region, upstream of the modABC operon. Acts also as an CC enhancer of the expression of genes coding for molybdoenzymes, CC both directly and indirectly (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ModE 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; M94855; AAA24984.1; -; Genomic_DNA. DR EMBL; L42023; AAC23340.1; -; Genomic_DNA. DR PIR; B64175; B64175. DR RefSeq; NP_439836.1; NC_000907.1. DR RefSeq; WP_005694183.1; NC_000907.1. DR ProteinModelPortal; P45324; -. DR STRING; 71421.HI1694; -. DR EnsemblBacteria; AAC23340; AAC23340; HI_1694. DR GeneID; 950754; -. DR KEGG; hin:HI1694; -. DR PATRIC; 20192139; VBIHaeInf48452_1773. DR eggNOG; ENOG4105F4R; Bacteria. DR eggNOG; COG2005; LUCA. DR KO; K02019; -. DR OMA; ITHDSTA; -. DR OrthoDB; EOG68Q0VP; -. DR PhylomeDB; P45324; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0015689; P:molybdate ion transport; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR004606; Mo-pterin-bd. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR016462; ModE. DR InterPro; IPR003725; ModE-bd_N. DR InterPro; IPR005116; Transp-assoc_OB_typ1. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03459; TOBE; 1. DR PIRSF; PIRSF005763; Txn_reg_ModE; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR TIGRFAMs; TIGR00637; ModE_repress; 1. DR TIGRFAMs; TIGR00638; Mop; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; Molybdenum; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Transport. FT CHAIN 1 255 Transcriptional regulator ModE. FT /FTId=PRO_0000201127. FT DNA_BIND 34 80 H-T-H motif. {ECO:0000250}. FT REGION 1 121 I. FT REGION 122 183 IIA (MOP1A). FT REGION 125 133 Required for dimer formation and FT molybdate binding. {ECO:0000250}. FT REGION 184 248 IIB (MOP2). FT REGION 249 255 IIA (MOP1B). FT CONFLICT 78 78 A -> V (in Ref. 1; AAA24984). FT {ECO:0000305}. FT CONFLICT 195 195 A -> E (in Ref. 1; AAA24984). FT {ECO:0000305}. FT CONFLICT 198 198 P -> S (in Ref. 1; AAA24984). FT {ECO:0000305}. FT CONFLICT 237 237 E -> G (in Ref. 1; AAA24984). FT {ECO:0000305}. SQ SEQUENCE 255 AA; 28898 MW; FA5B7D025E9EB271 CRC64; MKNTEILLTI KLQQALFIDP KRVRLLKEIQ QCGSINQAAK NAKVSYKSAW DHLEAMNKIS PRPLLERNTG GKNGGGTALT TYAERLLQLY DLLERTQEHA FHILQDESVP LDSLLTATAR FSLQSSARNQ FFGRVAQQRI IDSRCVVDVN VQGLPTPLQV SITTKSSARL KLITEKEVML MFKAPWVKIS EQPLANQPNQ FPVNIKSLNE EEAILQFAES NIEFCATVHQ PNQWQIEQQV WIHIDQEQII LATLG // ID MRAZ_HAEIN Reviewed; 151 AA. AC P45056; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Transcriptional regulator MraZ; GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; GN OrderedLocusNames=HI_1129; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22784.1; -; Genomic_DNA. DR PIR; E64167; E64167. DR RefSeq; NP_439287.1; NC_000907.1. DR RefSeq; WP_005686427.1; NC_000907.1. DR ProteinModelPortal; P45056; -. DR STRING; 71421.HI1129; -. DR EnsemblBacteria; AAC22784; AAC22784; HI_1129. DR GeneID; 950095; -. DR KEGG; hin:HI1129; -. DR PATRIC; 20190933; VBIHaeInf48452_1179. DR eggNOG; ENOG4108V6E; Bacteria. DR eggNOG; COG2001; LUCA. DR KO; K03925; -. DR OMA; SNRVEIW; -. DR OrthoDB; EOG6G4W1C; -. DR PhylomeDB; P45056; -. DR Proteomes; UP000000579; 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 1 151 Transcriptional regulator MraZ. FT /FTId=PRO_0000108487. FT DOMAIN 5 52 SpoVT-AbrB 1. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. FT DOMAIN 81 124 SpoVT-AbrB 2. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. SQ SEQUENCE 151 AA; 17162 MW; 5FB2CBB87AA852B5 CRC64; MFRGATAVNL DSKGRVAIPT RYRAEILEKN QGQMVCTVDI RQSCLLLYPL DEWEKIEQKL LALSNFDPTQ RRLQRVMLGH ATECEMDAQG RILLSGPLRQ HAKLEKGLML VGQLNKFEIW SDVEWHTQIA EDIEIGSSTD FAADALNDFS L // ID MREC_HAEIN Reviewed; 351 AA. AC P44475; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Cell shape-determining protein MreC; DE AltName: Full=Cell shape protein MreC; DE AltName: Full=Rod shape-determining protein MreC; GN Name=mreC; OrderedLocusNames=HI_0038; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in formation and maintenance of cell shape. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MreC 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; L42023; AAC21716.1; -; Genomic_DNA. DR PIR; F64044; F64044. DR RefSeq; NP_438211.1; NC_000907.1. DR RefSeq; WP_005687477.1; NC_000907.1. DR ProteinModelPortal; P44475; -. DR STRING; 71421.HI0038; -. DR EnsemblBacteria; AAC21716; AAC21716; HI_0038. DR GeneID; 950932; -. DR KEGG; hin:HI0038; -. DR PATRIC; 20188527; VBIHaeInf48452_0038. DR eggNOG; ENOG4105N3I; Bacteria. DR eggNOG; COG1792; LUCA. DR KO; K03570; -. DR OMA; TNKLQIE; -. DR OrthoDB; EOG6R5C3S; -. DR PhylomeDB; P44475; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR007221; MreC. DR Pfam; PF04085; MreC; 1. DR TIGRFAMs; TIGR00219; mreC; 1. PE 3: Inferred from homology; KW Cell shape; Complete proteome; Reference proteome. FT CHAIN 1 351 Cell shape-determining protein MreC. FT /FTId=PRO_0000062768. SQ SEQUENCE 351 AA; 39184 MW; 0C4B171027D42B42 CRC64; MKPIFGKAPP LGIRLLIAIF ASIALILADG RNSSITKARS AMETAIGGLY YLANSPRSIL DGISENLVDT NKLQIENKVL RQQLLEKNAD LLLLDQLKVE NQRLRLLLNS PLRTDEYKKI AEVLTAETDI YRQQIVINQG KKDGAYVGQP VIDEKGVIGQ IISVGENTSR VLLLTDVTHS IPVQVLRNDV RVIASGTGHT DELSLDNVPR SVDIEKGDLL VTSGLGGRFL EGYPVAVVQS VSRDSSNYFA IVKAKPLALL ERLRYVLLLW PSNLDISKVK SISPEEVRNL VQKRLESQAN EANYRVKKTP LTEKDFLENE EKTIIEPDIP TDFLQNEEDL PIEQQEERIE D // ID MNMC_HAEIN Reviewed; 670 AA. AC P44246; P44245; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 11-NOV-2015, entry version 92. DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000255|HAMAP-Rule:MF_01102}; DE Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000255|HAMAP-Rule:MF_01102}; DE Includes: DE RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01102}; DE EC=2.1.1.61 {ECO:0000255|HAMAP-Rule:MF_01102}; DE Includes: DE RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01102}; DE EC=1.5.-.- {ECO:0000255|HAMAP-Rule:MF_01102}; GN Name=mnmC {ECO:0000255|HAMAP-Rule:MF_01102}; GN OrderedLocusNames=HI_1534/HI_1535; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5- CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble CC position (U34) in tRNA. Catalyzes the FAD-dependent demodification CC of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a CC methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form CC mnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_01102}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA containing 5- CC aminomethyl-2-thiouridine = S-adenosyl-L-homocysteine + tRNA CC containing 5-methylaminomethyl-2-thiouridylate. CC {ECO:0000255|HAMAP-Rule:MF_01102}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01102}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01102}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC methyltransferase superfamily. tRNA (mnm(5)s(2)U34)- CC methyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01102}. CC -!- SIMILARITY: In the C-terminal section; belongs to the DAO family. CC {ECO:0000255|HAMAP-Rule:MF_01102}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23184.1; Type=Frameshift; Positions=181, 525; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; CC Sequence=AAC23185.1; Type=Frameshift; Positions=181, 525; Note=Produces two separate ORFs.; 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; L42023; AAC23184.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC23185.1; ALT_FRAME; Genomic_DNA. DR PIR; C64035; C64035. DR PIR; D64035; D64035. DR ProteinModelPortal; P44246; -. DR SMR; P44246; 3-240. DR STRING; 71421.HI1535; -. DR DNASU; 950397; -. DR EnsemblBacteria; AAC23184; AAC23184; HI_1534. DR EnsemblBacteria; AAC23185; AAC23185; HI_1535. DR PATRIC; 20191793; VBIHaeInf48452_1605. DR eggNOG; ENOG4105CWG; Bacteria. DR eggNOG; COG0665; LUCA. DR eggNOG; COG4121; LUCA. DR OrthoDB; EOG61P6QH; -. DR Proteomes; UP000000579; 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:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro. DR GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR Gene3D; 3.50.50.60; -; 3. DR HAMAP; MF_01102; MnmC; 1. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR008471; MnmC-like_methylTransf. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC. DR InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C. DR Pfam; PF01266; DAO; 1. DR Pfam; PF05430; Methyltransf_30; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR03197; MnmC_Cterm; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase; KW Multifunctional enzyme; Oxidoreductase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 670 tRNA 5-methylaminomethyl-2-thiouridine FT biosynthesis bifunctional protein MnmC. FT /FTId=PRO_0000095017. FT REGION 1 242 tRNA (mnm(5)s(2)U34)-methyltransferase. FT REGION 269 670 FAD-dependent cmnm(5)s(2)U34 FT oxidoreductase. SQ SEQUENCE 670 AA; 75691 MW; EB68D7BCA874B429 CRC64; MTFSVQHAEI HFNQNHIPVS DQFDDVYFSN ENGLAETDYV FLQGNQLWER WITHKDANFV IAETGFGTGL NFFAVTKLFR EFRQQHENHP LKRLNFISFE KYPLKITALL QAHLACPQFE DLSAHLQRYW PSLILGCHRI HFGETTLDLW FGDVSENLPQ LGDYMNERIN AWFLDGFAPS KNPEMWNDDL YNLMFRFTKP NGTFATFTAA SAVRKGLESA GFNVTKRKGF GKKRECLSGL KIQSKSTALS TPWYLAQPAK MEKQDVAIIG GGIASLCAAI SLIKRGAKVT IYCEDDALAL NASGNKQGAF YPQLSDDNAL TVDFYLHAFS YGRQLLDWAI EQNIVFEHEF CGVALCAYNE KSAVKLTKIS QLGLPNEIFQ MLSAEQLSEK VGLPLNCEGG WIEQGAWLAP RQFVQNAFSF LEKQGVVIKT AQKITALSQL EKGWELKNMQ GQKYCHEVVI LANGHKITDF VQTEKLPLYP IRGQVSQIPT SENLLKLKSV LCYDGYLTPA NQLKTSHCIG ASMFRDNVDR DFSEQEQQEN QQKLQQNIAQ PWTQDVDTSD NLARVGIRCS VRDLAPMVGN VPHFEQQQAD YYNLFNLRRR KQPIQSAANF QNLFLIAALG SRGLTSAPLL GETLASIIYG EPLPISEGIL HNLSANRAWV KKWLKGSKVE // ID MOAC_HAEIN Reviewed; 160 AA. AC P45310; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Cyclic pyranopterin monophosphate synthase accessory protein; DE AltName: Full=Molybdenum cofactor biosynthesis protein C; GN Name=moaC; OrderedLocusNames=HI_1675; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Together with MoaA, is involved in the conversion of 5'- CC GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin CC precursor Z). {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoaC 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; L42023; AAC23320.1; -; Genomic_DNA. DR PIR; A64136; A64136. DR RefSeq; NP_439817.1; NC_000907.1. DR RefSeq; WP_005642378.1; NC_000907.1. DR ProteinModelPortal; P45310; -. DR SMR; P45310; 11-150. DR STRING; 71421.HI1675; -. DR EnsemblBacteria; AAC23320; AAC23320; HI_1675. DR GeneID; 950864; -. DR KEGG; hin:HI1675; -. DR PATRIC; 20192101; VBIHaeInf48452_1754. DR eggNOG; ENOG4108YXW; Bacteria. DR eggNOG; COG0315; LUCA. DR KO; K03637; -. DR OMA; TTFTHIN; -. DR OrthoDB; EOG6SV58B; -. DR PhylomeDB; P45310; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.640; -; 1. DR HAMAP; MF_01224_B; MoaC_B; 1. DR InterPro; IPR023045; Mo_CF_biosynth-C. DR InterPro; IPR023046; Mo_CF_biosynth-C_bac. DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom. DR Pfam; PF01967; MoaC; 1. DR SUPFAM; SSF55040; SSF55040; 1. DR TIGRFAMs; TIGR00581; moaC; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 160 Cyclic pyranopterin monophosphate FT synthase accessory protein. FT /FTId=PRO_0000097803. FT ACT_SITE 128 128 {ECO:0000255}. SQ SEQUENCE 160 AA; 17467 MW; C588D33869C7DCED CRC64; MTTFTHINSQ GEANMVDVSA KAETVREARA EAIVTMSKET LSMIVEGKHH KGDVFATARI AGIQAAKRTW ELIPLCHPLL LSKVEVNLEP LLETNQVRIQ SLCKLTGKTG VEMEALTAAS VAALTIYDMC KAVQKDIVIE HVRLLEKSGG KSGHFIAEEK // ID MOBB_HAEIN Reviewed; 178 AA. AC P44902; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Molybdopterin-guanine dinucleotide biosynthesis adapter protein; DE Short=MGD biosynthesis adapter protein; DE AltName: Full=Molybdenum cofactor biosynthesis adapter protein; DE Short=Moco biosynthesis adapter protein; GN Name=mobB; OrderedLocusNames=HI_0851; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: GTP-binding protein that is not required for the CC biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) CC cofactor, and not necessary for the formation of active CC molybdoenzymes using this form of molybdenum cofactor. May act as CC an adapter protein to achieve the efficient biosynthesis and CC utilization of MGD. Displays a weak intrinsic GTPase activity (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MobB 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; L42023; AAC22508.1; -; Genomic_DNA. DR PIR; A64160; A64160. DR RefSeq; NP_439011.1; NC_000907.1. DR RefSeq; WP_005693199.1; NC_000907.1. DR ProteinModelPortal; P44902; -. DR STRING; 71421.HI0851; -. DR EnsemblBacteria; AAC22508; AAC22508; HI_0851. DR GeneID; 949864; -. DR KEGG; hin:HI0851; -. DR PATRIC; 20190357; VBIHaeInf48452_0892. DR eggNOG; ENOG4105FNP; Bacteria. DR eggNOG; COG1763; LUCA. DR KO; K03753; -. DR OMA; HTHHNMD; -. DR OrthoDB; EOG6PKFG0; -. DR PhylomeDB; P44902; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004435; MobB_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03205; MobB; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00176; mobB; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 178 Molybdopterin-guanine dinucleotide FT biosynthesis adapter protein. FT /FTId=PRO_0000096529. FT NP_BIND 22 26 GTP. {ECO:0000250}. FT NP_BIND 56 59 GTP. {ECO:0000255}. FT NP_BIND 103 106 GTP. {ECO:0000255}. SQ SEQUENCE 178 AA; 20532 MW; 456F8F8F6692174F CRC64; MIFKVIFMNN QIPLLGITGY SGSGKTTLLE KLIPELIARH IRVSVIKHSH HNMQVDKEGK DSWRMKEAGS SQVILANDER WAIMTETPKP VSLDYLAQQF DRTLTDLVLV EGFKQEPIPK ILLHRQEMTK PLPEIDEYVL AVATNYPLEI DRTLLDINRI PQIADFIENW LHHFHGAR // ID MOEB_HAEIN Reviewed; 243 AA. AC P45211; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Molybdopterin-synthase adenylyltransferase; DE EC=2.7.7.80; DE AltName: Full=MoaD protein adenylase; DE AltName: Full=Molybdopterin-converting factor subunit 1 adenylase; DE AltName: Full=Sulfur carrier protein MoaD adenylyltransferase; GN Name=moeB; Synonyms=chlN; OrderedLocusNames=HI_1449; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group CC of the C-terminal glycine of sulfur carrier protein MoaD. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + [molybdopterin-synthase sulfur-carrier CC protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur- CC carrier protein]-Gly-Gly-AMP. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SUBUNIT: Homodimer. Forms a stable heterotetrameric complex of 2 CC MoeB and 2 MoaD during adenylation of MoaD (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF 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; L42023; AAC23099.1; -; Genomic_DNA. DR PIR; C64124; C64124. DR RefSeq; NP_439601.1; NC_000907.1. DR RefSeq; WP_005693917.1; NC_000907.1. DR ProteinModelPortal; P45211; -. DR SMR; P45211; 3-241. DR STRING; 71421.HI1449; -. DR EnsemblBacteria; AAC23099; AAC23099; HI_1449. DR GeneID; 950565; -. DR KEGG; hin:HI1449; -. DR PATRIC; 20191603; VBIHaeInf48452_1511. DR eggNOG; ENOG4105D06; Bacteria. DR eggNOG; COG0476; LUCA. DR KO; K11996; -. DR OMA; EQLNQSC; -. DR OrthoDB; EOG628F8J; -. DR PhylomeDB; P45211; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006464; P:cellular protein modification process; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012730; Mopterin_Synthase_Sase_MoeB. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR Pfam; PF00899; ThiF; 1. DR SUPFAM; SSF69572; SSF69572; 1. DR TIGRFAMs; TIGR02355; moeB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 243 Molybdopterin-synthase FT adenylyltransferase. FT /FTId=PRO_0000120577. FT NP_BIND 69 73 ATP. {ECO:0000250}. FT NP_BIND 130 131 ATP. {ECO:0000250}. FT BINDING 41 41 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 62 62 ATP. {ECO:0000250}. FT BINDING 86 86 ATP. {ECO:0000250}. SQ SEQUENCE 243 AA; 26997 MW; 218A3382A975BDBD CRC64; MIELSHEEEL RYNRQIILKS VDFDGQEKLK ASKMLIVGLG GLGCAASQYL AAAGVGNLTL LDFDTVSLSN LQRQVLHCDA RLNMPKVESA KIALEQINPH INIETINAKL DEEKLAEIIP HFDIVLDCTD NVEIRNQLDR QCNHMKVPLI SGAAIRMEGQ VSVFTYEPNT PTYRDLSKLF RQNVLSCVEA GVLAPIVGIV GCIQALEAIK VRLKIGKNLC GRLLMIDGFS MNIREIKLPT NME // ID MOP_HAEIN Reviewed; 69 AA. AC P45183; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 82. DE RecName: Full=Probable molybdenum-pterin-binding protein; GN OrderedLocusNames=HI_1370; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds one mole of molybdenum per mole of protein and CC contains a pterin. {ECO:0000250}. CC -!- SIMILARITY: To C.pasteurianum MOP proteins. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23017.1; -; Genomic_DNA. DR PIR; I64119; I64119. DR RefSeq; NP_439521.1; NC_000907.1. DR RefSeq; WP_005631673.1; NC_000907.1. DR ProteinModelPortal; P45183; -. DR STRING; 71421.HI1370; -. DR EnsemblBacteria; AAC23017; AAC23017; HI_1370. DR GeneID; 950284; -. DR KEGG; hin:HI1370; -. DR PATRIC; 20191427; VBIHaeInf48452_1424. DR eggNOG; ENOG4105X1Q; Bacteria. DR eggNOG; COG3585; LUCA. DR OMA; SNVMVAV; -. DR OrthoDB; EOG68Q0VP; -. DR PhylomeDB; P45183; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR InterPro; IPR004606; Mo-pterin-bd. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR005116; Transp-assoc_OB_typ1. DR Pfam; PF03459; TOBE; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR TIGRFAMs; TIGR00638; Mop; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum; Reference proteome. FT CHAIN 1 69 Probable molybdenum-pterin-binding FT protein. FT /FTId=PRO_0000096535. SQ SEQUENCE 69 AA; 7122 MW; 1D32CE1C4C36310E CRC64; MKISARNQLK GKVVSIENGS VNAIVHIDIG GGNVLSSTVS LAAVKELNLE VGKEAYAIIK ATSVMVGVE // ID MPL_HAEIN Reviewed; 453 AA. AC P43948; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase {ECO:0000255|HAMAP-Rule:MF_02020}; DE EC=6.3.2.45 {ECO:0000255|HAMAP-Rule:MF_02020}; DE AltName: Full=Murein peptide ligase {ECO:0000255|HAMAP-Rule:MF_02020}; DE AltName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_02020}; GN Name=mpl {ECO:0000255|HAMAP-Rule:MF_02020}; OrderedLocusNames=HI_0121; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D- CC glutamyl-meso-diaminopimelate by linking it to UDP-N- CC acetylmuramate. {ECO:0000255|HAMAP-Rule:MF_02020}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + CC phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso- CC 2,6-diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_02020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02020}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_02020}. CC -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21795.1; -; Genomic_DNA. DR PIR; B64002; B64002. DR RefSeq; NP_438293.1; NC_000907.1. DR RefSeq; WP_005694412.1; NC_000907.1. DR ProteinModelPortal; P43948; -. DR STRING; 71421.HI0121; -. DR PRIDE; P43948; -. DR DNASU; 951026; -. DR EnsemblBacteria; AAC21795; AAC21795; HI_0121. DR GeneID; 951026; -. DR KEGG; hin:HI0121; -. DR PATRIC; 20188727; VBIHaeInf48452_0125. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR KO; K02558; -. DR OMA; CDANVYP; -. DR OrthoDB; EOG64BQ73; -. DR PhylomeDB; P43948; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02020; Mpl; 1. DR InterPro; IPR005757; Mpl. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01081; mpl; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Ligase; KW Magnesium; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 453 UDP-N-acetylmuramate--L-alanyl-gamma-D- FT glutamyl-meso-2,6-diaminoheptandioate FT ligase. FT /FTId=PRO_0000101709. FT NP_BIND 111 117 ATP. {ECO:0000255|HAMAP-Rule:MF_02020}. SQ SEQUENCE 453 AA; 50074 MW; 5E7E71A07646EB7D CRC64; MKHIHILGIC GTFMGGVAMI AKQMGYHVTG SDTNVYPPMS TFLEEQGIEI IPNYDVAQLQ PAPDMVIVGN AMKRGNPCVE YVLENNLKYT SGPQWLHDHL LRDRWVLAVS GTHGKTTTTG MLTWVLEQNG LKSGFLIGGI AGNFGISARL GDSPYFIIEA DEYDTAFFDK RSKFVHYNPR TLIVNNISFD HADIFDDLKA IQRQFHHMIR TIPASGLVLS SASEQSAKET LALGCWSQQQ FLGKDNEWFA ERITNDASHF AVFHHGEKVA EVKWNVVGQH NMHNALMAIA AAHHTGVAIE DACKALGSFV NAKRRLEVKG EVNSITVYDD FAHHPEAILA TLTALRDKVG GGVRILAVLE PRSNTMKMGV HKDDIAPALG RADAVFMLQP EQLSWEVADI ANQCVQPAYW NANLDRLVDM IVAKAQPTDH ILVMSNGSFG GIHQKILDKL KLK // ID MSRAB_HAEIN Reviewed; 353 AA. AC P45213; 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=Peptide methionine sulfoxide reductase MsrA/MsrB; DE Includes: 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; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrB; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase; GN Name=msrAB; OrderedLocusNames=HI_1455; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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 -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin. CC -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met CC sulfoxide reductase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met CC sulfoxide reductase family. {ECO:0000305}. 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; L42023; AAC23103.1; -; Genomic_DNA. DR PIR; E64124; E64124. DR RefSeq; NP_439606.1; NC_000907.1. DR RefSeq; WP_010869216.1; NC_000907.1. DR ProteinModelPortal; P45213; -. DR SMR; P45213; 41-202, 208-347. DR STRING; 71421.HI1455; -. DR EnsemblBacteria; AAC23103; AAC23103; HI_1455. DR GeneID; 950358; -. DR KEGG; hin:HI1455; -. DR PATRIC; 20191613; VBIHaeInf48452_1516. DR eggNOG; ENOG4105E0X; Bacteria. DR eggNOG; COG0225; LUCA. DR eggNOG; COG0229; LUCA. DR KO; K12267; -. DR OMA; VVKYEDD; -. DR OrthoDB; EOG6091JX; -. DR PhylomeDB; P45213; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC. 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 Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01400; MsrB; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR028427; Met_Sox_Rdtase. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB. DR InterPro; IPR011057; Mss4-like. DR PANTHER; PTHR10173; PTHR10173; 2. DR Pfam; PF01625; PMSR; 1. DR Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; SSF51316; 1. DR SUPFAM; SSF55068; SSF55068; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR TIGRFAMs; TIGR00357; TIGR00357; 1. DR PROSITE; PS51790; MSRB; 1. PE 1: Evidence at protein level; KW Complete proteome; Multifunctional enzyme; Oxidoreductase; KW Reference proteome. FT CHAIN 1 353 Peptide methionine sulfoxide reductase FT MsrA/MsrB. FT /FTId=PRO_0000138513. FT DOMAIN 213 336 MsrB. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. FT REGION 43 196 Peptide methionine sulfoxide reductase A. FT ACT_SITE 51 51 {ECO:0000250}. FT ACT_SITE 325 325 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01126}. SQ SEQUENCE 353 AA; 39864 MW; ADBCDDB4D90A8B1E CRC64; MKLSKTFLFI TALCCATPTL AIQNSTSSSG EQKMAMENTQ NIREIYLAGG CFWGMEAYME RIHGVKDAIS GYANGNTEKT SYQMIGLTDH AETVKVTYDA NQISLDKLLK YYFKVIDPTS VNKQGNDRGR QYRTGIYYQD GADKAVIGQA LAQLQTKYKK PVQIEVQPLK NYIVAEEYHQ DYLKKNPNGY CHIDITKADE PVIDEKDYPK PSDAELKAKL TPLQYSVTQN KHTERSFSNE YWDNFQPGIY VDITTGEPVF SSNDKFESGC GWPSFTKPII KDVVHYETDN SFNMQRTEVL SRAGNAHLGH VFDDGPKDKG GLRYCINSAS IKFIPLAEME KAGYGYLIQS IKK // ID MREB_HAEIN Reviewed; 351 AA. AC P44474; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Rod shape-determining protein MreB; GN Name=mreB; OrderedLocusNames=HI_0037; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in formation of the rod shape of the cell. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21715.1; 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; L42023; AAC21715.1; ALT_INIT; Genomic_DNA. DR PIR; E64044; E64044. DR RefSeq; NP_438210.2; NC_000907.1. DR RefSeq; WP_005657804.1; NC_000907.1. DR ProteinModelPortal; P44474; -. DR SMR; P44474; 13-342. DR STRING; 71421.HI0037; -. DR PRIDE; P44474; -. DR EnsemblBacteria; AAC21715; AAC21715; HI_0037. DR GeneID; 950934; -. DR KEGG; hin:HI0037; -. DR PATRIC; 20188525; VBIHaeInf48452_0037. DR eggNOG; ENOG4105DFF; Bacteria. DR eggNOG; COG1077; LUCA. DR KO; K03569; -. DR OMA; HETGIVT; -. DR OrthoDB; EOG66QM00; -. DR PhylomeDB; P44474; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR004753; MreB_Mrl. DR Pfam; PF06723; MreB_Mbl; 1. DR PRINTS; PR01652; SHAPEPROTEIN. DR TIGRFAMs; TIGR00904; mreB; 1. PE 3: Inferred from homology; KW Cell shape; Complete proteome; Reference proteome. FT CHAIN 1 351 Rod shape-determining protein MreB. FT /FTId=PRO_0000062761. SQ SEQUENCE 351 AA; 37616 MW; D97CA0686403B279 CRC64; MLFKKIRGLF SNDLSIDLGT ANTLIYVKRQ GIVLDEPSVV AIRQDRVGTL KSIAAVGKEA KLMLGRTPKS IVAIRPMKDG VIADFFVTEK MLQYFIKQVH SGNFMRPSPR VLVCVPAGAT QVERRAIKES AIGAGAREVY LIEEPMAAAI GAKLPVSTAV GSMVIDIGGG TTEVAVISLN GIVYSSSVRI GGDRFDEAII SYVRRTFGSV IGEPTAERIK QEIGSAYIQE GDEIKEMEVH GHNLAEGAPR SFTLTSRDVL EAIQQPLNGI VAAVRTALEE CQPEHAADIF ERGMVLTGGG ALLRNIDILL SKESGVPVII AEDPLTCVAR GGGEALEMID MHGGDIFSDE I // ID MTH5_HAEIN Reviewed; 304 AA. AC P45000; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 96. DE RecName: Full=Modification methylase HindV; DE Short=M.HindV; DE EC=2.1.1.37; DE AltName: Full=Cytosine-specific methyltransferase HindV; GN Name=hindVM; OrderedLocusNames=HI_1041; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GRCGYC, causes specific methylation on C-? on both strands, and CC protects the DNA from cleavage by the HindV endonuclease. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC {ECO:0000255|PROSITE-ProRule:PRU10018}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22700.1; -; Genomic_DNA. DR PIR; C64109; C64109. DR RefSeq; NP_439200.1; NC_000907.1. DR RefSeq; WP_010869113.1; NC_000907.1. DR ProteinModelPortal; P45000; -. DR STRING; 71421.HI1041; -. DR REBASE; 3574; M.HindV. DR EnsemblBacteria; AAC22700; AAC22700; HI_1041. DR GeneID; 950661; -. DR KEGG; hin:HI1041; -. DR PATRIC; 20190745; VBIHaeInf48452_1085. DR eggNOG; ENOG4105NI8; Bacteria. DR eggNOG; COG0270; LUCA. DR KO; K00558; -. DR OMA; RGVNRPI; -. DR OrthoDB; EOG664CK9; -. DR PhylomeDB; P45000; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018117; C5_DNA_meth_AS. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR031303; C5_meth_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00675; dcm; 1. DR PROSITE; PS00094; C5_MTASE_1; 1. DR PROSITE; PS00095; C5_MTASE_2; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 304 Modification methylase HindV. FT /FTId=PRO_0000087881. FT DOMAIN 1 299 SAM-dependent MTase C5-type. FT {ECO:0000255|PROSITE-ProRule:PRU01016}. FT ACT_SITE 75 75 {ECO:0000255|PROSITE-ProRule:PRU01016, FT ECO:0000255|PROSITE-ProRule:PRU10018}. SQ SEQUENCE 304 AA; 34366 MW; 03DA1EAB27C84BBD CRC64; MKCVDLFSGC GGLSLGFELA GFEICAAFEN WEKAIEIYKN NFSHPIYNID LRNEKEAVEK IKKYSPDLIM GGPPCQDFSS AGKRDISLGR ADLTYSFANI VCNIRPKWFV MENVEQIKKS HILQDIINQF IDFGYGLTSA ILDASYCGVP QSRTRFSLIG KLNSEHNFLI PTLSRKLSDK PMTVRDYLGN SLNLEFYYRH PRNYNRRGIF SIDEPSPTIR GVNRPIPKGY NINSCDPKGV ELAKVRPLTT IERSYIQTFP KSFLFSGTKT DLEQMIGNAV PVNLAKFVAS AIINFEKEPI RSMG // ID MUKF_HAEIN Reviewed; 444 AA. AC P45185; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 11-MAY-2016, entry version 98. DE RecName: Full=Chromosome partition protein MukF {ECO:0000255|HAMAP-Rule:MF_01803}; GN Name=mukF {ECO:0000255|HAMAP-Rule:MF_01803}; Synonyms=kicB; GN OrderedLocusNames=HI_1372; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in chromosome condensation, segregation and CC cell cycle progression. May participate in facilitating chromosome CC segregation by condensation DNA from both sides of a centrally CC located replisome during cell division. Not required for mini-F CC plasmid partitioning. Probably acts via its interaction with MukB CC and MukE. Overexpression results in anucleate cells. It has a CC calcium binding activity. {ECO:0000255|HAMAP-Rule:MF_01803}. CC -!- SUBUNIT: Interacts, and probably forms a ternary complex, with CC MukE and MukB via its C-terminal region. The complex formation is CC stimulated by calcium or magnesium. It is required for an CC interaction between MukE and MukB. {ECO:0000255|HAMAP- CC Rule:MF_01803}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01803}. Note=Restricted to the nucleoid region. CC {ECO:0000255|HAMAP-Rule:MF_01803}. CC -!- SIMILARITY: Belongs to the MukF family. {ECO:0000255|HAMAP- CC Rule:MF_01803}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23020.1; 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; L42023; AAC23020.1; ALT_INIT; Genomic_DNA. DR PIR; B64120; B64120. DR RefSeq; NP_439524.2; NC_000907.1. DR RefSeq; WP_010869195.1; NC_000907.1. DR ProteinModelPortal; P45185; -. DR SMR; P45185; 8-285. DR STRING; 71421.HI1372; -. DR EnsemblBacteria; AAC23020; AAC23020; HI_1372. DR GeneID; 950891; -. DR KEGG; hin:HI1372; -. DR PATRIC; 20191433; VBIHaeInf48452_1427. DR eggNOG; ENOG4105GHU; Bacteria. DR eggNOG; COG3006; LUCA. DR KO; K03633; -. DR OMA; NRVFSQR; -. DR OrthoDB; EOG6SV55C; -. DR PhylomeDB; P45185; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_01803; MukF; 1. DR InterPro; IPR005582; Chromosome_partition_MukF. DR InterPro; IPR033441; MukF_C. DR InterPro; IPR033440; MukF_M. DR InterPro; IPR033439; MukF_WHTH. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03882; KicB; 1. DR Pfam; PF17193; MukF_C; 1. DR Pfam; PF17192; MukF_M; 1. DR PIRSF; PIRSF018282; MukF; 1. DR SUPFAM; SSF140570; SSF140570; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Calcium; Cell cycle; Cell division; Chromosome partition; KW Complete proteome; Cytoplasm; DNA condensation; Reference proteome. FT CHAIN 1 444 Chromosome partition protein MukF. FT /FTId=PRO_0000211606. FT REGION 212 240 Leucine-zipper. SQ SEQUENCE 444 AA; 51557 MW; CC67916DC0D18759 CRC64; MIETSQTIPE LVSWAKDREF SLNLPTERLV FLLAIAIYNN ERLDGEMLEA DLVDIFRHTM NAFEQSTDAI ATRANNAINE LVKQRLLNRF SSEFTEGLAI YRLTPLGVGV SDYYIRQREF SALRLSVQLS IVADEIQRAS DSAEEGVENN ENEHYWRRNV FAPLKYSVAE IFDSIDLSQR IMDENQQSIK DEIAELLTKD WQAAISSCER LLDETSGNLR ELQDTLNAAG DKLQAQLLRI QDCVIGRDDL YFIDQLITDL QSKLDRIISW GQQAIDLWIG YDRHVHKFIR TAIDMDKNRV FSQRLRNSIH HYFDHPWFLW TAQAERLVDL RDEEMVLRED DALGELPEEL QYESLSDLHD QIVEHMQGLL IAYRENNRPI DLSLVLKEQL ENYPLSRHFD VARIIVDQAV RLGMANDDLS GIYPDWQAIN KRGAEVQAHV IDKY // ID MODC_HAEIN Reviewed; 351 AA. AC P45321; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Molybdenum import ATP-binding protein ModC {ECO:0000255|HAMAP-Rule:MF_01705}; DE EC=3.6.3.29 {ECO:0000255|HAMAP-Rule:MF_01705}; GN Name=modC {ECO:0000255|HAMAP-Rule:MF_01705}; GN OrderedLocusNames=HI_1691; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex ModABC involved in CC molybdenum import. Responsible for energy coupling to the CC transport system. {ECO:0000255|HAMAP-Rule:MF_01705}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + molybdate(Out) = ADP + phosphate CC + molybdate(In). {ECO:0000255|HAMAP-Rule:MF_01705}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ModC), two transmembrane proteins (ModB) and a solute-binding CC protein (ModA). {ECO:0000255|HAMAP-Rule:MF_01705}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01705}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01705}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate CC importer (TC 3.A.1.8) family. {ECO:0000255|HAMAP-Rule:MF_01705}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01705}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23337.1; -; Genomic_DNA. DR PIR; I64136; I64136. DR RefSeq; NP_439833.1; NC_000907.1. DR RefSeq; WP_005694180.1; NC_000907.1. DR ProteinModelPortal; P45321; -. DR STRING; 71421.HI1691; -. DR EnsemblBacteria; AAC23337; AAC23337; HI_1691. DR GeneID; 950518; -. DR KEGG; hin:HI1691; -. DR PATRIC; 20192133; VBIHaeInf48452_1770. DR eggNOG; ENOG4105CGB; Bacteria. DR eggNOG; COG4148; LUCA. DR KO; K02017; -. DR OMA; MLELDFS; -. DR OrthoDB; EOG664CG0; -. DR PhylomeDB; P45321; -. DR Proteomes; UP000000579; 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:0015412; F:molybdate transmembrane-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0042888; F:molybdenum ion transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015852; ABC_transpr_ModC. DR InterPro; IPR004606; Mo-pterin-bd. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR011868; ModC_ABC_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005116; Transp-assoc_OB_typ1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF03459; TOBE; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02142; modC_ABC; 1. DR TIGRFAMs; TIGR00638; Mop; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51241; MODC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Molybdenum; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 351 Molybdenum import ATP-binding protein FT ModC. FT /FTId=PRO_0000092542. FT DOMAIN 1 229 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01705}. FT NP_BIND 31 38 ATP. {ECO:0000255|HAMAP-Rule:MF_01705}. SQ SEQUENCE 351 AA; 39582 MW; A0948E393E92B2DE CRC64; MLQINVKKQL GQLALQANIQ VPDQGVTAIF GLSGSGKTSL INLVSGLIQP DEGFICLNDR TLVDMESQES LPTHLRKIGY VFQDARLFPH YTVKGNLRYG MKNVSQDDFN YIVDLLGITH LLKRYPLTLS GGEKQRVAIG RALLTDPDIL LMDEPLSALD VPRKRELMQY LERLSKEINI PILYVTHSLD ELLRLADRVV LMENGIVKAY DRVEKIWNSP IFAPWKGESE QSSVLALPVH LHNPPYKMTA LSLGEQVLWI HQVPANVGER VRVCIYSSDV SITLQKPEQT SIRNILRGKI TQIEIQDSRV DLAVLVEGHK IWASISKWAQ NELRFAIGQD VYVQIKAVSV M // ID MTR_HAEIN Reviewed; 418 AA. AC P44614; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Tryptophan-specific transport protein; DE AltName: Full=Tryptophan permease; GN Name=mtr; OrderedLocusNames=HI_0287; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transporting tryptophan across the CC cytoplasmic membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 CC family. Mtr/TnaB/TyrP permease 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; L42023; AAC21952.1; -; Genomic_DNA. DR PIR; F64059; F64059. DR RefSeq; NP_438454.1; NC_000907.1. DR RefSeq; WP_005694021.1; NC_000907.1. DR STRING; 71421.HI0287; -. DR EnsemblBacteria; AAC21952; AAC21952; HI_0287. DR GeneID; 949413; -. DR KEGG; hin:HI0287; -. DR PATRIC; 20189113; VBIHaeInf48452_0303. DR eggNOG; ENOG4105CIC; Bacteria. DR eggNOG; COG0814; LUCA. DR KO; K03835; -. DR OMA; LALIYTW; -. DR OrthoDB; EOG60394J; -. DR PhylomeDB; P44614; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002091; ArAA_permease. DR InterPro; IPR013061; Trp/try_permease_CS. DR InterPro; IPR013059; Trp_tyr_transpt. DR InterPro; IPR018227; Tryptophan/tyrosine_permease. DR Pfam; PF03222; Trp_Tyr_perm; 1. DR PRINTS; PR00166; AROAAPRMEASE. DR TIGRFAMs; TIGR00837; araaP; 1. DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 418 Tryptophan-specific transport protein. FT /FTId=PRO_0000093798. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 232 252 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 330 347 Helical. {ECO:0000255}. FT TRANSMEM 354 370 Helical. {ECO:0000255}. FT TRANSMEM 384 404 Helical. {ECO:0000255}. SQ SEQUENCE 418 AA; 45018 MW; B6DB96E6314A2A57 CRC64; MIQQKSPSLL GGAMIIAGTA IGAGMLANPT STAGVWFIGS ILALIYTWFC MTTSGLMILE ANLHYPTGSS FDTIVKDLLG KSWNTINGLS VAFVLYILTY AYITSGGGIT QNLLNQAFSS AESAVDIGRT SGSLIFCLIL AAFVWLSTKA VDRFTTVLIV GMVVAFFLST TGLLSSVKTA VLFNTVAESE QTYLPYLLTA LPVCLVSFGF HGNVPSLVKY YDRDGRRVMK SIFIGTGLAL VIYILWQLAV QGNLPRTEFA PVIEKGGDVS ALLEALHKYI EVEYLSVALN FFAYMAISTS FLGVTLGLFD YIADLFKFDD SLLGRTKTTL VTFLPPLLLS LQFPYGFVIA IGYAGLAATI WAAIVPALLA KASRQKFPQA SYKVYGGNFM IGFVILFGIL NIVAQIGANL GWFASFTG // ID MURB_HAEIN Reviewed; 341 AA. AC P44605; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=UDP-N-acetylenolpyruvoylglucosamine reductase; DE EC=1.3.1.98; DE AltName: Full=UDP-N-acetylmuramate dehydrogenase; GN Name=murB; OrderedLocusNames=HI_0268; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP- CC N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21934.1; -; Genomic_DNA. DR PIR; G64058; G64058. DR RefSeq; NP_438437.1; NC_000907.1. DR RefSeq; WP_005694036.1; NC_000907.1. DR ProteinModelPortal; P44605; -. DR SMR; P44605; 2-337. DR STRING; 71421.HI0268; -. DR EnsemblBacteria; AAC21934; AAC21934; HI_0268. DR GeneID; 949392; -. DR KEGG; hin:HI0268; -. DR PATRIC; 20189063; VBIHaeInf48452_0283. DR eggNOG; ENOG4105D4A; Bacteria. DR eggNOG; COG0812; LUCA. DR KO; K00075; -. DR OMA; MQNIGAY; -. DR OrthoDB; EOG60CWQ3; -. DR PhylomeDB; P44605; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 3.90.78.10; -; 1. DR HAMAP; MF_00037; MurB; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR003170; MurB. DR InterPro; IPR011601; MurB_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR PANTHER; PTHR21071; PTHR21071; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF02873; MurB_C; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR SUPFAM; SSF56194; SSF56194; 1. DR TIGRFAMs; TIGR00179; murB; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; FAD; KW Flavoprotein; NADP; Oxidoreductase; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 341 UDP-N-acetylenolpyruvoylglucosamine FT reductase. FT /FTId=PRO_0000179215. FT DOMAIN 12 182 FAD-binding PCMH-type. FT ACT_SITE 158 158 {ECO:0000250}. FT ACT_SITE 228 228 Proton donor. {ECO:0000250}. FT ACT_SITE 324 324 {ECO:0000250}. SQ SEQUENCE 341 AA; 38344 MW; B06F571EAC235E4F CRC64; MQNLQPFHTF HIQSNAREII EAHSIEQLQQ VWANSKSENL PTLFLGQGSN VLFLDDFNGI VILNRLMGIT HEQDANFHYL HVNGGENWHK LVEWSINNGI YGLENLALIP GCAGSAPIQN IGAYGVEFKD VCDYVEVLNL NTNETFRLDT EQCEFGYRES IFKHRYQQGY VITAVGLKLK KDWQPILKYG SLVEFDPKTV TAKQIFDEVC HIRQSKLPDP NEVGNAGSFF KNPVVSSEHF EEIKKHHENL PHFPQADGSV KLAAGWLIDQ CNLKGFQIGG AAVHKKQALV LINKNGATGQ DVVKLAHHVR QTVAEKFGVY LQPEVRFISA TGEVNSEQII T // ID MRAY_HAEIN Reviewed; 360 AA. AC P45062; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038}; DE EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038}; DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038}; GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; GN OrderedLocusNames=HI_1135; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: First step of the lipid cycle reactions in the CC biosynthesis of the cell wall peptidoglycan. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala- CC D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00038}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22790.1; -; Genomic_DNA. DR PIR; A64185; A64185. DR RefSeq; NP_439293.1; NC_000907.1. DR RefSeq; WP_010869136.1; NC_000907.1. DR STRING; 71421.HI1135; -. DR EnsemblBacteria; AAC22790; AAC22790; HI_1135. DR GeneID; 950102; -. DR KEGG; hin:HI1135; -. DR PATRIC; 20190945; VBIHaeInf48452_1185. DR eggNOG; ENOG4105CPY; Bacteria. DR eggNOG; COG0472; LUCA. DR KO; K01000; -. DR OMA; HQNKKDT; -. DR OrthoDB; EOG69GZPZ; -. DR PhylomeDB; P45062; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00038; MraY; 1. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase. DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR Pfam; PF10555; MraY_sig1; 1. DR TIGRFAMs; TIGR00445; mraY; 1. DR PROSITE; PS01347; MRAY_1; 1. DR PROSITE; PS01348; MRAY_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Membrane; Peptidoglycan synthesis; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 360 Phospho-N-acetylmuramoyl-pentapeptide- FT transferase. FT /FTId=PRO_0000108833. FT TRANSMEM 21 41 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 73 93 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 94 114 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 132 152 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 168 188 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 199 219 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 239 259 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 263 283 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 288 308 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. FT TRANSMEM 338 358 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00038}. SQ SEQUENCE 360 AA; 40315 MW; C10D066ADCA0508D CRC64; MLVWLAEYLV RYETAFNAIS YITVRANLAL LTALFISLWI GPKVIKRLQI LKFGQEVRND GPESHFAKKG TPTMGGVMIL FSIGVSTLLW ANLANPYIWV CLFVLFGYGA IGFVDDFRKI TRKNTDGLIA RWKYFWMSVV ALVAILWLYW LGHDTDATRL VIPFFKDIMP QLGLFYIVLS YFVIVGTGNA VNLTDGLDGL AIMPTALVAG AFALIAWATG NVNFAEYLHI PYIKYSSEVV VFCTAIVGAS LGFLWFNTYP AQVFMGDVGS LALGGALGVV AILVRQEFLL VIMGGVFVVE ALSVILQVGS YKLRKQRIFR MAPIHHHFEL KGWPEPRVII RFWIISLMLV LMGLVTLKLR // ID MSBA_HAEIN Reviewed; 587 AA. AC P44407; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 122. DE RecName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000255|HAMAP-Rule:MF_01703}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01703}; GN Name=msbA {ECO:0000255|HAMAP-Rule:MF_01703}; Synonyms=msh-1; GN OrderedLocusNames=HI_0060; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-458. RC STRAIN=BC200; RX PubMed=8063112; DOI=10.1016/0378-1119(94)90840-0; RA Clifton S.W., McCarthy D., Roe B.A.; RT "Sequence of the rec-2 locus of Haemophilus influenzae: homologies to RT comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli."; RL Gene 146:95-100(1994). CC -!- FUNCTION: Involved in lipid A export and possibly also in CC glycerophospholipid export and for biogenesis of the outer CC membrane. Transmembrane domains (TMD) form a pore in the inner CC membrane and the ATP-binding domain (NBD) is responsible for CC energy generation. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01703}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01703}. CC -!- DOMAIN: In MsbA the ATP-binding domain (NBD) and the transmembrane CC domain (TMD) are fused. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid CC exporter (TC 3.A.1.106) family. {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01703}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21738.1; -; Genomic_DNA. DR EMBL; L20805; AAC13734.1; -; Genomic_DNA. DR PIR; H64045; H64045. DR RefSeq; NP_438233.1; NC_000907.1. DR RefSeq; WP_010868928.1; NC_000907.1. DR ProteinModelPortal; P44407; -. DR SMR; P44407; 15-585. DR STRING; 71421.HI0060; -. DR EnsemblBacteria; AAC21738; AAC21738; HI_0060. DR GeneID; 950953; -. DR KEGG; hin:HI0060; -. DR PATRIC; 20188573; VBIHaeInf48452_0060. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K11085; -. DR OMA; ENCAVVS; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P44407; -. DR Proteomes; UP000000579; 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:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. 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; IPR011917; ABC_transpr_lipidA. 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 TIGRFAMs; TIGR02203; MsbA_lipidA; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51239; MSBA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Lipid transport; Membrane; Nucleotide-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 587 Lipid A export ATP-binding/permease FT protein MsbA. FT /FTId=PRO_0000092583. FT TRANSMEM 31 51 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 68 88 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 145 165 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 166 186 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT TRANSMEM 259 279 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT DOMAIN 31 315 ABC transmembrane type-1. FT {ECO:0000255|HAMAP-Rule:MF_01703}. FT DOMAIN 347 583 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01703}. FT NP_BIND 381 388 ATP. {ECO:0000255|HAMAP-Rule:MF_01703}. SQ SEQUENCE 587 AA; 64912 MW; 97F90D5537436123 CRC64; MQEQKLQEND FSTLQTFKRL WPMIKPFKAG LIVSGVALVF NALADSGLIY LLKPLLDDGF GKANHSFLKM MAFVVVGMII LRGITNFISN YCLAWVSGKV VMTMRRRLFK HLMFMPVSFF DQNSTGRLLS RITYDSQMIA SSSSGSLITI VREGAYIISL FAVMFYTSWE LTIVLFIIGP IIAVLIRLVS KIFRRLSKNL QDSMGELTSA TEQMLKGHKV VLSFGGQHVE EVHFNHVSND MRRKSMKMVT ANSISDPVVQ VIASLALATV LYLATTPLIA EDNLSAGSFT VVFSSMLAMM RPLKSLTAVN AQFQSGMAAC QTLFAILDLE PEKDDGAYKA EPAKGELEFK NVSFAYQGKD ELALNNISFS VPAGKTVALV GRSGSGKSTI ANLVTRFYDI EQGEILLDGV NIQDYRLSNL RENCAVVSQQ VHLFNDTIAN NIAYAAQDKY SREEIIAAAK AAYALEFIEK LPQVFDTVIG ENGTSLSGGQ RQRLAIARAL LRNSPVLILD EATSALDTES ERAIQSALEE LKKDRTVVVI AHRLSTIENA DEILVIDHGE IRERGNHKTL LEQNGAYKQL HSMQFTG // ID MTHD_HAEIN Reviewed; 518 AA. AC P44414; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable modification methylase HindII; DE Short=M.HindII; DE EC=2.1.1.72; DE AltName: Full=Adenine-specific methyltransferase HindII; GN Name=hindIIM; OrderedLocusNames=HI_0513; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GTYRAC, causes specific methylation on A-5 on both strands, and CC protects the DNA from cleavage by the HindII endonuclease. 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; L42023; AAC22171.1; -; Genomic_DNA. DR PIR; F64073; F64073. DR RefSeq; NP_438671.1; NC_000907.1. DR RefSeq; WP_010868995.1; NC_000907.1. DR ProteinModelPortal; P44414; -. DR STRING; 71421.HI0513; -. DR REBASE; 3427; M.HindII. DR EnsemblBacteria; AAC22171; AAC22171; HI_0513. DR GeneID; 950799; -. DR KEGG; hin:HI0513; -. DR PATRIC; 20189579; VBIHaeInf48452_0532. DR eggNOG; ENOG4107U4J; Bacteria. DR eggNOG; COG0827; LUCA. DR eggNOG; COG1002; LUCA. DR KO; K07317; -. DR OrthoDB; EOG61ZTDZ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; RM_methylase_Eco57I. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF07669; Eco57I; 1. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 518 Probable modification methylase HindII. FT /FTId=PRO_0000087974. SQ SEQUENCE 518 AA; 60410 MW; 2E0CAA5B9DBF2EF6 CRC64; MDESKKISLG QFFTPTHIVK YMIGLMTKNK NASILEPSSG NGVFLDSLIQ LGYTNLTSYE IDGDIISHPF VINSSFITSY DKPQYDSIIG NPPYVRWKNL SELQKKELKD NSIWKMYCNS LCDYFYIFII KSILQLKVGG ELIFICPDYF FSTKNAEGLR KFLINNGSFE KIILFNESKV FHGVSSSVVI FKYIKGKNID NINIINIDSK SPIKSEDIES LGESYYIPRF SSSDVWVTSP NHIKVALDKF ESYCKTIKKV QPKSLFDDLE FSRIGSVCDI GNGMVSGLDK AFQMNDINYS ELELLNSICV AKAKHLDAFC FSGYTRYKFI LDDINEDKLI TYFPNFFYEF NNYKDYLLKR YSYNKYLPYW KWAFLRNFSL FSKNEKKIFV PCKERISKKS NFRFSLVDEF IYPTQDVTAL YKKENVKESI EYITAYLNSK AVFLWMKYKG VVKGNVVEFS EKPLANIPFR RIDWQLKSEK KIHDDITNLV RKYLSNKEFS ILHEINLNLE KLGIKVEI // ID MTNN_HAEIN Reviewed; 229 AA. AC P45113; Q5SF30; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTA/SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTAN {ECO:0000255|HAMAP-Rule:MF_01684}; DE EC=3.2.2.9 {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=AdoHcy nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SRH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; GN Name=mtnN {ECO:0000255|HAMAP-Rule:MF_01684}; GN OrderedLocusNames=HI_1216; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=E1a; RX PubMed=15583146; DOI=10.1099/mic.0.27238-0; RA Morton D.J., Smith A., Ren Z., Madore L.L., VanWagoner T.M., RA Seale T.W., Whitby P.W., Stull T.L.; RT "Identification of a haem-utilization protein (Hup) in Haemophilus RT influenzae."; RL Microbiology 150:3923-3933(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic CC bond in both 5'-methylthioadenosine (MTA) and S- CC adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding CC thioribose, 5'-methylthioribose and S-ribosylhomocysteine, CC respectively. {ECO:0000255|HAMAP-Rule:MF_01684}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-(5- CC deoxy-D-ribos-5-yl)-L-homocysteine + adenine. {ECO:0000255|HAMAP- CC Rule:MF_01684}. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl- CC 5-thio-D-ribose + adenine. {ECO:0000255|HAMAP-Rule:MF_01684}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from CC S-methyl-5'-thioadenosine (hydrolase route): step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_01684}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY525146; AAS91661.1; -; Genomic_DNA. DR EMBL; L42023; AAC22869.1; -; Genomic_DNA. DR PIR; C64169; C64169. DR RefSeq; NP_439372.1; NC_000907.1. DR RefSeq; WP_005694230.1; NC_000907.1. DR ProteinModelPortal; P45113; -. DR SMR; P45113; 1-229. DR STRING; 71421.HI1216; -. DR EnsemblBacteria; AAC22869; AAC22869; HI_1216. DR GeneID; 950160; -. DR KEGG; hin:HI1216; -. DR PATRIC; 20191111; VBIHaeInf48452_1268. DR eggNOG; ENOG4105DUF; Bacteria. DR eggNOG; COG0775; LUCA. DR KO; K01243; -. DR OMA; QVCYAFN; -. DR OrthoDB; EOG64JFVR; -. DR PhylomeDB; P45113; -. DR UniPathway; UPA00904; UER00871. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1580; -; 1. DR HAMAP; MF_01684; Salvage_MtnN; 1. DR InterPro; IPR010049; MTA_SAH_Nsdase. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR PANTHER; PTHR21234; PTHR21234; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Hydrolase; KW Methionine biosynthesis; Reference proteome. FT CHAIN 1 229 5'-methylthioadenosine/S- FT adenosylhomocysteine nucleosidase. FT /FTId=PRO_0000164442. FT REGION 173 174 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01684}. FT ACT_SITE 12 12 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01684}. FT ACT_SITE 197 197 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01684}. FT BINDING 78 78 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01684}. FT BINDING 152 152 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01684}. FT CONFLICT 20 20 M -> T (in Ref. 1; AAS91661). FT {ECO:0000305}. FT CONFLICT 42 42 D -> N (in Ref. 1; AAS91661). FT {ECO:0000305}. FT CONFLICT 70 70 C -> F (in Ref. 1; AAS91661). FT {ECO:0000305}. FT CONFLICT 202 202 K -> E (in Ref. 1; AAS91661). FT {ECO:0000305}. SQ SEQUENCE 229 AA; 23965 MW; 37DC08101E193EA4 CRC64; MKIGIVGAMA QEVEILKNLM ADRTETRVAS AVIFEGKING KDVALLQSGI GKVAAAIGTT ALLQLAKPDC VINTGSAGGV AKGLKVGDIV ISDETRYHDA DVTAFGYEKG QLPANPAAFL SDKKLADLAQ EIAEKQGQSV KRGLICSGDS FINSEDKIAQ IKADFPNVTG VEMEATAIAQ VCYAFNVPFV VVRAISDGGD GKASMSFEEF LPLAAKQSSA LVLGMIDRL // ID MTH3_HAEIN Reviewed; 309 AA. AC P43871; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Modification methylase HindIII; DE Short=M.HindIII; DE EC=2.1.1.72; DE AltName: Full=Adenine-specific methyltransferase HindIII; GN Name=hindIIIM; OrderedLocusNames=HI_1392; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3; RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., RA Benner J.S., Wilson G.G.; RT "Cloning, analysis and expression of the HindIII R-M-encoding genes."; RL Gene 150:75-80(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC AAGCTT, causes specific methylation on A-1 on both strands, and CC protects the DNA from cleavage by the HindIII endonuclease. 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; L15391; AAA61959.1; -; Genomic_DNA. DR EMBL; L42023; AAC23039.1; -; Genomic_DNA. DR RefSeq; NP_439546.1; NC_000907.1. DR ProteinModelPortal; P43871; -. DR STRING; 71421.HI1392; -. DR REBASE; 3428; M.HindIII. DR EnsemblBacteria; AAC23039; AAC23039; HI_1392. DR GeneID; 950302; -. DR KEGG; hin:HI1392; -. DR PATRIC; 20191481; VBIHaeInf48452_1451. DR eggNOG; ENOG4107YVC; Bacteria. DR eggNOG; ENOG4111IE7; LUCA. DR KO; K00571; -. DR OMA; QLVRICE; -. DR OrthoDB; EOG6FV84T; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 2. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Methyltransferase; KW Reference proteome; Restriction system; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 309 Modification methylase HindIII. FT /FTId=PRO_0000087964. SQ SEQUENCE 309 AA; 35550 MW; 954E04023326E061 CRC64; MIDCIYNSDS IFEIKKLDSN SIHAIISDIP YGIDYDDWDI LHSNTNSALG GTSSAQHKTS LFKRRGKPLN GWSEADKKRP QEYQEWVESW SNEWFRVLKS GSSVFVFAGR QFAHRVVVAF ENSGFTFKDM LSWEKDKAPH RAQRISCVFE RRGDIANTNK WVGWRVANLR PLFEPILWFQ KPYKTGSTLA DNLIKHEVGA WNENSLTHWN IQQGALNHSN ILKVRITSED KGYHVAQKPL NLMKLLIDLV TKEEQIVLDP FAGSGTTLLA AKELNRHFIG YEKNNGIYNI AVNRLGIEKN NCFYNKEKK // ID MURD_HAEIN Reviewed; 437 AA. AC P45063; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 119. DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase; DE EC=6.3.2.9; DE AltName: Full=D-glutamic acid-adding enzyme; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; GN Name=murD; OrderedLocusNames=HI_1136; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate CC to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine CC + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanyl-D-glutamate. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22791.1; -; Genomic_DNA. DR PIR; B64185; B64185. DR RefSeq; NP_439294.1; NC_000907.1. DR RefSeq; WP_005693450.1; NC_000907.1. DR ProteinModelPortal; P45063; -. DR SMR; P45063; 4-436. DR STRING; 71421.HI1136; -. DR EnsemblBacteria; AAC22791; AAC22791; HI_1136. DR GeneID; 950103; -. DR KEGG; hin:HI1136; -. DR PATRIC; 20190947; VBIHaeInf48452_1186. DR eggNOG; ENOG4105DMZ; Bacteria. DR eggNOG; COG0771; LUCA. DR KO; K01925; -. DR OMA; PGIPYTN; -. DR OrthoDB; EOG6PKFCR; -. DR PhylomeDB; P45063; -. DR SABIO-RK; P45063; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00639; MurD; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005762; UDP-N-AcMur-Glu_ligase. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01087; murD; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 437 UDP-N-acetylmuramoylalanine--D-glutamate FT ligase. FT /FTId=PRO_0000109023. FT NP_BIND 112 118 ATP. {ECO:0000255}. SQ SEQUENCE 437 AA; 47907 MW; B7232D573856880B CRC64; MNAYQNKNIT IIGLGKTGLS CVDYLLSQQA NIRVIDTRKN PTGIDKLPQN IPLHTGSLNQ EWLLESDMIV ISPGLAVKTP EIQTALKAGV EVIGDIELFC RAATKPIVGI TGSNGKSTVT TLVYEMAKAA GVKVGMGGNI GIPALSLLNE DCELYVLELS SFQLETTYSL KAAAATVLNV TEDHMDRYMD LEDYRQAKLR IYHNAKVGVL NNEDRLTFGE NENQAKHTVS FAENSADYWL KTENGKQYLM VKDEVILPCE EATLVGRHNY MNILAATALA QAIGINLDSI RTALRHFKGL DHRFQLVHQA NGIRWINDSK ATNVGSTVAA LAGLYIEGKL HLLLGGDGKG ADFSELAELI NQPHIICYCF GRDGALLAKF SSQSYLFDTM EQAIEFLRPT LQSGDMVLLS PACASLDQFA SFEKRGEEFT HLAQCLT // ID MUTS_HAEIN Reviewed; 861 AA. AC P44834; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=DNA mismatch repair protein MutS; GN Name=mutS; OrderedLocusNames=HI_0707; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. RC STRAIN=Eagan / Serotype B; RX PubMed=9422600; RA Martin K., Morlin G., Smith A., Nordyke A., Eisenstark A., Golomb M.; RT "The tryptophanase gene cluster of Haemophilus influenzae type b: RT evidence for horizontal gene transfer."; RL J. Bacteriol. 180:107-118(1998). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is possible that it carries out the mismatch recognition CC step. This protein has a weak ATPase activity (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22364.1; -; Genomic_DNA. DR EMBL; AF003252; AAB96581.1; -; Genomic_DNA. DR PIR; G64087; G64087. DR RefSeq; NP_438865.1; NC_000907.1. DR RefSeq; WP_010869037.1; NC_000907.1. DR ProteinModelPortal; P44834; -. DR SMR; P44834; 5-802. DR STRING; 71421.HI0707; -. DR EnsemblBacteria; AAC22364; AAC22364; HI_0707. DR GeneID; 949732; -. DR KEGG; hin:HI0707; -. DR PATRIC; 20190031; VBIHaeInf48452_0737. DR eggNOG; ENOG4105D86; Bacteria. DR eggNOG; COG0249; LUCA. DR KO; K03555; -. DR OMA; CVTPMGS; -. DR OrthoDB; EOG6Q5NPV; -. DR PhylomeDB; P44834; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.110; -; 1. DR Gene3D; 3.40.1170.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00096; MutS; 1. DR InterPro; IPR005748; DNA_mismatch_repair_MutS-1. DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N. DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01624; MutS_I; 1. DR Pfam; PF05188; MutS_II; 1. DR Pfam; PF05192; MutS_III; 1. DR Pfam; PF05190; MutS_IV; 1. DR Pfam; PF00488; MutS_V; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SUPFAM; SSF48334; SSF48334; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF53150; SSF53150; 1. DR SUPFAM; SSF55271; SSF55271; 1. DR TIGRFAMs; TIGR01070; mutS1; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 861 DNA mismatch repair protein MutS. FT /FTId=PRO_0000115102. FT NP_BIND 616 623 ATP. {ECO:0000255}. SQ SEQUENCE 861 AA; 96339 MW; 9F5E7FC91ABB576F CRC64; MISEENFQQH TPMMQQYLKL KAENPDILLF YRMGDFYELF YDDAKKAAAL LDISLTKRGQ SAGQPIPMAG MPYHAVEGYL AKLVQLGESV AICEQIGDPT TSKGPVERQI VRIVTPGTVS DEALLPERQD NLIAAVYQEK EKFGLATLDM TSGRFQLCEP ADKETLRAEL QRIAPVELLY CEEFNEMAAI EHCKGLRRRP IWEFELSTAI TLLNRQFGTK DLRAFGVEKS PLGLSAAGCL LQYAKETQRT ALPHIQSISL IQNQDCIQLD AATRRNLELT QNLAGGTENT LASVLDKCVT PMGSRLLKRW IHQPVRDVEK LKQRQQSIAE ILNFDLVDEL QPYLQLVGDM ERILARVALR SARPRDLTRL RTALEQIPAL RAIVQQKTPP FLTALFSQIA DFSEQCDLLQ RALIETPPLL IRDGGVIAEG YNAELDEWRM LSDGATQYLE NLEKREREST GIDTLKIGFN AVHGYYIQIS QGQAHKAPIH YVRRQTLKNA ERYIIPELKE YEDKVLKSKG AALALEKQLY DELFDLLLPH LGSLQLASLA LSELDVLVNL AERADTLNYV MPTFCDEVSV KIKNGRHPVV EQVLKDPFIA NPVELNHNRH LLVITGPNMG GKSTYMRQTA LITLLAYIGS FVPADSARIG PIDRIFTRIG ASDDLASGRS TFMVEMTEMA NILHQATAQS LVLIDEIGRG TSTYDGLSLA WACAEWLSKK IRSLTLFATH YFELTALPEQ LEGIANIHLD ALEHNNTIAF MHAVQNGAAS KSYGLAVAAL AGVPQSVIKL AKQKLTQLEK NSSYSAEQQI QALREANHNQ GELFFEQETD ALREAIEKLD PDDLSPKQAL AYLYQLKKMV G // ID MURF_HAEIN Reviewed; 457 AA. AC P45061; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 116. DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019}; DE EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019}; DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019}; DE AltName: Full=UDP-MurNAc-pentapeptide synthetase; GN Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; GN OrderedLocusNames=HI_1134; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final CC step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the CC precursor of murein. {ECO:0000255|HAMAP-Rule:MF_02019}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- CC glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N- CC acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D- CC alanine. {ECO:0000255|HAMAP-Rule:MF_02019}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_02019}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily. CC {ECO:0000255|HAMAP-Rule:MF_02019}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22789.1; -; Genomic_DNA. DR PIR; I64184; I64184. DR RefSeq; NP_439292.1; NC_000907.1. DR RefSeq; WP_010869135.1; NC_000907.1. DR ProteinModelPortal; P45061; -. DR STRING; 71421.HI1134; -. DR EnsemblBacteria; AAC22789; AAC22789; HI_1134. DR GeneID; 950620; -. DR KEGG; hin:HI1134; -. DR PATRIC; 20190943; VBIHaeInf48452_1184. DR eggNOG; ENOG4108EQQ; Bacteria. DR eggNOG; COG0770; LUCA. DR KO; K01929; -. DR OMA; YTALHMP; -. DR OrthoDB; EOG6PKFCR; -. DR PhylomeDB; P45061; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_02019; MurF; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005863; UDP-N-AcMur_synth. DR PANTHER; PTHR23135:SF3; PTHR23135:SF3; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01143; murF; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 457 UDP-N-acetylmuramoyl-tripeptide--D- FT alanyl-D-alanine ligase. FT /FTId=PRO_0000101699. FT NP_BIND 109 115 ATP. {ECO:0000255|HAMAP-Rule:MF_02019}. SQ SEQUENCE 457 AA; 50073 MW; 095EFE74F27CD28B CRC64; MIKLSTVQLA QILQAKLIGD ENVQVEKINT DTRKSVSNSL FFALKGEKFD AHQYLDQAVS QGALALVVQQ ENSSISVPQL VVKDTRIALG ELAKWLREKI NPRTVAMTGS SGKTTVKEMT ASILQHTAAD SEAVLFTNGN FNNDIGVPLT LLRLTEKHRF AVIELGANHQ NEINYTTKLV QPNAALINNI APAHLEGFGS LAGVVQAKGE IYRGLTKNGV AIINAEHNHL DIWQKEISNH AIQYFNGKDY SAKNIHHTSQ GSTFTLISPQ GEIEITLPYL GEHNVKNALA ATALAMNVGA TLTDVKAGLE QRSQVKGRLF PIQVTPNLLL LDDTYNANKD SLCAAIDVLK GYDAFRILCV GDMKELGENS LAIHREVGQY INLVNLDLVC SYGNESAVIS EAVSGKHFTD KTEMVDFLVP LIENQLQQNK KVVVLGKGSR SMKMEDVIYS LKDKIKC // ID MUTL_HAEIN Reviewed; 629 AA. AC P44494; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=DNA mismatch repair protein MutL; GN Name=mutL; OrderedLocusNames=HI_0067; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is involved in the repair of mismatches in CC DNA. It is required for dam-dependent methyl-directed DNA mismatch CC repair. May act as a "molecular matchmaker", a protein that CC promotes the formation of a stable complex between two or more CC DNA-binding proteins in an ATP-dependent manner without itself CC being part of a final effector complex (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21745.1; -; Genomic_DNA. DR PIR; E64046; E64046. DR RefSeq; NP_438240.1; NC_000907.1. DR RefSeq; WP_005693855.1; NC_000907.1. DR ProteinModelPortal; P44494; -. DR SMR; P44494; 1-329. DR STRING; 71421.HI0067; -. DR EnsemblBacteria; AAC21745; AAC21745; HI_0067. DR GeneID; 950964; -. DR KEGG; hin:HI0067; -. DR PATRIC; 20188589; VBIHaeInf48452_0068. DR eggNOG; ENOG4105DC6; Bacteria. DR eggNOG; COG0323; LUCA. DR KO; K03572; -. DR OMA; EVANLFF; -. DR OrthoDB; EOG6P8TMH; -. DR PhylomeDB; P44494; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IBA:GO_Central. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR HAMAP; MF_00149; DNA_mis_repair; 1. DR InterPro; IPR013507; DNA_mismatch_repair_C. DR InterPro; IPR014762; DNA_mismatch_repair_CS. DR InterPro; IPR002099; DNA_mismatch_repair_fam. DR InterPro; IPR020667; DNA_mismatch_repair_MutL. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR014790; MutL_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF01119; DNA_mis_repair; 1. DR Pfam; PF08676; MutL_C; 1. DR SMART; SM01340; DNA_mis_repair; 1. DR SMART; SM00853; MutL_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR00585; mutl; 1. DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Reference proteome. FT CHAIN 1 629 DNA mismatch repair protein MutL. FT /FTId=PRO_0000177947. SQ SEQUENCE 629 AA; 71623 MW; 0ADC240FD94D1556 CRC64; MPIKILSPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAN KIQIDIENGG ANLIRIRDNG CGIPKEELSL ALARHATSKI ADLDDLEAIL SLGFRGEALA SISSVSRLTL TSRTEEQTEA WQVYAQGRDM ETTIKPASHP VGTTVEVANL FFNTPARRKF LRTDKTEFSH IDEVIRRIAL TKFNTAFTLT HNGKIIRQYR PAEAINQQLK RVAAICGDDF VKNALRIEWK HDDLHLSGWV ATPNFSRTQN DLSYCYINGR MVRDKVISHA IRQAYAQYLP TDAYPAFVLF IDLNPHDVDV NVHPTKHEVR FHQQRLIHDF IYEGISHALN NQEQINWHTD QSAVENHEEN TVREPQPNYS IRPNRATAGQ NSFAPQYHEK PQQNQPHFSN TPMFPNHVST GYRDYRSDAP SKTEQRLYAE LLRTLPPTAQ KDISDTAQQN ISDTAKIIST EIIECSSHLR ALSLIENRAL LLQQNQDFFL LSLEKLQRLQ WQLALKQIQI EQQALLIPIV FRLTESQFQA WQQYSDDFKK IGFEFIENQA QLRLTLNKVP SALRTQNLQK CVMAMLTRDE NSSSFLTALC AQLECKTFNA LADALNLLSE TERLLTQTNR TAFTQLLKPV NWQPLLDEI // ID MTGA_HAEIN Reviewed; 246 AA. AC P44890; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Monofunctional biosynthetic peptidoglycan transglycosylase {ECO:0000255|HAMAP-Rule:MF_00766}; DE Short=Monofunctional TGase {ECO:0000255|HAMAP-Rule:MF_00766}; DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_00766}; GN Name=mtgA {ECO:0000255|HAMAP-Rule:MF_00766}; GN OrderedLocusNames=HI_0831; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00766}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00766}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00766}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 51 family. CC {ECO:0000255|HAMAP-Rule:MF_00766}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22489.1; 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; L42023; AAC22489.1; ALT_INIT; Genomic_DNA. DR PIR; B64159; B64159. DR RefSeq; NP_438991.2; NC_000907.1. DR RefSeq; WP_005666147.1; NC_000907.1. DR ProteinModelPortal; P44890; -. DR STRING; 71421.HI0831; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; AAC22489; AAC22489; HI_0831. DR GeneID; 949845; -. DR KEGG; hin:HI0831; -. DR PATRIC; 20190317; VBIHaeInf48452_0872. DR eggNOG; ENOG4108VKV; Bacteria. DR eggNOG; COG0744; LUCA. DR KO; K03814; -. DR OMA; QISAWLS; -. DR OrthoDB; EOG6HMXCD; -. DR PhylomeDB; P44890; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00766; Mono_pep_trsgly; 1. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR011812; Mono_pep_trsgly. DR Pfam; PF00912; Transgly; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR TIGRFAMs; TIGR02070; mono_pep_trsgly; 1. PE 3: Inferred from homology; KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; KW Complete proteome; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 246 Monofunctional biosynthetic peptidoglycan FT transglycosylase. FT /FTId=PRO_0000083128. FT TRANSMEM 27 47 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00766}. SQ SEQUENCE 246 AA; 28700 MW; 835EA4C3FD8B12B7 CRC64; MKKTKRIFTA LSHLFSPKWW KKNWQRVVFC FFFAVFALLL IFRFVPIPFS AYMVQQKIAN LLQGDFRYQI QYNWVSLENI SPNIQLAVIS SEDQRFLEHL GFDFEAIQRA IRYNEKSNKG IRGASTISQQ TAKNLMLWHG QNWLRKGLEV PATMLLELTW SKKRILEVYL NIAEFGNGIF GVEAASRYYF KKSAKNLSQN EAALLAAVLP NPIIYKVNKP SLLVRKKQTW ILRQMGNLGT EYLSHL // ID MURJ_HAEIN Reviewed; 510 AA. AC P44958; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Putative lipid II flippase MurJ; GN Name=murJ; Synonyms=mviN; OrderedLocusNames=HI_0964; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in peptidoglycan biosynthesis. Transports CC lipid-linked peptidoglycan precursors from the inner to the outer CC leaflet of the cytoplasmic membrane (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurJ/MviN family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22623.1; -; Genomic_DNA. DR PIR; I64162; I64162. DR RefSeq; NP_439125.1; NC_000907.1. DR RefSeq; WP_010869096.1; NC_000907.1. DR STRING; 71421.HI0964; -. DR EnsemblBacteria; AAC22623; AAC22623; HI_0964. DR GeneID; 950595; -. DR KEGG; hin:HI0964; -. DR PATRIC; 20190587; VBIHaeInf48452_1006. DR eggNOG; ENOG4105CJR; Bacteria. DR eggNOG; COG0728; LUCA. DR KO; K03980; -. DR OMA; YFYSEYL; -. DR OrthoDB; EOG6C0131; -. DR PhylomeDB; P44958; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015648; F:lipid-linked peptidoglycan transporter activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0034204; P:lipid translocation; IBA:GO_Central. DR GO; GO:0015836; P:lipid-linked peptidoglycan transport; IBA:GOC. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR004268; MurJ. DR Pfam; PF03023; MVIN; 1. DR PIRSF; PIRSF002869; MviN; 1. DR PRINTS; PR01806; VIRFACTRMVIN. DR TIGRFAMs; TIGR01695; murJ_mviN; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Membrane; KW Peptidoglycan synthesis; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 510 Putative lipid II flippase MurJ. FT /FTId=PRO_0000182008. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 82 102 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. FT TRANSMEM 315 335 Helical. {ECO:0000255}. FT TRANSMEM 357 377 Helical. {ECO:0000255}. FT TRANSMEM 396 416 Helical. {ECO:0000255}. FT TRANSMEM 443 463 Helical. {ECO:0000255}. FT TRANSMEM 481 501 Helical. {ECO:0000255}. SQ SEQUENCE 510 AA; 56165 MW; 7E9FDD75F162ECC0 CRC64; MTLLSRVLGL VRDVVIAHLI GAGAAADVFL FANRIPNFLR RLFAEGAFSQ AFVPVLAEYQ QSGDMNKTRE FIGKVSGTLG GLVSIVTILA MVGSPHVAAL FGMGWFTDWM NDGPDAHKFE QASLLLKITF PYLWFVTFVA FSGAVLNTIG KFGVMSFSPV LLNIAMIATA LFLAPQMDNP DLALAIGIFL GGLLQFLFQI PFMKQAGLLV KPKWAWRDEG VTKIRKLMIP ALFGVSVSQI NLLLDTVIAS FLMTGSISWL YYSDRLLEFP LGLFGIAIST VILPTLARHH VNREGDSAKS AVDFRNTMDW GVRMIFLLGV PAAIGIAVLA QPMLLTLFMR GNFMLNDVYA ASYSLRAFNA GLLSFMLIKI LANGYYARQD TKTPVKIGII AMVSNMGFNL LAIPFSYVGL AIASAMSATL NAYLLYRGLA KADVYHFSRK SAVFFVKVLL AAIAMGAAVW YYVPEINQWA KMDFFMRVYW LVWLIVLAAI VYGATLILLG VRKHHLLTKN // ID MURQ_HAEIN Reviewed; 303 AA. AC P44862; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=N-acetylmuramic acid 6-phosphate etherase; DE Short=MurNAc-6-P etherase; DE EC=4.2.1.126; DE AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase; DE AltName: Full=N-acetylmuramic acid 6-phosphate lyase; GN Name=murQ; OrderedLocusNames=HI_0754; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RG Midwest center for structural genomics (MCSG); RT "Crystal structure of hypothetical protein HI0754 from Haemophilus RT influenzae."; RL Submitted (JAN-2005) to the PDB data bank. CC -!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl CC ether substituent of MurNAc 6-phosphate, producing GlcNAc 6- CC phosphate and D-lactate. Together with AnmK, is also required for CC the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either CC imported from the medium or derived from its own cell wall murein, CC and thus plays a role in cell wall recycling (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (R)-lactate + N-acetyl-D-glucosamine 6- CC phosphate = N-acetylmuramate 6-phosphate + H(2)O. CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate CC degradation. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is CC suggested for the cleavage of the lactyl ether bond of MurNAc 6- CC phosphate, with the formation of an alpha,beta-unsaturated CC aldehyde intermediate with (E)-stereochemistry, followed by the CC syn addition of water to give product. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SIS 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; L42023; AAC22413.1; -; Genomic_DNA. DR PIR; I64090; I64090. DR RefSeq; NP_438913.1; NC_000907.1. DR RefSeq; WP_005693153.1; NC_000907.1. DR PDB; 1NRI; X-ray; 1.90 A; A=1-303. DR PDB; 4LZJ; X-ray; 2.40 A; A/B/C/D=1-303. DR PDB; 4M0D; X-ray; 2.58 A; A/B/C/D=1-303. DR PDBsum; 1NRI; -. DR PDBsum; 4LZJ; -. DR PDBsum; 4M0D; -. DR ProteinModelPortal; P44862; -. DR SMR; P44862; 9-256. DR STRING; 71421.HI0754; -. DR EnsemblBacteria; AAC22413; AAC22413; HI_0754. DR GeneID; 949804; -. DR KEGG; hin:HI0754; -. DR PATRIC; 20190153; VBIHaeInf48452_0792. DR eggNOG; ENOG4105E15; Bacteria. DR eggNOG; COG2103; LUCA. DR KO; K07106; -. DR OMA; AIRIVMQ; -. DR OrthoDB; EOG6DG2VH; -. DR PhylomeDB; P44862; -. DR UniPathway; UPA00342; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR EvolutionaryTrace; P44862; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00068; MurQ; 1. DR InterPro; IPR005488; Etherase_MurQ. DR InterPro; IPR005486; Glucokinase_regulatory_CS. DR InterPro; IPR001347; SIS. DR Pfam; PF01380; SIS; 1. DR TIGRFAMs; TIGR00274; TIGR00274; 1. DR PROSITE; PS01272; GCKR; 1. DR PROSITE; PS51464; SIS; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Lyase; KW Reference proteome. FT CHAIN 1 303 N-acetylmuramic acid 6-phosphate FT etherase. FT /FTId=PRO_0000214836. FT DOMAIN 61 224 SIS. FT ACT_SITE 89 89 Proton donor. {ECO:0000250}. FT ACT_SITE 120 120 {ECO:0000250}. FT HELIX 4 10 {ECO:0000244|PDB:4LZJ}. FT HELIX 13 15 {ECO:0000244|PDB:1NRI}. FT HELIX 19 21 {ECO:0000244|PDB:1NRI}. FT HELIX 24 26 {ECO:0000244|PDB:1NRI}. FT HELIX 29 40 {ECO:0000244|PDB:1NRI}. FT HELIX 42 66 {ECO:0000244|PDB:1NRI}. FT STRAND 71 76 {ECO:0000244|PDB:1NRI}. FT HELIX 77 94 {ECO:0000244|PDB:1NRI}. FT STRAND 100 105 {ECO:0000244|PDB:1NRI}. FT HELIX 109 112 {ECO:0000244|PDB:1NRI}. FT HELIX 119 121 {ECO:0000244|PDB:1NRI}. FT HELIX 125 132 {ECO:0000244|PDB:1NRI}. FT STRAND 139 144 {ECO:0000244|PDB:1NRI}. FT HELIX 151 163 {ECO:0000244|PDB:1NRI}. FT STRAND 166 173 {ECO:0000244|PDB:1NRI}. FT HELIX 177 181 {ECO:0000244|PDB:1NRI}. FT STRAND 182 187 {ECO:0000244|PDB:1NRI}. FT TURN 199 201 {ECO:0000244|PDB:1NRI}. FT HELIX 202 221 {ECO:0000244|PDB:1NRI}. FT STRAND 224 226 {ECO:0000244|PDB:4LZJ}. FT HELIX 238 251 {ECO:0000244|PDB:1NRI}. FT HELIX 256 265 {ECO:0000244|PDB:4LZJ}. FT TURN 266 268 {ECO:0000244|PDB:4LZJ}. FT HELIX 270 279 {ECO:0000244|PDB:4LZJ}. FT HELIX 283 292 {ECO:0000244|PDB:4LZJ}. FT TURN 293 295 {ECO:0000244|PDB:4LZJ}. FT HELIX 297 302 {ECO:0000244|PDB:4LZJ}. SQ SEQUENCE 303 AA; 32532 MW; 789297C871248BD6 CRC64; MNDIILKSLS TLITEQRNPN SVDIDRQSTL EIVRLMNEED KLVPLAIESC LPQISLAVEQ IVQAFQQGGR LIYIGAGTSG RLGVLDASEC PPTFGVSTEM VKGIIAGGEC AIRHPVEGAE DNTKAVLNDL QSIHFSKNDV LVGIAASGRT PYVIAGLQYA KSLGALTISI ASNPKSEMAE IADIAIETIV GPEILTGSSR LKSGTAQKMV LNMLTTASMI LLGKCYENLM VDVQASNEKL KARAVRIVMQ ATDCNKTLAE QTLLEADQNA KLAIMMILST LSKSEAKVLL ERHQGKLRNA LSK // ID NANE_HAEIN Reviewed; 228 AA. AC P71340; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase; DE EC=5.1.3.9; DE AltName: Full=ManNAc-6-P epimerase; GN Name=nanE; OrderedLocusNames=HI_0145; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to CC N-acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: N-acyl-D-glucosamine 6-phosphate = N-acyl-D- CC mannosamine 6-phosphate. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; CC D-fructose 6-phosphate from N-acetylneuraminate: step 3/5. CC -!- SIMILARITY: Belongs to the NanE 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; L42023; AAC21817.1; -; Genomic_DNA. DR RefSeq; NP_438314.1; NC_000907.1. DR RefSeq; WP_010868945.1; NC_000907.1. DR ProteinModelPortal; P71340; -. DR STRING; 71421.HI0145; -. DR EnsemblBacteria; AAC21817; AAC21817; HI_0145. DR GeneID; 951054; -. DR KEGG; hin:HI0145; -. DR PATRIC; 20188781; VBIHaeInf48452_0147. DR eggNOG; ENOG4105C9S; Bacteria. DR eggNOG; COG3010; LUCA. DR KO; K01788; -. DR OMA; ITRPMEI; -. DR OrthoDB; EOG6NSGKX; -. DR PhylomeDB; P71340; -. DR UniPathway; UPA00629; UER00682. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01235; ManNAc6P_epimer; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007260; NanE. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF04131; NanE; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 228 Putative N-acetylmannosamine-6-phosphate FT 2-epimerase. FT /FTId=PRO_0000179776. SQ SEQUENCE 228 AA; 24353 MW; EDC795CB0501AB18 CRC64; MSKLSYQEVL SQIQYGLISS CQPVDDGPMD KPEIVSAMAQ ASVMGGRSGL RIEGVDNLKA TRPFVNVPII GIVKRDLPDS PVRITPFLQD IEDLANAGAD IIAVDGTSRP RPVDIESAVK KIHEMGCLAM ADCSNLEEGL YCKALGFDIV GSTMSGYTGG AVPEEPDYQL VKDLKSAGCF VMAEGRYNTP ELAKVAIEIG ADCVTVGSAL TRLEHIVSWF ANSVKSAR // ID MUKB_HAEIN Reviewed; 1510 AA. AC P45187; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Chromosome partition protein MukB {ECO:0000255|HAMAP-Rule:MF_01800}; DE AltName: Full=Structural maintenance of chromosome-related protein {ECO:0000255|HAMAP-Rule:MF_01800}; GN Name=mukB {ECO:0000255|HAMAP-Rule:MF_01800}; GN OrderedLocusNames=HI_1374; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a central role in chromosome condensation, CC segregation and cell cycle progression. Functions as a homodimer, CC which is essential for chromosome partition. Involved in negative CC DNA supercoiling in vivo, and by this means organize and compact CC chromosomes. May achieve or facilitate chromosome segregation by CC condensation DNA from both sides of a centrally located replisome CC during cell division. {ECO:0000255|HAMAP-Rule:MF_01800}. CC -!- SUBUNIT: Homodimerization via its hinge domain. Binds to DNA via CC its C-terminal region. Interacts, and probably forms a ternary CC complex, with MukE and MukF via its C-terminal region. The complex CC formation is stimulated by calcium or magnesium. Interacts with CC tubulin-related protein FtsZ. {ECO:0000255|HAMAP-Rule:MF_01800}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01800}. Note=Restricted to the nucleoid region. CC {ECO:0000255|HAMAP-Rule:MF_01800}. CC -!- DOMAIN: The hinge domain, which separates the large intramolecular CC coiled coil regions, allows the homodimerization, forming a V- CC shaped homodimer. {ECO:0000255|HAMAP-Rule:MF_01800}. CC -!- SIMILARITY: Belongs to the SMC family. MukB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01800}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23022.1; -; Genomic_DNA. DR PIR; D64120; D64120. DR RefSeq; NP_439526.1; NC_000907.1. DR RefSeq; WP_005693982.1; NC_000907.1. DR ProteinModelPortal; P45187; -. DR SMR; P45187; 45-264. DR STRING; 71421.HI1374; -. DR PRIDE; P45187; -. DR EnsemblBacteria; AAC23022; AAC23022; HI_1374. DR GeneID; 950289; -. DR KEGG; hin:HI1374; -. DR PATRIC; 20191437; VBIHaeInf48452_1429. DR eggNOG; ENOG4105DUC; Bacteria. DR eggNOG; COG3096; LUCA. DR KO; K03632; -. DR OMA; DRCEEIR; -. DR OrthoDB; EOG62C98M; -. DR PhylomeDB; P45187; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01800; MukB; 1. DR InterPro; IPR012090; MukB. DR InterPro; IPR032520; MukB_hinge. DR InterPro; IPR007406; MukB_N_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04310; MukB; 1. DR Pfam; PF16330; MukB_hinge; 1. DR PIRSF; PIRSF005246; MukB; 1. DR SUPFAM; SSF52540; SSF52540; 3. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Chromosome partition; KW Coiled coil; Complete proteome; Cytoplasm; DNA condensation; KW DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 1510 Chromosome partition protein MukB. FT /FTId=PRO_0000068220. FT NP_BIND 75 82 ATP. {ECO:0000255|HAMAP-Rule:MF_01800}. FT REGION 707 824 Flexible hinge. {ECO:0000255|HAMAP- FT Rule:MF_01800}. FT COILED 346 706 {ECO:0000255|HAMAP-Rule:MF_01800}. FT COILED 825 1154 {ECO:0000255|HAMAP-Rule:MF_01800}. FT COILED 1248 1304 {ECO:0000255|HAMAP-Rule:MF_01800}. SQ SEQUENCE 1510 AA; 173286 MW; 173EEC4198E3184F CRC64; MSDVFELENE IELESDEVIL ENENVEEIVD APIPFSMTTN NGIERGKFRS LTLINWNGFF ARTFDLDELV TTLSGGNGAG KSTTMAGFVT ALIPDLTLLH FRNTTEAGST GGSRDKGLHG KLRPGVCYAV LDTINSRHQR ILVGVRLQQI AGRDKKVDLK TFSIQGVELS QNPTALFTET VGEHQARVLN LNELKDKIEN IGAQFKQYHS ITDYHGMMFD LGIIPKRLRS ASDRSKFYKL IEASLYGGIS SAITRSLRDY LLPENLGVRK AFQDMESALR ENRMTLEAIK VTQSDRDLFK HLITETTNYV ASDYMRNANE RRGNIEAALE SRREWYKAKA EQNLSQHRLV DLSREVAELA ESERTLEVDH QSAVDHLNLV LNALRHQEKI TRYQEDIAEL TERLEEQKMV VEDANDALEE SQAQFEQTEI EIDAVRSQLA DYQQALDAQQ TRALQYQQAI AALEKAKTLC GLADLSVKNV EDYHAEFDAH AESLTETVLE LEHKMSISEA AKSQFDKAYQ LVCKIAGEMP RSTAWESAKE LLREYPSQKL QAQQTPQLRT KLHELEQRYA QQQSAVKLLN DFNQRANLSL QTAEELEDYH AEQEALIEDI SARLSEQVEN RSTLRQKREN LTALYDENAR KAPAWLTAQA ALERLEQQSG ERFEHSQDVM NFMQSQLVKE RELTMQRDQL EQKRLHLDEQ ISRLSQPDGS EDPRLNMLAE RFGGVLLSEL YDDVTIEDAP YFSALYGPSR HAIVVRDLNA VREQLAQLED CPDDLYLIEG DPTAFDDSVL SAQELELGVV VQVSDRELRY SRFPEIPLFG CAAREKRLEE LQIERDEVAE QHAQIAFDVQ KCQRLHEHFS QFVGLHLALA FQPNPEALMS EINRERNEID RELNQFNSGE QQLRIQLDNA KERLQLLNKL IPQLNVLADE DLIDRIEECR EQLDIAEQDE YFIRQHGVTL SQLEPIANSL QSDPENYEGL KNELTQAIER QKQVQQRVFA LADVVQRKPH FGYEDAGQAE TSELNEKLRQ RLEQMQAQRD TQREQVRQKQ SQFAEYNRVL IQLQSSYDSK YQLLNELIGE ISDLGVRADD GAEERARIRR DELHQQLSTS RQRRSYVEKQ LTLIESEADN LNRLIRKTER DYKTQRELVV AAKVSWCVVL RLSRNSDMEK RLNRRELAYL SADELRSMSD KALGALRTAV ADNEYLRDSL RVSEDSRKPE NKVRFFIAVY QHLRERIRQD IIKTDDPIDA IEQMEIELSR LTAELTGREK KLAISSESVA NIMRKTIQRE QNRIRMLNQG LQNIAFGQVK SVRLVVNIRD THAMLLDALS GQQDEYQDLF NDNRITFSEA MAKLYQRINP HIDMGQRTAQ TIGEELLDYR NYLELEVEVF RGADGWLRAE SGALSTGEAI GTGMSILLMV VQSWEEESRR IRGKDIVPCR LLFLDEAARL DGKSISTLFE LCERLDMQLL IAAPENISPE KGTTYKLVRK IAGNQEYVHV VGLRGFGATE // ID MUKE_HAEIN Reviewed; 243 AA. AC P45186; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Chromosome partition protein MukE {ECO:0000255|HAMAP-Rule:MF_01802}; GN Name=mukE {ECO:0000255|HAMAP-Rule:MF_01802}; Synonyms=kicA; GN OrderedLocusNames=HI_1373; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in chromosome condensation, segregation and CC cell cycle progression. May participate in facilitating chromosome CC segregation by condensation DNA from both sides of a centrally CC located replisome during cell division. Probably acts via its CC interaction with MukB and MukF. {ECO:0000255|HAMAP-Rule:MF_01802}. CC -!- SUBUNIT: Interacts, and probably forms a ternary complex, with CC MukF and MukB. The complex formation is stimulated by calcium or CC magnesium. {ECO:0000255|HAMAP-Rule:MF_01802}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01802}. Note=Restricted to the nucleoid region. CC {ECO:0000255|HAMAP-Rule:MF_01802}. CC -!- SIMILARITY: Belongs to the MukE family. {ECO:0000255|HAMAP- CC Rule:MF_01802}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23021.1; -; Genomic_DNA. DR PIR; C64120; C64120. DR RefSeq; NP_439525.1; NC_000907.1. DR RefSeq; WP_005693983.1; NC_000907.1. DR STRING; 71421.HI1373; -. DR EnsemblBacteria; AAC23021; AAC23021; HI_1373. DR GeneID; 950288; -. DR KEGG; hin:HI1373; -. DR PATRIC; 20191435; VBIHaeInf48452_1428. DR eggNOG; ENOG4105DAH; Bacteria. DR eggNOG; COG3095; LUCA. DR KO; K03804; -. DR OMA; FLMDYQE; -. DR OrthoDB; EOG6K13RB; -. DR PhylomeDB; P45186; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01802; MukE; 1. DR InterPro; IPR007385; Scp_MukE. DR Pfam; PF04288; MukE; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; DNA condensation; Reference proteome. FT CHAIN 1 243 Chromosome partition protein MukE. FT /FTId=PRO_0000206797. SQ SEQUENCE 243 AA; 27229 MW; 49DAC93A88B85216 CRC64; MTDIQDVISP KLAVAIANPI FPAVDSLLRS GRHISTEHLD NHAFLMDFQN ELDGFYRRYN VELIRAPEGF FYLRPKATTL IARSVLSELE MLVGKVLCYL YLSPERLAQQ GIFSTQEVYD ELLNLADEGK LLKAVNQRSS GSDLDKQKLA EKVRAAIGRL RRLGMIQTVG EQNSGKFTIS ESVFRFGAEV RSGDDPLESQ ARLIRDGEAA TPDSLALEKQ AQLMENDTKS ADEIDEEFDG EQE // ID MURA_HAEIN Reviewed; 424 AA. AC P45025; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 122. DE RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111}; DE Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111}; GN Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ; GN OrderedLocusNames=HI_1081; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N- CC acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D- CC glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha- CC D-glucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22737.1; -; Genomic_DNA. DR PIR; A64182; A64182. DR RefSeq; NP_439238.1; NC_000907.1. DR RefSeq; WP_005693405.1; NC_000907.1. DR PDB; 2RL1; X-ray; 2.20 A; A=1-424. DR PDB; 2RL2; X-ray; 2.30 A; A=1-424. DR PDB; 3SWE; X-ray; 2.20 A; A=1-424. DR PDBsum; 2RL1; -. DR PDBsum; 2RL2; -. DR PDBsum; 3SWE; -. DR ProteinModelPortal; P45025; -. DR SMR; P45025; 1-420. DR STRING; 71421.HI1081; -. DR EnsemblBacteria; AAC22737; AAC22737; HI_1081. DR GeneID; 950056; -. DR KEGG; hin:HI1081; -. DR PATRIC; 20190827; VBIHaeInf48452_1126. DR eggNOG; ENOG4105CDF; Bacteria. DR eggNOG; COG0766; LUCA. DR KO; K00790; -. DR OMA; IRTAPHP; -. DR OrthoDB; EOG68M4GK; -. DR PhylomeDB; P45025; -. DR BRENDA; 2.5.1.7; 2529. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P45025; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00111; MurA; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA. DR Pfam; PF00275; EPSP_synthase; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01072; murA; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase. FT CHAIN 1 424 UDP-N-acetylglucosamine 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000178876. FT ACT_SITE 117 117 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00111}. FT MOD_RES 117 117 2-(S-cysteinyl)pyruvic acid O- FT phosphothioketal. {ECO:0000255|HAMAP- FT Rule:MF_00111}. FT STRAND 2 8 {ECO:0000244|PDB:2RL1}. FT STRAND 14 17 {ECO:0000244|PDB:2RL1}. FT HELIX 22 31 {ECO:0000244|PDB:2RL1}. FT HELIX 32 34 {ECO:0000244|PDB:2RL1}. FT STRAND 35 37 {ECO:0000244|PDB:2RL1}. FT STRAND 39 43 {ECO:0000244|PDB:2RL1}. FT HELIX 48 58 {ECO:0000244|PDB:2RL1}. FT TURN 59 61 {ECO:0000244|PDB:2RL1}. FT STRAND 63 66 {ECO:0000244|PDB:2RL1}. FT STRAND 72 75 {ECO:0000244|PDB:2RL1}. FT HELIX 86 89 {ECO:0000244|PDB:2RL1}. FT HELIX 93 98 {ECO:0000244|PDB:2RL1}. FT HELIX 99 106 {ECO:0000244|PDB:2RL1}. FT STRAND 107 112 {ECO:0000244|PDB:2RL1}. FT STRAND 118 120 {ECO:0000244|PDB:2RL2}. FT HELIX 125 133 {ECO:0000244|PDB:2RL1}. FT STRAND 137 141 {ECO:0000244|PDB:2RL1}. FT STRAND 144 148 {ECO:0000244|PDB:2RL1}. FT STRAND 150 152 {ECO:0000244|PDB:2RL1}. FT STRAND 157 159 {ECO:0000244|PDB:2RL1}. FT HELIX 165 175 {ECO:0000244|PDB:2RL1}. FT STRAND 178 185 {ECO:0000244|PDB:2RL1}. FT HELIX 191 201 {ECO:0000244|PDB:2RL1}. FT TURN 202 204 {ECO:0000244|PDB:2RL1}. FT STRAND 212 218 {ECO:0000244|PDB:2RL1}. FT STRAND 226 229 {ECO:0000244|PDB:2RL1}. FT HELIX 234 245 {ECO:0000244|PDB:2RL1}. FT TURN 246 248 {ECO:0000244|PDB:2RL1}. FT STRAND 250 255 {ECO:0000244|PDB:2RL1}. FT HELIX 258 260 {ECO:0000244|PDB:2RL1}. FT HELIX 262 270 {ECO:0000244|PDB:2RL1}. FT STRAND 274 277 {ECO:0000244|PDB:2RL1}. FT STRAND 279 285 {ECO:0000244|PDB:2RL1}. FT STRAND 296 298 {ECO:0000244|PDB:2RL1}. FT HELIX 306 308 {ECO:0000244|PDB:2RL1}. FT HELIX 309 317 {ECO:0000244|PDB:2RL1}. FT STRAND 319 326 {ECO:0000244|PDB:2RL1}. FT HELIX 336 341 {ECO:0000244|PDB:2RL1}. FT TURN 342 344 {ECO:0000244|PDB:2RL1}. FT STRAND 346 350 {ECO:0000244|PDB:2RL1}. FT STRAND 353 357 {ECO:0000244|PDB:2RL1}. FT STRAND 366 368 {ECO:0000244|PDB:2RL1}. FT TURN 372 375 {ECO:0000244|PDB:2RL1}. FT HELIX 376 384 {ECO:0000244|PDB:2RL1}. FT STRAND 385 392 {ECO:0000244|PDB:2RL1}. FT HELIX 395 400 {ECO:0000244|PDB:2RL1}. FT HELIX 404 409 {ECO:0000244|PDB:2RL1}. FT TURN 410 412 {ECO:0000244|PDB:2RL1}. FT STRAND 415 419 {ECO:0000244|PDB:2RL1}. SQ SEQUENCE 424 AA; 45187 MW; EAB3170DF91F17C3 CRC64; MDKFRVYGQS RLSGSVNISG AKNAALPILF AAILATEPVK LTNVPELKDI ETTLKILRQL GVVVDRDATG AVLLDASNIN HFTAPYELVK TMRASIWALA PLVARFHQGQ VSLPGGCSIG ARPVDLHISG LEKLGADIVL EEGYVKAQVS DRLVGTRIVI EKVSVGATLS IMMAATLAKG TTVIENAARE PEIVDTADFL NKMGAKITGA GSAHITIEGV ERLTGCEHSV VPDRIETGTF LIAAAISGGC VVCQNTKADT LDAVIDKLRE AGAQVDVTEN SITLDMLGNR PKAVNIRTAP HPGFPTDMQA QFTLLNMVAE GTSIITETIF ENRFMHIPEL IRMGGKAEIE GNTAVCHGVE QLSGTEVIAT DLRASISLVL AGCIATGETI VDRIYHIDRG YEHIEDKLRG LGAKIERFSG SDEA // ID MURC_HAEIN Reviewed; 475 AA. AC P45066; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 128. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase; DE EC=6.3.2.8; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase; GN Name=murC; OrderedLocusNames=HI_1139; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L- CC alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanine. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22794.1; -; Genomic_DNA. DR PIR; E64185; E64185. DR RefSeq; NP_439297.1; NC_000907.1. DR RefSeq; WP_005693453.1; NC_000907.1. DR PDB; 1GQQ; X-ray; 3.10 A; A/B=1-475. DR PDB; 1GQY; X-ray; 1.80 A; A/B=1-475. DR PDB; 1P31; X-ray; 1.85 A; A/B=1-475. DR PDB; 1P3D; X-ray; 1.70 A; A/B=1-475. DR PDBsum; 1GQQ; -. DR PDBsum; 1GQY; -. DR PDBsum; 1P31; -. DR PDBsum; 1P3D; -. DR ProteinModelPortal; P45066; -. DR SMR; P45066; 6-474. DR STRING; 71421.HI1139; -. DR EnsemblBacteria; AAC22794; AAC22794; HI_1139. DR GeneID; 949618; -. DR KEGG; hin:HI1139; -. DR PATRIC; 20190953; VBIHaeInf48452_1189. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR KO; K01924; -. DR OMA; FHFIGIG; -. DR OrthoDB; EOG64BQ73; -. DR PhylomeDB; P45066; -. DR BRENDA; 6.3.2.8; 2529. DR UniPathway; UPA00219; -. DR EvolutionaryTrace; P45066; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01082; murC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 475 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_0000182100. FT NP_BIND 125 131 ATP. {ECO:0000255}. FT HELIX 3 9 {ECO:0000244|PDB:1GQY}. FT STRAND 20 25 {ECO:0000244|PDB:1P3D}. FT HELIX 31 41 {ECO:0000244|PDB:1P3D}. FT STRAND 44 50 {ECO:0000244|PDB:1P3D}. FT HELIX 54 61 {ECO:0000244|PDB:1P3D}. FT STRAND 65 69 {ECO:0000244|PDB:1P3D}. FT HELIX 72 75 {ECO:0000244|PDB:1P3D}. FT STRAND 79 83 {ECO:0000244|PDB:1P3D}. FT STRAND 85 87 {ECO:0000244|PDB:1GQQ}. FT HELIX 92 99 {ECO:0000244|PDB:1P3D}. FT STRAND 104 106 {ECO:0000244|PDB:1P3D}. FT HELIX 107 116 {ECO:0000244|PDB:1P3D}. FT STRAND 118 127 {ECO:0000244|PDB:1P3D}. FT HELIX 129 142 {ECO:0000244|PDB:1P3D}. FT STRAND 148 150 {ECO:0000244|PDB:1P3D}. FT TURN 156 158 {ECO:0000244|PDB:1P3D}. FT STRAND 159 163 {ECO:0000244|PDB:1P3D}. FT STRAND 166 173 {ECO:0000244|PDB:1P3D}. FT HELIX 180 183 {ECO:0000244|PDB:1P3D}. FT STRAND 187 191 {ECO:0000244|PDB:1P3D}. FT HELIX 199 202 {ECO:0000244|PDB:1P3D}. FT HELIX 206 217 {ECO:0000244|PDB:1P3D}. FT STRAND 225 229 {ECO:0000244|PDB:1P3D}. FT HELIX 233 242 {ECO:0000244|PDB:1P3D}. FT STRAND 244 252 {ECO:0000244|PDB:1P3D}. FT STRAND 256 265 {ECO:0000244|PDB:1P3D}. FT STRAND 268 274 {ECO:0000244|PDB:1P3D}. FT STRAND 280 287 {ECO:0000244|PDB:1P3D}. FT HELIX 290 305 {ECO:0000244|PDB:1P3D}. FT HELIX 310 318 {ECO:0000244|PDB:1P3D}. FT STRAND 326 335 {ECO:0000244|PDB:1P3D}. FT STRAND 338 345 {ECO:0000244|PDB:1P3D}. FT HELIX 350 364 {ECO:0000244|PDB:1P3D}. FT STRAND 369 373 {ECO:0000244|PDB:1P3D}. FT HELIX 378 383 {ECO:0000244|PDB:1P3D}. FT HELIX 385 392 {ECO:0000244|PDB:1P3D}. FT STRAND 395 401 {ECO:0000244|PDB:1P3D}. FT HELIX 416 426 {ECO:0000244|PDB:1P3D}. FT STRAND 432 435 {ECO:0000244|PDB:1P3D}. FT HELIX 437 439 {ECO:0000244|PDB:1P3D}. FT HELIX 440 447 {ECO:0000244|PDB:1P3D}. FT STRAND 453 457 {ECO:0000244|PDB:1P3D}. FT HELIX 462 472 {ECO:0000244|PDB:1P3D}. SQ SEQUENCE 475 AA; 51994 MW; 5748EDD753D6F8D3 CRC64; MKHSHEEIRK IIPEMRRVQQ IHFIGIGGAG MSGIAEILLN EGYQISGSDI ADGVVTQRLA QAGAKIYIGH AEEHIEGASV VVVSSAIKDD NPELVTSKQK RIPVIQRAQM LAEIMRFRHG IAVAGTHGKT TTTAMISMIY TQAKLDPTFV NGGLVKSAGK NAHLGASRYL IAEADESDAS FLHLQPMVSV VTNMEPDHMD TYEGDFEKMK ATYVKFLHNL PFYGLAVMCA DDPVLMELVP KVGRQVITYG FSEQADYRIE DYEQTGFQGH YTVICPNNER INVLLNVPGK HNALNATAAL AVAKEEGIAN EAILEALADF QGAGRRFDQL GEFIRPNGKV RLVDDYGHHP TEVGVTIKAA REGWGDKRIV MIFQPHRYSR TRDLFDDFVQ VLSQVDALIM LDVYAAGEAP IVGADSKSLC RSIRNLGKVD PILVSDTSQL GDVLDQIIQD GDLILAQGAG SVSKISRGLA ESWKN // ID MURI_HAEIN Reviewed; 269 AA. AC P52973; O86245; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 16-MAR-2016, entry version 109. DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258}; DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258}; GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; GN OrderedLocusNames=HI_1739.2; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RX PubMed=8805245; DOI=10.1016/S0960-9822(02)00478-5; RA Tatusov R.L., Mushegian A.R., Bork P., Brown N.P., Hayes W.S., RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Metabolism and evolution of Haemophilus influenzae deduced from a RT whole-genome comparison with Escherichia coli."; RL Curr. Biol. 6:279-291(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}. CC -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_00258}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00258}. CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family. CC {ECO:0000255|HAMAP-Rule:MF_00258}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23386.1; -; Genomic_DNA. DR PIR; T09430; T09430. DR RefSeq; NP_439883.1; NC_000907.1. DR RefSeq; WP_010869285.1; NC_000907.1. DR ProteinModelPortal; P52973; -. DR STRING; 71421.HI1739.2; -. DR EnsemblBacteria; AAC23386; AAC23386; HI_1739.2. DR GeneID; 950882; -. DR KEGG; hin:HI1739.2; -. DR PATRIC; 20192249; VBIHaeInf48452_1822. DR eggNOG; ENOG4105F03; Bacteria. DR eggNOG; COG0796; LUCA. DR KO; K01776; -. DR OMA; LDFFKPH; -. DR OrthoDB; EOG6B6296; -. DR PhylomeDB; P52973; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008881; F:glutamate racemase activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1860; -; 1. DR HAMAP; MF_00258; Glu_racemase; 1. DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase. DR InterPro; IPR001920; Asp/Glu_race. DR InterPro; IPR018187; Asp/Glu_racemase_AS_1. DR InterPro; IPR033134; Asp/Glu_racemase_AS_2. DR InterPro; IPR004391; Glu_race. DR Pfam; PF01177; Asp_Glu_race; 1. DR SUPFAM; SSF53681; SSF53681; 2. DR TIGRFAMs; TIGR00067; glut_race; 1. DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1. DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Isomerase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 269 Glutamate racemase. FT /FTId=PRO_0000095475. FT REGION 14 15 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 46 47 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 79 80 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 190 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT ACT_SITE 78 78 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. FT ACT_SITE 189 189 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. SQ SEQUENCE 269 AA; 30535 MW; F64A6E741154CC0D CRC64; MDKKEKRPTV LFFDSGVGGF SVYREAKKLL PNWHYLYCFD NAGFPYSERK EESIIHRTLA ACQLINQRYP LDAMVIACNT ASTVVLPPLR AAFDIPIIGT VPAIKPASEI TKTKHIGLLA TKGTVKRHYI DELIDKFAQD CIVERLGTTK LVEIAEQKIR GHSVDLISLK DELSSWAGMA DLDTLVLGCT HFPLIKDEIQ LCLPQVKYFM EPSAAIAKRI KYLLDDKNLQ AQNEKYNQMF CTAHFPEESQ FKKALHLWGF ESLEVIKID // ID MUTH_HAEIN Reviewed; 223 AA. AC P44688; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=DNA mismatch repair protein MutH {ECO:0000255|HAMAP-Rule:MF_00759}; DE AltName: Full=Methyl-directed mismatch repair protein {ECO:0000255|HAMAP-Rule:MF_00759}; GN Name=mutH {ECO:0000255|HAMAP-Rule:MF_00759}; GN OrderedLocusNames=HI_0403; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Sequence-specific endonuclease that cleaves unmethylated CC GATC sequences. It is involved in DNA mismatch repair. CC {ECO:0000255|HAMAP-Rule:MF_00759}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00759}. CC -!- SIMILARITY: Belongs to the MutH family. {ECO:0000255|HAMAP- CC Rule:MF_00759}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22062.1; -; Genomic_DNA. DR PIR; H64065; H64065. DR RefSeq; NP_438565.1; NC_000907.1. DR RefSeq; WP_005693765.1; NC_000907.1. DR PDB; 2AOQ; X-ray; 2.20 A; A=1-223. DR PDB; 2AOR; X-ray; 2.00 A; A/B=1-223. DR PDBsum; 2AOQ; -. DR PDBsum; 2AOR; -. DR ProteinModelPortal; P44688; -. DR SMR; P44688; 1-221. DR STRING; 71421.HI0403; -. DR EnsemblBacteria; AAC22062; AAC22062; HI_0403. DR GeneID; 949640; -. DR KEGG; hin:HI0403; -. DR PATRIC; 20189357; VBIHaeInf48452_0422. DR eggNOG; ENOG4105IRT; Bacteria. DR eggNOG; COG3066; LUCA. DR KO; K03573; -. DR OMA; VMQLRPK; -. DR OrthoDB; EOG6CGCC0; -. DR PhylomeDB; P44688; -. DR EvolutionaryTrace; P44688; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.600.10; -; 1. DR HAMAP; MF_00759; MutH; 1. DR InterPro; IPR004230; DNA_mismatch_repair_MutH. DR InterPro; IPR011337; DNA_rep_MutH/RE_typeII. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF02976; MutH; 1. DR SMART; SM00927; MutH; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR02248; mutH_TIGR; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; KW Endonuclease; Hydrolase; Nuclease; Reference proteome. FT CHAIN 1 223 DNA mismatch repair protein MutH. FT /FTId=PRO_0000198669. FT HELIX 6 16 {ECO:0000244|PDB:2AOR}. FT HELIX 21 27 {ECO:0000244|PDB:2AOR}. FT HELIX 42 51 {ECO:0000244|PDB:2AOR}. FT STRAND 59 61 {ECO:0000244|PDB:2AOR}. FT TURN 64 67 {ECO:0000244|PDB:2AOR}. FT STRAND 68 75 {ECO:0000244|PDB:2AOR}. FT STRAND 81 83 {ECO:0000244|PDB:2AOR}. FT STRAND 85 89 {ECO:0000244|PDB:2AOR}. FT HELIX 100 102 {ECO:0000244|PDB:2AOQ}. FT HELIX 104 109 {ECO:0000244|PDB:2AOR}. FT STRAND 110 118 {ECO:0000244|PDB:2AOR}. FT HELIX 125 127 {ECO:0000244|PDB:2AOR}. FT STRAND 134 136 {ECO:0000244|PDB:2AOR}. FT HELIX 140 158 {ECO:0000244|PDB:2AOR}. FT HELIX 162 164 {ECO:0000244|PDB:2AOR}. FT STRAND 171 177 {ECO:0000244|PDB:2AOR}. FT STRAND 179 181 {ECO:0000244|PDB:2AOR}. FT STRAND 186 189 {ECO:0000244|PDB:2AOR}. FT STRAND 195 198 {ECO:0000244|PDB:2AOR}. FT STRAND 201 205 {ECO:0000244|PDB:2AOR}. FT HELIX 207 218 {ECO:0000244|PDB:2AOR}. SQ SEQUENCE 223 AA; 24906 MW; 339A4EF9DA0E622A CRC64; MIPQTLEQLL SQAQSIAGLT FGELADELHI PVPIDLKRDK GWVGMLLERA LGATAGSKAE QDFSHLGVEL KTLPINAEGY PLETTFVSLA PLVQNSGVKW ENSHVRHKLS CVLWMPIEGS RHIPLRERHI GAPIFWKPTA EQERQLKQDW EELMDLIVLG KLDQITARIG EVMQLRPKGA NSRAVTKGIG KNGEIIDTLP LGFYLRKEFT AQILNAFLET KSL // ID NAGB_HAEIN Reviewed; 270 AA. AC P44538; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Glucosamine-6-phosphate deaminase; DE EC=3.5.99.6; DE AltName: Full=GlcN6P deaminase; DE Short=GNPDA; DE AltName: Full=Glucosamine-6-phosphate isomerase; GN Name=nagB; OrderedLocusNames=HI_0141; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate CC (Fru6P) and ammonium ion. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D- CC fructose 6-phosphate + NH(3). CC -!- ENZYME REGULATION: Allosterically activated by N-acetylglucosamine CC 6-phosphate (GlcNAc6P). {ECO:0000250}. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; CC D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. NagB 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; L42023; AAC21813.1; -; Genomic_DNA. DR PIR; F64050; F64050. DR RefSeq; NP_438310.1; NC_000907.1. DR RefSeq; WP_005668148.1; NC_000907.1. DR ProteinModelPortal; P44538; -. DR SMR; P44538; 1-260. DR STRING; 71421.HI0141; -. DR EnsemblBacteria; AAC21813; AAC21813; HI_0141. DR GeneID; 951053; -. DR KEGG; hin:HI0141; -. DR PATRIC; 20188773; VBIHaeInf48452_0143. DR eggNOG; ENOG4105CKA; Bacteria. DR eggNOG; COG0363; LUCA. DR KO; K02564; -. DR OMA; FFDNDMS; -. DR OrthoDB; EOG6WX4S3; -. DR PhylomeDB; P44538; -. DR UniPathway; UPA00629; UER00684. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-EC. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01241; GlcN6P_deamin; 1. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR004547; Glucosamine6P_isomerase. DR InterPro; IPR018321; Glucosamine6P_isomerase_CS. DR PANTHER; PTHR11280; PTHR11280; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR00502; nagB; 1. DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Carbohydrate metabolism; Complete proteome; KW Hydrolase; Reference proteome. FT CHAIN 1 270 Glucosamine-6-phosphate deaminase. FT /FTId=PRO_0000160149. FT ACT_SITE 72 72 Proton acceptor; for enolization step. FT {ECO:0000250}. FT ACT_SITE 141 141 For ring-opening step. {ECO:0000250}. FT ACT_SITE 143 143 Proton acceptor; for ring-opening step. FT {ECO:0000250}. FT ACT_SITE 148 148 For ring-opening step. {ECO:0000250}. FT SITE 151 151 Part of the allosteric site. FT {ECO:0000250}. FT SITE 158 158 Part of the allosteric site. FT {ECO:0000250}. FT SITE 160 160 Part of the allosteric site. FT {ECO:0000250}. FT SITE 161 161 Part of the allosteric site. FT {ECO:0000250}. FT SITE 254 254 Part of the allosteric site. FT {ECO:0000250}. SQ SEQUENCE 270 AA; 30501 MW; D06C651C1A41C235 CRC64; MRFIPLQTEQ QVSCWAAQHI INRINDFKPT AERPFVLGLP TGGTPLKTYQ ELIRLYQAGK VSFKHVVTFN MDEYVALPEE HPESYHSFMY NNFFNHIDIL PENINILNGN TDDHNAECRR YEEKIKSYGK IHLFMGGVGV DGHIAFNEPA SSLSSRTRIK TLTQDTLIAN SRFFNNDVTQ VPKYALTIGV GTLLDAEEVM ILATGHQKAL AVQAAVEGSI NHLWTVSALQ MHRHFLLVCD EAAQQELKVK TVKYFTELEG AVAGTDYQDK // ID NAPC_HAEIN Reviewed; 200 AA. AC P44655; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Cytochrome c-type protein NapC; GN Name=napC; OrderedLocusNames=HI_0348; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Mediates electron flow from quinones to the NapAB CC complex. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane CC protein. CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22009.1; -; Genomic_DNA. DR PIR; H64062; H64062. DR RefSeq; NP_438512.1; NC_000907.1. DR RefSeq; WP_010868977.1; NC_000907.1. DR ProteinModelPortal; P44655; -. DR STRING; 71421.HI0348; -. DR DNASU; 949803; -. DR EnsemblBacteria; AAC22009; AAC22009; HI_0348. DR GeneID; 949803; -. DR KEGG; hin:HI0348; -. DR PATRIC; 20189243; VBIHaeInf48452_0367. DR eggNOG; ENOG4105CUW; Bacteria. DR eggNOG; COG3005; LUCA. DR KO; K02569; -. DR OMA; CTGCHEM; -. DR OrthoDB; EOG6RNQDS; -. DR PhylomeDB; P44655; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central. DR GO; GO:0019333; P:denitrification pathway; IEA:InterPro. DR InterPro; IPR011031; Multihaem_cyt. DR InterPro; IPR024717; NapC/NirT/NrfH. DR InterPro; IPR005126; NapC/NirT_cyt_c_N. DR InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT. DR Pfam; PF03264; Cytochrom_NNT; 1. DR PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1. DR SUPFAM; SSF48695; SSF48695; 1. DR TIGRFAMs; TIGR02161; napC_nirT; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Heme; Iron; Membrane; Metal-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 200 Cytochrome c-type protein NapC. FT /FTId=PRO_0000108435. FT TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TOPO_DOM 43 200 Periplasmic. {ECO:0000255}. FT METAL 59 59 Iron (heme 1 axial ligand). FT {ECO:0000250}. FT METAL 87 87 Iron (heme 2 axial ligand). FT {ECO:0000250}. FT METAL 147 147 Iron (heme 3 axial ligand). FT {ECO:0000250}. FT METAL 179 179 Iron (heme 4 axial ligand). FT {ECO:0000250}. FT BINDING 55 55 Heme 1 (covalent). {ECO:0000250}. FT BINDING 58 58 Heme 1 (covalent). {ECO:0000250}. FT BINDING 83 83 Heme 2 (covalent). {ECO:0000250}. FT BINDING 86 86 Heme 2 (covalent). {ECO:0000250}. FT BINDING 143 143 Heme 3 (covalent). {ECO:0000250}. FT BINDING 146 146 Heme 3 (covalent). {ECO:0000250}. FT BINDING 175 175 Heme 4 (covalent). {ECO:0000250}. FT BINDING 178 178 Heme 4 (covalent). {ECO:0000250}. SQ SEQUENCE 200 AA; 22957 MW; 6B6434D8B882D922 CRC64; MSEKKPNILK RFWQWFRKPS RMAIGTIIIL SAIGGILSWV GFNYGLEKTN TEQFCASCHM QDAYPEYLHS VHYQTRTGVG ASCPDCHVPH EFGAKMKRKI IAAKEVYAHY TGKVDTLEKF NAHRLEMAQN EWARMKANDS KECRNCHNVD RMTFNDQRSV AARMHQKMKT EGKTCIDCHK GIAHQLPDMS GVESGFKDEK // ID NAPH_HAEIN Reviewed; 287 AA. AC P44653; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=Ferredoxin-type protein NapH homolog; GN Name=napH; OrderedLocusNames=HI_0346; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in electron transfer. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22007.1; -; Genomic_DNA. DR PIR; B64149; B64149. DR RefSeq; NP_438510.1; NC_000907.1. DR RefSeq; WP_005694327.1; NC_000907.1. DR ProteinModelPortal; P44653; -. DR STRING; 71421.HI0346; -. DR EnsemblBacteria; AAC22007; AAC22007; HI_0346. DR GeneID; 949454; -. DR KEGG; hin:HI0346; -. DR PATRIC; 20189239; VBIHaeInf48452_0365. DR eggNOG; ENOG4105GXZ; Bacteria. DR eggNOG; COG0348; LUCA. DR KO; K02574; -. DR OMA; CIDACEP; -. DR OrthoDB; EOG6G7R1W; -. DR PhylomeDB; P44653; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR011886; NapH_MauN. DR Pfam; PF12801; Fer4_5; 2. DR Pfam; PF12837; Fer4_6; 1. DR TIGRFAMs; TIGR02163; napH_; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 287 Ferredoxin-type protein NapH homolog. FT /FTId=PRO_0000159284. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT DOMAIN 217 247 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 252 281 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 226 226 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 229 229 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 232 232 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 236 236 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 261 261 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 264 264 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 267 267 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 271 271 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 287 AA; 31753 MW; D2E20FC4E3C3C197 CRC64; MANAPKFAGK ESREKWGWWY ANRFLFWRRL SQLSILAMFL SGPYFGVWIL KGNYSGSLLL DTIPLSDPLI TAESLAARHL PDALTLIGAA IIVLFYAVLG SKVFCGWVCP LNVVTDCAAW LRRKLGIRQT AKISRGLRYG ILVLILLGSS VSGMLLWEWV NPVAALGRAF VFGFGATGWL LLVIFLFDLL IAEHGWCGHL CPIGAAYGVI GAKSLIRIKV IDRAKCDNCM DCYNVCPEAQ VLRSPLHGKK DESLLVLSKD CISCGRCIDV CAEKVFKFST RFDHSGE // ID MURE_HAEIN Reviewed; 488 AA. AC P45060; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 121. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; GN OrderedLocusNames=HI_1133; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl- CC D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + CC UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6- CC diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22788.1; -; Genomic_DNA. DR PIR; H64184; H64184. DR RefSeq; NP_439291.1; NC_000907.1. DR RefSeq; WP_005693448.1; NC_000907.1. DR ProteinModelPortal; P45060; -. DR SMR; P45060; 15-487. DR STRING; 71421.HI1133; -. DR EnsemblBacteria; AAC22788; AAC22788; HI_1133. DR GeneID; 949983; -. DR KEGG; hin:HI1133; -. DR PATRIC; 20190941; VBIHaeInf48452_1183. DR eggNOG; ENOG4107EEN; Bacteria. DR eggNOG; COG0769; LUCA. DR KO; K01928; -. DR OMA; HNHNIKF; -. DR OrthoDB; EOG6PKFCR; -. DR PhylomeDB; P45060; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.40.1390.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00208; MurE; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR SUPFAM; SSF63418; SSF63418; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Nucleotide-binding; Peptidoglycan synthesis; KW Reference proteome. FT CHAIN 1 488 UDP-N-acetylmuramoyl-L-alanyl-D- FT glutamate--2,6-diaminopimelate ligase. FT /FTId=PRO_0000101900. FT NP_BIND 113 119 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 41 43 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 155 156 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT REGION 410 413 Meso-diaminopimelate binding. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT MOTIF 410 413 Meso-diaminopimelate recognition motif. FT BINDING 24 24 UDP-MurNAc-L-Ala-D-Glu; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 26 26 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 154 154 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 182 182 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 188 188 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 190 190 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000255|HAMAP-Rule:MF_00208}. FT BINDING 386 386 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 461 461 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT BINDING 465 465 Meso-diaminopimelate. {ECO:0000255|HAMAP- FT Rule:MF_00208}. FT MOD_RES 222 222 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 488 AA; 53523 MW; 46E20FF7491BC45A CRC64; MKKLTALFNL PELKNDIELH NMVLDSRKVK AGDLFVAIKG HQVDGNQFID SALHSGASAV VSETELSSEH LTVAFIGNVP VVKYYQLAHH LSSLADVFYD SPSNNLTLVG VTGTNGKTTI SQLLAQWAEL LGHRAAVMGT IGNGLFGQIV EAKNTTGSAV EIQSSLSAFK HAGADFTSIE VSSHGLAQHR VEALHFKAAI FTNLTRDHLD YHQSMENYAA AKKRLFTELD TQIKVINADD EIGYQWLTEL PDAIAVSMNA DFKVGSHQWM KAINIHYHFK GADITFESSW GNGVLHSPLI GAFNVSNLLL VMTTLLSFGY PLENLLATAK SLKGVCGRME MIQYPNKPTV IVDYAHTPDA LEKALIAARE HCQGELWCIF GCGGDRDRGK RPLMAQVAEQ FAEKIIVTKD NPRTESQSQI ETDIVAGFKN MEKVGIIPDR AQAIQFAIES AVENDVILIA GKGHEHYQII GSEVVHFSDQ EIALDFLK // ID MURG_HAEIN Reviewed; 351 AA. AC P45065; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 123. DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033}; DE EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033}; DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033}; GN Name=murG {ECO:0000255|HAMAP-Rule:MF_00033}; GN OrderedLocusNames=HI_1138; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc CC subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid CC intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- CC (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala- CC gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + CC GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphosphoundecaprenol. {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00033}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22793.1; -; Genomic_DNA. DR PIR; D64185; D64185. DR RefSeq; NP_439296.1; NC_000907.1. DR RefSeq; WP_005693451.1; NC_000907.1. DR ProteinModelPortal; P45065; -. DR SMR; P45065; 4-348. DR STRING; 71421.HI1138; -. DR CAZy; GT28; Glycosyltransferase Family 28. DR EnsemblBacteria; AAC22793; AAC22793; HI_1138. DR GeneID; 949484; -. DR KEGG; hin:HI1138; -. DR PATRIC; 20190951; VBIHaeInf48452_1188. DR eggNOG; ENOG4105DVQ; Bacteria. DR eggNOG; COG0707; LUCA. DR KO; K02563; -. DR OMA; EQNALPG; -. DR OrthoDB; EOG61VZFD; -. DR PhylomeDB; P45065; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0030259; P:lipid glycosylation; IEA:UniProtKB-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00033; MurG; 1. DR InterPro; IPR006009; GlcNAc_MurG. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR004276; GlycoTrans_28_N. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR Pfam; PF03033; Glyco_transf_28; 1. DR TIGRFAMs; TIGR01133; murG; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase. FT CHAIN 1 351 UDP-N-acetylglucosamine--N-acetylmuramyl- FT (pentapeptide) pyrophosphoryl- FT undecaprenol N-acetylglucosamine FT transferase. FT /FTId=PRO_0000109177. SQ SEQUENCE 351 AA; 38307 MW; 41067F379BB30B27 CRC64; MKNKKLLVMA GGTGGHVFPA IAVAQTLQKQ EWDICWLGTK DRMEAQLVPK YGIPIRFIQI SGLRGKGIKA LLNAPFAIFR AVLQAKKIIQ EEKPDAVLGM GGYVSGPAGV AAKLCGVPII LHEQNAIAGL TNKLLGKIAT CVLQAFPTAF PHAEVVGNPV REDLFEMPNP DIRFSDREEK LRVLVVGGSQ GARVLNHTLP KVVAQLADKL EFRHQVGKGA VEEVSQLYGE NLEQVKITEF IDNMAEAYAW ADVVICRSGA LTVCEIAAVG AAAIFVPFQH KDRQQYLNAK YLSDVGAAKI IEQADLTPEI LVNYLKNLTR ENLLQMALKA KTMSMPNAAQ RVAEVIKQYS N // ID MUTY_HAEIN Reviewed; 378 AA. AC P44320; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 113. DE RecName: Full=Adenine DNA glycosylase; DE EC=3.2.2.-; GN Name=mutY; OrderedLocusNames=HI_0759; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Adenine glycosylase active on G-A and C-A mispairs. CC {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play CC a role in catalysis, but is probably involved in the proper CC positioning of the enzyme along the DNA strand. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the Nth/MutY 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; L42023; AAC22418.1; -; Genomic_DNA. DR PIR; C64091; C64091. DR RefSeq; NP_438918.1; NC_000907.1. DR RefSeq; WP_005693157.1; NC_000907.1. DR ProteinModelPortal; P44320; -. DR SMR; P44320; 11-230. DR STRING; 71421.HI0759; -. DR EnsemblBacteria; AAC22418; AAC22418; HI_0759. DR GeneID; 950824; -. DR KEGG; hin:HI0759; -. DR PATRIC; 20190165; VBIHaeInf48452_0798. DR eggNOG; ENOG4105CEN; Bacteria. DR eggNOG; COG1194; LUCA. DR KO; K03575; -. DR OMA; EADWLWY; -. DR OrthoDB; EOG6RNQH0; -. DR PhylomeDB; P44320; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR005760; A/G_AdeGlyc_MutY. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR029119; MutY_C. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF14815; NUDIX_4; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR01084; mutY; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Iron; Iron-sulfur; Metal-binding; Reference proteome. FT CHAIN 1 378 Adenine DNA glycosylase. FT /FTId=PRO_0000102236. FT ACT_SITE 42 42 Proton donor/acceptor. FT {ECO:0000250|UniProtKB:P83847}. FT METAL 197 197 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 204 204 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 207 207 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 213 213 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT SITE 143 143 Transition state stabilizer. FT {ECO:0000250|UniProtKB:P83847}. SQ SEQUENCE 378 AA; 43505 MW; C443F625131B2A21 CRC64; MLAKSSINAP FAKSVLAWYD KFGRKHLPWQ QNKTLYGVWL SEVMLQQTQV ATVIPYFERF IKTFPNITAL ANASQDEVLH LWTGLGYYAR ARNLHKAAQK VRDEFNGNFP TNFEQVWALS GVGRSTAGAI LSSVLNQPYP ILDGNVKRVL ARYFAVEGWS GEKKVENRLW ALTEQVTPTT RVADFNQAMM DIGAMVCMRT KPKCDLCPLN IDCLAYKNTN WEKFPAKKPK KAMPEKTTYF LILSKNGKVC LEQRENSGLW GGLFCFPQFE DKSSLLHFLA QEKVTHYQEW PSFRHTFSHF HLDIHPIYAE MESTLCVEQA NLDWRKVMES TKEYQSNLSS AVKYWYDPQN PEPIGLAQPV KNLLIQFVRN HYGKNSIL // ID NADK_HAEIN Reviewed; 285 AA. AC P44497; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 04-MAY-2001, sequence version 3. DT 11-MAY-2016, entry version 108. 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}; GN OrderedLocusNames=HI_0072; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC21749.1; 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; L42023; AAC21749.1; ALT_INIT; Genomic_DNA. DR PIR; I64141; I64141. DR RefSeq; NP_438244.1; NC_000907.1. DR ProteinModelPortal; P44497; -. DR SMR; P44497; 7-278. DR STRING; 71421.HI0072; -. DR EnsemblBacteria; AAC21749; AAC21749; HI_0072. DR GeneID; 950969; -. DR KEGG; hin:HI0072; -. DR PATRIC; 20188597; VBIHaeInf48452_0072. DR eggNOG; ENOG4105F91; Bacteria. DR eggNOG; COG0061; LUCA. DR KO; K00858; -. DR OMA; SAYRENT; -. DR OrthoDB; EOG6PZXDR; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 1. DR HAMAP; MF_00361; NAD_kinase; 1. DR InterPro; IPR017438; ATP-NAD_kinase_dom_1. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b. DR InterPro; IPR016064; NAD/diacylglycerol_kinase. DR InterPro; IPR002504; NADK. DR PANTHER; PTHR20275; PTHR20275; 1. DR Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 285 NAD kinase. FT /FTId=PRO_0000120622. FT NP_BIND 76 77 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 151 152 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 192 197 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT ACT_SITE 76 76 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT BINDING 162 162 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 179 179 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 181 181 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 252 252 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. SQ SEQUENCE 285 AA; 31828 MW; D49647085A2025AB CRC64; MNHLYRSFKT IALVGKPRND INLQMHKNLF HWLMERGYQV LVEKEVAITL ELPFEHLATL EEIGHRAQLA IVIGGDGNML GRARVLAKYD IPLIGINRGN LGFLTDIDPK NAYSQLEACL ERGEFFVEER FLLEAKIERA SEIVSTSNAV NEAVIHPAKI AHMIDFHVYI NDKFAFSQRS DGLIVSTPTG STAYSLSAGG PILTPNLNAI ALVPMFPHTL TSRPLVVDGD SKISIRFAEH NTSQLEVGCD SQITLPFTPD DVVHIQKSEH KLRLLHLKII IITMC // ID NADR_HAEIN Reviewed; 421 AA. AC P44308; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 113. DE RecName: Full=Bifunctional NAD biosynthesis protein NadR; DE Includes: DE RecName: Full=Nicotinamide mononucleotide adenylyltransferase; DE Short=NMN adenylyltransferase; DE Short=NMN-AT; DE Short=NMNAT; DE EC=2.7.7.1; DE AltName: Full=Nicotinamide ribonucleotide adenylyltransferase; DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase; DE Includes: DE RecName: Full=Ribosylnicotinamide kinase; DE Short=RNK; DE EC=2.7.1.22; DE AltName: Full=Nicotinamide riboside kinase; DE Short=NRK; DE Short=NmR-K; GN Name=nadR; OrderedLocusNames=HI_0763; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=12446641; DOI=10.1128/JB.184.24.6906-6917.2002; RA Kurnasov O.V., Polanuyer B.M., Ananta S., Sloutsky R., Tam A., RA Gerdes S.Y., Osterman A.L.; RT "Ribosylnicotinamide kinase domain of NadR protein: identification and RT implications in NAD biosynthesis."; RL J. Bacteriol. 184:6906-6917(2002). RN [3] RP MUTAGENESIS OF LYS-126; GLY-238; TRP-256; TYR-292; ASP-304 AND RP ARG-352, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15968050; DOI=10.1128/JB.187.13.4410-4420.2005; RA Merdanovic M., Sauer E., Reidl J.; RT "Coupling of NAD+ biosynthesis and nicotinamide ribosyl transport: RT characterization of NadR ribonucleotide kinase mutants of Haemophilus RT influenzae."; RL J. Bacteriol. 187:4410-4420(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 57-421 IN COMPLEX WITH NAD, RP AND SUBUNIT. RX PubMed=12068016; DOI=10.1074/jbc.M204368200; RA Singh S.K., Kurnasov O.V., Chen B., Robinson H., Grishin N.V., RA Osterman A.L., Zhang H.; RT "Crystal structure of Haemophilus influenzae NadR protein. A RT bifunctional enzyme endowed with NMN adenyltransferase and RT ribosylnicotinimide kinase activities."; RL J. Biol. Chem. 277:33291-33299(2002). CC -!- FUNCTION: This enzyme has two activities: nicotinamide CC mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide CC (RN) kinase. The RN kinase activity catalyzes the phosphorylation CC of RN to form nicotinamide ribonucleotide. The NMN CC adenylyltransferase activity catalyzes the transfer of the AMP CC moiety of ATP to nicotinamide ribonucleotide to form NAD(+). CC {ECO:0000269|PubMed:12446641}. CC -!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide = CC diphosphate + NAD(+). {ECO:0000269|PubMed:12446641}. CC -!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = CC ADP + beta-nicotinamide D-ribonucleotide. CC {ECO:0000269|PubMed:12446641}. CC -!- ENZYME REGULATION: Feed-back regulated by NAD. At high levels of CC NAD the RN kinase activity is inhibited. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.14 mM for NMN {ECO:0000269|PubMed:12446641}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis [regulation]. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC nicotinamide D-ribonucleotide: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12068016}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15968050}; CC Peripheral membrane protein {ECO:0000269|PubMed:15968050}. CC Cytoplasm {ECO:0000269|PubMed:15968050}. Note=Found as a soluble CC cytoplasmic protein as well as a membrane-associated protein. In CC combination with corepressor (NAD), the cytoplasmic form of NadR CC would be capable of acting as a transcriptional repressor. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P44308-1; Sequence=Displayed; CC Name=Short; CC IsoId=P44308-2; Sequence=VSP_040071; CC Note=Shows the same catalytic activity as isoform Long.; CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial CC NMN adenylyltransferase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the bacterial CC RNK 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; L42023; AAC22421.1; -; Genomic_DNA. DR PIR; D64091; D64091. DR RefSeq; NP_438922.1; NC_000907.1. [P44308-1] DR RefSeq; WP_005690353.1; NC_000907.1. DR PDB; 1LW7; X-ray; 2.90 A; A=57-421. DR PDBsum; 1LW7; -. DR ProteinModelPortal; P44308; -. DR SMR; P44308; 57-411. DR STRING; 71421.HI0763; -. DR TCDB; 4.B.1.1.2; the nicotinamide ribonucleoside (nr) uptake permease (pnuc) family. DR EnsemblBacteria; AAC22421; AAC22421; HI_0763. DR GeneID; 950800; -. DR KEGG; hin:HI0763; -. DR PATRIC; 20190177; VBIHaeInf48452_0802. DR eggNOG; ENOG4107VZS; Bacteria. DR eggNOG; COG1056; LUCA. DR eggNOG; COG3172; LUCA. DR KO; K06211; -. DR OMA; TAIRQKG; -. DR OrthoDB; EOG6P06X5; -. DR PhylomeDB; P44308; -. DR BioCyc; MetaCyc:MONOMER-8322; -. DR UniPathway; UPA00253; UER00600. DR UniPathway; UPA00253; -. DR EvolutionaryTrace; P44308; -. DR Proteomes; UP000000579; 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-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR016429; Bifunc_transcrip_reg_NadR. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR006417; NadR_NMN_Atrans. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR PIRSF; PIRSF004776; NadR_NMNAT/RNK; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. DR TIGRFAMs; TIGR01526; nadR_NMN_Atrans; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; ATP-binding; Cell membrane; KW Complete proteome; Cytoplasm; Kinase; Membrane; KW Multifunctional enzyme; NAD; Nucleotide-binding; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 421 Bifunctional NAD biosynthesis protein FT NadR. FT /FTId=PRO_0000096689. FT NP_BIND 64 67 NAD 1. {ECO:0000269|PubMed:12068016}. FT NP_BIND 139 152 NAD 1. {ECO:0000269|PubMed:12068016}. FT NP_BIND 172 174 NAD 1. {ECO:0000269|PubMed:12068016}. FT NP_BIND 199 201 NAD 1. {ECO:0000269|PubMed:12068016}. FT NP_BIND 254 256 NAD 2. {ECO:0000269|PubMed:12068016}. FT NP_BIND 289 292 NAD 2. {ECO:0000269|PubMed:12068016}. FT REGION 57 224 Nicotinamide mononucleotide FT adenylyltransferase. FT REGION 225 421 Ribosylnicotinamide kinase. FT BINDING 71 71 NAD 1. {ECO:0000269|PubMed:12068016}. FT BINDING 98 98 NAD 1. {ECO:0000269|PubMed:12068016}. FT VAR_SEQ 1 51 Missing (in isoform Short). FT {ECO:0000305}. FT /FTId=VSP_040071. FT MUTAGEN 126 126 K->A,T: Significant reduction of RNK FT activity, also NMN adenylyltransferase FT activity is impaired. FT {ECO:0000269|PubMed:15968050}. FT MUTAGEN 238 238 G->N,S: Complete loss of RNK activity, no FT effect on NMN adenylyltransferase FT activity. {ECO:0000269|PubMed:15968050}. FT MUTAGEN 256 256 W->F: No effect on enzyme activities, but FT NAD feedback inhibition is almost lost. FT {ECO:0000269|PubMed:15968050}. FT MUTAGEN 292 292 Y->I: Almost no effect. FT {ECO:0000269|PubMed:15968050}. FT MUTAGEN 304 304 D->C,N,S: Complete loss of RNK activity, FT no effect on NMN adenylyltransferase FT activity. {ECO:0000269|PubMed:15968050}. FT MUTAGEN 352 352 R->A,C,M,N: Complete loss of RNK FT activity, no effect on NMN FT adenylyltransferase activity. FT {ECO:0000269|PubMed:15968050}. FT STRAND 60 65 {ECO:0000244|PDB:1LW7}. FT HELIX 72 82 {ECO:0000244|PDB:1LW7}. FT STRAND 86 94 {ECO:0000244|PDB:1LW7}. FT HELIX 96 105 {ECO:0000244|PDB:1LW7}. FT HELIX 114 124 {ECO:0000244|PDB:1LW7}. FT TURN 127 131 {ECO:0000244|PDB:1LW7}. FT STRAND 132 138 {ECO:0000244|PDB:1LW7}. FT STRAND 140 142 {ECO:0000244|PDB:1LW7}. FT HELIX 149 162 {ECO:0000244|PDB:1LW7}. FT STRAND 168 171 {ECO:0000244|PDB:1LW7}. FT HELIX 175 177 {ECO:0000244|PDB:1LW7}. FT HELIX 178 184 {ECO:0000244|PDB:1LW7}. FT STRAND 188 190 {ECO:0000244|PDB:1LW7}. FT HELIX 203 208 {ECO:0000244|PDB:1LW7}. FT HELIX 210 216 {ECO:0000244|PDB:1LW7}. FT TURN 219 221 {ECO:0000244|PDB:1LW7}. FT HELIX 222 224 {ECO:0000244|PDB:1LW7}. FT STRAND 227 232 {ECO:0000244|PDB:1LW7}. FT HELIX 238 249 {ECO:0000244|PDB:1LW7}. FT STRAND 253 255 {ECO:0000244|PDB:1LW7}. FT HELIX 260 265 {ECO:0000244|PDB:1LW7}. FT STRAND 266 269 {ECO:0000244|PDB:1LW7}. FT TURN 276 278 {ECO:0000244|PDB:1LW7}. FT HELIX 279 296 {ECO:0000244|PDB:1LW7}. FT STRAND 298 305 {ECO:0000244|PDB:1LW7}. FT HELIX 307 318 {ECO:0000244|PDB:1LW7}. FT HELIX 323 331 {ECO:0000244|PDB:1LW7}. FT STRAND 335 341 {ECO:0000244|PDB:1LW7}. FT HELIX 360 372 {ECO:0000244|PDB:1LW7}. FT HELIX 373 375 {ECO:0000244|PDB:1LW7}. FT STRAND 379 382 {ECO:0000244|PDB:1LW7}. FT HELIX 386 400 {ECO:0000244|PDB:1LW7}. SQ SEQUENCE 421 AA; 49432 MW; D9A4FD4970A6E7E8 CRC64; MGFTTGREFH PALRMRAKYN AKYLGTKSER EKYFHLAYNK HTQFLRYQEQ IMSKTKEKKV GVIFGKFYPV HTGHINMIYE AFSKVDELHV IVCSDTVRDL KLFYDSKMKR MPTVQDRLRW MQQIFKYQKN QIFIHHLVED GIPSYPNGWQ SWSEAVKTLF HEKHFEPSIV FSSEPQDKAP YEKYLGLEVS LVDPDRTFFN VSATKIRTTP FQYWKFIPKE ARPFFAKTVA ILGGESSGKS VLVNKLAAVF NTTSAWEYGR EFVFEKLGGD EQAMQYSDYP QMALGHQRYI DYAVRHSHKI AFIDTDFITT QAFCIQYEGK AHPFLDSMIK EYPFDVTILL KNNTEWVDDG LRSLGSQKQR QQFQQLLKKL LDKYKVPYIE IESPSYLDRY NQVKAVIEKV LNEEEISELQ NTTFPIKGTS Q // ID NANA_HAEIN Reviewed; 293 AA. AC P44539; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=N-acetylneuraminate lyase; DE Short=NAL; DE Short=Neu5Ac lyase; DE EC=4.1.3.3; DE AltName: Full=N-acetylneuraminate pyruvate-lyase; DE AltName: Full=N-acetylneuraminic acid aldolase; DE AltName: Full=Sialate lyase; DE AltName: Full=Sialic acid aldolase; DE AltName: Full=Sialic acid lyase; GN Name=nanA; OrderedLocusNames=HI_0142; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES RP WITH SIALIC ACID ALDITOL; 4-DEOXY-SIALIC ACID AND 4-OXO-SIALIC ACID. RX PubMed=11031117; DOI=10.1006/jmbi.2000.4138; RA Barbosa J.A.R.G., Smith B.J., DeGori R., Ooi H.C., Marcuccio S.M., RA Campi E.M., Jackson W.R., Brossmer R., Sommer M., Lawrence M.C.; RT "Active site modulation in the N-acetylneuraminate lyase sub-family as RT revealed by the structure of the inhibitor-complexed Haemophilus RT influenzae enzyme."; RL J. Mol. Biol. 303:405-421(2000). CC -!- FUNCTION: Catalyzes the reversible aldol cleavage of N- CC acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and CC N-acetylmannosamine (ManNAc) via a Schiff base intermediate. CC -!- CATALYTIC ACTIVITY: N-acetylneuraminate = N-acetyl-D-mannosamine + CC pyruvate. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the DapA family. NanA 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; L42023; AAC21814.1; -; Genomic_DNA. DR PIR; G64050; G64050. DR RefSeq; NP_438311.1; NC_000907.1. DR RefSeq; WP_005694428.1; NC_000907.1. DR PDB; 1F5Z; X-ray; 1.88 A; A/B/C/D=1-293. DR PDB; 1F6K; X-ray; 1.60 A; A/C=1-293. DR PDB; 1F6P; X-ray; 2.25 A; A/B/C/D=1-293. DR PDB; 1F73; X-ray; 1.95 A; A/B/C/D=1-293. DR PDB; 1F74; X-ray; 1.60 A; A/C=1-293. DR PDB; 1F7B; X-ray; 1.80 A; A/C=1-293. DR PDBsum; 1F5Z; -. DR PDBsum; 1F6K; -. DR PDBsum; 1F6P; -. DR PDBsum; 1F73; -. DR PDBsum; 1F74; -. DR PDBsum; 1F7B; -. DR ProteinModelPortal; P44539; -. DR SMR; P44539; 1-293. DR STRING; 71421.HI0142; -. DR EnsemblBacteria; AAC21814; AAC21814; HI_0142. DR GeneID; 951045; -. DR KEGG; hin:HI0142; -. DR PATRIC; 20188775; VBIHaeInf48452_0144. DR eggNOG; ENOG4105CDP; Bacteria. DR eggNOG; COG0329; LUCA. DR KO; K01639; -. DR OMA; YWNAISA; -. DR OrthoDB; EOG6W7235; -. DR PhylomeDB; P44539; -. DR EvolutionaryTrace; P44539; -. DR PRO; PR:P44539; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01237; N_acetylneuram_lyase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR005264; NanA. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00683; nanA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Lyase; Reference proteome; Schiff base. FT CHAIN 1 293 N-acetylneuraminate lyase. FT /FTId=PRO_0000103214. FT REGION 47 48 Substrate binding. {ECO:0000250}. FT ACT_SITE 164 164 Schiff-base intermediate with substrate. FT SITE 136 136 Involved in proton transfer during FT cleavage. FT STRAND 6 10 {ECO:0000244|PDB:1F6K}. FT STRAND 19 21 {ECO:0000244|PDB:1F7B}. FT HELIX 23 35 {ECO:0000244|PDB:1F6K}. FT STRAND 40 46 {ECO:0000244|PDB:1F6K}. FT HELIX 47 49 {ECO:0000244|PDB:1F6K}. FT HELIX 51 53 {ECO:0000244|PDB:1F6K}. FT HELIX 56 70 {ECO:0000244|PDB:1F6K}. FT STRAND 73 79 {ECO:0000244|PDB:1F6K}. FT HELIX 85 98 {ECO:0000244|PDB:1F6K}. FT STRAND 101 106 {ECO:0000244|PDB:1F6K}. FT HELIX 115 129 {ECO:0000244|PDB:1F6K}. FT STRAND 133 137 {ECO:0000244|PDB:1F6K}. FT HELIX 139 142 {ECO:0000244|PDB:1F6K}. FT HELIX 148 155 {ECO:0000244|PDB:1F6K}. FT STRAND 160 165 {ECO:0000244|PDB:1F6K}. FT HELIX 170 179 {ECO:0000244|PDB:1F6K}. FT STRAND 183 187 {ECO:0000244|PDB:1F6K}. FT HELIX 190 192 {ECO:0000244|PDB:1F6K}. FT HELIX 193 198 {ECO:0000244|PDB:1F6K}. FT STRAND 202 207 {ECO:0000244|PDB:1F6K}. FT HELIX 209 224 {ECO:0000244|PDB:1F6K}. FT HELIX 228 248 {ECO:0000244|PDB:1F6K}. FT HELIX 250 260 {ECO:0000244|PDB:1F6K}. FT HELIX 278 291 {ECO:0000244|PDB:1F6K}. SQ SEQUENCE 293 AA; 32565 MW; ACA755D0A5D93D33 CRC64; MRDLKGIFSA LLVSFNEDGT INEKGLRQII RHNIDKMKVD GLYVGGSTGE NFMLSTEEKK EIFRIAKDEA KDQIALIAQV GSVNLKEAVE LGKYATELGY DCLSAVTPFY YKFSFPEIKH YYDTIIAETG NNMIVYSIPF LTGVNMGIEQ FGELYKNPKV LGVKFTAGDF YLLERLKKAY PNHLIWAGFD EMMLPAASLG VDGAIGSTFN VNGVRARQIF ELTKAGKLAE ALEIQHVTND LIEGILANGL YLTIKELLKL EGVDAGYCRE PMTSKATEEQ LAKAKDLKAK FLS // ID NANK_HAEIN Reviewed; 300 AA. AC P44541; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=N-acetylmannosamine kinase; DE EC=2.7.1.60; DE AltName: Full=ManNAc kinase; DE AltName: Full=N-acetyl-D-mannosamine kinase; GN Name=nanK; OrderedLocusNames=HI_0144; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine CC (ManNAc) to ManNAc-6-P. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D- CC mannosamine 6-phosphate. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; CC D-fructose 6-phosphate from N-acetylneuraminate: step 2/5. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK 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; L42023; AAC21816.1; -; Genomic_DNA. DR PIR; H64050; H64050. DR RefSeq; NP_438313.1; NC_000907.1. DR RefSeq; WP_005648623.1; NC_000907.1. DR ProteinModelPortal; P44541; -. DR STRING; 71421.HI0144; -. DR EnsemblBacteria; AAC21816; AAC21816; HI_0144. DR GeneID; 951055; -. DR KEGG; hin:HI0144; -. DR PATRIC; 20188779; VBIHaeInf48452_0146. DR eggNOG; ENOG41061DF; Bacteria. DR eggNOG; COG1940; LUCA. DR KO; K00885; -. DR OMA; CIQSIAD; -. DR OrthoDB; EOG618QQT; -. DR PhylomeDB; P44541; -. DR UniPathway; UPA00629; UER00681. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01234; ManNAc_kinase; 1. DR InterPro; IPR023945; ManNAc_kinase_bac. DR InterPro; IPR000600; ROK. DR Pfam; PF00480; ROK; 1. DR PROSITE; PS01125; ROK; 1. PE 1: Evidence at protein level; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 300 N-acetylmannosamine kinase. FT /FTId=PRO_0000095699. FT NP_BIND 5 12 ATP. {ECO:0000255}. FT NP_BIND 132 139 ATP. {ECO:0000255}. FT METAL 156 156 Zinc. {ECO:0000250}. FT METAL 166 166 Zinc. {ECO:0000250}. FT METAL 168 168 Zinc. {ECO:0000250}. FT METAL 173 173 Zinc. {ECO:0000250}. SQ SEQUENCE 300 AA; 31918 MW; 8EDCF138D6EDC533 CRC64; MRCLALDIGG TKIAAAIVKN GEIEQRQQIH TPRENVVEGM HQALGKLLAD YEGQFDYVAV ASTGIINNGI LSALNPKNLG GLAEFPLKAS IAKHTDKPIG LLNDAQAATY AEYQLQNSEQ VSNFVFITVS TGVGGGIVLN QILQTGSRGI AGHIGHTLAD PNGAICGCGR RGCVEAIASG RAIEAVSSQW EEPCDPKEVF ERFRKNDEKA TALVERSAKA IANLIADLVI SLDIQKIAIG GSVGLAEGYL SLVEKYLQDF PSIYCCEIET AKFGQDAGLI GAAYWVKDVL LDKPEGTIYG // ID NARP_HAEIN Reviewed; 208 AA. AC P44845; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Nitrate/nitrite response regulator protein homolog; GN Name=narP; OrderedLocusNames=HI_0726; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could activate the expression of a formate dehydrogenase CC operon and could repress the transcription of the fumarate CC reductase (frdABCD) operon. CC -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00411}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22384.1; -; Genomic_DNA. DR PIR; A64089; A64089. DR RefSeq; NP_438884.1; NC_000907.1. DR RefSeq; WP_005652269.1; NC_000907.1. DR ProteinModelPortal; P44845; -. DR STRING; 71421.HI0726; -. DR EnsemblBacteria; AAC22384; AAC22384; HI_0726. DR GeneID; 949754; -. DR KEGG; hin:HI0726; -. DR PATRIC; 20190085; VBIHaeInf48452_0758. DR eggNOG; ENOG4105WH1; Bacteria. DR eggNOG; COG2197; LUCA. DR KO; K07685; -. DR OMA; LQWIATG; -. DR OrthoDB; EOG69GZGV; -. DR PhylomeDB; P44845; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR000792; Tscrpt_reg_LuxR_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00196; GerE; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00038; HTHLUXR. DR SMART; SM00421; HTH_LUXR; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF46894; SSF46894; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS00622; HTH_LUXR_1; 1. DR PROSITE; PS50043; HTH_LUXR_2; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Activator; ATP-binding; Complete proteome; DNA-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; KW Two-component regulatory system. FT CHAIN 1 208 Nitrate/nitrite response regulator FT protein homolog. FT /FTId=PRO_0000081150. FT DOMAIN 6 122 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DOMAIN 142 207 HTH luxR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00411}. FT DNA_BIND 166 185 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00411}. FT MOD_RES 57 57 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 208 AA; 23079 MW; 0B72119BEC4906C7 CRC64; MQDKLKVLLI DDHPLMRRGI KQLVELDDNF EVVADVSSGT EGISVALQTS PDVIILDLNM KGLSGLDTLK GLRAEGVDAR ILILTVSDAK NDIYTLIDAG ADGYLLKDTE PDTLLEQIKR IAQGEVILSD SIKNLLLERT HEDNPLDSLT DREMGVLRQI ATGLSNKQIA AQLFISEETV KVHIRNLLRK LNVHSRVAAT VLFFEQNR // ID NDK_HAEIN Reviewed; 141 AA. AC P43802; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Nucleoside diphosphate kinase; DE Short=NDK; DE Short=NDP kinase; DE EC=2.7.4.6; DE AltName: Full=Nucleoside-2-P kinase; GN Name=ndk; OrderedLocusNames=HI_0876; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates CC other than ATP. The ATP gamma phosphate is transferred to the NDP CC beta phosphate via a ping-pong mechanism, using a phosphorylated CC active-site intermediate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NDK 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; L42023; AAC22532.1; -; Genomic_DNA. DR PIR; D64099; D64099. DR RefSeq; NP_439037.1; NC_000907.1. DR RefSeq; WP_005693229.1; NC_000907.1. DR ProteinModelPortal; P43802; -. DR SMR; P43802; 4-141. DR STRING; 71421.HI0876; -. DR EnsemblBacteria; AAC22532; AAC22532; HI_0876. DR GeneID; 949884; -. DR KEGG; hin:HI0876; -. DR PATRIC; 20190409; VBIHaeInf48452_0918. DR eggNOG; ENOG4108UGX; Bacteria. DR eggNOG; COG0105; LUCA. DR KO; K00940; -. DR OMA; AEHSERP; -. DR OrthoDB; EOG67DPRV; -. DR PhylomeDB; P43802; -. DR Proteomes; UP000000579; 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:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0006163; P:purine nucleotide metabolic process; IBA:GO_Central. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IBA:GO_Central. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00451; NDP_kinase; 1. DR InterPro; IPR001564; Nucleoside_diP_kinase. DR InterPro; IPR023005; Nucleoside_diP_kinase_AS. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR PROSITE; PS00469; NDP_KINASES; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1 141 Nucleoside diphosphate kinase. FT /FTId=PRO_0000136990. FT ACT_SITE 117 117 Pros-phosphohistidine intermediate. FT {ECO:0000250}. FT BINDING 11 11 ATP. {ECO:0000250}. FT BINDING 59 59 ATP. {ECO:0000250}. FT BINDING 87 87 ATP. {ECO:0000250}. FT BINDING 93 93 ATP. {ECO:0000250}. FT BINDING 104 104 ATP. {ECO:0000250}. FT BINDING 114 114 ATP. {ECO:0000250}. SQ SEQUENCE 141 AA; 16106 MW; 00071DFD5F791C57 CRC64; MMTERTFSII KPDVVKRNLI GAILTRFEQN GFKIIASKMV RLTREQAEGF YAEHQGKEFF VPLVEYMMSS PIVVSVLEKE NAVKDYRTLI GTTNPETAAE GTIRKDFALS QRENSVHGSD SIESANREIA YFFTNSEIFE R // ID MUTT_HAEIN Reviewed; 136 AA. AC P44932; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=8-oxo-dGTP diphosphatase; DE Short=8-oxo-dGTPase; DE EC=3.6.1.55; DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase; DE AltName: Full=Mutator protein MutT; DE AltName: Full=dGTP pyrophosphohydrolase; GN Name=mutT; OrderedLocusNames=HI_0910; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the GO system responsible for removing an CC oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) CC from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite CC dA and dC residues of template DNA with almost equal efficiency CC thus leading to A.T to G.C transversions. MutT specifically CC degrades 8-oxo-dGTP to the monophosphate (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22567.1; -; Genomic_DNA. DR RefSeq; NP_439070.1; NC_000907.1. DR RefSeq; WP_010869085.1; NC_000907.1. DR ProteinModelPortal; P44932; -. DR STRING; 71421.HI0910; -. DR EnsemblBacteria; AAC22567; AAC22567; HI_0910. DR GeneID; 949912; -. DR KEGG; hin:HI0910; -. DR PATRIC; 20190475; VBIHaeInf48452_0951. DR eggNOG; ENOG4105M6F; Bacteria. DR eggNOG; COG0494; LUCA. DR KO; K03574; -. DR OMA; RLHWCKV; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; P44932; -. DR BioCyc; RETL1328306-WGS:GSTH-3845-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR003561; Mutator_MutT. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR PANTHER; PTHR22769:SF36; PTHR22769:SF36; 1. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01401; MUTATORMUTT. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR TIGRFAMs; TIGR00586; mutt; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; DNA replication; Hydrolase; KW Magnesium; Metal-binding; Mutator protein; Reference proteome. FT CHAIN 1 136 8-oxo-dGTP diphosphatase. FT /FTId=PRO_0000056946. FT DOMAIN 4 130 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT MOTIF 40 61 Nudix box. FT METAL 40 40 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 55 55 Magnesium. {ECO:0000250}. FT METAL 58 58 Magnesium. {ECO:0000250}. FT METAL 59 59 Magnesium. {ECO:0000250}. SQ SEQUENCE 136 AA; 15648 MW; 67F80E6EAC5D17F4 CRC64; MDKKIIQVAA GIIRNEFGQI YLTQRLEGQD FAQSLEFPGG KVDAGETPEQ ALKRELEEEI GIVALNAELY ERFQFEYPTK IISFFFYLVN EWIGEPFGRE GQEGFWVEQH ALDAGQFPPA NAKLIHRLLN ETHNFI // ID NAPG_HAEIN Reviewed; 279 AA. AC P44652; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Ferredoxin-type protein NapG homolog; DE Flags: Precursor; GN Name=napG; OrderedLocusNames=HI_0345; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in electron transfer. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22006.1; -; Genomic_DNA. DR PIR; A64149; A64149. DR RefSeq; NP_438509.1; NC_000907.1. DR RefSeq; WP_005694328.1; NC_000907.1. DR ProteinModelPortal; P44652; -. DR STRING; 71421.HI0345; -. DR EnsemblBacteria; AAC22006; AAC22006; HI_0345. DR GeneID; 950819; -. DR KEGG; hin:HI0345; -. DR PATRIC; 20189237; VBIHaeInf48452_0364. DR eggNOG; ENOG4108BGM; Bacteria. DR eggNOG; COG1145; LUCA. DR KO; K02573; -. DR OMA; LIDHETC; -. DR OrthoDB; EOG6QK4R9; -. DR PhylomeDB; P44652; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004494; MauM_NapG. DR InterPro; IPR019546; TAT_signal_bac_arc. DR Pfam; PF12800; Fer4_4; 2. DR Pfam; PF12838; Fer4_7; 1. DR TIGRFAMs; TIGR00397; mauM_napG; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Signal; Transport. FT SIGNAL 1 50 Tat-type signal. {ECO:0000255}. FT CHAIN 51 279 Ferredoxin-type protein NapG homolog. FT /FTId=PRO_0000159282. FT DOMAIN 63 92 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 100 132 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 141 177 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 188 219 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 72 72 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 75 75 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 78 78 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 82 82 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 110 110 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 113 113 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 118 118 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 122 122 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 150 150 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 158 158 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 161 161 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 165 165 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 197 197 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 200 200 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 203 203 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 207 207 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 279 AA; 30227 MW; F77B6801E220955A CRC64; MKVRLKSKKK MKKPALNPER RKFLKEATRT AGGLAGVGIL LGLQQNQSLA REGVPLRPPF ALQDAKAFSA ACIRCGQCVQ ACPYDMLHLA SLLSPVEAGT PYFIARDKPC EMCPDIPCAK ACPSGALDRQ ATDINESRMG LSVLLDHETC LNYQGLRCDV CYRVCPLIDK AITLETQHNP RSDKHALFIP TVHSDACTGC GKCEQACVLE EAAIKILPMD LAKGMLGKHY RLGWEEKAKA GHSLAPKDMI SLPTRTPEGT TVIPEPAEPV LAPILGSGK // ID NAPD_HAEIN Reviewed; 93 AA. AC P44651; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Protein NapD; GN Name=napD; OrderedLocusNames=HI_0343; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a role in the correct assembly of subunits of the CC periplasmic NapAB enzyme. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22005.1; -; Genomic_DNA. DR PIR; I64148; I64148. DR RefSeq; NP_438507.1; NC_000907.1. DR RefSeq; WP_005694331.1; NC_000907.1. DR ProteinModelPortal; P44651; -. DR STRING; 71421.HI0343; -. DR EnsemblBacteria; AAC22005; AAC22005; HI_0343. DR GeneID; 949452; -. DR KEGG; hin:HI0343; -. DR PATRIC; 20189231; VBIHaeInf48452_0361. DR eggNOG; COG3062; LUCA. DR KO; K02570; -. DR OMA; ENWYVCS; -. DR OrthoDB; EOG6HF65Q; -. DR PhylomeDB; P44651; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR InterPro; IPR005623; Chaperone_NapD_NO3_reduct. DR Pfam; PF03927; NapD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 93 Protein NapD. FT /FTId=PRO_0000096714. SQ SEQUENCE 93 AA; 10516 MW; 6CF771F31660446F CRC64; MNNTNLILEN ARDWHVVGLI VQGNPKKLSA IQTALLAIEH TEIPTLDEKL GKFVVVMQSN DQHLLLEKME SVKDIDGVIN VSLVYHEQDE QNK // ID NAPF_HAEIN Reviewed; 176 AA. AC P44650; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 11-MAY-2016, entry version 90. DE RecName: Full=Ferredoxin-type protein NapF homolog; GN Name=napF; OrderedLocusNames=HI_0342; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in electron transfer. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 4 [4Fe-4S] clusters or perhaps rather 3 [4Fe-4S] CC clusters and 1 3Fe-4S cluster, leaving Cys-113 out of the cluster CC ligands. {ECO:0000305}; CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22004.1; Type=Frameshift; Positions=111; 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; L42023; AAC22004.1; ALT_FRAME; Genomic_DNA. DR PIR; H64148; H64148. DR ProteinModelPortal; P44650; -. DR EnsemblBacteria; AAC22004; AAC22004; HI_0342. DR OMA; FSCKDPC; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004496; NapF. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF13187; Fer4_9; 1. DR TIGRFAMs; TIGR00402; napF; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 176 Ferredoxin-type protein NapF homolog. FT /FTId=PRO_0000159278. FT DOMAIN 39 68 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 71 100 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 109 138 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 143 172 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 48 48 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 51 51 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 54 54 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 58 58 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 80 80 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 86 86 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 90 90 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 113 113 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 121 121 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 124 124 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 128 128 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 152 152 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 155 155 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 158 158 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 162 162 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 176 AA; 19604 MW; 71E1E18DD2DFF049 CRC64; MTVENLPRRQ FLRGKFSTLS CLENNQKQNF VGIRPPWSVE NSIFVARCTR CGDCLSVCET NILVKGDAGF PEVRFDNGEC TFCGKCVDAC KQPIFYPRDQ LPWSHKIDIS VSCLTLHRIE CRTCQDNCPA NAIRFKLQMG GVAQPLVNFD ACNGCGACVQ GCPVNAITMN DLKQNE // ID NHAB_HAEIN Reviewed; 514 AA. AC P44706; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 17-FEB-2016, entry version 96. DE RecName: Full=Na(+)/H(+) antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599}; DE AltName: Full=Sodium/proton antiporter NhaB {ECO:0000255|HAMAP-Rule:MF_01599}; GN Name=nhaB {ECO:0000255|HAMAP-Rule:MF_01599}; GN OrderedLocusNames=HI_0427; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange CC for external protons. {ECO:0000255|HAMAP-Rule:MF_01599}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01599}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01599}. CC -!- SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter CC family. {ECO:0000255|HAMAP-Rule:MF_01599}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22086.1; 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; L42023; AAC22086.1; ALT_INIT; Genomic_DNA. DR PIR; B64067; B64067. DR RefSeq; NP_438588.2; NC_000907.1. DR RefSeq; WP_010868985.1; NC_000907.1. DR STRING; 71421.HI0427; -. DR EnsemblBacteria; AAC22086; AAC22086; HI_0427. DR GeneID; 949530; -. DR KEGG; hin:HI0427; -. DR PATRIC; 20189407; VBIHaeInf48452_0447. DR eggNOG; ENOG4105DKR; Bacteria. DR eggNOG; COG3067; LUCA. DR KO; K03314; -. DR OMA; QFEMLAV; -. DR OrthoDB; EOG6XDGRV; -. DR PhylomeDB; P44706; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015385; F:sodium:proton antiporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR HAMAP; MF_01599; NhaB; 1. DR InterPro; IPR004671; Na+/H+_antiporter_NhaB. DR Pfam; PF06450; NhaB; 1. DR TIGRFAMs; TIGR00774; NhaB; 1. PE 3: Inferred from homology; KW Antiport; Cell inner membrane; Cell membrane; Complete proteome; KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 514 Na(+)/H(+) antiporter NhaB. FT /FTId=PRO_0000052414. FT TRANSMEM 21 41 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 43 63 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 88 108 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 143 163 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 203 223 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 239 259 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 304 324 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 349 369 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 390 410 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 448 468 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. FT TRANSMEM 484 504 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01599}. SQ SEQUENCE 514 AA; 56540 MW; 0383B94D24C1B7DE CRC64; MTNIQAFMKN FLGASPEWYK LAIVVFLIIN PIVFFFISPF IAGWLLVAEF IFTLAMALKC YPLQPGGLLA IEAIIIGMTN AKHVKAEIMA NFEVILLLIF MVAGIFFMKQ LLLYVFTKLL VKIRSKIALS IAFCFSAAFL SAFLDALTVV AVIISVAMGF YGVYHKVASG NNLIDAVDIS DDRKIIEQQH EILEKFRAFL RSLMMHAGVG TALGGVMTVV GEPQNLIIAE QAKWNFMEFF LRMAPVTIPV FICGLLTCFL VEKFKLFGYG EKLPDEVWKI LSDLDRTNSE KMSKQDKIKL GMQALIAIWL IVGLAFHLAA VGLIGLSIII FATSFTGVTD EHTIGKAFQE SLPFTALLVV FFSVVAVIID QKLFSPIIHF VLSAEENTQL ALFYLFNGLL SSISDNVFVA TVYINEAKAA LTNGVIAPHQ FELLSVAINT GTNLPSVATP NGQAAFLFLL TSSISPLIRL SYGRMVYMAL PYTIVLSIIG LLAIEFILPA ATIWLASLGL ILPI // ID NAGA_HAEIN Reviewed; 381 AA. AC P44537; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 98. DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:P0AF18}; DE Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:P0AF18}; DE EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18}; GN Name=nagA; OrderedLocusNames=HI_0140; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the first committed step in the biosynthesis CC of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N- CC acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to CC yield glucosamine 6-phosphate and acetate. CC {ECO:0000250|UniProtKB:P0AF18}. CC -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O = CC D-glucosamine 6-phosphate + acetate. CC {ECO:0000250|UniProtKB:P0AF18}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P0AF18}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000250|UniProtKB:P0AF18}; CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; CC D-fructose 6-phosphate from N-acetylneuraminate: step 4/5. CC {ECO:0000250|UniProtKB:P0AF18}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AF18}. CC -!- SIMILARITY: Belongs to the NagA 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; L42023; AAC21812.1; -; Genomic_DNA. DR PIR; E64050; E64050. DR RefSeq; NP_438309.1; NC_000907.1. DR RefSeq; WP_005694427.1; NC_000907.1. DR ProteinModelPortal; P44537; -. DR SMR; P44537; 3-379. DR STRING; 71421.HI0140; -. DR EnsemblBacteria; AAC21812; AAC21812; HI_0140. DR GeneID; 951049; -. DR KEGG; hin:HI0140; -. DR PATRIC; 20188771; VBIHaeInf48452_0142. DR eggNOG; ENOG4105CE4; Bacteria. DR eggNOG; COG1820; LUCA. DR KO; K01443; -. DR OMA; NLYPARA; -. DR OrthoDB; EOG6B09R2; -. DR PhylomeDB; P44537; -. DR UniPathway; UPA00629; UER00683. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; ISS:UniProtKB. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR Gene3D; 2.30.40.10; -; 2. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR003764; GlcNAc_6-P_deAcase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 1. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00221; nagA; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Metal-binding; KW Reference proteome. FT CHAIN 1 381 N-acetylglucosamine-6-phosphate FT deacetylase. FT /FTId=PRO_0000170917. FT REGION 140 141 Substrate binding. FT {ECO:0000250|UniProtKB:P0AF18}. FT REGION 217 218 Substrate binding. FT {ECO:0000250|UniProtKB:P0AF18}. FT REGION 246 249 Substrate binding. FT {ECO:0000250|UniProtKB:P0AF18}. FT REGION 306 308 Substrate binding. FT {ECO:0000250|UniProtKB:P0AF18}. FT ACT_SITE 271 271 Proton donor/acceptor. FT {ECO:0000250|UniProtKB:P0AF18}. FT METAL 129 129 Divalent metal cation. FT {ECO:0000250|UniProtKB:P0AF18}. FT METAL 193 193 Divalent metal cation; via tele nitrogen. FT {ECO:0000250|UniProtKB:P0AF18}. FT METAL 214 214 Divalent metal cation; via tele nitrogen. FT {ECO:0000250|UniProtKB:P0AF18}. FT BINDING 226 226 Substrate. FT {ECO:0000250|UniProtKB:P0AF18}. SQ SEQUENCE 381 AA; 41593 MW; A502DF70BC03965A CRC64; MKYALINCVI YTKYDVLRDF AVIINGEIIE AVIPQAELET GIKTIDLQGN NLTAGFIDLQ LNGCGGVMFN DQTSVETLEI MQETNLKSGC TSFLPTFITA PDENIKSAVK IMREYLNKHK NQALGLHIEG PYLSIEKKGV HRPEYIREIT PEMKDFLCEN GDVITKMTIA AENPTINYTP DFVKAGIIVS VGHSNATYEV AKAAFHKGAT FATHLHNAMS PISSGREMGV VGAVLDSDVY TGIIVDGVHI NYGNVRIDKK IKGDKLCIVT DSIAAAGAPP ELESFTFVGK TIYIKEGRCY DANDTIAGAS ITMMESIKNA VEYVEIPLAE AIRMSNLYPA RAIGIDDRLG SVEKGKIANL AVFTPNYQVI GTVVNGKWKE N // ID NAGK_HAEIN Reviewed; 304 AA. AC P44554; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 11-NOV-2015, entry version 92. DE RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_01271}; DE EC=2.7.1.59 {ECO:0000255|HAMAP-Rule:MF_01271}; DE AltName: Full=GlcNAc kinase {ECO:0000255|HAMAP-Rule:MF_01271}; GN Name=nagK {ECO:0000255|HAMAP-Rule:MF_01271}; GN OrderedLocusNames=HI_0182; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine CC (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. CC {ECO:0000255|HAMAP-Rule:MF_01271}. CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl- CC D-glucosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_01271}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_01271}. CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01271}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21851.1; 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; L42023; AAC21851.1; ALT_INIT; Genomic_DNA. DR PIR; H64144; H64144. DR RefSeq; NP_438350.2; NC_000907.1. DR RefSeq; WP_005694104.1; NC_000907.1. DR ProteinModelPortal; P44554; -. DR SMR; P44554; 1-303. DR STRING; 71421.HI0182; -. DR EnsemblBacteria; AAC21851; AAC21851; HI_0182. DR GeneID; 951092; -. DR KEGG; hin:HI0182; -. DR PATRIC; 20188859; VBIHaeInf48452_0186. DR eggNOG; ENOG4105EZX; Bacteria. DR eggNOG; COG1940; LUCA. DR KO; K00884; -. DR OMA; AGEFGHF; -. DR OrthoDB; EOG61P6P0; -. DR PhylomeDB; P44554; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01271; GlcNAc_kinase; 1. DR InterPro; IPR023505; N-acetyl-D-glucosamine_kinase. DR InterPro; IPR000600; ROK. DR Pfam; PF00480; ROK; 1. DR PROSITE; PS01125; ROK; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; KW Zinc. FT CHAIN 1 304 N-acetyl-D-glucosamine kinase. FT /FTId=PRO_0000095719. FT NP_BIND 4 11 ATP. {ECO:0000255|HAMAP-Rule:MF_01271}. FT NP_BIND 133 140 ATP. {ECO:0000255|HAMAP-Rule:MF_01271}. FT METAL 157 157 Zinc. {ECO:0000255|HAMAP-Rule:MF_01271}. FT METAL 178 178 Zinc. {ECO:0000255|HAMAP-Rule:MF_01271}. FT METAL 180 180 Zinc. {ECO:0000255|HAMAP-Rule:MF_01271}. FT METAL 185 185 Zinc. {ECO:0000255|HAMAP-Rule:MF_01271}. SQ SEQUENCE 304 AA; 33107 MW; 97E174C5EF48CB7F CRC64; MYYGLDIGGT KIELAVFNEK LEKLYSERVP TPKTDYEEWL NTIVDLVNRA DEKFGEVGTV GLGVPGFVNQ QTGLAEIANI RVADNKPILC DLSTRLGREV RAENDANCFA LSEAWDTENQ QYSTVLGLIL GTGFGGGFVL NGKVHSGQVG MAGELGHLQL NYHALKLLGW DNAPIYQCGC GNKACLDNYL SGRGFEMLYQ DLKGETLSAR KIINLFYQSN ESAVDFVNLF VELAAISIGN IITAFDPHMI VLGGGLSNFD YLYEALPKAL PPHLMRKAKV PPIKKAKHGD SGGVRGAAAL FLTK // ID NAGZ_HAEIN Reviewed; 351 AA. AC P44955; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Beta-hexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE EC=3.2.1.52 {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000255|HAMAP-Rule:MF_00364}; GN Name=nagZ {ECO:0000255|HAMAP-Rule:MF_00364}; GN OrderedLocusNames=HI_0959; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from CC peptide-linked peptidoglycan fragments, giving rise to free CC GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic CC acid-linked peptides. {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl- CC D-hexosamine residues in N-acetyl-beta-D-hexosaminides. CC {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- SUBUNIT: Monomer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00364}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00364}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22620.1; -; Genomic_DNA. DR PIR; F64162; F64162. DR RefSeq; NP_439120.1; NC_000907.1. DR RefSeq; WP_005693307.1; NC_000907.1. DR ProteinModelPortal; P44955; -. DR SMR; P44955; 1-298. DR STRING; 71421.HI0959; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAC22620; AAC22620; HI_0959. DR GeneID; 949658; -. DR KEGG; hin:HI0959; -. DR PATRIC; 20190577; VBIHaeInf48452_1001. DR eggNOG; ENOG4107QPA; Bacteria. DR eggNOG; COG1472; LUCA. DR KO; K01207; -. DR OMA; DMVLICN; -. DR OrthoDB; EOG6BCT06; -. DR PhylomeDB; P44955; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.300; -; 1. DR HAMAP; MF_00364; NagZ; 1. DR InterPro; IPR022956; Beta_hexosaminidase_bac. DR InterPro; IPR019800; Glyco_hydro_3_AS. DR InterPro; IPR001764; Glyco_hydro_3_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00933; Glyco_hydro_3; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; KW Glycosidase; Hydrolase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 351 Beta-hexosaminidase. FT /FTId=PRO_0000210789. FT REGION 163 164 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT ACT_SITE 176 176 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00364}. FT ACT_SITE 248 248 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 62 62 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 70 70 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT BINDING 133 133 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00364}. FT SITE 174 174 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00364}. SQ SEQUENCE 351 AA; 39704 MW; D33A955A65DEDA05 CRC64; MSSLLIDLKG KELEQEEVEL LSHPLVAGLI LFTRNFENRE QIQELIRSVR QRVKKPLLIT VDQEGGRVQR FRDGFTMLPS MQAFQETLSA TEQVSFAKEA GWQMAAEMIA LDIDLSFAPV LDLGHECRAI GDRSFSSDVK SAVNLATAFI DGMHQAGMAS TGKHFPGHGH VLADSHLETP YDDRTKEEIF SGDLQPFQQL ISQNKLDAIM PAHVIYSQCD SQPASGSKYW LKEILRKKLN FQGTIFSDDL GMKGAGVMGN FVERSKKALN AGCDLLLLCN EREGVIQVLD NLKLTENQPH FMARQARLQS LFKRRVINWN DLISDQRWRL NYQKLADIQS RWLDIQAAKN D // ID NANM_HAEIN Reviewed; 375 AA. AC P44544; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 11-MAY-2016, entry version 107. DE RecName: Full=N-acetylneuraminate epimerase; DE EC=5.1.3.24; DE AltName: Full=N-acetylneuraminate mutarotase; DE Short=Neu5Ac mutarotase; DE AltName: Full=Sialic acid epimerase; DE Flags: Precursor; GN Name=nanM; OrderedLocusNames=HI_0148; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 23-32, IDENTIFICATION BY MASS SPECTROMETRY, AND RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INVOLVEMENT IN SIALIC ACID RP CATABOLISM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15121896; DOI=10.1093/nar/gkh555; RA Kolker E., Makarova K.S., Shabalina S., Picone A.F., Purvine S., RA Holzman T., Cherny T., Armbruster D., Munson R.S. Jr., Kolesov G., RA Frishman D., Galperin M.Y.; RT "Identification and functional analysis of 'hypothetical' genes RT expressed in Haemophilus influenzae."; RL Nucleic Acids Res. 32:2353-2361(2004). CC -!- FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the CC beta-anomer, accelerating the equilibrium between the alpha- and CC beta-anomers. Probably facilitates sialidase-negative bacteria to CC compete sucessfully for limited amounts of extracellular Neu5Ac, CC which is likely taken up in the beta-anomer. In addition, the CC rapid removal of sialic acid from solution might be advantageous CC to the bacterium to damp down host responses (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: N-acetyl-alpha-neuraminate = N-acetyl-beta- CC neuraminate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10675023}. CC -!- SIMILARITY: Belongs to the NanM family. {ECO:0000305}. CC -!- SIMILARITY: Contains 7 Kelch repeats. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21820.1; 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; L42023; AAC21820.1; ALT_INIT; Genomic_DNA. DR PIR; A64144; A64144. DR RefSeq; NP_438317.1; NC_000907.1. DR ProteinModelPortal; P44544; -. DR STRING; 71421.HI0148; -. DR EnsemblBacteria; AAC21820; AAC21820; HI_0148. DR GeneID; 951058; -. DR KEGG; hin:HI0148; -. DR PATRIC; 20188787; VBIHaeInf48452_0150. DR eggNOG; ENOG4108MX5; Bacteria. DR eggNOG; COG3055; LUCA. DR KO; K17948; -. DR OMA; GAAFTIQ; -. DR OrthoDB; EOG6RC3QP; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.120.10.80; -; 2. DR HAMAP; MF_01195; NanM; 1. DR InterPro; IPR015915; Kelch-typ_b-propeller. DR InterPro; IPR006652; Kelch_1. DR InterPro; IPR019936; Mutatrotase_YjhT-like. DR Pfam; PF01344; Kelch_1; 1. DR TIGRFAMs; TIGR03547; muta_rot_YjhT; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing; KW Isomerase; Kelch repeat; Periplasm; Reference proteome; Repeat; KW Signal. FT SIGNAL 1 22 {ECO:0000269|PubMed:10675023}. FT CHAIN 23 375 N-acetylneuraminate epimerase. FT /FTId=PRO_0000016656. FT REPEAT 43 87 Kelch 1. FT REPEAT 89 140 Kelch 2. FT REPEAT 142 176 Kelch 3. FT REPEAT 177 222 Kelch 4. FT REPEAT 225 273 Kelch 5. FT REPEAT 295 344 Kelch 6. FT REPEAT 346 375 Kelch 7. SQ SEQUENCE 375 AA; 40343 MW; 05EC99114EAC27BE CRC64; MKLTKTALCT ALFATFTFSA NAQTYPDLPV GIKGGTGALI GDTVYVGLGS GGDKFYTLDL KDPSAQWKEI ATFPGGERNQ PVAAAVDGKL YVFGGLQKNE KGELQLVNDA YRYNPSDNTW MKLPTRSPRG LVGSSGASHG DKVYILGGSN LSIFNGFFQD TVAAGEDKAK KDEIAAAYFD QRPEDYFFTT ELLSYEPSTN KWRNEGRIPF SGRAGAAFTI QGNELVVVNG EIKPGLRTAE THQGKFTAKG VQWKNLPDLP APKGKSQDGL AGALSGYSNG HYLVTGGANF PGSIKQFKEG KLHAHKGLSK AWHNEVYTLN NGKWRIVGEL PMNIGYGFSV SYNNKVLLIG GETDGGKALT SVKAISYDGK KLTIE // ID NAPB_HAEIN Reviewed; 150 AA. AC P44654; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 113. DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit; DE AltName: Full=Diheme cytochrome c NapB; DE Flags: Precursor; GN Name=napB; OrderedLocusNames=HI_0347; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 27-31, FUNCTION, ABSORPTION SPECTROSCOPY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PTM, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11389694; DOI=10.1042/0264-6021:3560851; RA Brige A., Cole J.A., Hagen W.R., Guisez Y., Van Beeumen J.J.; RT "Overproduction, purification and novel redox properties of the dihaem RT cytochrome c, NapB, from Haemophilus influenzae."; RL Biochem. J. 356:851-858(2001). RN [3] RP CRYSTALLIZATION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11223519; DOI=10.1107/S0907444900018011; RA Brige A., Leys D., Van Beeumen J.J.; RT "Crystallization and preliminary X-ray analysis of the recombinant RT dihaem cytochrome c (NapB) from Haemophilus influenzae."; RL Acta Crystallogr. D 57:418-420(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 28-150 IN COMPLEX WITH HEME RP C, AND PTM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11939777; DOI=10.1021/bi012144b; RA Brige A., Leys D., Meyer T.E., Cusanovich M.A., Van Beeumen J.J.; RT "The 1.25 A resolution structure of the diheme NapB subunit of soluble RT nitrate reductase reveals a novel cytochrome c fold with a stacked RT heme arrangement."; RL Biochemistry 41:4827-4836(2002). CC -!- FUNCTION: Electron transfer subunit of the periplasmic nitrate CC reductase complex NapAB. Receives electrons from the membrane- CC anchored tetraheme c-type NapC protein and transfers these to NapA CC subunit, thus allowing electron flow between membrane and CC periplasm. Essential for periplasmic nitrate reduction with CC nitrate as the terminal electron acceptor. CC {ECO:0000269|PubMed:11389694}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) are -25 mV and -175 mV. {ECO:0000269|PubMed:11389694}; CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB CC complex composed of NapA and NapB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11223519, CC ECO:0000269|PubMed:11389694}. CC -!- PTM: Binds 2 heme C groups per subunit. CC -!- MASS SPECTROMETRY: Mass=14748.68; Method=Electrospray; Range=27- CC 150; Evidence={ECO:0000269|PubMed:11223519}; CC -!- SIMILARITY: Belongs to the NapB 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; L42023; AAC22008.1; -; Genomic_DNA. DR PIR; C64149; C64149. DR RefSeq; NP_438511.1; NC_000907.1. DR RefSeq; WP_005691774.1; NC_000907.1. DR PDB; 1JNI; X-ray; 1.25 A; A=28-150. DR PDBsum; 1JNI; -. DR ProteinModelPortal; P44654; -. DR SMR; P44654; 64-130. DR STRING; 71421.HI0347; -. DR EnsemblBacteria; AAC22008; AAC22008; HI_0347. DR GeneID; 949780; -. DR KEGG; hin:HI0347; -. DR PATRIC; 20189241; VBIHaeInf48452_0366. DR eggNOG; ENOG4105IYZ; Bacteria. DR eggNOG; COG3043; LUCA. DR KO; K02568; -. DR OMA; PRVPESH; -. DR OrthoDB; EOG6CGCD3; -. DR PhylomeDB; P44654; -. DR EvolutionaryTrace; P44654; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 4.10.1020.10; -; 1. DR InterPro; IPR011031; Multihaem_cyt. DR InterPro; IPR005591; NapB. DR InterPro; IPR027406; NapB_heme-bd. DR Pfam; PF03892; NapB; 1. DR PIRSF; PIRSF006105; NapB; 1. DR SUPFAM; SSF48695; SSF48695; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Electron transport; Heme; Iron; Metal-binding; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1 26 {ECO:0000269|PubMed:11389694}. FT CHAIN 27 150 Periplasmic nitrate reductase, electron FT transfer subunit. FT /FTId=PRO_0000006589. FT COMPBIAS 115 118 Poly-Ser. FT METAL 70 70 Iron (heme C 1 axial ligand); via tele FT nitrogen. FT METAL 88 88 Iron (heme C 1 axial ligand); via tele FT nitrogen. FT METAL 105 105 Iron (heme C 2 axial ligand); via tele FT nitrogen. FT METAL 128 128 Iron (heme C 2 axial ligand); via tele FT nitrogen. FT BINDING 84 84 Heme C 1 (covalent). FT {ECO:0000269|PubMed:11939777}. FT BINDING 87 87 Heme C 1 (covalent). FT {ECO:0000269|PubMed:11939777}. FT BINDING 124 124 Heme C 2 (covalent). FT {ECO:0000269|PubMed:11939777}. FT BINDING 127 127 Heme C 2 (covalent). FT {ECO:0000269|PubMed:11939777}. FT HELIX 85 88 {ECO:0000244|PDB:1JNI}. FT TURN 90 92 {ECO:0000244|PDB:1JNI}. FT HELIX 93 96 {ECO:0000244|PDB:1JNI}. FT HELIX 103 105 {ECO:0000244|PDB:1JNI}. FT HELIX 124 126 {ECO:0000244|PDB:1JNI}. SQ SEQUENCE 150 AA; 16255 MW; C5E98C4E1B29E01F CRC64; MINMTKQVSK ILAGLFTALF AGSLMASDAP AVGKDLTQAA ENIPPAFHNA PRQGELPALN YVNQPPMVPH SVANYQVTKN VNQCLNCHSP ENSRLSGATR ISPTHFMDRD GKVGSSSSPR RYFCLQCHVS QANVDPIVPN DFKPMKGYGN // ID NDPA_HAEIN Reviewed; 338 AA. AC P44896; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 21-NOV-2003, sequence version 2. DT 11-NOV-2015, entry version 83. DE RecName: Full=Nucleoid-associated protein HI_0839; GN OrderedLocusNames=HI_0839; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}. CC -!- SIMILARITY: Belongs to the YejK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22497.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22497.1; ALT_INIT; Genomic_DNA. DR PIR; D64159; D64159. DR RefSeq; NP_438999.2; NC_000907.1. DR RefSeq; WP_010869067.1; NC_000907.1. DR STRING; 71421.HI0839; -. DR EnsemblBacteria; AAC22497; AAC22497; HI_0839. DR GeneID; 949853; -. DR KEGG; hin:HI0839; -. DR PATRIC; 20190333; VBIHaeInf48452_0880. DR eggNOG; ENOG4106V8H; Bacteria. DR eggNOG; COG3081; LUCA. DR KO; K06899; -. DR OMA; FFMDFLA; -. DR OrthoDB; EOG6DVJNP; -. DR PhylomeDB; P44896; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. DR HAMAP; MF_00730; NdpA; 1. DR InterPro; IPR007358; Nucleoid_associated_NdpA. DR Pfam; PF04245; NA37; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 338 Nucleoid-associated protein HI_0839. FT /FTId=PRO_0000210908. SQ SEQUENCE 338 AA; 38516 MW; A24194F803151E5E CRC64; MSITVNQTVL HQLVKNVDGD SIKMESVLRD ELLSITPEVE QMMLQLHQSY QNKAKAFGVF QEKSIFAQHL NRLLEQEIEF LGFSQYSTKL LADELGKYNF AESGTLILCQ YNFLATDYLF IALLDSRHSM LVDEHLDIRR TEYLDITQFD IAARINLTDL QVNANSNRYL TFIKGRVGRK ISDFFMDFLG AEEGLNPQVQ NQCLLQAVSD YCDQGELNKE QTQAVKKQVF EYCKGQLSNG NNIELRELSD SLPTLNEQPF VVFTEKQNYG LEESIPPIRS TLKSLTKFSG SGKGVTLSFD AELLNTRIQW DPMTDTLTIK GLPPNLKDQL QKALKSEN // ID NLPC_HAEIN Reviewed; 183 AA. AC P45296; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Probable endopeptidase NlpC homolog; DE EC=3.4.-.-; DE AltName: Full=Probable lipoprotein NlpC homolog; DE Flags: Precursor; GN Name=nlpC; OrderedLocusNames=HI_1652; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase C40 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; L42023; AAC23297.1; -; Genomic_DNA. DR PIR; H64173; H64173. DR RefSeq; NP_439794.1; NC_000907.1. DR RefSeq; WP_005659678.1; NC_000907.1. DR ProteinModelPortal; P45296; -. DR SMR; P45296; 70-183. DR STRING; 71421.HI1652; -. DR MEROPS; C40.004; -. DR DNASU; 950494; -. DR EnsemblBacteria; AAC23297; AAC23297; HI_1652. DR GeneID; 950494; -. DR KEGG; hin:HI1652; -. DR PATRIC; 20192051; VBIHaeInf48452_1729. DR eggNOG; ENOG4107TT5; Bacteria. DR eggNOG; COG0791; LUCA. DR KO; K13694; -. DR OMA; SEWVGTR; -. DR OrthoDB; EOG60CWQW; -. DR PhylomeDB; P45296; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.1720.10; -; 1. DR InterPro; IPR000064; NLP_P60_dom. DR Pfam; PF00877; NLPC_P60; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Lipoprotein; Membrane; KW Palmitate; Protease; Reference proteome; Signal; Thiol protease. FT SIGNAL 1 17 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 18 183 Probable endopeptidase NlpC homolog. FT /FTId=PRO_0000019755. FT ACT_SITE 95 95 Nucleophile. {ECO:0000250}. FT ACT_SITE 143 143 Proton acceptor. {ECO:0000250}. FT LIPID 18 18 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 18 18 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 183 AA; 20586 MW; 772BE57F79452E38 CRC64; MLKRILVIIG LAVLATACSN APRTVSHQVI SENDDIQLTG LINNLEKDNR TGIFHKVRTN RSSALMGDKA LASVYNEWVG TRYRMGGTTK RGIDCSAFMQ TTFSEVFGIE LPRSTAEQRH LGRKINKSEL KKGDLVFFRK NNHVGVYIGN NQFMHASTGQ GVTISSLDEK YWARTYTQSR RIM // ID NARQ_HAEIN Reviewed; 567 AA. AC P44604; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Sensor protein NarQ homolog; DE EC=2.7.13.3; GN Name=narQ; OrderedLocusNames=HI_0267; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable member of a two-component regulatory system. It CC is not known what protein it phosphorylates and in which CC regulatory pathway it acts, as the narL and other nar genes do not CC exist in H.influenzae. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00102}. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21933.1; -; Genomic_DNA. DR PIR; F64058; F64058. DR RefSeq; NP_438436.1; NC_000907.1. DR RefSeq; WP_005694037.1; NC_000907.1. DR ProteinModelPortal; P44604; -. DR STRING; 71421.HI0267; -. DR EnsemblBacteria; AAC21933; AAC21933; HI_0267. DR GeneID; 949389; -. DR KEGG; hin:HI0267; -. DR PATRIC; 20189061; VBIHaeInf48452_0282. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR KO; K07674; -. DR OMA; FLQIQLT; -. DR OrthoDB; EOG6JX7HQ; -. DR PhylomeDB; P44604; -. DR BRENDA; 2.7.13.3; 2529. DR Proteomes; UP000000579; 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR029095; NarX-like_N. DR InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ. DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF07730; HisKA_3; 1. DR Pfam; PF13675; PilJ; 1. DR PIRSF; PIRSF003167; STHK_NarX/NarQ; 1. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; KW Two-component regulatory system. FT CHAIN 1 567 Sensor protein NarQ homolog. FT /FTId=PRO_0000074811. FT TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TOPO_DOM 35 147 Periplasmic. {ECO:0000255}. FT TRANSMEM 148 172 Helical. {ECO:0000255}. FT TOPO_DOM 173 567 Cytoplasmic. {ECO:0000255}. FT DOMAIN 175 228 HAMP. {ECO:0000255|PROSITE- FT ProRule:PRU00102}. FT DOMAIN 367 566 Histidine kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00107}. FT MOD_RES 373 373 Phosphohistidine; by autocatalysis. FT {ECO:0000255|PROSITE-ProRule:PRU00107}. SQ SEQUENCE 567 AA; 65238 MW; A74F54998C6ECAB9 CRC64; MYTKGSVSTR IAKYLFIILI VAGVISSLSL AIMSSNKYDA EAINISGSLR MQSYRLLYEM QEQPESVETN LRRYHISLHS SALLEVQNQF FTPNVLKHSY QNILQRWTNM EKYARQQDVK NYSKQLTDYV ADVDYFVFEL QRFSEQKWIL GVSVLGFAML LILLMVSYVI WYTNREVVKP LHLMTKASMQ VQMRQFNHIP LDTRKQNELG TLARVFTQMS TELGQLYSRL EEAVNEKTQK LRQTNRTLST LYQSAQLLNT NTINDKILNQ VLNYIFISDH LNFVKVEVMG AEHWDITLGK QDANNELQIE TLSVDNEELG VLSWQAGLPC PDPRIMQNLA QMLARALYFH KNLRQKEQLL LMEERSIIAR ELHDSLAQVL SFLQIQLTLL KHNLKKEDEQ SKEKSLAIIA NFEQALSGGY AQLRELLATF RLTIQEANLQ LALKQVIDSL RSQTTMQMNV NCQLPSQSLN PQQLVHVLQI VREATTNAIK HSQGTVIEIS ARINAEGEYE ILVEDDGVGI PNLEEPEGHY GLNIMAERCR QLNAQLHIHR REQGGTQVKI TLPHTLY // ID NEUA_HAEIN Reviewed; 228 AA. AC Q57140; O05051; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Probable N-acylneuraminate cytidylyltransferase; DE EC=2.7.7.43; DE AltName: Full=CMP-N-acetylneuraminic acid synthase; DE Short=CMP-NeuNAc synthase; DE AltName: Full=CMP-sialic acid synthase; GN Name=neuA; OrderedLocusNames=HI_1279; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: CTP + N-acylneuraminate = diphosphate + CMP-N- CC acylneuraminate. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22927.1; -; Genomic_DNA. DR PIR; C64114; C64114. DR RefSeq; NP_439432.1; NC_000907.1. DR RefSeq; WP_005694522.1; NC_000907.1. DR ProteinModelPortal; Q57140; -. DR STRING; 71421.HI1279; -. DR EnsemblBacteria; AAC22927; AAC22927; HI_1279. DR GeneID; 950022; -. DR KEGG; hin:HI1279; -. DR PATRIC; 20191237; VBIHaeInf48452_1330. DR eggNOG; ENOG4105F0R; Bacteria. DR eggNOG; COG1083; LUCA. DR KO; K00983; -. DR OMA; QPIHELT; -. DR OrthoDB; EOG6HXJ57; -. DR PhylomeDB; Q57140; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 228 Probable N-acylneuraminate FT cytidylyltransferase. FT /FTId=PRO_0000213204. SQ SEQUENCE 228 AA; 25308 MW; B3CC7674CA379551 CRC64; MKIIMTRIAI IPARAGSKGI KDKNLQLVGG VSLVGRAILA AQESGMFDQI VVTSDGENIL KEATKYGAKP VARPESLAQS DTRTIDAILH CLETLNISQG TAALLQPTSP LRNALDIRNA MEIFLGGKYK SVVSACECEH HPYKSFTLEG TEVQPIHELT DFESPRQKLP KSYRANGAIY INDIQSLFEE KRFFIAPMRF YLMPTYRSID IDSTLDLQLA ESLISKEF // ID NFUA_HAEIN Reviewed; 198 AA. AC P31774; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 108. DE RecName: Full=Fe/S biogenesis protein NfuA {ECO:0000255|HAMAP-Rule:MF_01637}; GN Name=nfuA {ECO:0000255|HAMAP-Rule:MF_01637}; Synonyms=gntY; GN OrderedLocusNames=HI_0433; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1856167; RA Larson T.G., Goodgal S.H.; RT "Sequence and transcriptional regulation of com101A, a locus required RT for genetic transformation in Haemophilus influenzae."; RL J. Bacteriol. 173:4683-4691(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Involved in iron-sulfur cluster biogenesis. Binds a 4Fe- CC 4S cluster, can transfer this cluster to apoproteins, and thereby CC intervenes in the maturation of Fe/S proteins. Could also act as a CC scaffold/chaperone for damaged Fe/S proteins. {ECO:0000255|HAMAP- CC Rule:MF_01637}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01637}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is CC presumably bound at the interface of two monomers. CC {ECO:0000255|HAMAP-Rule:MF_01637}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01637}. CC -!- SIMILARITY: Belongs to the NfuA family. {ECO:0000255|HAMAP- CC Rule:MF_01637}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25015.1; -; Genomic_DNA. DR EMBL; M59751; AAA24950.1; -; Genomic_DNA. DR EMBL; L42023; AAC22092.1; -; Genomic_DNA. DR PIR; F64067; F64067. DR RefSeq; NP_438594.1; NC_000907.1. DR RefSeq; WP_005693730.1; NC_000907.1. DR ProteinModelPortal; P31774; -. DR STRING; 71421.HI0433; -. DR EnsemblBacteria; AAC22092; AAC22092; HI_0433. DR GeneID; 950313; -. DR KEGG; hin:HI0433; -. DR PATRIC; 20189419; VBIHaeInf48452_0453. DR eggNOG; ENOG4107RUK; Bacteria. DR eggNOG; COG0316; LUCA. DR eggNOG; COG0694; LUCA. DR KO; K07400; -. DR OMA; ETCLAYC; -. DR OrthoDB; EOG6VXF8J; -. DR PhylomeDB; P31774; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central. DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central. DR Gene3D; 2.60.300.12; -; 1. DR HAMAP; MF_01637; Fe_S_biogen_NfuA; 1. DR InterPro; IPR017726; Fe/S_biogenesis_protein_NfuA. DR InterPro; IPR000361; FeS_biogenesis. DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C. DR Pfam; PF01521; Fe-S_biosyn; 1. DR Pfam; PF01106; NifU; 1. DR ProDom; PD002830; NIF_FeS_clus_asmbl_NifU_C; 1. DR SUPFAM; SSF89360; SSF89360; 1. DR TIGRFAMs; TIGR03341; YhgI_GntY; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 198 Fe/S biogenesis protein NfuA. FT /FTId=PRO_0000209476. FT METAL 155 155 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01637}. FT METAL 158 158 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01637}. FT CONFLICT 35 35 V -> A (in Ref. 1; AAA25015). FT {ECO:0000305}. SQ SEQUENCE 198 AA; 21907 MW; E9963A6826F2118A CRC64; MEQATQQIAI SDAAQAHFRK LLDTQEEGTH IRIFVVNPGT PNAECGVSYC PPNAVEESDI EMKYNTFSAF IDEVSLPFLE EAEIDYVTEE LGAQLTLKAP NAKMRKVADD APLIERVEYV IQTQINPQLA NHGGRITLIE ITEDGYAVLQ FGGGCNGCSM VDVTLKDGVE KQLVSLFPNE LKGAKDITEH QRGEHSYY // ID NLPI_HAEIN Reviewed; 314 AA. AC P44585; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=Lipoprotein NlpI homolog; DE Flags: Precursor; GN Name=nlpI; OrderedLocusNames=HI_0230; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: May be involved in cell division. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 3 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21899.1; -; Genomic_DNA. DR PIR; G64145; G64145. DR RefSeq; NP_438402.1; NC_000907.1. DR RefSeq; WP_005694062.1; NC_000907.1. DR ProteinModelPortal; P44585; -. DR STRING; 71421.HI0230; -. DR EnsemblBacteria; AAC21899; AAC21899; HI_0230. DR GeneID; 951148; -. DR KEGG; hin:HI0230; -. DR PATRIC; 20188983; VBIHaeInf48452_0244. DR eggNOG; ENOG4105RT1; Bacteria. DR eggNOG; COG4785; LUCA. DR KO; K05803; -. DR OMA; YEAFDST; -. DR OrthoDB; EOG6P8TKS; -. DR PhylomeDB; P44585; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR023605; Lipoprotein_NlpI. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR PIRSF; PIRSF004654; NlpI; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS50005; TPR; 4. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cell membrane; Complete proteome; KW Lipoprotein; Membrane; Palmitate; Reference proteome; Repeat; Signal; KW TPR repeat. FT SIGNAL 1 25 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 26 314 Lipoprotein NlpI homolog. FT /FTId=PRO_0000035693. FT REPEAT 74 107 TPR 1. FT REPEAT 108 141 TPR 2. FT REPEAT 246 279 TPR 3. 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 314 AA; 36434 MW; 0E87CAE286CC5722 CRC64; MRCFRLSRHF IVYLFSLCAI LLLAGCVQSR GGFVSKNHVV LAEQNPNTHF EQEVMIVRLS QVLLVGKMSN EERASLHFER GVLYDSLGLW GLARYDLTQA LALQPKMASV YNYLGLYLLL EEDYDGALDA FNTVFELDSG YDYTHLNRGL NFYYVGRYHL AQQDFLQFYQ ADKKDPYRVL WLYLNEQKLK PQEAQTNLVE RAKGLSEDFW GTHIVQYYLG HISVEELQQR ASEFAENSQQ YAEILTETYF YLAKQKLNVG LVDEAAALFK LAMANQVYNF VEYRFAAFEL MKLKPVQTED EKEEKSAVTK AIVF // ID NER_HAEIN Reviewed; 89 AA. AC P46496; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Mu-like prophage FluMu DNA-binding protein Ner; GN Name=nlp; OrderedLocusNames=HI_1477; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Negative regulator of transcription starting from the Pe CC and Pc promoters of Mu. Also negatively regulates its own gene CC transcription (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ner transcriptional regulatory 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; L42023; AAC23124.1; -; Genomic_DNA. DR RefSeq; NP_439628.1; NC_000907.1. DR RefSeq; WP_005693493.1; NC_000907.1. DR ProteinModelPortal; P46496; -. DR STRING; 71421.HI1477; -. DR EnsemblBacteria; AAC23124; AAC23124; HI_1477. DR GeneID; 950789; -. DR KEGG; hin:HI1477; -. DR PATRIC; 20191671; VBIHaeInf48452_1545. DR eggNOG; ENOG4105R8V; Bacteria. DR eggNOG; COG3423; LUCA. DR KO; K07724; -. DR OMA; VSPAEIW; -. DR OrthoDB; EOG60CWRG; -. DR PhylomeDB; P46496; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR SUPFAM; SSF47413; SSF47413; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 89 Mu-like prophage FluMu DNA-binding FT protein Ner. FT /FTId=PRO_0000062785. FT DNA_BIND 57 76 H-T-H motif. {ECO:0000250}. SQ SEQUENCE 89 AA; 10262 MW; D6A755071E861FB1 CRC64; MSVLEKPKKT AEQDWHRADI LAELKKNGWS LRSLAKEGQV SYNTLKTVLD KSYPKMERLV ANAIGVPPEV IWAGRFAERN KRPTLQHKY // ID NHAA_HAEIN Reviewed; 400 AA. AC P44581; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Na(+)/H(+) antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844}; DE AltName: Full=Sodium/proton antiporter NhaA {ECO:0000255|HAMAP-Rule:MF_01844}; GN Name=nhaA {ECO:0000255|HAMAP-Rule:MF_01844}; GN OrderedLocusNames=HI_0225; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange CC for external protons. {ECO:0000255|HAMAP-Rule:MF_01844}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01844}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01844}. CC -!- SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter CC family. {ECO:0000255|HAMAP-Rule:MF_01844}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21894.1; -; Genomic_DNA. DR PIR; C64056; C64056. DR RefSeq; NP_438397.1; NC_000907.1. DR RefSeq; WP_005694067.1; NC_000907.1. DR ProteinModelPortal; P44581; -. DR SMR; P44581; 23-395. DR STRING; 71421.HI0225; -. DR EnsemblBacteria; AAC21894; AAC21894; HI_0225. DR GeneID; 951141; -. DR KEGG; hin:HI0225; -. DR PATRIC; 20188971; VBIHaeInf48452_0238. DR eggNOG; ENOG4105DRC; Bacteria. DR eggNOG; COG3004; LUCA. DR KO; K03313; -. DR OMA; IGYFWLS; -. DR OrthoDB; EOG61VZ7F; -. DR PhylomeDB; P44581; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central. DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central. DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central. DR GO; GO:0015992; P:proton transport; IBA:GO_Central. DR GO; GO:0006885; P:regulation of pH; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central. DR Gene3D; 1.20.1530.10; -; 1. DR HAMAP; MF_01844; NhaA; 1. DR InterPro; IPR023171; Na/H_antiporter_dom. DR InterPro; IPR004670; NhaA. DR PANTHER; PTHR30341:SF0; PTHR30341:SF0; 1. DR Pfam; PF06965; Na_H_antiport_1; 1. DR TIGRFAMs; TIGR00773; NhaA; 1. PE 3: Inferred from homology; KW Antiport; Cell inner membrane; Cell membrane; Complete proteome; KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 400 Na(+)/H(+) antiporter NhaA. FT /FTId=PRO_0000052411. FT TRANSMEM 26 46 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 71 91 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 107 127 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 137 157 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 166 186 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 189 209 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 225 245 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 273 293 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 299 319 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 340 360 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. FT TRANSMEM 373 393 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01844}. SQ SEQUENCE 400 AA; 42763 MW; C15A161C29489644 CRC64; MNFLLCIFKG VYVIKLIQRF FKLESAGGIL LLFSAVVAML LANSPLSNQY NDFLNLPVSL QIGSFSINKT LIHWINDGFM AVFFVLVGME VKKELFEGAL STYQQAIFPA IAAIGGMVIP AVVYWFIAKQ DPSLANGWAI PMATDIAFAL GIMALLSKQV PLPLKIFLLA LAIIDDLGAI VVIALFFSHG LSVQALIFSA VAIIVLILLN RFRVSALCAY MVVGAILWAS VLKSGVHATL AGVIIGFSIP LKGKKGERPL DDFEHILASW SSFVILPLFA FANAGVSFAG IDVNMISSPL LLAIASGLII GKPVGIFGFS YISVKLGLAK LPDGINFKQI FAVAVLCGIG FTMSMFLASL AFDANAGESV NTLSRLGILL GSTVSAILGY LFLKQTTKLN // ID NRFC_HAEIN Reviewed; 225 AA. AC P45015; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Protein NrfC homolog; DE Flags: Precursor; GN Name=nrfC; OrderedLocusNames=HI_1067; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probably involved in the transfer of electrons from the CC quinone pool to the type-c cytochromes. {ECO:0000250}. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22725.1; -; Genomic_DNA. DR PIR; A64181; A64181. DR RefSeq; NP_439225.1; NC_000907.1. DR RefSeq; WP_005647733.1; NC_000907.1. DR ProteinModelPortal; P45015; -. DR STRING; 71421.HI1067; -. DR EnsemblBacteria; AAC22725; AAC22725; HI_1067. DR GeneID; 950045; -. DR KEGG; hin:HI1067; -. DR PATRIC; 20190797; VBIHaeInf48452_1111. DR eggNOG; ENOG4105D3S; Bacteria. DR eggNOG; COG0437; LUCA. DR KO; K04014; -. DR OMA; CANACIA; -. DR OrthoDB; EOG6JTC8Q; -. DR PhylomeDB; P45015; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR017567; Cyt_c_NO2Rdtase_NrfC. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF13247; Fer4_11; 1. DR TIGRFAMs; TIGR03149; cyt_nit_nrfC; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Signal; KW Transport. FT SIGNAL 1 28 Tat-type signal. {ECO:0000255|PROSITE- FT ProRule:PRU00648}. FT CHAIN 29 225 Protein NrfC homolog. FT /FTId=PRO_0000008846. FT DOMAIN 39 67 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 85 116 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 118 147 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 48 48 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 51 51 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 58 58 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 94 94 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 97 97 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 102 102 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 106 106 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 127 127 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 130 130 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 133 133 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 137 137 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 154 154 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 157 157 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 170 170 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 174 174 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 225 AA; 25105 MW; F2E28CA9C9471CAB CRC64; MTVCSRRNFV SGMGAVILMT GTSLPAFAKE NKADKPKRYA MIHDENACIG CTACMDSCRD VNQVPEGVSR LEILRSEPYG EFPNQEYEFF RQSCQHCTNA PCVAVCPTGA SFIDKETGIV DVHKDLCIGC QYCIAVCPYR VRFIHPIHRT ADKCNFCRDT NLANGKQPAC VEACPTKALT FGDMNDPTSA VSRKVKEKPV YRTKVELGTQ PNLYHIPFQH GEPRR // ID NQRA_HAEIN Reviewed; 447 AA. AC P43955; P43956; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE Short=Na(+)-NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE Short=Na(+)-translocating NQR subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00425}; DE AltName: Full=NQR complex subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; DE AltName: Full=NQR-1 subunit A {ECO:0000255|HAMAP-Rule:MF_00425}; GN Name=nqrA {ECO:0000255|HAMAP-Rule:MF_00425}; GN OrderedLocusNames=HI_0164; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00425}. CC -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000255|HAMAP- CC Rule:MF_00425}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA62134.1; Type=Frameshift; Positions=63; 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; L42023; AAC21836.1; -; Genomic_DNA. DR EMBL; U20229; AAA62134.1; ALT_FRAME; Genomic_DNA. DR PIR; I64002; I64002. DR RefSeq; NP_438334.1; NC_000907.1. DR RefSeq; WP_005694115.1; NC_000907.1. DR ProteinModelPortal; P43955; -. DR STRING; 71421.HI0164; -. DR DNASU; 951076; -. DR EnsemblBacteria; AAC21836; AAC21836; HI_0164. DR GeneID; 951076; -. DR KEGG; hin:HI0164; -. DR PATRIC; 20188827; VBIHaeInf48452_0170. DR eggNOG; ENOG4105DWQ; Bacteria. DR eggNOG; COG1726; LUCA. DR KO; K00346; -. DR OMA; DYHGMKP; -. DR OrthoDB; EOG6VMTG5; -. DR PhylomeDB; P43955; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00425; NqrA; 1. DR InterPro; IPR008703; NqrA. DR InterPro; IPR022615; NqrA_C_domain. DR Pfam; PF05896; NQRA; 1. DR Pfam; PF11973; NQRA_SLBB; 1. DR TIGRFAMs; TIGR01936; nqrA; 1. PE 1: Evidence at protein level; KW Complete proteome; Ion transport; NAD; Oxidoreductase; KW Reference proteome; Sodium; Sodium transport; Transport; Ubiquinone. FT CHAIN 1 447 Na(+)-translocating NADH-quinone FT reductase subunit A. FT /FTId=PRO_0000214198. SQ SEQUENCE 447 AA; 48884 MW; 4670C93FB5FF0912 CRC64; MITIKKGLDL PIAGKPAQVI HSGNAVNQVA ILGEEYVGMR PSMKVREGDV VKKGQVLFED KKNPGVIFTA PASGTITAIN RGEKRVLQSV VINVEGDEKI TFAKYSTEQL NTLSSEQVKQ NLIESGLWTA LRTRPFSKVP SIESEASSIF VNAMDTNPLA ADPSVVLKEY SQDFTNGLTV LSRLFPSKPL HLCKAGDSNI PTADLENLQI HDFTGVHPAG LVGTHIHFID PVGIQKTVWH INYQDVIAVG KLFTTGELYS ERVISLAGPQ VKEPRLVRTT IGANLSQLTQ NELSAGKNRV ISGSVLCGQI AKDSHDYLGR YALQVSVIAE GNEKEFFGWI MPQANKYSVT RTVLGHFSKK LFNFTTSENG GERAMVPIGS YERVMPLDIL PTLLLRDLIV GDTDGAQELG CLELDEEDLA LCSFVCPGKY EYGSILRQVL DKIEKEG // ID NRFA_HAEIN Reviewed; 538 AA. AC P45017; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 128. DE RecName: Full=Cytochrome c-552 {ECO:0000255|HAMAP-Rule:MF_01182}; DE EC=1.7.2.2 {ECO:0000255|HAMAP-Rule:MF_01182}; DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182}; DE Short=Cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182}; DE Flags: Precursor; GN Name=nrfA {ECO:0000255|HAMAP-Rule:MF_01182}; GN OrderedLocusNames=HI_1069; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming CC six electrons in the process. {ECO:0000255|HAMAP-Rule:MF_01182}. CC -!- CATALYTIC ACTIVITY: NH(3) + 2 H(2)O + 6 ferricytochrome c = CC nitrite + 6 ferrocytochrome c + 7 H(+). {ECO:0000255|HAMAP- CC Rule:MF_01182}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01182}; CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP- CC Rule:MF_01182}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01182}; CC Note=Binds 5 heme groups covalently per monomer. CC {ECO:0000255|HAMAP-Rule:MF_01182}; CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC {ECO:0000255|HAMAP-Rule:MF_01182}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01182}. CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. CC {ECO:0000255|HAMAP-Rule:MF_01182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22727.1; -; Genomic_DNA. DR PIR; C64181; C64181. DR RefSeq; NP_439227.3; NC_000907.1. DR RefSeq; WP_005690769.1; NC_000907.1. DR ProteinModelPortal; P45017; -. DR SMR; P45017; 75-532. DR STRING; 71421.HI1069; -. DR EnsemblBacteria; AAC22727; AAC22727; HI_1069. DR GeneID; 950047; -. DR KEGG; hin:HI1069; -. DR PATRIC; 20190801; VBIHaeInf48452_1113. DR eggNOG; ENOG4105EAU; Bacteria. DR eggNOG; COG3303; LUCA. DR KO; K03385; -. DR OMA; CHEKGKS; -. DR OrthoDB; EOG6K3ZWZ; -. DR PhylomeDB; P45017; -. DR UniPathway; UPA00653; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0020037; F:heme binding; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IBA:GO_Central. DR GO; GO:0019645; P:anaerobic electron transport chain; IBA:GO_Central. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01182; Cytochrom_C552; 1. DR InterPro; IPR003321; Cyt_c552. DR InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF02335; Cytochrom_C552; 1. DR PIRSF; PIRSF000243; Cyt_c552; 1. DR SUPFAM; SSF48695; SSF48695; 1. DR TIGRFAMs; TIGR03152; cyto_c552_HCOOH; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 3: Inferred from homology; KW Calcium; Complete proteome; Electron transport; Heme; Iron; KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal; KW Transport. FT SIGNAL 1 55 {ECO:0000255|HAMAP-Rule:MF_01182}. FT CHAIN 56 538 Cytochrome c-552. FT /FTId=PRO_0000006579. FT METAL 133 133 Iron (heme 3 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 165 165 Iron (heme 1 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 203 203 Iron (heme 2 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 268 268 Iron (heme 3 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 270 270 Calcium. {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT METAL 271 271 Calcium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 316 316 Calcium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 318 318 Calcium. {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT METAL 330 330 Iron (heme 5 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 341 341 Iron (heme 4 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 356 356 Iron (heme 2 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 373 373 Iron (heme 5 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT METAL 448 448 Iron (heme 4 axial ligand). FT {ECO:0000255|HAMAP-Rule:MF_01182}. FT BINDING 161 161 Heme 1 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 164 164 Heme 1 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 199 199 Heme 2 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 202 202 Heme 2 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 264 264 Heme 3 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 267 267 Heme 3 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 271 271 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 319 319 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 337 337 Heme 4 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 340 340 Heme 4 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 369 369 Heme 5 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. FT BINDING 372 372 Heme 5 (covalent). {ECO:0000255|HAMAP- FT Rule:MF_01182}. SQ SEQUENCE 538 AA; 60400 MW; 48E64B46F2FB9CBB CRC64; MKIYLRFVWI LIIILNFLLN LFITTNGVII VNAFKKSLIV AASFASLSLF NSATAELVYK PLEQPVEPAK PDLKIESVNE KFAEKYPNQY NSWRSTANGD GENIIYADEE NPRLIVLWGG YAFAKEYNAP RGHFYAVTDV RNILRTGAPK TANDGPQAMA CWTCKGPDVP RLIAEWGEKD YFNAKWAKGG PEIVNSIGCA DCHDTTSKDF AEGKPALRIA RPHVLRALDA LEKATAEKDK AEGRPHNNLS FNTAARTEKR AEICANCHVE YYFAGDIKQV TFPWDNGQTV DDIEKYYDDI GFTDWTHSLS KAPMLKAQHP DFEIWSLGMH GKNGVTCVDC HMPKVQGADG KVYTDHQIQN PFEAFDSTCA NCHDQSKEKL RDIVTSRKKE VKDVMGRLED QVVKAHFEAK EAWDAGATKK EMEAALMDIR HAQWRWDYTA ASHGGHMHAP EVVLRVLASG LDKVADARTK LAVILTKHGV KTPVQIPDIS TADKAWKVMG IDIEKERKAK EEFLKTVVPQ WEQQAREKGL LVDPPAQK // ID NRFB_HAEIN Reviewed; 226 AA. AC P45016; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=Cytochrome c-type protein NrfB; DE Flags: Precursor; GN Name=nrfB; OrderedLocusNames=HI_1068; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a role in nitrite reduction. {ECO:0000250}. CC -!- PATHWAY: Energy metabolism; nitrogen metabolism. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- PTM: Binds 5 heme groups per subunit. {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; L42023; AAC22726.1; -; Genomic_DNA. DR PIR; B64181; B64181. DR RefSeq; NP_439226.2; NC_000907.1. DR ProteinModelPortal; P45016; -. DR STRING; 71421.HI1068; -. DR EnsemblBacteria; AAC22726; AAC22726; HI_1068. DR GeneID; 950046; -. DR KEGG; hin:HI1068; -. DR PATRIC; 20190799; VBIHaeInf48452_1112. DR eggNOG; ENOG4105JJ8; Bacteria. DR eggNOG; ENOG411128Q; LUCA. DR KO; K04013; -. DR OMA; EQNQVCF; -. DR OrthoDB; EOG62ZHTD; -. DR UniPathway; UPA00045; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017564; Cyt_c_NO2Rdtase_pentahaem-su. DR InterPro; IPR011031; Multihaem_cyt. DR SUPFAM; SSF48695; SSF48695; 1. DR TIGRFAMs; TIGR03146; cyt_nit_nrfB; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Heme; Iron; Metal-binding; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 39 {ECO:0000255}. FT CHAIN 40 226 Cytochrome c-type protein NrfB. FT /FTId=PRO_0000006586. FT METAL 69 69 Iron (heme 1 axial ligand). FT {ECO:0000250}. FT METAL 114 114 Iron (heme 2 axial ligand). FT {ECO:0000250}. FT METAL 156 156 Iron (heme 3 axial ligand). FT {ECO:0000250}. FT METAL 181 181 Iron (heme 4 axial ligand). FT {ECO:0000250}. FT METAL 206 206 Iron (heme 5 axial ligand). FT {ECO:0000250}. FT BINDING 65 65 Heme 1 (covalent). {ECO:0000250}. FT BINDING 68 68 Heme 1 (covalent). {ECO:0000250}. FT BINDING 110 110 Heme 2 (covalent). {ECO:0000250}. FT BINDING 113 113 Heme 2 (covalent). {ECO:0000250}. FT BINDING 152 152 Heme 3 (covalent). {ECO:0000250}. FT BINDING 155 155 Heme 3 (covalent). {ECO:0000250}. FT BINDING 177 177 Heme 4 (covalent). {ECO:0000250}. FT BINDING 180 180 Heme 4 (covalent). {ECO:0000250}. FT BINDING 202 202 Heme 5 (covalent). {ECO:0000250}. FT BINDING 205 205 Heme 5 (covalent). {ECO:0000250}. SQ SEQUENCE 226 AA; 25664 MW; 959F2DCEA668030A CRC64; MIFKVKFEVT QMILTSLINK SAKALVIVAF VAAPFLAHAD DAQKPAVHVT YEPQLDNQRD PNQYCAKCHK FDKIDKNQTL DQSGGELHFG KFHGAHLDKK NPNNGKAITC VSCHGNISEN HRRGAKDVMR FEGDIFGNKK PMYSVQEQNQ VCFACHQPDK LREKLWAHDV HAMKLPCASC HTLHPKEDAM KGIQPKQRVK LCVDCHGEQQ KRKAEQDKLI EQKDKL // ID NRFF_HAEIN Reviewed; 384 AA. AC P44942; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 11-MAY-2016, entry version 111. DE RecName: Full=Formate-dependent nitrite reductase complex bifunctional subunit NrfFG; DE Flags: Precursor; GN Name=nrfF; OrderedLocusNames=HI_0934; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Possible subunit of a heme lyase. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CcmH/CycL/Ccl2/NrfF family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22592.1; -; Genomic_DNA. DR PIR; H64161; H64161. DR RefSeq; NP_439094.1; NC_000907.1. DR RefSeq; WP_005693281.1; NC_000907.1. DR ProteinModelPortal; P44942; -. DR SMR; P44942; 37-114. DR STRING; 71421.HI0934; -. DR EnsemblBacteria; AAC22592; AAC22592; HI_0934. DR GeneID; 949938; -. DR KEGG; hin:HI0934; -. DR PATRIC; 20190525; VBIHaeInf48452_0975. DR eggNOG; ENOG4108DMF; Bacteria. DR eggNOG; COG3088; LUCA. DR eggNOG; COG4235; LUCA. DR KO; K04017; -. DR KO; K04018; -. DR OMA; EQVIARM; -. DR OrthoDB; EOG679TDV; -. DR PhylomeDB; P44942; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005616; CcmH/CycL/Ccl2/NrfF. DR InterPro; IPR017565; For-dep_Cytc_NO2Rdtase_NrfF. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF03918; CcmH; 1. DR SMART; SM00028; TPR; 1. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR03147; cyt_nit_nrfF; 1. DR PROSITE; PS50005; TPR; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Heme; Iron; Metal-binding; Periplasm; KW Reference proteome; Repeat; Signal; TPR repeat. FT SIGNAL 1 35 {ECO:0000255}. FT CHAIN 36 384 Formate-dependent nitrite reductase FT complex bifunctional subunit NrfFG. FT /FTId=PRO_0000006616. FT REPEAT 221 254 TPR 1. FT REPEAT 255 288 TPR 2. FT REGION 36 144 NrfF. FT REGION 180 384 NrfG. FT BINDING 61 61 Heme (covalent). {ECO:0000255}. FT BINDING 64 64 Heme (covalent). {ECO:0000255}. SQ SEQUENCE 384 AA; 43780 MW; 0321F4A7704964C4 CRC64; MKSILDIFTR GFIQVQKTVF FATALLFAFS LFTQAEMVDT YQFQNQDDRT RAVELAKSLR CPQCQNQNLV ESNSPIAYDL RLEVYKMVDE GKSNQQIIDK MTARFGDFVN YKPPFKWNTA LLWLLPVALL ILAAVLLYFS NRKKQFSEKV VAQQLENDEI ISLPSTFGSS PRKQGEPSKL SKGKVNSKIY FVLFTLLIAI PATYYFSLDR FSRVQQGEQS MIEQHNQNVE MNDEHKNENV IEKLQNKLRT DPNNAETWLQ LGEAYVQNNE FDSALVAYSN AEKLSGSKPN ILGLAATALY YQAGQQMTQK VEQLLNEALA KDKNEVSSLS LLATIALENR QYQQAGMYLQ QLLDSGNAAV DRRSVIQRMK MLDFLQRGEK GQNP // ID NQRD_HAEIN Reviewed; 208 AA. AC P43958; P43959; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 105. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE Short=Na(+)-NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE Short=Na(+)-translocating NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00428}; DE AltName: Full=NQR complex subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; DE AltName: Full=NQR-1 subunit D {ECO:0000255|HAMAP-Rule:MF_00428}; GN Name=nqrD {ECO:0000255|HAMAP-Rule:MF_00428}; GN OrderedLocusNames=HI_0168; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00428}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00428}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00428}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00428}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21839.1; -; Genomic_DNA. DR PIR; C64003; C64003. DR PIR; D64003; D64003. DR RefSeq; NP_438337.1; NC_000907.1. DR RefSeq; WP_005648665.1; NC_000907.1. DR STRING; 71421.HI0168; -. DR EnsemblBacteria; AAC21839; AAC21839; HI_0168. DR GeneID; 951073; -. DR KEGG; hin:HI0168; -. DR PATRIC; 20188833; VBIHaeInf48452_0173. DR eggNOG; ENOG4105F5D; Bacteria. DR eggNOG; COG1347; LUCA. DR KO; K00349; -. DR OMA; PSKIRII; -. DR OrthoDB; EOG6GBMG7; -. DR PhylomeDB; P43958; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00428; NqrD; 1. DR InterPro; IPR011292; NqrD. DR InterPro; IPR003667; Rnf-Nqr. DR PANTHER; PTHR30586:SF1; PTHR30586:SF1; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01939; nqrD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 208 Na(+)-translocating NADH-quinone FT reductase subunit D. FT /FTId=PRO_0000214234. FT TRANSMEM 42 62 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 72 92 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 103 123 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 131 151 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. FT TRANSMEM 178 198 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00428}. SQ SEQUENCE 208 AA; 22528 MW; EC988B5A1BC87C79 CRC64; MSGKTSYKDL LLAPIAKNNP IALQILGICS ALAVTTKLET AFVMAIAVTL VTGLSNLFVS LIRNYIPNSI RIIVQLAIIA SLVIVVDQIL KAYAYGLSKQ LSVFVGLIIT NCIVMGRAEA FAMKSPPVES FVDGIGNGLG YGSMLIIVAF FRELIGSGKL FGMTIFETIQ NGGWYQANGL FLLAPSAFFI IGFVIWGLRT WKPEQQEK // ID NRFE_HAEIN Reviewed; 635 AA. AC P44944; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Cytochrome c-type biogenesis protein NrfE; GN Name=nrfE; OrderedLocusNames=HI_0936; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the biogenesis of c-type cytochromes. CC Possible subunit of a heme lyase (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA 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; L42023; AAC22594.1; -; Genomic_DNA. DR PIR; A64162; A64162. DR RefSeq; NP_439096.1; NC_000907.1. DR RefSeq; WP_005693283.1; NC_000907.1. DR STRING; 71421.HI0936; -. DR EnsemblBacteria; AAC22594; AAC22594; HI_0936. DR GeneID; 950731; -. DR KEGG; hin:HI0936; -. DR PATRIC; 20190529; VBIHaeInf48452_0977. DR eggNOG; ENOG4105DA4; Bacteria. DR eggNOG; COG1138; LUCA. DR KO; K04016; -. DR OMA; IPERRYY; -. DR OrthoDB; EOG6RRKJ4; -. DR PhylomeDB; P44944; -. DR Proteomes; UP000000579; 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:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0015232; F:heme transporter activity; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR InterPro; IPR032523; CcmF_C. DR InterPro; IPR002541; Cyt_c_assembly. DR InterPro; IPR003567; Cyt_c_biogenesis. DR InterPro; IPR003568; Cyt_c_biogenesis_CcmF. DR InterPro; IPR003570; Cyt_c_biogenesis_NrfE. DR InterPro; IPR017563; CytC_NO3Rdtase_biogenesis_NrfE. DR PANTHER; PTHR30009:SF0; PTHR30009:SF0; 2. DR Pfam; PF16327; CcmF_C; 1. DR Pfam; PF01578; Cytochrom_C_asm; 1. DR PRINTS; PR01410; CCBIOGENESIS. DR PRINTS; PR01413; NRFEBIOGNSIS. DR TIGRFAMs; TIGR03145; cyt_nit_nrfE; 1. DR TIGRFAMs; TIGR00353; nrfE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 635 Cytochrome c-type biogenesis protein FT NrfE. FT /FTId=PRO_0000201590. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 209 229 Helical. {ECO:0000255}. FT TRANSMEM 239 259 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. FT TRANSMEM 390 410 Helical. {ECO:0000255}. FT TRANSMEM 421 441 Helical. {ECO:0000255}. FT TRANSMEM 452 472 Helical. {ECO:0000255}. FT TRANSMEM 483 503 Helical. {ECO:0000255}. FT TRANSMEM 570 590 Helical. {ECO:0000255}. FT TRANSMEM 607 627 Helical. {ECO:0000255}. SQ SEQUENCE 635 AA; 71274 MW; B979E54F1ED534FC CRC64; MLPELGFFLL LLATASAFFL ALVPQFGLFK KNPTLINAAW PLSYIFTLAT TLSIGLLAYS FAVDDFTLEY VAAHSNSQLP TFFKVAATWG GHEGSMLFWL FSLSLWLAAF AFFNRKNDRT FSAQSLSLLG LICFGFAVFI LFYSNPFGRI FPAPAEGRDL NPMLQDVGLI FHPPLLYVGY VGFAVNFAMS LSALIYNQSA RQIARSMRGW VLVSWLFLTI GIVLGAWWAY YELGWGGWWF WDPVENASLM PWLLGLALLH SLMATEKQGV FSYWTTLFSL LAFAFSVLGT FIVRSGALTS VHAFALDNTR GYVLLLIFFV LTALAFGLFA LRAGSSSESA VKFQFISKSG GILLLNILLT IATVSTFLGT FYPMLFQAMN WGSISVGSPY FNSIFFPIIT AILILMVIVL SIRKGQFDRT LLIRCGWLLI PSLILAGLMI WQQLRNNSAL HFHAFAFVLL TLAIWLLFVT LWQNWRQIRL SQFGMILAHC GVAIVTIGAV MSGYFGSEIG VRLAPQQSQT LGQYEFHYRQ FSNEIGPNFT AEVAFFDVTK NGKPYAEIIP ERRYYDVRTM TMSEVGLDGG FWGDLYIVMG DSLGKGEFTF RLHYKPLIRW LWAGGILMAF GALFSVFGLR RKQEK // ID NRFX_HAEIN Reviewed; 176 AA. AC P44943; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Probable thiol:disulfide interchange protein DsbE-2; DE AltName: Full=Cytochrome c biogenesis protein NrfX; GN Name=nrfX; Synonyms=dsbE-2; OrderedLocusNames=HI_0935; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be involved in disulfide bond formation. Could CC catalyzes a late, reductive step in the assembly of periplasmic CC NrfA c-type cytochrome, probably the reduction of disulfide bonds CC of the apocytochrome c to allow covalent linkage with the heme. CC Possible subunit of a heme lyase. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass membrane protein {ECO:0000305}; Periplasmic side CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22593.1; -; Genomic_DNA. DR PIR; I64161; I64161. DR RefSeq; NP_439095.1; NC_000907.1. DR RefSeq; WP_005693282.1; NC_000907.1. DR ProteinModelPortal; P44943; -. DR STRING; 71421.HI0935; -. DR EnsemblBacteria; AAC22593; AAC22593; HI_0935. DR GeneID; 949930; -. DR KEGG; hin:HI0935; -. DR PATRIC; 20190527; VBIHaeInf48452_0976. DR eggNOG; ENOG4107QX9; Bacteria. DR eggNOG; COG0526; LUCA. DR KO; K02199; -. DR OMA; APETYLV; -. DR OrthoDB; EOG6WX4Q5; -. DR PhylomeDB; P44943; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00385; dsbE; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Cytochrome c-type biogenesis; Disulfide bond; Membrane; KW Redox-active center; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 176 Probable thiol:disulfide interchange FT protein DsbE-2. FT /FTId=PRO_0000201307. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TOPO_DOM 26 176 Periplasmic. {ECO:0000255}. FT DOMAIN 35 175 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 75 78 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 176 AA; 19926 MW; 078B408F97A8E48B CRC64; MNKKLIFFTP LFVLLGVCIL LIAGLNQDPK KIASALIDKP VPEFYQANLH EPSQIVSPKE FPKQPFLLNV WGSWCGYCKE EHPLLIEIAK TLPIVGVDYR DNRQNGIKML KRMGNPFILT IDDSHGELGL KLGVDGAPET YLVDENGVIR YRHSGLLDKE TWQTVFLPKI EALKNK // ID NQRC_HAEIN Reviewed; 244 AA. AC P43957; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE Short=Na(+)-NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE Short=Na(+)-translocating NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR complex subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR-1 subunit C {ECO:0000255|HAMAP-Rule:MF_00427}; GN Name=nqrC {ECO:0000255|HAMAP-Rule:MF_00427}; GN OrderedLocusNames=HI_0167; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00427}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00427}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00427}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00427}. CC -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP- CC Rule:MF_00427}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21838.1; -; Genomic_DNA. DR PIR; B64003; B64003. DR RefSeq; NP_438336.1; NC_000907.1. DR RefSeq; WP_005653794.1; NC_000907.1. DR STRING; 71421.HI0167; -. DR EnsemblBacteria; AAC21838; AAC21838; HI_0167. DR GeneID; 951074; -. DR KEGG; hin:HI0167; -. DR PATRIC; 20188831; VBIHaeInf48452_0172. DR eggNOG; ENOG4106I92; Bacteria. DR eggNOG; COG2869; LUCA. DR KO; K00348; -. DR OMA; IKGITYY; -. DR OrthoDB; EOG6F2981; -. DR PhylomeDB; P43957; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. 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:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00427; NqrC; 1. DR InterPro; IPR007329; FMN-bd. DR InterPro; IPR010204; NqrC. DR Pfam; PF04205; FMN_bind; 1. DR PIRSF; PIRSF009437; NQR-1_subunit_C; 1. DR SMART; SM00900; FMN_bind; 1. DR TIGRFAMs; TIGR01938; nqrC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein; KW FMN; Ion transport; Membrane; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 244 Na(+)-translocating NADH-quinone FT reductase subunit C. FT /FTId=PRO_0000214216. FT TRANSMEM 13 33 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00427}. FT MOD_RES 213 213 FMN phosphoryl threonine. FT {ECO:0000255|HAMAP-Rule:MF_00427}. SQ SEQUENCE 244 AA; 26662 MW; 852560EE2CF1FAC8 CRC64; MAKFNKDSVG GTILVVLLLS LVCSIIVAGS AVMLKPAQEE QKLLDKQKNI LNVAGLLQEN TNVKETYAKF IEPRFVDLAT GEYTQQADDS QQAIPADADK ARIRSRSKTT EVYLVKDEQG QTQQVILPIY GTGLWSVMYG LVSVQPDGNT INGITYYQHG ETPGLGGEIE NPNWASLFKG KKLFDEQHQP AIRIVKGQAP QDEHSIDGLS GATLTGNGVQ GTFNYWFSKD GFGPYLEKLH SGAN // ID NQRE_HAEIN Reviewed; 198 AA. AC P71342; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE Short=Na(+)-NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE Short=Na(+)-translocating NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00429}; DE AltName: Full=NQR complex subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; DE AltName: Full=NQR-1 subunit E {ECO:0000255|HAMAP-Rule:MF_00429}; GN Name=nqrE {ECO:0000255|HAMAP-Rule:MF_00429}; GN OrderedLocusNames=HI_0170; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00429}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00429}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00429}. CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP- CC Rule:MF_00429}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21840.1; -; Genomic_DNA. DR RefSeq; NP_438338.1; NC_000907.1. DR RefSeq; WP_010868950.1; NC_000907.1. DR STRING; 71421.HI0170; -. DR EnsemblBacteria; AAC21840; AAC21840; HI_0170. DR GeneID; 951077; -. DR KEGG; hin:HI0170; -. DR PATRIC; 20188835; VBIHaeInf48452_0174. DR eggNOG; ENOG4108IUB; Bacteria. DR eggNOG; COG2209; LUCA. DR KO; K00350; -. DR OMA; YFLGMCS; -. DR OrthoDB; EOG6GBMG7; -. DR PhylomeDB; P71342; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. 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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00429; NqrE; 1. DR InterPro; IPR010967; NqrE. DR InterPro; IPR003667; Rnf-Nqr. DR PANTHER; PTHR30335:SF1; PTHR30335:SF1; 1. DR Pfam; PF02508; Rnf-Nqr; 1. DR PIRSF; PIRSF006102; NQR_DE; 1. DR TIGRFAMs; TIGR01940; nqrE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 198 Na(+)-translocating NADH-quinone FT reductase subunit E. FT /FTId=PRO_0000214252. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 35 55 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 77 97 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 110 130 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 140 160 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. FT TRANSMEM 176 196 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00429}. SQ SEQUENCE 198 AA; 21306 MW; 29C6544D4BF71BDE CRC64; MEHYISLFVK AVFIENMALS FFLGMCTFLA VSKKVSPAFG LGIAVTFVLG IAVPVNQLIY ANVLKENALI EGVDLSFLNF ITFIGVIAGL VQILEMVLDK FMPSLYNALG IFLPLIAVNC AIFGGVSFMV QRDYNFPESI VYGFGSGLGW MLAIVALAGL TEKMKYADIP AGLKGLGITF ISVGLMALGF MSFSGIQL // ID NQRF_HAEIN Reviewed; 411 AA. AC O05012; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 124. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE Short=Na(+)-NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE Short=Na(+)-translocating NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00430}; DE AltName: Full=NQR complex subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; DE AltName: Full=NQR-1 subunit F {ECO:0000255|HAMAP-Rule:MF_00430}; GN Name=nqrF {ECO:0000255|HAMAP-Rule:MF_00430}; GN OrderedLocusNames=HI_0171; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. The first step CC is catalyzed by NqrF, which accepts electrons from NADH and CC reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer CC pathway. {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00430}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00430}. CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP- CC Rule:MF_00430}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00430}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00430}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21841.1; -; Genomic_DNA. DR PIR; D64052; D64052. DR RefSeq; NP_438339.1; NC_000907.1. DR RefSeq; WP_005648666.1; NC_000907.1. DR ProteinModelPortal; O05012; -. DR SMR; O05012; 132-410. DR STRING; 71421.HI0171; -. DR EnsemblBacteria; AAC21841; AAC21841; HI_0171. DR GeneID; 951079; -. DR KEGG; hin:HI0171; -. DR PATRIC; 20188837; VBIHaeInf48452_0175. DR eggNOG; ENOG4105D26; Bacteria. DR eggNOG; COG2871; LUCA. DR KO; K00351; -. DR OMA; EEHGIIM; -. DR OrthoDB; EOG6JHRM2; -. DR PhylomeDB; O05012; -. DR Proteomes; UP000000579; 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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.30; -; 1. DR HAMAP; MF_00430; NqrF; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR010205; NqrF. DR InterPro; IPR008333; OxRdtase_FAD-bd_dom. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000044; Cis_Diol_DH_RD; 1. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF54292; SSF54292; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR TIGRFAMs; TIGR01941; nqrF; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 3: Inferred from homology; KW 2Fe-2S; Cell inner membrane; Cell membrane; Complete proteome; FAD; KW Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Sodium; KW Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubiquinone. FT CHAIN 1 411 Na(+)-translocating NADH-quinone FT reductase subunit F. FT /FTId=PRO_0000074496. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT DOMAIN 36 130 2Fe-2S ferredoxin-type. FT {ECO:0000255|HAMAP-Rule:MF_00430}. FT DOMAIN 133 273 FAD-binding FR-type. {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT REGION 276 393 Catalytic. FT METAL 73 73 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 79 79 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 82 82 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. FT METAL 114 114 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_00430}. SQ SEQUENCE 411 AA; 45705 MW; ED560053E66D23E0 CRC64; MSDSVILALG IAAFTVIVLV LVAIILFAKS KLVDSGDITI DINDDPEKAI TLPAGGKLLG ALASKGIFVS SACGGGGSCG QCIVKVKNGG GEILPTELSH INKREAKEGY RLACQVNVKG NMEVELPEEI FGVKKWECTV ISNDNKATFI KELKLAIPEG EEVPFRAGGY IQIEAEPHVV NYKDFDIPEE YHEDWDKYDL WRYVSKVDEH IIRAYSMASY PEEKGIIMLN VRIATPPPRQ PDAPPGQMSS YIWSLKAGDK VTISGPFGEF FAKETDAEMV FIGGGAGMAP MRSHIFDQLK RLHSKRKMSF WYGARSKREI FYQEDFDQLQ AENPNFVWHV ALSDALPEDN WTGYTGFIHN VLYENYLKNH EAPEDCEYYM CGPPVMNAAV IKMLKDLGVE DENILLDDFG G // ID NQRB_HAEIN Reviewed; 411 AA. AC O05011; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE Short=Na(+)-NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE Short=Na(+)-translocating NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE EC=1.6.5.8 {ECO:0000255|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR complex subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR-1 subunit B {ECO:0000255|HAMAP-Rule:MF_00426}; GN Name=nqrB {ECO:0000255|HAMAP-Rule:MF_00426}; GN OrderedLocusNames=HI_0166; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION AS NQR SYSTEM. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7; RA Hayashi M., Nakayama Y., Unemoto T.; RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus RT influenzae."; RL FEBS Lett. 381:174-176(1996). CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport CC of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE CC are probably involved in the second step, the conversion of CC ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000255|HAMAP-Rule:MF_00426}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00426}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00426}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP- CC Rule:MF_00426}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21837.1; -; Genomic_DNA. DR PIR; C64052; C64052. DR RefSeq; NP_438335.1; NC_000907.1. DR RefSeq; WP_005653793.1; NC_000907.1. DR STRING; 71421.HI0166; -. DR EnsemblBacteria; AAC21837; AAC21837; HI_0166. DR GeneID; 951078; -. DR KEGG; hin:HI0166; -. DR PATRIC; 20188829; VBIHaeInf48452_0171. DR eggNOG; ENOG4108J5C; Bacteria. DR eggNOG; COG1805; LUCA. DR KO; K00347; -. DR OMA; TVFYTPG; -. DR OrthoDB; EOG65BDMX; -. DR PhylomeDB; O05011; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00426; NqrB; 1. DR InterPro; IPR004338; NADH_Q_Rdtase_NQR2_RnfD. DR InterPro; IPR010966; NqrB. DR PANTHER; PTHR30578:SF1; PTHR30578:SF1; 1. DR Pfam; PF03116; NQR2_RnfD_RnfE; 1. DR PIRSF; PIRSF016055; NADH-UbQ_OxRdtase_B_su; 1. DR TIGRFAMs; TIGR01937; nqrB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Flavoprotein; KW FMN; Ion transport; Membrane; NAD; Oxidoreductase; Phosphoprotein; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 411 Na(+)-translocating NADH-quinone FT reductase subunit B. FT /FTId=PRO_0000074437. FT TRANSMEM 56 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 120 140 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 166 186 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 272 292 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 294 314 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 319 339 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 348 368 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 378 398 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00426}. FT MOD_RES 233 233 FMN phosphoryl threonine. FT {ECO:0000255|HAMAP-Rule:MF_00426}. SQ SEQUENCE 411 AA; 44729 MW; 73FF259A9ED9DAC2 CRC64; MGLKNLFEKM EPAFLPGGKY SKLYPIFESI YTLLYTPGTV THKNTHVRDA LDSKRMMITV FLALFPAIFY GMYNVGNQAI PALNQLGNLD QLIANDWHYA LASSLGLDLT ANATWGSKMA LGAIFFLPIY LVVFTVCTIW ELLFSVVRGH EVNEGMFVST ILFALIVPPT LPLWQAALGI TFGIIVAKEI FGGVGRNFMN PALAGRAFLF FAYPAQISGD TVWTAADGFS GATALSQWSQ GGQGALQHTV TGAPITWMDA FVGNLPGSMG EVSTLAILIG GAVIVFTRIA AWRIIAGVMI GMIATSTLFN LIGSETNPMF SMPWHWHFVL GGFALGMVFM ATDPVSASFT NTGKWWYGAL IGVMAVLIRT VNPAYPEGMM LAILFANLFA PIFDYIVVQA NIKRRRARTN G // ID NRDD_HAEIN Reviewed; 707 AA. AC P43752; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 102. DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase; DE EC=1.17.4.2; GN Name=nrdD; OrderedLocusNames=HI_0075; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside triphosphate + CC thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + CC thioredoxin. CC -!- SUBUNIT: Tetramer consisting of 2 alpha (NrdD) and 2 beta (NrdG) CC subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate CC reductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|PROSITE- CC ProRule:PRU00492}. CC -!- SIMILARITY: Contains 1 glycine radical domain. CC {ECO:0000255|PROSITE-ProRule:PRU00493}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21751.1; -; Genomic_DNA. DR PIR; A64047; A64047. DR RefSeq; NP_438248.1; NC_000907.1. DR RefSeq; WP_005693847.1; NC_000907.1. DR ProteinModelPortal; P43752; -. DR SMR; P43752; 124-670. DR STRING; 71421.HI0075; -. DR EnsemblBacteria; AAC21751; AAC21751; HI_0075. DR GeneID; 950970; -. DR KEGG; hin:HI0075; -. DR PATRIC; 20188605; VBIHaeInf48452_0076. DR eggNOG; ENOG4105CJD; Bacteria. DR eggNOG; COG1328; LUCA. DR KO; K00527; -. DR OMA; YSYDRVP; -. DR OrthoDB; EOG622PMK; -. DR PhylomeDB; P43752; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR019777; Form_AcTrfase_GR_CS. DR InterPro; IPR001150; Gly_radical. DR InterPro; IPR012833; NrdD. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF13597; NRDD; 1. DR TIGRFAMs; TIGR02487; NrdD; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00850; GLY_RADICAL_1; 1. DR PROSITE; PS51149; GLY_RADICAL_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; Organic radical; KW Oxidoreductase; Reference proteome. FT CHAIN 1 707 Anaerobic ribonucleoside-triphosphate FT reductase. FT /FTId=PRO_0000166684. FT DOMAIN 4 95 ATP-cone. {ECO:0000255|PROSITE- FT ProRule:PRU00492}. FT DOMAIN 584 707 Glycine radical. {ECO:0000255|PROSITE- FT ProRule:PRU00493}. FT MOD_RES 682 682 Glycine radical. {ECO:0000255|PROSITE- FT ProRule:PRU00493}. SQ SEQUENCE 707 AA; 80233 MW; A3795F7921A6781D CRC64; MSNFGVIKRD GSRAEFEIQR IINAIKKAAS AVNISDEFYC HQIGQEVGNE IFTRHQGEID INQIQKIVED KLMASRYPEV ARAYIEYRHD RDLAREKRSQ LTKEIEGLIE QSNVELLNEN ANKDAKVIPT QRDLLAGIVA KHYAKHNILP RDVVEAHEKG EIHYHDLDYA PFFPMFNCML VDLEGMLSRG FKMGNAEIEP PKSIGTATAV TAQIIAQVAS HIYGGTTINR IDEVLSPYVQ ISYEKHLKHA QEWNVPDVEG YAKALIEKEC FDAFQSLEYE VNTLHTSNGQ TPFVTFGFGL GTSWQSRLIQ QAILKNRIRG LGKNHKTPVF PKLVFTIKKG LNQNKGDPNY DIKQLALECA SKRMYPDILN YDQVVKVTGS FKAPMGCRSF LGAYEEKGHE IHDGRNNLGV VSLNLPRIAL ESKNEEDFYR TLDERLAIAK KALMTRIARL ENTKARVAPI LYMEGACGVR LKADENVAQI FKNGRASISL GYIGIHETIN ALYNKGHIFD DEQLREKGIA IVRHLSEAVK RWQKETGYAF SLYSTPSENL CDRFCRLDTK KFGVIEGVTD KGYYTNSYHL DVEKKVNPYD KLDFEMTYPP LASGGFICYG EYPNIQHNLK ALEDVWDYSY DRVPYYGTNT PIDECYECGF TGEFECTSKG FVCPKCGNHD STKVSVTRRV CGYLGSPDAR PFNAGKQEEV KRRVKHL // ID NRDG_HAEIN Reviewed; 155 AA. AC P45080; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 100. DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein; DE EC=1.97.1.-; DE AltName: Full=Class III anaerobic ribonucleotide reductase small component; GN Name=nrdG; OrderedLocusNames=HI_1155; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activation of anaerobic ribonucleoside-triphosphate CC reductase under anaerobic conditions by generation of an organic CC free radical, using S-adenosylmethionine and reduced flavodoxin as CC cosubstrates to produce 5'-deoxy-adenosine. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- SUBUNIT: Tetramer consisting of 2 alpha (NrdD) and 2 beta (NrdG) CC subunits. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes 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; L42023; AAC22810.1; -; Genomic_DNA. DR PIR; E64168; E64168. DR RefSeq; NP_439313.1; NC_000907.1. DR RefSeq; WP_005693470.1; NC_000907.1. DR STRING; 71421.HI1155; -. DR EnsemblBacteria; AAC22810; AAC22810; HI_1155. DR GeneID; 949759; -. DR KEGG; hin:HI1155; -. DR PATRIC; 20190987; VBIHaeInf48452_1206. DR eggNOG; ENOG4108RDD; Bacteria. DR eggNOG; COG0602; LUCA. DR KO; K04068; -. DR OMA; CPRECPG; -. DR OrthoDB; EOG628F9X; -. DR PhylomeDB; P45080; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012837; NrdG. DR InterPro; IPR001989; Radical_activat_CS. DR PIRSF; PIRSF000368; NrdG; 1. DR TIGRFAMs; TIGR02491; NrdG; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 155 Anaerobic ribonucleoside-triphosphate FT reductase-activating protein. FT /FTId=PRO_0000200537. FT REGION 32 34 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 26 26 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 30 30 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 33 33 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 74 74 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 155 AA; 17856 MW; 4CB5A1D44260C7EC CRC64; MNYLQYYPTD VINGEGTRCT LFVSGCTHAC KGCYNQKSWS FSAGVLFDDV MEQQIINDLK DTRIKRQGLT LSGGDPLHPL NVETLLPFVQ RVKRECPDKD IWVWTGYKLD ELDKQQRAML PYIDVLIDGK FIQEQADPSL VWRGSANQII HRFKL // ID NRDR_HAEIN Reviewed; 149 AA. AC P44946; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Transcriptional repressor NrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN Name=nrdR {ECO:0000255|HAMAP-Rule:MF_00440}; GN OrderedLocusNames=HI_0943; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Negatively regulates transcription of bacterial CC ribonucleotide reductase nrd genes and operons by binding to NrdR- CC boxes. {ECO:0000255|HAMAP-Rule:MF_00440}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00440}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00440}; CC -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|HAMAP- CC Rule:MF_00440}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22597.1; -; Genomic_DNA. DR PIR; B64162; B64162. DR RefSeq; NP_439103.1; NC_000907.1. DR RefSeq; WP_005648026.1; NC_000907.1. DR STRING; 71421.HI0943; -. DR EnsemblBacteria; AAC22597; AAC22597; HI_0943. DR GeneID; 949508; -. DR KEGG; hin:HI0943; -. DR PATRIC; 20190543; VBIHaeInf48452_0984. DR eggNOG; ENOG4108Z11; Bacteria. DR eggNOG; COG1327; LUCA. DR KO; K07738; -. DR OMA; RFTTYET; -. DR OrthoDB; EOG6XM7J6; -. DR PhylomeDB; P44946; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00440; NrdR; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR003796; RNR_NrdR-like. DR Pfam; PF03477; ATP-cone; 1. DR TIGRFAMs; TIGR00244; TIGR00244; 1. DR PROSITE; PS51161; ATP_CONE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Metal-binding; KW Nucleotide-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 149 Transcriptional repressor NrdR. FT /FTId=PRO_0000182304. FT DOMAIN 49 139 ATP-cone. {ECO:0000255|HAMAP- FT Rule:MF_00440}. FT ZN_FING 3 34 {ECO:0000255|HAMAP-Rule:MF_00440}. SQ SEQUENCE 149 AA; 17279 MW; AC34FAB7E2D69B0C CRC64; MHCPFCDTEE TKVIDSRLVS DGYQVRRRRE CGHCHERFTT FEMAELIIPK IIKTDGTREP FNEDKLRSGI QHALEKRPVS ADDVEKAINH IILQLRATGE REVPSKLVGK LAMNELKKLD KVAYIRFASV YLSFDDIDQF TIEIEKLKD // ID NTPA_HAEIN Reviewed; 195 AA. AC P44598; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE EC=3.6.1.19 {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01405}; DE Short=NTPase {ECO:0000255|HAMAP-Rule:MF_01405}; GN OrderedLocusNames=HI_0260; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP/dITP to their respective CC monophosphate derivatives. Might exclude non-canonical purines CC from DNA precursor pool, thus preventing their incorporation into CC DNA and avoiding chromosomal lesions. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01405}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_01405}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21925.1; -; Genomic_DNA. DR PIR; D64146; D64146. DR RefSeq; NP_438428.1; NC_000907.1. DR RefSeq; WP_005694045.1; NC_000907.1. DR ProteinModelPortal; P44598; -. DR SMR; P44598; 3-195. DR STRING; 71421.HI0260; -. DR EnsemblBacteria; AAC21925; AAC21925; HI_0260. DR GeneID; 949383; -. DR KEGG; hin:HI0260; -. DR PATRIC; 20189045; VBIHaeInf48452_0274. DR eggNOG; ENOG4108V82; Bacteria. DR eggNOG; COG0127; LUCA. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG6CZQQP; -. DR PhylomeDB; P44598; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 195 Non-canonical purine NTP pyrophosphatase. FT /FTId=PRO_0000178174. FT REGION 9 14 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT REGION 70 71 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT METAL 41 41 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT METAL 70 70 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01405}. FT BINDING 158 158 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 178 178 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. FT BINDING 184 184 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01405}. SQ SEQUENCE 195 AA; 20972 MW; 4D94711A70907C00 CRC64; MKQKIVLATG NKGKVKEMAD VLSDFGFEVI AQTDLGIESP EETGLTFVEN ALLKARYASE KSGLPAIADD SGLVVSALNG APGLYSARYA GEEGNDAKNR EKLLAELAHI AQEQRQAKFV SCIVFLQHPT DPSPIIAEGE CCGVIGFEEK GENGFGYDSL FFSPEQGCTF AELETAEKKK ISHRAKALSV LKSKL // ID NUDC_HAEIN Reviewed; 264 AA. AC P44710; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=NADH pyrophosphatase; DE EC=3.6.1.22; GN Name=nudC; OrderedLocusNames=HI_0432; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: NAD(H) + H(2)O = AMP + NMN(H). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Divalent metal cations. Mg(2+) or Mn(2+). {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase 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; L42023; AAC22091.1; -; Genomic_DNA. DR PIR; F64152; F64152. DR RefSeq; NP_438593.1; NC_000907.1. DR RefSeq; WP_005693731.1; NC_000907.1. DR ProteinModelPortal; P44710; -. DR STRING; 71421.HI0432; -. DR EnsemblBacteria; AAC22091; AAC22091; HI_0432. DR GeneID; 949531; -. DR KEGG; hin:HI0432; -. DR PATRIC; 20189417; VBIHaeInf48452_0452. DR eggNOG; ENOG4105E09; Bacteria. DR eggNOG; COG2816; LUCA. DR KO; K03426; -. DR OMA; DHGWWIV; -. DR OrthoDB; EOG6S26JD; -. DR PhylomeDB; P44710; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.79.10; -; 1. DR HAMAP; MF_00297; Nudix_NudC; 1. DR InterPro; IPR022925; NADH_pyroPase_NudC. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR015376; Znr_NADH_PPase. DR Pfam; PF00293; NUDIX; 1. DR Pfam; PF09297; zf-NADH-PPase; 1. DR SUPFAM; SSF55811; SSF55811; 2. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW NAD; Reference proteome; Zinc. FT CHAIN 1 264 NADH pyrophosphatase. FT /FTId=PRO_0000056967. FT DOMAIN 126 253 Nudix hydrolase. FT MOTIF 163 184 Nudix box. FT METAL 99 99 Zinc. {ECO:0000250}. FT METAL 102 102 Zinc. {ECO:0000250}. FT METAL 117 117 Zinc. {ECO:0000250}. FT METAL 120 120 Zinc. {ECO:0000250}. FT METAL 178 178 Divalent metal cation. {ECO:0000250}. FT METAL 182 182 Divalent metal cation. {ECO:0000250}. SQ SEQUENCE 264 AA; 30163 MW; 1720219015B9922E CRC64; MKILQQDDFG YWLLTQGSNL YLVNNELPFG IAKDIDLEGL QAMQIGEWKN YPLWLVAEQE SDEREYVSLS NLLSLPEDEF HILSRGVEIN HFLKTHKFCG KCGHKTQQTQ DELAVQCIHC GYQTYPVICP SIIVAVRRGH EILLANHKRH YSPNGGIYTT LAGFVEVGET FEQAVQREVF EETGISIKNL RYFGSQPWAF PNSQMVGFLA DYESGEITLQ ESEIHDAQWF SYDQPLPELP PTGTIARKLI HVTLELCKAE HKCD // ID NUSB_HAEIN Reviewed; 144 AA. AC P45150; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=N utilization substance protein B homolog; DE Short=Protein NusB; GN Name=nusB; OrderedLocusNames=HI_1304; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the transcription termination process. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NusB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22951.1; -; Genomic_DNA. DR PIR; D64115; D64115. DR RefSeq; NP_439455.1; NC_000907.1. DR RefSeq; WP_005650345.1; NC_000907.1. DR ProteinModelPortal; P45150; -. DR SMR; P45150; 9-142. DR STRING; 71421.HI1304; -. DR EnsemblBacteria; AAC22951; AAC22951; HI_1304. DR GeneID; 950225; -. DR KEGG; hin:HI1304; -. DR PATRIC; 20191291; VBIHaeInf48452_1356. DR eggNOG; ENOG4107YIM; Bacteria. DR eggNOG; COG0781; LUCA. DR KO; K03625; -. DR OMA; WIGVYEF; -. DR OrthoDB; EOG6RJV9B; -. DR PhylomeDB; P45150; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.940.10; -; 1. DR HAMAP; MF_00073; NusB; 1. DR InterPro; IPR011605; NusB_fam. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR PANTHER; PTHR11078; PTHR11078; 1. DR Pfam; PF01029; NusB; 1. DR SUPFAM; SSF48013; SSF48013; 1. DR TIGRFAMs; TIGR01951; nusB; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding; Transcription; KW Transcription regulation; Transcription termination. FT CHAIN 1 144 N utilization substance protein B FT homolog. FT /FTId=PRO_0000176543. SQ SEQUENCE 144 AA; 16486 MW; 213A6D820CB9F1CA CRC64; MTEQKQVKKP SARRRARECT VQALYSWAVS GNTAEQVELA FVLDQDMDGV DKPYFRKLFR QTIENIETVD FSISPYIDRA FDELDPIETA ILRLAVYELR FELDVPYKVV INEAIEVAKV FGADESHKYI NGVLDKIAPA LGRK // ID OBG_HAEIN Reviewed; 390 AA. AC P44915; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 104. 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=HI_0877; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22533.1; -; Genomic_DNA. DR PIR; E64099; E64099. DR RefSeq; NP_439038.1; NC_000907.1. DR RefSeq; WP_005693230.1; NC_000907.1. DR ProteinModelPortal; P44915; -. DR STRING; 71421.HI0877; -. DR EnsemblBacteria; AAC22533; AAC22533; HI_0877. DR GeneID; 949885; -. DR KEGG; hin:HI0877; -. DR PATRIC; 20190411; VBIHaeInf48452_0919. DR eggNOG; ENOG4105C9R; Bacteria. DR eggNOG; COG0536; LUCA. DR KO; K03979; -. DR OMA; WTLFHLK; -. DR OrthoDB; EOG6H1Q1M; -. DR PhylomeDB; P44915; -. DR Proteomes; UP000000579; 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; IPR006074; GTP1-OBG_CS. DR InterPro; IPR006169; GTP1_OBG_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11702:SF3; PTHR11702:SF3; 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; SSF52540; SSF52540; 1. DR SUPFAM; SSF82051; SSF82051; 1. DR TIGRFAMs; TIGR02729; Obg_CgtA; 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 1 390 GTPase Obg. FT /FTId=PRO_0000205434. FT DOMAIN 160 333 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 213 216 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 283 286 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}. FT NP_BIND 314 316 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 390 AA; 43377 MW; F380CE342DF1FDF6 CRC64; MKFIDESLIR IEAGDGGNGC VSFRREKFIP KGGPDGGDGG DGGDVYLQAD ENLNTLIDYR FNKRFAAERG ENGRSSDCTG RRGKDIILPV PVGTRAIDND TKETLGDLTQ HGQKMLVAKG GYHGLGNTRF KSSVNRAPRQ KTMGTPGEKR DLLLELMLLA DVGMLGLPNA GKSTFIRAVS AAKPKVADYP FTTLVPSLGV VKVDDSHSFV VADIPGLIEG AADGAGLGIR FLKHLERCRV LIHLVDIAPI DGSNPADNMA IIESELFQYS EKLSEKPRWL VFNKIDTMSD EEAEERAREI AEQLGWEEDY YFISAATGKN VSPLCRDIMD FIIANPREAE TQQVAPEEVK FKWEDYHQER LAEHQFDDDE DWDDDWSEED DEGIEFIYKP // ID NRFD_HAEIN Reviewed; 321 AA. AC P45014; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Protein NrfD homolog; GN Name=nrfD; OrderedLocusNames=HI_1066; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probably involved in the transfer of electrons from the CC quinone pool to the type-c cytochromes. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NrfD 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; L42023; AAC22724.1; -; Genomic_DNA. DR PIR; I64180; I64180. DR RefSeq; NP_439224.1; NC_000907.1. DR RefSeq; WP_005693393.1; NC_000907.1. DR STRING; 71421.HI1066; -. DR EnsemblBacteria; AAC22724; AAC22724; HI_1066. DR GeneID; 950044; -. DR KEGG; hin:HI1066; -. DR PATRIC; 20190795; VBIHaeInf48452_1110. DR eggNOG; ENOG4105DVI; Bacteria. DR eggNOG; COG3301; LUCA. DR KO; K04015; -. DR OMA; IMVTELG; -. DR OrthoDB; EOG6ZWJDG; -. DR PhylomeDB; P45014; -. DR Proteomes; UP000000579; 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; IPR017566; NrfD. DR InterPro; IPR005614; NrfD_fam. DR Pfam; PF03916; NrfD; 1. DR TIGRFAMs; TIGR03148; cyt_nit_nrfD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 321 Protein NrfD homolog. FT /FTId=PRO_0000159323. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. FT TRANSMEM 293 313 Helical. {ECO:0000255}. SQ SEQUENCE 321 AA; 35944 MW; 1D0ECFA241B5EB64 CRC64; MTLDYPVPFH TPNLVWDYTI AIYLFLLGIS SGAVQLAIAY KRSNKLENLS QNWIIRSGVI LGSVPTLIGL TLLIFHLTRP WTFWKLMFNY QFNSVMSMGV MLFQIYMLFL VIWGVVIFKK EIEALINRFI PKLQFVMKLI GIAERIVSPV EVILFILAAV LGAYTGFLLS ALISYPMLNN PVLPALFLAS GTSSGIAATF LIILIAGKLK GDSHESHFIH KFEVPIMVTE LGLIVCFFVG LHFGGGQKTV ALHNALSGFW GVVFWVGVLI IGILIPLIAN MFVNDRLKYN RNFIILVSIF DLIGVFCLRF FILYAGQLTV A // ID NUDB_HAEIN Reviewed; 158 AA. AC P44635; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Dihydroneopterin triphosphate diphosphatase; DE EC=3.6.1.67; DE AltName: Full=Dihydroneopterin triphosphate pyrophosphatase; DE AltName: Full=dATP pyrophosphohydrolase; GN Name=nudB; Synonyms=ntpA; OrderedLocusNames=HI_0316; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the hydrolysis of dihydroneopterin CC triphosphate to dihydroneopterin monophosphate and pyrophosphate. CC Required for efficient folate biosynthesis. Can also hydrolyze CC nucleoside triphosphates with a preference for dATP. CC {ECO:0000250|UniProtKB:P0AFC0}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O = CC 7,8-dihydroneopterin 3'-phosphate + diphosphate. CC {ECO:0000250|UniProtKB:P0AFC0}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0AFC0}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P0AFC0}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21980.1; -; Genomic_DNA. DR PIR; H64147; H64147. DR RefSeq; NP_438482.2; NC_000907.1. DR ProteinModelPortal; P44635; -. DR STRING; 71421.HI0316; -. DR EnsemblBacteria; AAC21980; AAC21980; HI_0316. DR GeneID; 949449; -. DR KEGG; hin:HI0316; -. DR PATRIC; 20189173; VBIHaeInf48452_0333. DR eggNOG; ENOG4108TIT; Bacteria. DR eggNOG; COG0494; LUCA. DR KO; K08310; -. DR OMA; VTRNTEH; -. DR OrthoDB; EOG69WFKW; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008828; F:dATP pyrophosphohydrolase activity; IEA:InterPro. DR GO; GO:0019177; F:dihydroneopterin triphosphate pyrophosphohydrolase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR003564; DHNTPase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01404; NPPPHYDRLASE. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome; Folate biosynthesis; Hydrolase; Magnesium; KW Metal-binding; Reference proteome. FT CHAIN 1 158 Dihydroneopterin triphosphate FT diphosphatase. FT /FTId=PRO_0000056955. FT DOMAIN 14 153 Nudix hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00794}. FT REGION 88 91 Substrate binding. {ECO:0000255}. FT MOTIF 48 69 Nudix box. FT METAL 63 63 Magnesium. {ECO:0000250}. FT METAL 67 67 Magnesium. {ECO:0000250}. FT METAL 124 124 Magnesium. {ECO:0000250}. FT BINDING 14 14 Substrate. {ECO:0000250}. FT BINDING 36 36 Substrate. {ECO:0000250}. FT BINDING 47 47 Substrate. {ECO:0000250}. FT BINDING 142 142 Substrate. {ECO:0000255}. SQ SEQUENCE 158 AA; 18826 MW; A82B3750A5631553 CRC64; MRSDLTAFLM MQYKNNQSVL VVIYTKDTNR VLMLQRQDDP DFWQSVTGTI ESDETPKKTA IRELWEEVRL DISENSTALF DCNESIEFEI FPHFRYKYAP NITHCKEHWF LCEVEKEFIP VLSEHLDFCW VSAKKAVEMT KSQNNAEAIK KYLFNLRR // ID OAPA_HAEIN Reviewed; 431 AA. AC P44415; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Opacity-associated protein OapA; GN Name=oapA; OrderedLocusNames=HI_0330; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Rd / H175; RX PubMed=8559074; DOI=10.1111/j.1365-2958.1995.mmi_17030555.x; RA Weiser J.N., Chong S.T., Greenberg D., Fong W.; RT "Identification and characterization of a cell envelope protein of RT Haemophilus influenzae contributing to phase variation in colony RT opacity and nasopharyngeal colonization."; RL Mol. Microbiol. 17:555-564(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell envelope protein involved in phase variation. CC -!- SUBCELLULAR LOCATION: Secreted. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U17037; AAA56761.1; -; Genomic_DNA. DR EMBL; L42023; AAC21992.1; -; Genomic_DNA. DR PIR; A64062; A64062. DR RefSeq; NP_438494.1; NC_000907.1. DR RefSeq; WP_005694343.1; NC_000907.1. DR ProteinModelPortal; P44415; -. DR STRING; 71421.HI0330; -. DR EnsemblBacteria; AAC21992; AAC21992; HI_0330. DR GeneID; 949442; -. DR KEGG; hin:HI0330; -. DR PATRIC; 20189203; VBIHaeInf48452_0347. DR eggNOG; ENOG4108UBT; Bacteria. DR eggNOG; COG3061; LUCA. DR KO; K07268; -. DR OMA; QSLDQSQ; -. DR OrthoDB; EOG6X10X7; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR InterPro; IPR013731; OapA_N. DR InterPro; IPR007340; Opacity-associatedA. DR Pfam; PF04225; OapA; 1. DR Pfam; PF08525; OapA_N; 1. PE 4: Predicted; KW Complete proteome; Reference proteome; Secreted. FT CHAIN 1 431 Opacity-associated protein OapA. FT /FTId=PRO_0000058016. SQ SEQUENCE 431 AA; 47009 MW; E80EF3358DB63179 CRC64; MNSMDKNQQS SQNELDLGLN QEPITPKKTI QPSSSILGKA KGLFAKKNHV QTNFQQRKEP TFGDSSTQEN DPLIPSENLK KVQKPVLQTS STEENISAVD EEISAENNAD EPVEKAEKPI LAQPEKWKIL QVLPAKHRRL FMAIFVLVIL LIIFFALKPS SDTVESFTQS NSNEVPVQFQ SLDQSQPLET TILDNPPAQN QMAVEQANQS EFAPKAEEAA NNTTAQNPLV ENAPMQQNVV QSPSQMPNEM AAASVAPMQP AQAEQPKATV PVQPMKKAVE PQVAHKDTVK KEVKVAEKAQ APAKATEQNV AKTAGNAPIV EAKPVQAKKE KKVQIVDAKP VSKSTASRLS AKTLTVPKGV SLMQLFRDNQ LNISDVNAMS KATGAGNVLS SFKSGDKVTV SVNNQGRVNE MRLSNGARFV RQSDGSYQYK K // ID OGT_HAEIN Reviewed; 179 AA. AC P44687; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 11-MAY-2016, entry version 101. DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; DE EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772}; DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772}; DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772}; Synonyms=dat1; GN OrderedLocusNames=HI_0402; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the cellular defense against the biological CC effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated CC guanine in DNA by stoichiometrically transferring the alkyl group CC at the O-6 position to a cysteine residue in the enzyme. This is a CC suicide reaction: the enzyme is irreversibly inactivated. CC {ECO:0000255|HAMAP-Rule:MF_00772}. CC -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein CC L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- CC cysteine. {ECO:0000255|HAMAP-Rule:MF_00772}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}. CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and CC therefore is not strictly catalytic. According to one definition, CC an enzyme is a biocatalyst that acts repeatedly and over many CC reaction cycles. CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP- CC Rule:MF_00772}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22061.1; 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; L42023; AAC22061.1; ALT_INIT; Genomic_DNA. DR PIR; G64065; G64065. DR RefSeq; NP_438564.1; NC_000907.1. DR RefSeq; WP_005693766.1; NC_000907.1. DR ProteinModelPortal; P44687; -. DR STRING; 71421.HI0402; -. DR EnsemblBacteria; AAC22061; AAC22061; HI_0402. DR GeneID; 949561; -. DR KEGG; hin:HI0402; -. DR PATRIC; 20189355; VBIHaeInf48452_0421. DR eggNOG; ENOG4105K85; Bacteria. DR eggNOG; COG0350; LUCA. DR KO; K00567; -. DR OMA; NDLPIFV; -. DR OrthoDB; EOG6DJZ5C; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central. DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00772; OGT; 1. DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS. DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd. DR InterPro; IPR008332; MethylG_MeTrfase_N. DR InterPro; IPR023546; MGMT. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01035; DNA_binding_1; 1. DR Pfam; PF02870; Methyltransf_1N; 1. DR SUPFAM; SSF46767; SSF46767; 1. DR SUPFAM; SSF53155; SSF53155; 1. DR TIGRFAMs; TIGR00589; ogt; 1. DR PROSITE; PS00374; MGMT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; KW Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 179 Methylated-DNA--protein-cysteine FT methyltransferase. FT /FTId=PRO_0000139366. FT ACT_SITE 130 130 Nucleophile; methyl group acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00772}. SQ SEQUENCE 179 AA; 20455 MW; 9A83D5AFFC91D896 CRC64; MTALYYTYYP SPVGRLLILS DGESITHIDF EKEQYAPNPK WHKQDELPVF QKVRLAFERY FNGEVECFSN IPLKPEGTAF QQAIWQALRE IDYGELSTYG ELALRINNPK AVRAVGGAVG SNPISIIIPC HRILGKDRTL TGFGGGLEAK RFLLQLEKIP YIDKGTENTK PRFFKKYHE // ID OPA_HAEIN Reviewed; 121 AA. AC P45088; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Protein opa; GN Name=opa; OrderedLocusNames=HI_1174; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-121. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8550458; RA Preston A., Maskell D., Johnson A., Moxon E.R.; RT "Altered lipopolysaccharide characteristic of the I69 phenotype in RT Haemophilus influenzae results from mutations in a novel gene, isn."; RL J. Bacteriol. 178:396-402(1996). CC -!- SIMILARITY: Belongs to the opacity porin 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; L42023; AAC22827.1; -; Genomic_DNA. DR EMBL; U17295; AAA95981.1; -; Genomic_DNA. DR PIR; I64187; I64187. DR RefSeq; NP_439332.2; NC_000907.1. DR ProteinModelPortal; P45088; -. DR STRING; 71421.HI1174; -. DR EnsemblBacteria; AAC22827; AAC22827; HI_1174. DR GeneID; 950130; -. DR KEGG; hin:HI1174; -. DR PATRIC; 20191027; VBIHaeInf48452_1226. DR eggNOG; ENOG41065S8; Bacteria. DR eggNOG; COG3637; LUCA. DR OMA; ADANIYA; -. DR OrthoDB; EOG6TJ7Z1; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0015288; F:porin activity; IEA:InterPro. DR Gene3D; 2.40.160.20; -; 1. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Protein opa. FT /FTId=PRO_0000058056. SQ SEQUENCE 121 AA; 13153 MW; 6647D8B471F42223 CRC64; MGYKVGNTRV AGDYTHHGKV DGTKIQGLGA SVLYDFDTNS KVQPYVGARV ATNQFKYTNR AEQKFKSSSD IKLGYGVVAG AKYKLDGNWY ANGGVEYNRL GNFDSTKVNN YGAKVGVGYG F // ID OPPC_HAEIN Reviewed; 311 AA. AC P45053; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Oligopeptide transport system permease protein OppC; GN Name=oppC; OrderedLocusNames=HI_1122; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22776.1; -; Genomic_DNA. DR PIR; D64184; D64184. DR RefSeq; NP_439279.1; NC_000907.1. DR RefSeq; WP_005651799.1; NC_000907.1. DR ProteinModelPortal; P45053; -. DR STRING; 71421.HI1122; -. DR EnsemblBacteria; AAC22776; AAC22776; HI_1122. DR GeneID; 950091; -. DR KEGG; hin:HI1122; -. DR PATRIC; 20190917; VBIHaeInf48452_1171. DR eggNOG; ENOG4105C2T; Bacteria. DR eggNOG; COG1173; LUCA. DR KO; K15582; -. DR OMA; CYLFLAR; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45053; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR025966; OppC_N. DR Pfam; PF00528; BPD_transp_1; 1. DR Pfam; PF12911; OppC_N; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 311 Oligopeptide transport system permease FT protein OppC. FT /FTId=PRO_0000060152. FT TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 70 113 Periplasmic. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 135 159 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 181 222 Periplasmic. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 244 246 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 268 278 Periplasmic. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 300 311 Cytoplasmic. {ECO:0000255}. FT DOMAIN 110 299 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 311 AA; 34632 MW; D55C49A361BED3C8 CRC64; MTDYRTQPIN QKNADFVEQV ADRIEEMQLE GRSLWQDAKR RFFRNKAAVA SLIILAFIII FITVAPWFFP FTYEDTDWNM MSAAPTMEGY HFFGTDASGR DLLVRTAIGG RISLLVGIAG AFISVTIGTI YGAISGYVGG KTDMLMMRFL EILSSFPFMF FVILLVTLFG QNIFLIFIAI GAIAWLGLAR IVRGQTLSLK NKEFVEAAIV CGVPRRQIIL KHIIPNVLGL VAVYASLEVP GLILFESFLS FLGLGTQEPM SSWGALLSDG AAQMEVSPWL LIFPAFFLCL TLFCFNFIGD GLRDALDPKD R // ID NUSA_HAEIN Reviewed; 495 AA. AC P43915; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 121. DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN OrderedLocusNames=HI_1283; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22932.1; -; Genomic_DNA. DR RefSeq; NP_439435.1; NC_000907.1. DR RefSeq; WP_005691699.1; NC_000907.1. DR ProteinModelPortal; P43915; -. DR SMR; P43915; 354-419, 433-495. DR STRING; 71421.HI1283; -. DR PRIDE; P43915; -. DR EnsemblBacteria; AAC22932; AAC22932; HI_1283. DR GeneID; 950214; -. DR KEGG; hin:HI1283; -. DR PATRIC; 20191249; VBIHaeInf48452_1335. DR eggNOG; ENOG4105CHV; Bacteria. DR eggNOG; COG0195; LUCA. DR KO; K02600; -. DR OMA; QLFMDKL; -. DR OrthoDB; EOG6NSGHW; -. DR PhylomeDB; P43915; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0031564; P:transcription antitermination; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1480.10; -; 1. DR Gene3D; 3.30.300.20; -; 2. DR HAMAP; MF_00945_B; NusA_B; 1. DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx. 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; IPR010214; Tscrpt_termin_fac_NusA_C_rpt. DR InterPro; IPR010213; Tscrpt_termination_fac_NusA. DR Pfam; PF13184; KH_5; 1. DR Pfam; PF08529; NusA_N; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00322; KH; 2. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF47794; SSF47794; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54814; SSF54814; 2. DR SUPFAM; SSF69705; SSF69705; 1. DR TIGRFAMs; TIGR01953; NusA; 1. DR TIGRFAMs; TIGR01954; nusA_Cterm_rpt; 2. 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 1 495 Transcription termination/antitermination FT protein NusA. FT /FTId=PRO_0000181968. FT DOMAIN 135 200 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_00945}. FT DOMAIN 302 374 KH. {ECO:0000255|HAMAP-Rule:MF_00945}. SQ SEQUENCE 495 AA; 55263 MW; 4730D27ED109A95C CRC64; MSKEILLAAE AVSNEKLLPR EKIFEALESA IAISTKKKFE YETDIRVSIN PKTGEFDTFR RWLVVDEVKV PTKEITLEAA QFDDPNLQLG EYVEDQIESI AFDRIAMQTA RQVISTKIRE AERAKVVEQF REEEGKIVTG TVKKVSRDSI ILDLGNKAEA MIAREDMLPR ENFRPGDRVR GVLYKVNPEG KTAQLFVTRS KPEMLIELFR IEVPEIGEEM IEIRGAARDA GSRAKIAVKS NDKRIDPVGA CVGMRGARVQ VITNELGGER VDIVLWDDNP AQFVINAMAP ADVSSIIVDE DNHSMDIAVE ADNLAQAIGR NGQNVRLATQ LTGWTLNVMT TDELNAKHQA EDNKVLNLFI NALELDEEFA QILVEEGFTS LEEIAYVPMN ELTAIDGLED EDLVEELQTR AKNAITAAAV AEEEALKKAN VEDRLLNLEG MNRHVAIKLA EKQITTLEEL AEQGVDDLTD IEELTAEQAA DLIMAARNIC WFGEE // ID OAPB_HAEIN Reviewed; 134 AA. AC P44416; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Opacity-associated protein OapB; GN Name=oapB; OrderedLocusNames=HI_0331; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Rd / H175; RX PubMed=8559074; DOI=10.1111/j.1365-2958.1995.mmi_17030555.x; RA Weiser J.N., Chong S.T., Greenberg D., Fong W.; RT "Identification and characterization of a cell envelope protein of RT Haemophilus influenzae contributing to phase variation in colony RT opacity and nasopharyngeal colonization."; RL Mol. Microbiol. 17:555-564(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; U17037; AAA56762.1; -; Genomic_DNA. DR EMBL; L42023; AAC21993.1; -; Genomic_DNA. DR PIR; B64062; B64062. DR RefSeq; NP_438495.1; NC_000907.1. DR RefSeq; WP_005694341.1; NC_000907.1. DR STRING; 71421.HI0331; -. DR EnsemblBacteria; AAC21993; AAC21993; HI_0331. DR GeneID; 950648; -. DR KEGG; hin:HI0331; -. DR PATRIC; 20189205; VBIHaeInf48452_0348. DR OMA; WLERKEF; -. DR OrthoDB; EOG6Q8J3M; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR018660; C-type_lysozyme_inhibitor. DR InterPro; IPR012097; OapB. DR Pfam; PF09864; MliC; 1. DR PIRSF; PIRSF007352; OapB; 1. DR SUPFAM; SSF141488; SSF141488; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 134 Opacity-associated protein OapB. FT /FTId=PRO_0000058017. FT CONFLICT 133 134 GQ -> DNNRAKRTSTWFCFASSPL (in Ref. 1; FT AAA56762). {ECO:0000305}. SQ SEQUENCE 134 AA; 15355 MW; 2F26A9397A9F6137 CRC64; MLKKTSLIFT ALLMTGCVQN ANVTTPQAQK MQVEKVDKAL QKGEADRYLC QDDRVVRVVH ATHKKYKKNL HYVTVTFQGV SEKLTLMISE RGKNYANIRW MWQERDDFST LKTNLGEILA TQCVSQTSER LSGQ // ID OPDA_HAEIN Reviewed; 681 AA. AC P44573; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Oligopeptidase A; DE EC=3.4.24.70; GN Name=prlC; OrderedLocusNames=HI_0214; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May play a specific role in the degradation of signal CC peptides after they are released from precursor forms of secreted CC proteins. Can cleave N-acetyl-L-Ala(4) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of oligopeptides, with broad CC specificity. Gly or Ala commonly occur as P1 or P1' residues, but CC more distant residues are also important, as is shown by the fact CC that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5). 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 M3 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; L42023; AAC21882.1; -; Genomic_DNA. DR PIR; C64055; C64055. DR RefSeq; NP_438383.2; NC_000907.1. DR ProteinModelPortal; P44573; -. DR STRING; 71421.HI0214; -. DR MEROPS; M03.004; -. DR EnsemblBacteria; AAC21882; AAC21882; HI_0214. DR GeneID; 951121; -. DR KEGG; hin:HI0214; -. DR PATRIC; 20188925; VBIHaeInf48452_0219. DR eggNOG; ENOG4105DGW; Bacteria. DR eggNOG; COG0339; LUCA. DR KO; K01414; -. DR OMA; NQTPPVD; -. DR OrthoDB; EOG6WHNPN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central. DR Gene3D; 1.10.1370.10; -; 2. DR Gene3D; 1.20.1050.40; -; 1. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR024077; Neurolysin/TOP_dom2. DR InterPro; IPR024080; Neurolysin/TOP_N. DR InterPro; IPR001567; Pept_M3A_M3B. DR Pfam; PF01432; Peptidase_M3; 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 1 681 Oligopeptidase A. FT /FTId=PRO_0000078161. FT ACT_SITE 471 471 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 470 470 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 474 474 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 477 477 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 681 AA; 78017 MW; 1452905A001ECFC5 CRC64; MSMSNPLLNI QGLPPFSQIK PEHIRPAVEK LIQDCRNTIE QVLKQPHFTW ENFILPLTET NDRLNRAWSP VSHLNSVKNS TELREAYQTC LPLLSEYSTW VGQHKGLYNA YLALKNSAEF ADYSIAQKKA IENSLRDFEL SGIGLSEEKQ QRYGEIVARL SELNSQFSNN VLDATMGWEK LIENEAELAG LPESALQAAQ QSAESKGLKG YRFTLEIPSY LPVMTYCENR ALREEMYRAY ATRASEQGPN AGKWDNSKVM EEILTLRVEL AKLLGFNTYT ELSLATKMAE NPQQVLDFLD HLAERAKPQG EKELQELKGY CEKEFGVTEL APWDIGFYSE KQKQHLYAIN DEELRPYFPE NRVISGLFEL IKRIFNIRAV ERKGVDTWHK DVRFFDLIDE NDQLRGSFYL DLYAREHKRG GAWMDDCIGR KRKLDGSIET PVAYLTCNFN APIGNKPALF THNEVTTLFH EFGHGIHHML TQIDVSDVAG INGVPWDAVE LPSQFMENWC WEEEALAFIS GHYETGEPLP KEKLTQLLKA KNFQAAMFIL RQLEFGIFDF RLHHTFDAEK TNQILDTLKS VKSQVAVIKG VDWARAPHSF SHIFAGGYAA GYYSYLWAEV LSADAYSRFE EEGIFNPITG KSFLDEILTR GGSEEPMELF KRFRGREPQL DALLRHKGIM N // ID OPPD_HAEIN Reviewed; 323 AA. AC P45052; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Oligopeptide transport ATP-binding protein OppD; GN Name=oppD; OrderedLocusNames=HI_1121; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22775.1; -; Genomic_DNA. DR PIR; C64184; C64184. DR RefSeq; NP_439278.1; NC_000907.1. DR RefSeq; WP_005651797.1; NC_000907.1. DR ProteinModelPortal; P45052; -. DR STRING; 71421.HI1121; -. DR EnsemblBacteria; AAC22775; AAC22775; HI_1121. DR GeneID; 950089; -. DR KEGG; hin:HI1121; -. DR PATRIC; 20190915; VBIHaeInf48452_1170. DR eggNOG; ENOG4105C3U; Bacteria. DR eggNOG; COG0444; LUCA. DR KO; K15583; -. DR OMA; YSDYPHE; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45052; -. DR Proteomes; UP000000579; 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; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 323 Oligopeptide transport ATP-binding FT protein OppD. FT /FTId=PRO_0000092660. FT DOMAIN 5 254 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 41 48 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 323 AA; 35721 MW; D182EBDFDCADD49A CRC64; MNPLLDVKNL YVRFKTPDGV VTAVNDLNFT LNAGSTLGIV GESGSGKSQT AFALMGLLAA NGEVEGSAIF EGKELVNLPN AELNKIRAEQ ISMIFQDPMT SLNPYMKIGE QLMEVLQLHK GYDKQTAFAE SVKMLDAVKM PEAKKRMGMY PHEFSGGMRQ RVMIAMALLC RPKLLIADEP TTALDVTVQA QIMTLLNELK REFNTAIIMI THDLGVVAGI CDQVMVMYAG RTMEYGTAEQ IFYHPTHPYS IGLMDAIPRL DGNEEHLVTI PGNPPNLLHL PKGCPFSPRC QFATEQCQIA PKLTTFNHGQ LRNCWLSAEK FNL // ID OPPA_HAEIN Reviewed; 541 AA. AC P71370; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Periplasmic oligopeptide-binding protein; DE Flags: Precursor; GN Name=oppA; OrderedLocusNames=HI_1124; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is a component of the oligopeptide CC permease, a binding protein-dependent transport system, it binds CC peptides up to five amino acids long with high affinity. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 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; L42023; AAC22778.1; -; Genomic_DNA. DR RefSeq; NP_439281.1; NC_000907.1. DR RefSeq; WP_010869134.1; NC_000907.1. DR ProteinModelPortal; P71370; -. DR STRING; 71421.HI1124; -. DR EnsemblBacteria; AAC22778; AAC22778; HI_1124. DR GeneID; 950086; -. DR KEGG; hin:HI1124; -. DR PATRIC; 20190921; VBIHaeInf48452_1173. DR eggNOG; ENOG4108J59; Bacteria. DR eggNOG; COG4166; LUCA. DR KO; K15580; -. DR OMA; AWVKKEN; -. DR OrthoDB; EOG6V7BH5; -. DR PhylomeDB; P71370; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 3: Inferred from homology; KW Complete proteome; Peptide transport; Periplasm; Protein transport; KW Reference proteome; Signal; Transport. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 541 Periplasmic oligopeptide-binding protein. FT /FTId=PRO_0000031799. SQ SEQUENCE 541 AA; 60911 MW; 1B949C9617514A99 CRC64; MQHKLLFSAI ALALSYSAQA VIVPEGTQLD EKQHIVINNG AEPQSFDPHK TEGVPESNVA YQLLEGLVTS DSEGKLQPGA AESWENTPDF KTWTFHLRKD AKWSNGDPVT AHDFVFAWRR LVDPATAAPY ASYLSYLQVE NAQDIIDGKK KPAELGVEXK DDYTFVVHTT NPVPYTVSXX THQSLLPLPX KVVEKLGDAW VKKENYVGNG AYKLANHIIN EKIEFERNPL YWNDKETVIN SATFLAIENP STDVARYRAG DLDMTSYGLP PEQFAKLQKE LPGEVYVTRT LGTYSYELNN KKAPFDNVNI RKALNLSLDR NVITDKVLGQ GQTPTYVFTP TYIEEGHLIQ QPAYSKEPMA QRNEEAIKLL EEAGYSKANP LKFSILYNTN ENHKKVAIAA ASMWKANTKG LIDVKLENQE WKTYIDSRRA GRYDVARAGW NADYNQATTF GNYFLSNSSN NTAKYANPEY DKAMAESYAA TDAEGRAKAY AKAEEILGKD YGIVPIFNYV NPRLVKPYVK GYSGKDPQDH IYLRNLYIIK H // ID NUSG_HAEIN Reviewed; 185 AA. AC P43916; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; GN OrderedLocusNames=HI_0717; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SIMILARITY: Contains 1 KOW domain. {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; L42023; AAC22374.1; -; Genomic_DNA. DR PIR; G64088; G64088. DR RefSeq; NP_438875.1; NC_000907.1. DR RefSeq; WP_010869041.1; NC_000907.1. DR ProteinModelPortal; P43916; -. DR STRING; 71421.HI0717; -. DR EnsemblBacteria; AAC22374; AAC22374; HI_0717. DR GeneID; 950637; -. DR KEGG; hin:HI0717; -. DR PATRIC; 20190057; VBIHaeInf48452_0749. DR eggNOG; ENOG4105E5V; Bacteria. DR eggNOG; COG0250; LUCA. DR KO; K02601; -. DR OMA; AVHTYVG; -. DR OrthoDB; EOG6FFS95; -. DR PhylomeDB; P43916; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-HAMAP. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 3.30.70.940; -; 1. DR HAMAP; MF_00948; NusG; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR001062; Transcrpt_antiterm_NusG. DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF02357; NusG; 1. DR PRINTS; PR00338; NUSGTNSCPFCT. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF82679; SSF82679; 1. DR TIGRFAMs; TIGR00922; nusG; 1. DR PROSITE; PS01014; NUSG; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transcription; KW Transcription antitermination; Transcription regulation; KW Transcription termination. FT CHAIN 1 185 Transcription termination/antitermination FT protein NusG. FT /FTId=PRO_0000113929. FT DOMAIN 133 161 KOW. {ECO:0000255|HAMAP-Rule:MF_00948}. SQ SEQUENCE 185 AA; 21381 MW; C6EED5D8CCCF493D CRC64; MTEETTVSKK RWYVLQAFSG FESRVALTLR EYIKQQQMED QFGEVLVPTE EVVENVAGKR RKSERKFFPG YVLVEMEMND ETWHLVKSVP RVMGFIGGTP DKPAPISKRE ADTILNRLEQ NTDKPRHRNE YHPGEEVRVT EGPFADFNGT VEEVDYEKGR LKVSVSMFGR ATPVELEFGQ VEKIH // ID ODO1_HAEIN Reviewed; 935 AA. AC P45303; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=sucA; OrderedLocusNames=HI_1662; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23308.1; 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; L42023; AAC23308.1; ALT_INIT; Genomic_DNA. DR PIR; E64135; E64135. DR RefSeq; NP_439804.2; NC_000907.1. DR RefSeq; WP_010869267.1; NC_000907.1. DR ProteinModelPortal; P45303; -. DR SMR; P45303; 88-934. DR STRING; 71421.HI1662; -. DR PRIDE; P45303; -. DR EnsemblBacteria; AAC23308; AAC23308; HI_1662. DR GeneID; 950496; -. DR KEGG; hin:HI1662; -. DR PATRIC; 20192073; VBIHaeInf48452_1740. DR eggNOG; ENOG4105C7P; Bacteria. DR eggNOG; COG0567; LUCA. DR KO; K00164; -. DR OMA; DWLDGRW; -. DR OrthoDB; EOG6V1M1F; -. DR PhylomeDB; P45303; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR032106; 2-oxogl_dehyd_N. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR031717; KGD_C. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR PANTHER; PTHR23152; PTHR23152; 1. DR Pfam; PF16078; 2-oxogl_dehyd_N; 1. DR Pfam; PF00676; E1_dh; 1. DR Pfam; PF16870; OxoGdeHyase_C; 1. DR Pfam; PF02779; Transket_pyr; 1. DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Reference proteome; KW Thiamine pyrophosphate. FT CHAIN 1 935 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_0000162194. SQ SEQUENCE 935 AA; 106806 MW; 33607F3C3AFDDC78 CRC64; MQQNKAFDDW LASTALGGAN QSYIEELYES YLSDPQSVEE SWRKTFDSLP KTTALEQPHT PVRDYFRRLA RENHNEAVTV IDPAAGAKLV KVLQFINAYR FRGHLEANLD PLNYYRWKVS FVPELDYRHH GFTEQDLNET FNINHYVYKR DTIKLGELAQ MLKETYCGSI GLEFMHVQDM EQKMWLQSKM ESLLDKPLFT SEERVNFLRE LTAADGLERY LGAKFPGAKR FSLEGSDAFI PLMKEIIRHS SRQGVNDVVM GMAHRGRLNM LVNVLGKKPE NLFDEFAGKH SSERTGDVKY HQGFSSDFAV DDKRVHLTLA FNPSHLEIVS PVVIGSVRSR QTRMNDTEHS KVLAITVHGD SAVAGQGVVQ ETLNMSNTRG YSVGGTIRIV INNQIGFTTS NPNDTRSTEY CTDIAKMIQA PIIHVNGDDP EAVAFAARMA VEYRNLFKRD IFIDLISYRR HGHNEADEPL ATQPMMYSII KKHPTPRKVY ADRLVSEGVM TEEQVTEMAN DYRDALDNGD RVVSEWREMD TAKMDWLQYL NYDWTAPYES KFSQERFLTL AKRVCEYPES LRAHPRVEKI YNDRKAMYQG EKLLDWGMAE TMAYATLLDE GVNVRLSGED AGRGTFFHRH AVVHNQNDGT GYVPLTHLHA NQGRFEVWDS VLSEESVLAF EYGYATTDPK TLTIWEAQFG DFANGAQIVI DQFISSGEQK WGRMCGLVML LPHGYEGQGP EHSSARLERY LQLCAEQNMQ VCVPSTPAQV YHMLRRQSLR KMRRPLIAIS PKSLLRHPLA VSSLDELING TFQTVIGEID ELDPKDVKRV VMCSGKVYYD LLEQRRANNQ KDVAIIRIEQ LYPFPHEDVK KALEPYAHVT DYVWCQEEPL NQGAWYCSKH NFESAIPESV KLKYAGRPAS ASPAVGYMSL HTKQQKQLVE DALSF // ID ODP1_HAEIN Reviewed; 886 AA. AC P45119; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 114. DE RecName: Full=Pyruvate dehydrogenase E1 component; DE Short=PDH E1 component; DE EC=1.2.4.1; GN Name=aceE; OrderedLocusNames=HI_1233; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, CC that catalyzes the overall conversion of pyruvate to acetyl-CoA CC and CO(2). {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: Homodimer. Part of the PDH complex, consisting of CC multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide CC acetyltransferase (E2) and lipoamide dehydrogenase (E3). CC {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; L42023; AAC22886.1; -; Genomic_DNA. DR PIR; A64112; A64112. DR RefSeq; NP_439389.1; NC_000907.1. DR RefSeq; WP_005694293.1; NC_000907.1. DR ProteinModelPortal; P45119; -. DR SMR; P45119; 57-886. DR STRING; 71421.HI1233; -. DR PRIDE; P45119; -. DR EnsemblBacteria; AAC22886; AAC22886; HI_1233. DR GeneID; 950116; -. DR KEGG; hin:HI1233; -. DR PATRIC; 20191145; VBIHaeInf48452_1285. DR eggNOG; ENOG4105DAQ; Bacteria. DR eggNOG; COG2609; LUCA. DR KO; K00163; -. DR OMA; GFVPQRR; -. DR OrthoDB; EOG6BW4TW; -. DR PhylomeDB; P45119; -. DR Proteomes; UP000000579; 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; -; 2. DR InterPro; IPR004660; 2-oxoA_DH_E1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 5. DR Pfam; PF00456; Transketolase_N; 1. DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00759; aceE; 1. PE 3: Inferred from homology; KW Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 886 Pyruvate dehydrogenase E1 component. FT /FTId=PRO_0000162245. SQ SEQUENCE 886 AA; 99131 MW; 1B936A75DD69E71D CRC64; MSEILKNDVD PIETQDWLQS LDSLIREEGV ERAQYIVEQV IGQARTSGVS LPTGVTTDYV NTIPVAEQPA YPGDHAIERR IRSAVRWNAI AMVLRSQKKD LDLGGHISTF QSAATMYEVC YNHFFKAATE KNGGDLIFFQ GHAAPGMYAR AFLEGRLTEE QMDNFRQEAF TDGLSSYPHP KLMPEFWQFS TVSMGLGPVN AIYQARFLKY LDNRGLKDTK DQKVYAFLGD GEMDEIESKG ALTFAAREHL DNLIFTISCN LQRLDGPVNG NGKIVQELEG LFTGAGWEVI KVLWGSDWDK LFAKDTSGKL TQLMMEVVDG DYLTFKSKDG AYIREHFFGR YPETAALVAD MTDDEIWALR RGAHDSEKLY AAYAKAQNAT KPVVILAHQV KGYKIPEAES KNTAHQSKKM SYESLKGFRD FFELPLTDEQ VEKLEYIKFA EGTPEYEYLH GHRKALNGYV PARRTKFDVE YKVPALEEFK ALLEEQPRGI STTMAFTRAL NILLKDKNIG KTIVPMIADE ARTFGMEGLF RQVGIYNPHG QNYIPSDRDL VAYYREAKDG QVLQEGINEL GATASWLAAA NSYSVNNQPM IPFFIYYSMF GFQRVGDMMW AAGDQLARGF MVGGTSGRTT LNGEGLQHED GHSHIQAGII PNCITYDPSF AFEVAVIMQD GINRMYGEKQ EDVFYYMTTL NEVMDQPAMP AGAEEGIRKG LYKFETVEGK KGKGHVQLLG SGAIMRHVRE AAQILANDYG VTSDVFSAPS FNELAREGHD AARWNLLHPT ETQRVPYVAQ VLADLPTVAS TDYVKGYADQ IRAFVPSKHY HVLGTDGFGR SDSRANLREH FEVDARYVVV AALSQLAKEG TVSNQVVADA IAKFGLNVDR INPLYA // ID OPP11_HAEIN Reviewed; 459 AA. AC P43838; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Outer membrane protein P1; DE Short=OMP P1; DE Flags: Precursor; GN Name=ompP1; OrderedLocusNames=HI_0401; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the OmpP1/FadL 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; L42023; AAC22060.1; -; Genomic_DNA. DR PIR; F64065; F64065. DR RefSeq; NP_438563.1; NC_000907.1. DR RefSeq; WP_005693768.1; NC_000907.1. DR ProteinModelPortal; P43838; -. DR STRING; 71421.HI0401; -. DR TCDB; 1.B.9.1.4; the fadl outer membrane protein (fadl) family. DR EnsemblBacteria; AAC22060; AAC22060; HI_0401. DR GeneID; 949945; -. DR KEGG; hin:HI0401; -. DR PATRIC; 20189353; VBIHaeInf48452_0420. DR eggNOG; ENOG4105CKF; Bacteria. DR eggNOG; COG2067; LUCA. DR KO; K06076; -. DR OMA; FNEANRI; -. DR OrthoDB; EOG6Z0Q6D; -. DR PhylomeDB; P43838; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR005017; OMPP1/FadL/TodX. DR Pfam; PF03349; Toluene_X; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 22 {ECO:0000250}. FT CHAIN 23 459 Outer membrane protein P1. FT /FTId=PRO_0000025199. SQ SEQUENCE 459 AA; 49478 MW; 43BDC98E5A39366F CRC64; MKKFNQSLLA TAMLLAAGGA NAAAFQLAEV STSGLGRAYA GEAAIADNAS VVATNPALMS LFKTAQFSTG GVYVDSRINM NGDVTSHATI ITSSSGIKAI EGGSASARNV VPGAFVPNLY FVAPVNDKFA LGAGMNVNFG LKSEYDDSYD AGIFGGKTDL SAINLNLSGA YRVTEGLSLG LGVNAVYAKA QVERNAGIIA DSVKDNQVKT ALTVQQEPLK FLDKYLPSKD TSVVSLQDRA AWGFGWNAGV MYQFNEANRI GLAYHSKVDI DFTDRTATSV EANVIKAGKK GDLTLTLPDY LELSGFHQLT DKLAVHYSYK YTHWSRLTKL NASFEDGKKA FDKELQYSNN SRVALGASYN LDEKLTLRAG IAYDQAASRH QRSAAIPDTD RTWYSLGATY KFTPNLSVDL GYAYLKGKKV HFKEVKTIGD ERSLTLNTTA NYTSQAHANL YGLNLNYSF // ID OPPF_HAEIN Reviewed; 332 AA. AC P45051; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Oligopeptide transport ATP-binding protein OppF; GN Name=oppF; OrderedLocusNames=HI_1120; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22774.1; -; Genomic_DNA. DR PIR; B64184; B64184. DR RefSeq; NP_439277.1; NC_000907.1. DR RefSeq; WP_005657282.1; NC_000907.1. DR ProteinModelPortal; P45051; -. DR STRING; 71421.HI1120; -. DR EnsemblBacteria; AAC22774; AAC22774; HI_1120. DR GeneID; 950088; -. DR KEGG; hin:HI1120; -. DR PATRIC; 20190913; VBIHaeInf48452_1169. DR eggNOG; ENOG4108JQ7; Bacteria. DR eggNOG; COG4608; LUCA. DR KO; K10823; -. DR OMA; YVACHLM; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45051; -. DR BioCyc; RETL1328306-WGS:GSTH-3146-MONOMER; -. DR Proteomes; UP000000579; 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; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 332 Oligopeptide transport ATP-binding FT protein OppF. FT /FTId=PRO_0000092673. FT DOMAIN 23 264 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 56 63 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 332 AA; 36760 MW; 45B6A3085431E3D9 CRC64; MTVSNNKELL LEVNHLGVSF KIKNDKSLFF AKPQTLKAVK DVSFKLYAGE TLGVVGESGC GKSTLARAII GLVEASEGEI LWLGKHLRKQ SAKQWKETRK DIQMIFQDPL ASLNPRMNIG EIIAEPLKIY QPHLSAAEVK EKVQAMMLKV GLLPNLINRY PHEFSGGQCQ RIGIARALII EPKMIICDEP VSALDVSIQA QVVNLLKSLQ KEMGLSLIFI AHDLAVVKHI SDRVLVMYLG NAMELGSDVE VYNDTKHPYT KALMSAVPIP DPKLERNKSI ELLEGDLPSP INPPSGCVFR TRCLKADENC AKQKPPFTSQ NNSHFVACLK VL // ID ODO2_HAEIN Reviewed; 409 AA. AC P45302; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 119. DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; DE EC=2.3.1.61; DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2; DE Short=OGDC-E2; DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; GN Name=sucB; OrderedLocusNames=HI_1661; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)- CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S- CC succinyldihydrolipoyl)lysine. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. 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; L42023; AAC23307.1; -; Genomic_DNA. DR PIR; D64135; D64135. DR RefSeq; NP_439803.1; NC_000907.1. DR RefSeq; WP_005694387.1; NC_000907.1. DR ProteinModelPortal; P45302; -. DR SMR; P45302; 2-76, 111-153, 177-409. DR STRING; 71421.HI1661; -. DR EnsemblBacteria; AAC23307; AAC23307; HI_1661. DR GeneID; 950492; -. DR KEGG; hin:HI1661; -. DR PATRIC; 20192071; VBIHaeInf48452_1739. DR eggNOG; ENOG4105C7S; Bacteria. DR eggNOG; COG0508; LUCA. DR KO; K00658; -. DR OMA; GTDKVDT; -. DR OrthoDB; EOG610413; -. DR PhylomeDB; P45302; -. DR UniPathway; UPA00868; UER00840. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. DR Gene3D; 4.10.320.10; -; 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; IPR004167; E3-bd. DR InterPro; IPR011053; Single_hybrid_motif. DR InterPro; IPR006255; SucB. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR01347; sucB; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Lipoyl; Reference proteome; KW Transferase; Tricarboxylic acid cycle. FT CHAIN 1 409 Dihydrolipoyllysine-residue FT succinyltransferase component of 2- FT oxoglutarate dehydrogenase complex. FT /FTId=PRO_0000162264. FT DOMAIN 2 77 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT ACT_SITE 380 380 {ECO:0000255}. FT ACT_SITE 384 384 {ECO:0000255}. FT MOD_RES 43 43 N6-lipoyllysine. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. SQ SEQUENCE 409 AA; 45163 MW; 3FBF62BC17433839 CRC64; MAIEILVPDL PESVADATVA TWHKKLGDTV KRDEVIVEIE TDKVVLEVPA LSDGVLAEVV QAEGETVVSK QLLGKISTAQ EGDVSSATLK ATNEPTPSDR QNAAIENSHN HNADQSPVIR RLLAEHDLQA DQIQGSGVGG RLTREDIERE IAKRQAQQVK QEAATEQNTI STVAYSARSE KRVPMTRLRK RIAERLLEAK NSTAMLTTFN EVDMQPIMTL RKTYGEKFEK QHSVRLGFMS FYIKAVVEAL KRYPEVNASI DGDDVVYHNY FDISIAVSTP RGLVTPVLRD CDKLSMAEIE KQIKALAEKG RDGKLTVEDL TGGNFTITNG GVFGSLMSTP IINPPQSAIL GMHAIKERPI ALNGQVVIRP MMYLALSYDH RLIDGRESVG FLVTIKELLE DPTRLLLEI // ID ODP2_HAEIN Reviewed; 567 AA. AC P45118; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. 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=aceF; OrderedLocusNames=HI_1232; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 2 lipoyl cofactors 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 2 lipoyl-binding domains. 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; L42023; AAC22885.1; -; Genomic_DNA. DR PIR; I64111; I64111. DR RefSeq; NP_439388.1; NC_000907.1. DR RefSeq; WP_010869159.1; NC_000907.1. DR ProteinModelPortal; P45118; -. DR SMR; P45118; 1-80, 108-186, 324-567. DR STRING; 71421.HI1232; -. DR PRIDE; P45118; -. DR EnsemblBacteria; AAC22885; AAC22885; HI_1232. DR GeneID; 949836; -. DR KEGG; hin:HI1232; -. DR PATRIC; 20191143; VBIHaeInf48452_1284. DR eggNOG; ENOG4107QSN; Bacteria. DR eggNOG; COG0508; LUCA. DR KO; K00627; -. DR OMA; GKEFEPR; -. DR OrthoDB; EOG610413; -. DR PhylomeDB; P45118; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro. 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 Gene3D; 4.10.320.10; -; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR004167; E3-bd. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 2. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 2. DR TIGRFAMs; TIGR01348; PDHac_trf_long; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2. DR PROSITE; PS00189; LIPOYL; 2. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Glycolysis; Lipoyl; KW Reference proteome; Repeat; Transferase. FT CHAIN 1 567 Dihydrolipoyllysine-residue FT acetyltransferase component of pyruvate FT dehydrogenase complex. FT /FTId=PRO_0000162279. FT DOMAIN 2 75 Lipoyl-binding 1. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT DOMAIN 108 181 Lipoyl-binding 2. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT REGION 247 567 Subunit binding, catalytic. FT ACT_SITE 484 484 {ECO:0000255}. FT ACT_SITE 540 540 {ECO:0000255}. FT ACT_SITE 544 544 {ECO:0000255}. FT MOD_RES 41 41 N6-lipoyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. FT MOD_RES 147 147 N6-lipoyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. SQ SEQUENCE 567 AA; 59411 MW; 891DBCDEB388C5B0 CRC64; MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEILVK VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA TAPTASAIVE VNVPDIGGDE VNVTEIMVAV GDTITEEQSL ITVEGDKASM EVPAPFGGVV KEILVKSGDK VSTGSLIMRF EVLGAAPAES ASAPASTSAP QTAAPATTAQ APQAAAPDTT AQAPQAAAPD TTAQAAQSNN NVSGLSQEQV EASTGYAHAT PVIRRLAREF GVNLDKVKGT GRKGRIVKED IEAYVKTAVK AYESGATAQA TGNGVANGAG LGLLPWPKVD FSKFGEIEEV ELSRINKISG ANLHRNWVII PHVTHFDKAD ITDLEAFRKE QNALREKQKL GVKITPVVFI MKAVAKALEA YPRFNSSITE DAQRLILKKY INIGVAVDTP NGLVVPVFKN VNKKGIIELS RELMEVSKKA REGKLTASDM QGGCFTISSL GGIGTTHFAP IVNAPEVAIL GVSKSSMEPV WNGKEFAPRL ILPMSLSFDH RVIDGADGAR FISYLGSVLA DLRRLVM // ID ORDL_HAEIN Reviewed; 431 AA. AC P44732; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable oxidoreductase OrdL; DE EC=1.-.-.-; GN Name=ordL; OrderedLocusNames=HI_0499; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22156.1; -; Genomic_DNA. DR PIR; F64072; F64072. DR RefSeq; NP_438657.1; NC_000907.1. DR RefSeq; WP_005693676.1; NC_000907.1. DR ProteinModelPortal; P44732; -. DR STRING; 71421.HI0499; -. DR EnsemblBacteria; AAC22156; AAC22156; HI_0499. DR GeneID; 949572; -. DR KEGG; hin:HI0499; -. DR PATRIC; 20189549; VBIHaeInf48452_0517. DR eggNOG; ENOG4105CJP; Bacteria. DR eggNOG; ENOG410XWBT; LUCA. DR KO; K09471; -. DR OMA; AIMRKNM; -. DR OrthoDB; EOG67DPGV; -. DR PhylomeDB; P44732; -. DR BioCyc; RETL1328306-WGS:GSTH-4811-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 431 Probable oxidoreductase OrdL. FT /FTId=PRO_0000058078. SQ SEQUENCE 431 AA; 48026 MW; 76C691B6978069F7 CRC64; MLNFAYQEHV RSYYFDSRNQ DFQFPPLTQI EHADVCVIGA GFFGLSAALE LAEKGKKVIV LEGARVGFGA SGRSGGQAIN GFEEGIDEYI KQVGEDKAHK LWNMSLETID IIDERIEKYS IQCDWKKGYA TLALNERRMD DLIEMEKESH KNFGYQNMQL WDKTKLKQHL GSDIYVGGLF DSNSGHLHPL NYCLGLAKAC VDLGVQIFEQ SPVVDMVEKN GCVEVKTAKS AVISQDVILA TNAYIDVLPK SIHHGINRKI LPVESFIIAT EPLSQAVADS VINNGMSVCD NNLLLDYYRL SADNRLLFGS DSSSEKDMVA IMRKNMLCVF PQLENVKIDY GWAGPIDMTL NSTPHFGRIS PHIYFAHGYS GHGVALTGLA GRIVAEAILG DDERLSIFEG LKVPSVYGGR IIKDLATKIG VQYYKFLDKY R // ID ORN_HAEIN Reviewed; 182 AA. AC P45340; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Oligoribonuclease; DE EC=3.1.-.-; GN Name=orn; OrderedLocusNames=HI_1715; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: 3'-to-5' exoribonuclease specific for small CC oligoribonucleotides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the oligoribonuclease family. CC {ECO:0000305}. 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; L42023; AAC23360.1; -; Genomic_DNA. DR PIR; C64176; C64176. DR RefSeq; NP_439857.1; NC_000907.1. DR RefSeq; WP_005694199.1; NC_000907.1. DR PDB; 1J9A; X-ray; 2.50 A; A=1-182. DR PDBsum; 1J9A; -. DR ProteinModelPortal; P45340; -. DR SMR; P45340; 1-182. DR STRING; 71421.HI1715; -. DR EnsemblBacteria; AAC23360; AAC23360; HI_1715. DR GeneID; 950529; -. DR KEGG; hin:HI1715; -. DR PATRIC; 20192181; VBIHaeInf48452_1794. DR eggNOG; ENOG4108RBP; Bacteria. DR eggNOG; COG1949; LUCA. DR KO; K13288; -. DR OMA; AFFHYRN; -. DR OrthoDB; EOG6Z9B51; -. DR PhylomeDB; P45340; -. DR EvolutionaryTrace; P45340; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central. DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00045; Oligoribonuclease; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR022894; Oligoribonuclease. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Exonuclease; Hydrolase; KW Nuclease; Reference proteome. FT CHAIN 1 182 Oligoribonuclease. FT /FTId=PRO_0000111039. FT DOMAIN 8 171 Exonuclease. FT ACT_SITE 129 129 {ECO:0000255}. FT STRAND 8 18 {ECO:0000244|PDB:1J9A}. FT TURN 20 22 {ECO:0000244|PDB:1J9A}. FT STRAND 25 33 {ECO:0000244|PDB:1J9A}. FT STRAND 39 42 {ECO:0000244|PDB:1J9A}. FT HELIX 52 56 {ECO:0000244|PDB:1J9A}. FT HELIX 60 69 {ECO:0000244|PDB:1J9A}. FT HELIX 71 75 {ECO:0000244|PDB:1J9A}. FT HELIX 82 93 {ECO:0000244|PDB:1J9A}. FT TURN 94 96 {ECO:0000244|PDB:1J9A}. FT TURN 99 101 {ECO:0000244|PDB:1J9A}. FT STRAND 104 108 {ECO:0000244|PDB:1J9A}. FT HELIX 109 119 {ECO:0000244|PDB:1J9A}. FT HELIX 121 125 {ECO:0000244|PDB:1J9A}. FT STRAND 131 133 {ECO:0000244|PDB:1J9A}. FT HELIX 134 144 {ECO:0000244|PDB:1J9A}. FT HELIX 146 151 {ECO:0000244|PDB:1J9A}. FT HELIX 160 177 {ECO:0000244|PDB:1J9A}. SQ SEQUENCE 182 AA; 21199 MW; B78FF5D619915D29 CRC64; MSFDKQNLIW IDLEMTGLDP EKERIIEIAT IVTDKNLNIL AEGPVLAVHQ SDELLNKMND WCQKTHSENG LIERIKASKL TERAAELQTL DFLKKWVPKG ASPICGNSIA QDKRFLVKYM PDLADYFHYR HLDVSTLKEL AARWKPEILE GFKKENTHLA LDDIRESIKE LAYYREHFMK LD // ID OTCC_HAEIN Reviewed; 334 AA. AC P44770; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. DE RecName: Full=Ornithine carbamoyltransferase, catabolic; DE Short=OTCase; DE EC=2.1.3.3; GN Name=arcB; OrderedLocusNames=HI_0596; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group CC from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine CC (ORN) to produce L-citrulline. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate CC + L-citrulline. CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI CC pathway; carbamoyl phosphate from L-arginine: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22253.1; -; Genomic_DNA. DR PIR; H64079; H64079. DR RefSeq; NP_438753.1; NC_000907.1. DR RefSeq; WP_005651072.1; NC_000907.1. DR ProteinModelPortal; P44770; -. DR SMR; P44770; 2-334. DR STRING; 71421.HI0596; -. DR EnsemblBacteria; AAC22253; AAC22253; HI_0596. DR GeneID; 950778; -. DR KEGG; hin:HI0596; -. DR PATRIC; 20189749; VBIHaeInf48452_0617. DR eggNOG; ENOG4105DBV; Bacteria. DR eggNOG; COG0078; LUCA. DR KO; K00611; -. DR OMA; MGMEIRL; -. DR OrthoDB; EOG690MGV; -. DR PhylomeDB; P44770; -. DR UniPathway; UPA00254; UER00365. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central. DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway. DR GO; GO:0019546; P:arginine deiminase pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_01109; OTCase; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR002292; Orn/put_carbamltrans. DR InterPro; IPR024904; OTCase_ArgI. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00658; orni_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Arginine metabolism; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 334 Ornithine carbamoyltransferase, FT catabolic. FT /FTId=PRO_0000112930. FT REGION 57 61 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 135 138 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 236 237 Ornithine binding. {ECO:0000250}. FT REGION 273 276 Carbamoyl phosphate binding. FT {ECO:0000250}. FT BINDING 11 11 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 73 73 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 84 84 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 108 108 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 168 168 Ornithine. {ECO:0000250}. FT BINDING 232 232 Ornithine. {ECO:0000250}. FT BINDING 303 303 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 321 321 Carbamoyl phosphate. {ECO:0000250}. FT SITE 32 32 Important for structural integrity. FT {ECO:0000250}. FT SITE 148 148 Important for structural integrity. FT {ECO:0000250}. SQ SEQUENCE 334 AA; 37647 MW; B44B9ED2C1BB57F5 CRC64; MAFNMKNRHL LSLVHHTERE IKYLLDLSRD LKRAKYAGTE QQKLKGKNIA LIFEKTSTRT RCAFEVAAYD QGAQVTYIDP NSSQIGHKES MKDTARVLGR MYDGIEYRGF KQSIVQELAD YAGVPVFNGL TDEFHPTQML ADVLTMIEHC DKPLSEISYV YIGDARNNMG NSLLLIGAKL GMDVRICGPK ALLPEANLVE MCEKFAKESG ARITVTEDID KAVKGVDFIH TDVWVSMGEP LETWGERIKL LLPYQVTPEL MKRTGNPKVK FMHCLPAFHN SETKVGRQIA EKYPELANGI EVTEEVFESP MNIAFEQAEN RMHTIKAVMV ASLA // ID P5CR_HAEIN Reviewed; 271 AA. AC P43869; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925}; DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925}; DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925}; DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925}; DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925}; GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925}; GN OrderedLocusNames=HI_0307; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate CC (PCA) to L-proline. {ECO:0000255|HAMAP-Rule:MF_01925}. CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5- CC carboxylate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_01925}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC proline from L-glutamate 5-semialdehyde: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01925}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}. CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase CC family. {ECO:0000255|HAMAP-Rule:MF_01925}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21972.1; -; Genomic_DNA. DR PIR; I64060; I64060. DR RefSeq; NP_438474.1; NC_000907.1. DR RefSeq; WP_005694358.1; NC_000907.1. DR ProteinModelPortal; P43869; -. DR STRING; 71421.HI0307; -. DR EnsemblBacteria; AAC21972; AAC21972; HI_0307. DR GeneID; 949427; -. DR KEGG; hin:HI0307; -. DR PATRIC; 20189155; VBIHaeInf48452_0324. DR eggNOG; ENOG4105II7; Bacteria. DR eggNOG; COG0345; LUCA. DR KO; K00286; -. DR OMA; RTFNEHQ; -. DR OrthoDB; EOG6JB16S; -. DR PhylomeDB; P43869; -. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.3730.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01925; P5C_reductase; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029036; P5CR_dimer. DR InterPro; IPR028939; ProC_N. DR InterPro; IPR000304; Pyrroline-COOH_reductase. DR PANTHER; PTHR11645; PTHR11645; 1. DR Pfam; PF03807; F420_oxidored; 1. DR Pfam; PF14748; P5CR_dimer; 1. DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00112; proC; 1. DR PROSITE; PS00521; P5CR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Proline biosynthesis; Reference proteome. FT CHAIN 1 271 Pyrroline-5-carboxylate reductase. FT /FTId=PRO_0000187290. SQ SEQUENCE 271 AA; 29124 MW; 132B69A9CEAE8B35 CRC64; MQHKLIAFIG GGNMAQAIIL GLLKQGYPAE QIIVNDPNEE KRAFFANLDV ATSENNVGSA IKAEVVLLAV KPQMMAEVCS PLSAVDFSDK LLISIAAGIS TERLNALIPS VKSIVRVMPN TPALVGEGMA GLFAPKNTSE NYRTFAQDLL GAVGRTVWVN DETQMHAVTA ASGSSPAYFF LMLEAMQKAL IKMNIDEKTA RELVQQSMLG AAKMVTENPQ IALSTLRENV TSKGGTTAAA LAVFDAQHFN QTIEQAMQAC LSRSQEMETL F // ID PAL_HAEIN Reviewed; 153 AA. AC P10324; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 11-MAY-2016, entry version 121. DE RecName: Full=Outer membrane protein P6; DE Short=OMP P6; DE AltName: Full=15 kDa peptidoglycan-associated lipoprotein; DE Short=PC protein; DE Flags: Precursor; GN Name=pal; Synonyms=ompP6; OrderedLocusNames=HI_0381; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, RP DIACYLGLYCEROL AT CYS-20, AND PALMITOYLATION AT CYS-20. RX PubMed=2828309; RA Deich R.A., Metcalf B.J., Finn C.W., Farley J.E., Green B.A.; RT "Cloning of genes encoding a 15,000-dalton peptidoglycan-associated RT outer membrane lipoprotein and an antigenically related 15,000-dalton RT protein from Haemophilus influenzae."; RL J. Bacteriol. 170:489-498(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3257200; RA Nelson M.B., Apicella M.A., Murphy T.F., Vankeulen H., Spotila L.D., RA Rekosh D.; RT "Cloning and sequencing of Haemophilus influenzae outer membrane RT protein P6."; RL Infect. Immun. 56:128-134(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [4] RP STRUCTURE BY NMR OF 20-153 IN COMPLEX WITH PEPTIDOGLYCAN. RX PubMed=16475801; DOI=10.1021/bi052227i; RA Parsons L.M., Lin F., Orban J.; RT "Peptidoglycan recognition by Pal, an outer membrane lipoprotein."; RL Biochemistry 45:2122-2128(2006). CC -!- FUNCTION: Thought to play a role in bacterial envelope integrity. CC Links the outer membrane to the peptidoglycan layer. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. CC -!- SIMILARITY: Belongs to the OmpA family. Pal subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 OmpA-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M19391; AAA24994.1; -; Genomic_DNA. DR EMBL; M18878; AAA24940.1; -; Genomic_DNA. DR EMBL; L42023; AAC22039.1; -; Genomic_DNA. DR PIR; A28543; A28543. DR RefSeq; NP_438542.1; NC_000907.1. DR RefSeq; WP_005652235.1; NC_000907.1. DR PDB; 2AIZ; NMR; -; P=20-153. DR PDBsum; 2AIZ; -. DR ProteinModelPortal; P10324; -. DR SMR; P10324; 20-153. DR STRING; 71421.HI0381; -. DR Allergome; 7668; Hae in P6. DR EnsemblBacteria; AAC22039; AAC22039; HI_0381. DR GeneID; 949485; -. DR KEGG; hin:HI0381; -. DR PATRIC; 20189311; VBIHaeInf48452_0399. DR eggNOG; ENOG4105KCK; Bacteria. DR eggNOG; COG2885; LUCA. DR KO; K03640; -. DR OMA; QLNVVSY; -. DR OrthoDB; EOG6PP9QB; -. DR PhylomeDB; P10324; -. DR EvolutionaryTrace; P10324; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR Gene3D; 3.30.1330.60; -; 1. DR InterPro; IPR006664; OMP_bac. DR InterPro; IPR006665; OmpA-like. DR InterPro; IPR006690; OMPA-like_CS. DR InterPro; IPR014169; Pal_lipo. DR Pfam; PF00691; OmpA; 1. DR PRINTS; PR01021; OMPADOMAIN. DR SUPFAM; SSF103088; SSF103088; 1. DR TIGRFAMs; TIGR02802; Pal_lipo; 1. DR PROSITE; PS01068; OMPA_1; 1. DR PROSITE; PS51123; OMPA_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell outer membrane; Complete proteome; KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal. FT SIGNAL 1 19 FT CHAIN 20 153 Outer membrane protein P6. FT /FTId=PRO_0000020123. FT DOMAIN 40 153 OmpA-like. {ECO:0000255|PROSITE- FT ProRule:PRU00473}. FT REGION 55 56 Peptidoglycan binding. FT REGION 97 101 Peptidoglycan binding. FT LIPID 20 20 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:2828309}. FT LIPID 20 20 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:2828309}. FT STRAND 26 29 {ECO:0000244|PDB:2AIZ}. FT HELIX 41 44 {ECO:0000244|PDB:2AIZ}. FT TURN 45 47 {ECO:0000244|PDB:2AIZ}. FT STRAND 50 52 {ECO:0000244|PDB:2AIZ}. FT HELIX 62 77 {ECO:0000244|PDB:2AIZ}. FT STRAND 83 88 {ECO:0000244|PDB:2AIZ}. FT STRAND 91 93 {ECO:0000244|PDB:2AIZ}. FT HELIX 95 115 {ECO:0000244|PDB:2AIZ}. FT HELIX 120 122 {ECO:0000244|PDB:2AIZ}. FT STRAND 123 127 {ECO:0000244|PDB:2AIZ}. FT TURN 129 131 {ECO:0000244|PDB:2AIZ}. FT HELIX 140 146 {ECO:0000244|PDB:2AIZ}. FT STRAND 147 152 {ECO:0000244|PDB:2AIZ}. SQ SEQUENCE 153 AA; 16108 MW; 3DF358122EF17A11 CRC64; MNKFVKSLLV AGSVAALAAC SSSNNDAAGN GAAQTFGGYS VADLQQRYNT VYFGFDKYDI TGEYVQILDA HAAYLNATPA AKVLVEGNTD ERGTPEYNIA LGQRRADAVK GYLAGKGVDA GKLGTVSYGE EKPAVLGHDE AAYSKNRRAV LAY // ID OPP21_HAEIN Reviewed; 359 AA. AC P43839; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Outer membrane protein P2; DE Short=OMP P2; DE Flags: Precursor; GN Name=ompP2; OrderedLocusNames=HI_0139; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Forms pores that allow passive diffusion of small CC molecules across the outer membrane. {ECO:0000250}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the Gram-negative porin 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; L42023; AAC21810.1; -; Genomic_DNA. DR PIR; D64050; D64050. DR RefSeq; NP_438308.1; NC_000907.1. DR RefSeq; WP_005694426.1; NC_000907.1. DR ProteinModelPortal; P43839; -. DR STRING; 71421.HI0139; -. DR EnsemblBacteria; AAC21810; AAC21810; HI_0139. DR GeneID; 951048; -. DR KEGG; hin:HI0139; -. DR PATRIC; 20188769; VBIHaeInf48452_0141. DR eggNOG; COG3203; LUCA. DR KO; K03285; -. DR OMA; FHIKATH; -. DR OrthoDB; EOG6GR372; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.160.10; -; 1. DR InterPro; IPR023614; Porin_dom. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Ion transport; Membrane; KW Porin; Reference proteome; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 359 Outer membrane protein P2. FT /FTId=PRO_0000025258. SQ SEQUENCE 359 AA; 39375 MW; 7E9EFFFC2BD50314 CRC64; MKKTLAALIV GAFAASAANA AVVYNNEGTN VELGGRLSII AEQSNSTVDN QKQQHGALRN QGSRFHIKAT HNFGDGFYAQ GYLETRFVTK ASENGSDNFG DITSKYAYVT LGNKAFGEVK LGRAKTIADG ITSAEDKEYG VLNNSDYIPT SGNTVGYTFK GIDGLVLGAN YLLAQKREGA KNTNKQPNDK AGEVRIGEIN NGIQVGAKYD ANDIVAKIAY GRTNYKYNEA DEHTQQLNGV LATLGYRFSD LGLLVSLDSG YAKTKNYKTK HEKRYFVSPG FQYELMEDTN VYGNFKYERT SVDQGEKTRE QAVLFGVDHK LHKQLLTYIE GAYARTKTTN GGVKTEKEKS VGVGLRVYF // ID OPPB_HAEIN Reviewed; 306 AA. AC P45054; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Oligopeptide transport system permease protein OppB; GN Name=oppB; OrderedLocusNames=HI_1123; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22777.1; -; Genomic_DNA. DR PIR; E64184; E64184. DR RefSeq; NP_439280.1; NC_000907.1. DR RefSeq; WP_005647620.1; NC_000907.1. DR STRING; 71421.HI1123; -. DR EnsemblBacteria; AAC22777; AAC22777; HI_1123. DR GeneID; 950094; -. DR KEGG; hin:HI1123; -. DR PATRIC; 20190919; VBIHaeInf48452_1172. DR eggNOG; ENOG4105CJM; Bacteria. DR eggNOG; COG0601; LUCA. DR KO; K15581; -. DR OMA; STQYFNY; -. DR OrthoDB; EOG66F098; -. DR PhylomeDB; P45054; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015421; F:oligopeptide-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0042937; F:tripeptide transporter activity; IBA:GO_Central. DR GO; GO:0035672; P:oligopeptide transmembrane transport; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042939; P:tripeptide transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 306 Oligopeptide transport system permease FT protein OppB. FT /FTId=PRO_0000060148. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 10 30 Helical. {ECO:0000305}. FT TOPO_DOM 31 99 Extracellular. {ECO:0000305}. FT TRANSMEM 100 121 Helical. {ECO:0000305}. FT TOPO_DOM 122 137 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 138 158 Helical. {ECO:0000305}. FT TOPO_DOM 159 172 Extracellular. {ECO:0000305}. FT TRANSMEM 173 190 Helical. {ECO:0000305}. FT TOPO_DOM 191 226 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 227 250 Helical. {ECO:0000305}. FT TOPO_DOM 251 271 Extracellular. {ECO:0000305}. FT TRANSMEM 272 293 Helical. {ECO:0000305}. FT TOPO_DOM 294 306 Cytoplasmic. {ECO:0000305}. FT DOMAIN 94 293 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 306 AA; 33690 MW; 5239D859C336E5B8 CRC64; MLKFIFKRLL EALPTLFILI TFSFFLMRLA PGSPFTSERA YPPEVMANIE AKYHLNEPLY KQYFLYLENL SKGDFGPSFK YKDQSVNDLI ASAFPVSIKL GMVAFAFAVV LGVTAGTLAA LNQNSRWDYI LMSFSMLGVI MPSFVFAPVL VLIFAIYLGW LPAGGWNGGT AMYMILPVAS LTIAYVAGIA RIMRGSMIEV LHSNFIRTAK AKGLSMSRII LKHALRPALL PVITYLGPAF VGIITGSMVI ESVFGLPGMG LLFVNGALNR DYSLVLSLTI LVGTLTILFN AIVDILYAII DPKIRY // ID OM26_HAEIN Reviewed; 197 AA. AC Q57483; Q9S690; Q9S691; Q9S692; Q9S699; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 100. DE RecName: Full=Outer membrane protein 26; DE Flags: Precursor; GN Name=omp26; Synonyms=skp; OrderedLocusNames=HI_0916; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=NTHi 289, UC1, UC10, and UC2; RX PubMed=10085039; RA El-Adhami W., Kyd J.M., Bastin D.A., Cripps A.W.; RT "Characterization of the gene encoding a 26-kilodalton protein (OMP26) RT from nontypeable Haemophilus influenzae and immune responses to the RT recombinant protein."; RL Infect. Immun. 67:1935-1942(1999). RN [3] RP PROTEIN SEQUENCE OF 24-30. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Cell outer membrane. CC -!- SIMILARITY: Belongs to the Skp 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; L42023; AAC22574.1; -; Genomic_DNA. DR EMBL; AF109085; AAD23967.1; -; Genomic_DNA. DR EMBL; AF109086; AAD23968.1; -; Genomic_DNA. DR EMBL; AF109087; AAD23969.1; -; Genomic_DNA. DR EMBL; AF109094; AAD23976.1; -; Genomic_DNA. DR PIR; E64102; E64102. DR RefSeq; NP_439076.1; NC_000907.1. DR RefSeq; WP_005693263.1; NC_000907.1. DR ProteinModelPortal; Q57483; -. DR STRING; 71421.HI0916; -. DR EnsemblBacteria; AAC22574; AAC22574; HI_0916. DR GeneID; 949929; -. DR KEGG; hin:HI0916; -. DR PATRIC; 20190487; VBIHaeInf48452_0957. DR eggNOG; COG2825; LUCA. DR KO; K06142; -. DR OMA; KDNQTRQ; -. DR OrthoDB; EOG6F297R; -. DR PhylomeDB; Q57483; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR005632; Chaperone_Skp. DR InterPro; IPR024930; Skp_domain. DR Pfam; PF03938; OmpH; 1. DR PIRSF; PIRSF002094; OMP26_Skp; 1. DR SMART; SM00935; OmpH; 1. DR SUPFAM; SSF111384; SSF111384; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Direct protein sequencing; KW Membrane; Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000269|PubMed:10675023}. FT CHAIN 24 197 Outer membrane protein 26. FT /FTId=PRO_0000020183. FT VARIANT 102 102 Q -> E (in strain: NTHI 289 and UC1). FT VARIANT 146 146 D -> N (in strain: UC1). FT VARIANT 157 157 K -> R (in strain: NTHI 289 and UC10). FT VARIANT 170 170 I -> V (in strain: NTHI 289, UC1 and FT UC2). SQ SEQUENCE 197 AA; 21718 MW; 0C53927521EDB5DC CRC64; MKNIAKVTAL ALGIALASGY ASAEEKIAFI NAGYIFQHHP DRQAVADKLD AEFKPVAEKL AASKKEVDDK IAAARKKVEA KVAALEKDAP RLRQADIQKR QQEINKLGAA EDAELQKLMQ EQDKKVQEFQ AQNEKRQAEE RGKLLDSIQT ATNNLAKAKG YTYVLDANSI VFAVEGKDIT EEVLKSIPAS EKAQEKK // ID OMP51_HAEIN Reviewed; 353 AA. AC P43840; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Outer membrane protein P5; DE Short=OMP P5; DE Flags: Precursor; GN Name=ompA; Synonyms=ompP5; OrderedLocusNames=HI_1164; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane CC protein. CC -!- SIMILARITY: Belongs to the OmpA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 OmpA-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22819.1; -; Genomic_DNA. DR PIR; C64187; C64187. DR RefSeq; NP_439322.1; NC_000907.1. DR RefSeq; WP_010869142.1; NC_000907.1. DR ProteinModelPortal; P43840; -. DR STRING; 71421.HI1164; -. DR EnsemblBacteria; AAC22819; AAC22819; HI_1164. DR GeneID; 950124; -. DR KEGG; hin:HI1164; -. DR PATRIC; 20191007; VBIHaeInf48452_1216. DR eggNOG; ENOG4105W44; Bacteria. DR eggNOG; COG2885; LUCA. DR KO; K03286; -. DR OMA; EYALTKN; -. DR OrthoDB; EOG6PP9QB; -. DR PhylomeDB; P43840; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW. DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.160.20; -; 1. DR Gene3D; 3.30.1330.60; -; 1. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR006664; OMP_bac. DR InterPro; IPR002368; OmpA. DR InterPro; IPR006665; OmpA-like. DR InterPro; IPR006690; OMPA-like_CS. DR InterPro; IPR000498; OmpA-like_TM_dom. DR Pfam; PF00691; OmpA; 1. DR Pfam; PF01389; OmpA_membrane; 1. DR PRINTS; PR01021; OMPADOMAIN. DR PRINTS; PR01022; OUTRMMBRANEA. DR SUPFAM; SSF103088; SSF103088; 1. DR SUPFAM; SSF56925; SSF56925; 1. DR PROSITE; PS01068; OMPA_1; 1. DR PROSITE; PS51123; OMPA_2; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Disulfide bond; Ion transport; KW Membrane; Porin; Reference proteome; Signal; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 21 {ECO:0000250}. FT CHAIN 22 353 Outer membrane protein P5. FT /FTId=PRO_0000020107. FT DOMAIN 227 353 OmpA-like. {ECO:0000255|PROSITE- FT ProRule:PRU00473}. FT DISULFID 326 338 {ECO:0000250}. SQ SEQUENCE 353 AA; 37744 MW; 64ACB3E7BFF96B39 CRC64; MKKTAIALVV AGLAAASVAQ AAPQENTFYA GVKAGQASFH DGLRALAREY KVGYHRNSFT YGVFGGYQIL NQNNLGLAVE LGYDDFGRAK GREKGKTVVK HTNHGTHLSL KGSYEVLEGL DVYGKAGVAL VRSDYKLYNE NSSTLKKLGE HHRARASGLF AVGAEYAVLP ELAVRLEYQW LTRVGKYRPQ DKPNTALNYN PWIGSINAGI SYRFGQGAAP VVAAPEVVSK TFSLNSDVTF AFGKANLKPQ AQATLDSIYG EMSQVKSAKV AVAGYTDRIG SDAFNVKLSQ ERADSVANYF VAKGVAADAI SATGYGKANP VTGATCDQVK GRKALIACFA PDRRVEIAVN GTK // ID OXYR_HAEIN Reviewed; 301 AA. AC P44418; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 98. DE RecName: Full=Hydrogen peroxide-inducible genes activator; GN Name=oxyR; OrderedLocusNames=HI_0571; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=8890216; RA Maciver I., Hansen E.J.; RT "Lack of expression of the global regulator OxyR in Haemophilus RT influenzae has a profound effect on growth phenotype."; RL Infect. Immun. 64:4618-4629(1996). CC -!- FUNCTION: Required for the induction of a regulon of hydrogen CC peroxide inducible genes such as catalase and glutathione- CC reductase. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22229.1; -; Genomic_DNA. DR EMBL; U49355; AAB48948.1; -; Genomic_DNA. DR PIR; C64078; C64078. DR RefSeq; NP_438728.1; NC_000907.1. DR RefSeq; WP_005649559.1; NC_000907.1. DR ProteinModelPortal; P44418; -. DR SMR; P44418; 89-289. DR STRING; 71421.HI0571; -. DR EnsemblBacteria; AAC22229; AAC22229; HI_0571. DR GeneID; 950698; -. DR KEGG; hin:HI0571; -. DR PATRIC; 20189697; VBIHaeInf48452_0591. DR eggNOG; ENOG4105C5Q; Bacteria. DR eggNOG; ENOG410XNR2; LUCA. DR KO; K04761; -. DR OMA; CPEFARF; -. DR OrthoDB; EOG6N6848; -. DR PhylomeDB; P44418; -. DR Proteomes; UP000000579; 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; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 301 Hydrogen peroxide-inducible genes FT activator. FT /FTId=PRO_0000105733. FT DOMAIN 1 58 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 18 37 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 301 AA; 33761 MW; 1CAF1FBC3E41F9DE CRC64; MNIRDLEYLV ALSEYKHFRR AADSCNVSQP TLSGQIRKLE DELGIILLER TSRKVLFTQS GMLLVDQART VLREVKLLKE MASNQGKEMT GPLHIGLIPT VGPYLLPYIV PMLKAAFPDL EVFLYEAQTH QLLEQLETGR LDCAIVATVP ETEAFIEVPI FNEKMLLAVS EHHPWAQESK LPMNQLNGQE MLMLDDGHCL RNQALDYCFT AGAKENSHFQ ATSLETLRNM VAANAGITFM PELAVLNEGT RKGVKYIPCY SPEPSRTIAL VYRPGSPLRN RYERVASAVS DEVKSILDGL K // ID PARE_HAEIN Reviewed; 632 AA. AC P43703; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00938}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00938}; DE AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00938}; GN Name=parE {ECO:0000255|HAMAP-Rule:MF_00938}; GN OrderedLocusNames=HI_1528; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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_00938}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00938}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00938}; 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_00938}; CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00938}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type CC 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00938}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00938}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23174.1; -; Genomic_DNA. DR PIR; E64127; E64127. DR RefSeq; NP_439677.1; NC_000907.1. DR RefSeq; WP_005693553.1; NC_000907.1. DR ProteinModelPortal; P43703; -. DR SMR; P43703; 5-383. DR STRING; 71421.HI1528; -. DR EnsemblBacteria; AAC23174; AAC23174; HI_1528. DR GeneID; 950390; -. DR KEGG; hin:HI1528; -. DR PATRIC; 20191781; VBIHaeInf48452_1599. DR eggNOG; ENOG4105C7D; Bacteria. DR eggNOG; COG0187; LUCA. DR KO; K02622; -. DR OMA; TPDRIKL; -. DR OrthoDB; EOG6P334W; -. DR PhylomeDB; P43703; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR HAMAP; MF_00938; ParE_type1; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. 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; IPR005737; TopoIV_B_Gneg. 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; TIGR01055; parE_Gneg; 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 1 632 DNA topoisomerase 4 subunit B. FT /FTId=PRO_0000145430. FT DOMAIN 412 525 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT NP_BIND 110 116 ATP. {ECO:0000255|HAMAP-Rule:MF_00938}. FT METAL 418 418 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00938}. FT METAL 490 490 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00938}. FT METAL 490 490 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT METAL 492 492 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT BINDING 5 5 ATP. {ECO:0000255|HAMAP-Rule:MF_00938}. FT BINDING 42 42 ATP. {ECO:0000255|HAMAP-Rule:MF_00938}. FT BINDING 69 69 ATP. {ECO:0000255|HAMAP-Rule:MF_00938}. FT BINDING 334 334 ATP. {ECO:0000255|HAMAP-Rule:MF_00938}. FT SITE 443 443 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT SITE 446 446 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT SITE 497 497 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00938}. FT SITE 617 617 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00938}. SQ SEQUENCE 632 AA; 70173 MW; 6224F4E3D2A063CE CRC64; MTTNYSAQEI TVLKDLEPVQ IRPGMYTDTT RPNHLAQEVI DNSVDEALAG FATKIEVILH PDQSIEVTDN GRGMPVDIHP TEGVSGVEVI LTKLHAGGKF SNKNYEFAGG LHGVGISVVN ALSERVDIQV KRNGEIYKIA FENGSKVEEL EIIGTCGRRT TGTIVHFKPN PKYFDSAKFS VSRLRHLLRA KAVLCSGLEI KFIDKVNNTQ DIWLYEDGLS DYLIEAVNGF ETLPKKPFVG EFKGANEAVS WALLWLPEGG ELIGESYVNL IPTIQGGTHV NGLRQGLLDA IREFCEFRNL LPRGVKLTAD DIWDRCSYIL SLKMQDAQFA GQTKERLSSR QSAVFVSGVL KDAFSLWLNQ NVQDAEKLAE IAISSAQRRL RAAKKVVRKK LVSGPALPGK LADCGSQDLE KTELFLVEGD SAGGSAKQAR DREYQAILPL RGKILNTWEV SPDQVLGSTE IHDIAVALGI DPDSNDLSQL RYGKVCILAD ADSDGLHIAT LLCALFLRHF PKLVQDGHVY VAMPPLYRID LNKEVFYALD ENEKEAILDR LKNKKGKPNV QRFKGLGEMN PSQLRETTMD PNTRRLVQLT YDLGEDQGSD TLELMDMLLA KKRSEDRKNW LQAKGDQVDL SV // ID PANF_HAEIN Reviewed; 484 AA. AC P44963; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Sodium/pantothenate symporter; DE AltName: Full=Pantothenate permease; GN Name=panF; OrderedLocusNames=HI_0975; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular CC pantothenate. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) CC (TC 2.A.21) 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; L42023; AAC22634.1; -; Genomic_DNA. DR PIR; H64105; H64105. DR RefSeq; NP_439137.1; NC_000907.1. DR RefSeq; WP_005647973.1; NC_000907.1. DR STRING; 71421.HI0975; -. DR EnsemblBacteria; AAC22634; AAC22634; HI_0975. DR GeneID; 950256; -. DR KEGG; hin:HI0975; -. DR PATRIC; 20190609; VBIHaeInf48452_1017. DR eggNOG; ENOG4108IA2; Bacteria. DR eggNOG; COG4145; LUCA. DR KO; K14392; -. DR OMA; ILMLGMH; -. DR OrthoDB; EOG6HB9QC; -. DR PhylomeDB; P44963; -. DR Proteomes; UP000000579; 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:0015233; F:pantothenate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0031402; F:sodium ion binding; IEA:InterPro. DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0071436; P:sodium ion export; IEA:InterPro. DR InterPro; IPR011849; Na/pantothenate_symporter. DR InterPro; IPR001734; Na/solute_symporter. DR InterPro; IPR018212; Na/solute_symporter_CS. DR PANTHER; PTHR11819; PTHR11819; 1. DR Pfam; PF00474; SSF; 1. DR TIGRFAMs; TIGR02119; panF; 1. DR TIGRFAMs; TIGR00813; sss; 1. DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1. DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1. DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; Reference proteome; Sodium; Sodium transport; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 484 Sodium/pantothenate symporter. FT /FTId=PRO_0000105403. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 307 327 Helical. {ECO:0000255}. FT TRANSMEM 366 386 Helical. {ECO:0000255}. FT TRANSMEM 397 417 Helical. {ECO:0000255}. FT TRANSMEM 424 444 Helical. {ECO:0000255}. FT TRANSMEM 446 466 Helical. {ECO:0000255}. SQ SEQUENCE 484 AA; 52501 MW; BE6EFB27C1DE9C06 CRC64; MNLGIILPLI IYLTFVFGAA IFAYVKRTKG DFLTEYYVGN RSMTGFVLAM TTASTYASAS SFVGGPGAAY KYGLGWVLLA MIQVPVVWLA LGALGKKFAL LSRETNALTI NDLFFYRYKN KYLVWLSSLA LLLAFFAAMT VQFIGGARLL ETTIGISYTQ ALLLFALTVG IYTFIGGFRA VVLTDTIQGT VMIFGTIILL IGTIYALGGV ESAVNKLTEI DPDLVTPYGP NGMLDFQFMA SFWILVCFGV VGLPHTAVRC MAFKDSKALH RGMLIGTIVL SIIMLGMHLA GALGRAVIPN LTVSDQVIPT LMIKVLPPIV AGIFLAAPMS AIMSTIDAQL IQSSSIFVKD LYLSAKPEAA KNEKKVSYFS SIITLILTAL LIFAALNPPD MIIWLNLFAF GGLEAAFLWV IVLGIYWDKA NAYGALSSMI IGLGSYILLT QLGIKLFNFH QIVPSLVFGL IAFLVGNKLG ERRIEKTQLK VTAL // ID PBP7_HAEIN Reviewed; 292 AA. AC P44664; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=D-alanyl-D-alanine endopeptidase; DE Short=DD-endopeptidase; DE EC=3.4.21.-; DE AltName: Full=Penicillin-binding protein 7 homolog; DE Short=PBP-7; DE Flags: Precursor; GN Name=pbpG; OrderedLocusNames=HI_0364; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. May play a specialized role in CC remodeling the cell wall. Specifically hydrolyzes the DD- CC diaminopimelate-alanine bonds in high-molecular-mass murein CC sacculi (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S11 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; L42023; AAC22022.1; -; Genomic_DNA. DR PIR; H64149; H64149. DR RefSeq; NP_438525.1; NC_000907.1. DR RefSeq; WP_005693802.1; NC_000907.1. DR ProteinModelPortal; P44664; -. DR STRING; 71421.HI0364; -. DR MEROPS; S11.002; -. DR EnsemblBacteria; AAC22022; AAC22022; HI_0364. DR GeneID; 949374; -. DR KEGG; hin:HI0364; -. DR PATRIC; 20189271; VBIHaeInf48452_0381. DR eggNOG; ENOG41061WM; Bacteria. DR eggNOG; COG1686; LUCA. DR KO; K07262; -. DR OMA; QFIKKMN; -. DR OrthoDB; EOG6RJV2H; -. DR PhylomeDB; P44664; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IBA:GO_Central. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR018044; Peptidase_S11. DR InterPro; IPR001967; Peptidase_S11_N. DR Pfam; PF00768; Peptidase_S11; 1. DR PRINTS; PR00725; DADACBPTASE1. DR SUPFAM; SSF56601; SSF56601; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Hydrolase; Peptidoglycan synthesis; Periplasm; Reference proteome; KW Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 292 D-alanyl-D-alanine endopeptidase. FT /FTId=PRO_0000027238. FT ACT_SITE 45 45 Acyl-ester intermediate. {ECO:0000250}. FT ACT_SITE 48 48 Proton acceptor. {ECO:0000250}. FT ACT_SITE 102 102 {ECO:0000250}. FT BINDING 207 207 Substrate. {ECO:0000250}. SQ SEQUENCE 292 AA; 32620 MW; 919633D863314FF7 CRC64; MFKKALFILS LCPSFALAQS YVVYDFTHNR VLESHASDSI QPIASVTKLM TANVFLENNK NPNCRIAITK EDTDRIKGTG TKLPKNIPIS CNELLKAMLV HSDNYAAHAL SRAAGISRRQ FIKKMNEKAH QLGMYSTRFH DSSGLSSYNI SSPMDLVKLA KYSLNKSDIK RLSNLSATYI QAGKQKLYIK NTNKLVRDEI FDAAVNKTGY IQESGYNLVF INKHRCKNAT IGVISLNNTS SAYRSSFTKS KLEKFGCTAL NGRTIRDVAG EAQYEDGYDE VGFNTLIQKL SK // ID PCKA_HAEIN Reviewed; 538 AA. AC P43923; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Phosphoenolpyruvate carboxykinase [ATP] {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453}; DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453}; DE EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453}; GN Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; GN OrderedLocusNames=HI_0809; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the CC conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) CC through direct phosphoryl transfer between the nucleoside CC triphosphate and OAA. {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- CATALYTIC ACTIVITY: ATP + oxaloacetate = ADP + phosphoenolpyruvate CC + CO(2). {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00453}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00453}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [ATP] CC family. {ECO:0000255|HAMAP-Rule:MF_00453}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22468.1; -; Genomic_DNA. DR PIR; E64095; E64095. DR RefSeq; NP_438969.1; NC_000907.1. DR RefSeq; WP_010869059.1; NC_000907.1. DR ProteinModelPortal; P43923; -. DR SMR; P43923; 3-537. DR STRING; 71421.HI0809; -. DR EnsemblBacteria; AAC22468; AAC22468; HI_0809. DR GeneID; 950742; -. DR KEGG; hin:HI0809; -. DR PATRIC; 20190273; VBIHaeInf48452_0850. DR eggNOG; ENOG4105DJ1; Bacteria. DR eggNOG; COG1866; LUCA. DR KO; K01610; -. DR OMA; RFIVKEP; -. DR OrthoDB; EOG6DG2RK; -. DR PhylomeDB; P43923; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR Gene3D; 3.40.449.10; -; 1. DR Gene3D; 3.90.228.20; -; 2. DR HAMAP; MF_00453; PEPCK_ATP; 1. DR InterPro; IPR001272; PEP_carboxykinase_ATP. DR InterPro; IPR013035; PEP_carboxykinase_C. DR InterPro; IPR008210; PEP_carboxykinase_N. DR InterPro; IPR015994; PEPCK_ATP_CS. DR Pfam; PF01293; PEPCK_ATP; 1. DR PIRSF; PIRSF006294; PEP_crbxkin; 1. DR SUPFAM; SSF68923; SSF68923; 1. DR TIGRFAMs; TIGR00224; pckA; 1. DR PROSITE; PS00532; PEPCK_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Decarboxylase; KW Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 538 Phosphoenolpyruvate carboxykinase [ATP]. FT /FTId=PRO_0000203824. FT NP_BIND 246 254 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT NP_BIND 447 448 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT METAL 211 211 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT METAL 230 230 Manganese; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00453}. FT METAL 267 267 Manganese. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT BINDING 64 64 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT BINDING 205 205 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT BINDING 211 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT BINDING 211 211 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT BINDING 230 230 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT BINDING 295 295 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT BINDING 331 331 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. FT BINDING 331 331 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00453}. FT BINDING 453 453 ATP. {ECO:0000255|HAMAP-Rule:MF_00453}. SQ SEQUENCE 538 AA; 59404 MW; EF7AD503933DB3E6 CRC64; MTDLNKVVKE LEALGIYDVK EVVYNPSYEQ LFEEETKPGL EGFEKGTLTT TGAVAVDTGI FTGRSPKDKY IVLDEKTKDT VWWTSETAKN DNKPMNQATW QSLKDLVTNQ LSRKRLFVVD GFCGASEHDR IAVRIVTEVA WQAHFVKNMF IRPTEEQLKN FEPDFVVMNG SKVTNPNWKE QGLNSENFVA FNLTERIQLI GGTWYGGEMK KGMSSMMNYF LPLKGVGAMH CSANVGKDGD VAIFFGLSGT GKTTLSTDPK RELIGDDEHG WDDVGIFNFE GGCYAKTIHL SEENEPDIYR AIRRDALLEN VVVRSDGSVD FDDGSKTENT RVSYPIYHID NIVKPVSRAG HATKVIFLTA DAFGVLPPVS KLTPEQTKYY FLSGFTAKLA GTERGITEPT PTFSACFGAA FLTLHPTQYA EVLVKRMQAA GAEAYLVNTG WNGTGKRISI KDTRGIIDAI LDGSIEKAEM GELPIFNLAI PKALPGVDSA ILDPRDTYAD KAQWQSKAED LAGRFVKNFV KYATNEEGKA LIAAGPKA // ID PDXS_HAEIN Reviewed; 291 AA. AC P45293; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE Short=PLP synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01824}; DE AltName: Full=Pdx1 {ECO:0000255|HAMAP-Rule:MF_01824}; GN Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824}; GN OrderedLocusNames=HI_1647; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from CC ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and CC ammonia. The ammonia is provided by the PdxT subunit. Can also use CC ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, CC resulting from enzyme-catalyzed isomerization of RBP and G3P, CC respectively. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of CC heterodimers. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP- CC Rule:MF_01824}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23294.1; -; Genomic_DNA. DR PIR; F64173; F64173. DR RefSeq; NP_439789.1; NC_000907.1. DR RefSeq; WP_005654219.1; NC_000907.1. DR ProteinModelPortal; P45293; -. DR SMR; P45293; 1-274. DR STRING; 71421.HI1647; -. DR EnsemblBacteria; AAC23294; AAC23294; HI_1647. DR GeneID; 950488; -. DR KEGG; hin:HI1647; -. DR PATRIC; 20192039; VBIHaeInf48452_1723. DR eggNOG; ENOG4105CD9; Bacteria. DR eggNOG; COG0214; LUCA. DR KO; K06215; -. DR OMA; MVGINES; -. DR OrthoDB; EOG6W9XBJ; -. DR PhylomeDB; P45293; -. DR UniPathway; UPA00245; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_01824; PdxS; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001852; PdxS/SNZ. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF01680; SOR_SNZ; 1. DR PIRSF; PIRSF029271; Pdx1; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00343; TIGR00343; 1. DR PROSITE; PS01235; PDXS_SNZ_1; 1. DR PROSITE; PS51129; PDXS_SNZ_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Schiff base. FT CHAIN 1 291 Pyridoxal 5'-phosphate synthase subunit FT PdxS. FT /FTId=PRO_0000109397. FT REGION 234 235 D-ribose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT ACT_SITE 80 80 Schiff-base intermediate with D-ribose 5- FT phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824}. FT BINDING 23 23 D-ribose 5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824}. FT BINDING 152 152 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT BINDING 164 164 Glyceraldehyde 3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT BINDING 213 213 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824}. SQ SEQUENCE 291 AA; 31682 MW; FBF41E74103536AD CRC64; MAENRYELNK NLAQMLKGGV IMDVQNPEQA RIAEAAGAAA VMALERIPAD IRAVGGVSRM SDPKMIKEIQ GAVSIPVMAK VRIGHFVEAQ ILEAIEIDYI DESEVLSPAD NRFHVDKKEF QVPFVCGAKD LGEALRRIAE GASMIRTKGE PGTGDIVQAV RHMRMMSQEI RRIQNLREDE LYVAAKDLQV PVELVQYVHK HGKLPVVNFA AGGIATPADA ALMMQLGAEG VFVGSGIFKS GDPIKRASAI VKAVTNYRNP QILAQISEDL GEAMVGINEN EIQILMAERG K // ID PEPT_HAEIN Reviewed; 412 AA. AC P45172; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Peptidase T {ECO:0000255|HAMAP-Rule:MF_00550}; DE EC=3.4.11.4 {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Aminotripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE Short=Tripeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; DE AltName: Full=Tripeptide aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00550}; GN Name=pepT {ECO:0000255|HAMAP-Rule:MF_00550}; GN OrderedLocusNames=HI_1348; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. CC {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a CC tripeptide. {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00550}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00550}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}. CC -!- SIMILARITY: Belongs to the peptidase M20B family. CC {ECO:0000255|HAMAP-Rule:MF_00550}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22995.1; -; Genomic_DNA. DR PIR; C64118; C64118. DR RefSeq; NP_439499.1; NC_000907.1. DR RefSeq; WP_005694011.1; NC_000907.1. DR ProteinModelPortal; P45172; -. DR SMR; P45172; 9-408. DR STRING; 71421.HI1348; -. DR MEROPS; M20.003; -. DR EnsemblBacteria; AAC22995; AAC22995; HI_1348. DR GeneID; 950265; -. DR KEGG; hin:HI1348; -. DR PATRIC; 20191381; VBIHaeInf48452_1401. DR eggNOG; ENOG4105D42; Bacteria. DR eggNOG; COG2195; LUCA. DR KO; K01258; -. DR OMA; PNHKPIR; -. DR OrthoDB; EOG6SV59Q; -. DR PhylomeDB; P45172; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.360; -; 1. DR HAMAP; MF_00550; Aminopeptidase_M20; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR010161; Peptidase_M20B. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF037215; Peptidase_M20B; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01882; peptidase-T; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. FT CHAIN 1 412 Peptidase T. FT /FTId=PRO_0000185298. FT ACT_SITE 86 86 {ECO:0000255|HAMAP-Rule:MF_00550}. FT ACT_SITE 179 179 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 84 84 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 146 146 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 146 146 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 180 180 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 202 202 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_00550}. FT METAL 385 385 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_00550}. SQ SEQUENCE 412 AA; 45986 MW; 7922E34B2B904A49 CRC64; MISQIDKTEL LERFLHYVSF HTQSKPNAKH SPSSVGQMKL AMQLQKELIQ LGLENVEVSK YAVVTAFLPA NDPNLTKTIG LVAHLDTSPQ CSGKNVRPEV IEEYRGGDIA LGIGEEFISP VYYSFMQKLV GQTLIVTDGT TLLGADNKAG IAEIMTALSI LQKENIPHCN IRVAFTPDEE IGLGIHYFPM EKFSCDWAYT IDGGEVGELE YENFNAATAK VRFFGRNIHT GYAKGKMLNA LTLACEFQQV FPVDEVPEKT DGKVGFYHLE DFSGDIEQVE LTYLIRDFDE QNFAQRKAFI KNQVEKFNAK KGLKKPIELE IQDSYQNMYD VVKNVPQSIE LADRAMKAVG IKPNHKPIRG GTDGAFLASK GLACPNIFTG GYNFHSKHEL VSLQGMENTV QVIIEMLKCK DL // ID PERM_HAEIN Reviewed; 349 AA. AC P43969; P43970; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 20-JAN-2016, entry version 77. DE RecName: Full=Putative permease PerM homolog; GN Name=perM; OrderedLocusNames=HI_0237; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0118 (PerM) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=201; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; F64004; F64004. DR OMA; MPVAWQQ; -. DR Proteomes; UP000000579; 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; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 349 Putative permease PerM homolog. FT /FTId=PRO_0000148296. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 221 241 Helical. {ECO:0000255}. FT TRANSMEM 251 271 Helical. {ECO:0000255}. FT TRANSMEM 282 302 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. SQ SEQUENCE 349 AA; 39307 MW; 523E015BF9ADB0E7 CRC64; MLEMLKSWYS RRLSDPQAMG LLAILLFGFI SIYFFGDLIA PLLIALVLSY LLEIPINFLN QYLKCPRMLA TILIFGSFIG LAAVFFLVLV PMLWNQTISL LSDLPAMFNK SNEWLLNLPK NYPELIDYSM VDSIFNSVRE KILGFGESAV KLSLASIMNL VSLGIYAFLV PLMMFFMLKD KSELLQGVSR FLPKNRNLAF XRWKEMQQQI SNYIHGKLLE ILIVTLITYI IFLIFGLNYP LLLAFAVGLS VLVPYIGAVI VTIPVALVAL FQFGISPTFW YIIIAFAVSQ LLDGNLLVPY LFSEAVNLHP LIIIISVLIF GGLWGFWGVF FAIPLATLVK AVINALPQD // ID PARC_HAEIN Reviewed; 747 AA. AC P43702; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00936}; DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936}; GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00936}; GN OrderedLocusNames=HI_1529; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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_00936}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00936}. CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. CC {ECO:0000255|HAMAP-Rule:MF_00936}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00936}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00936}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit CC family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23175.1; -; Genomic_DNA. DR PIR; F64127; F64127. DR RefSeq; NP_439678.1; NC_000907.1. DR RefSeq; WP_005693555.1; NC_000907.1. DR ProteinModelPortal; P43702; -. DR SMR; P43702; 32-737. DR STRING; 71421.HI1529; -. DR DrugBank; DB06771; Besifloxacin. DR DrugBank; DB00537; Ciprofloxacin. DR DrugBank; DB00467; Enoxacin. DR DrugBank; DB09047; Finafloxacin. DR DrugBank; DB04576; Fleroxacin. DR DrugBank; DB01155; Gemifloxacin. DR DrugBank; DB01137; Levofloxacin. DR DrugBank; DB00978; Lomefloxacin. DR DrugBank; DB00218; Moxifloxacin. DR DrugBank; DB01059; Norfloxacin. DR DrugBank; DB01165; Ofloxacin. DR DrugBank; DB00487; Pefloxacin. DR DrugBank; DB01208; Sparfloxacin. DR DrugBank; DB00685; Trovafloxacin. DR EnsemblBacteria; AAC23175; AAC23175; HI_1529. DR GeneID; 950391; -. DR KEGG; hin:HI1529; -. DR PATRIC; 20191783; VBIHaeInf48452_1600. DR eggNOG; ENOG4105C24; Bacteria. DR eggNOG; COG0188; LUCA. DR KO; K02621; -. DR OMA; RFTEDAY; -. DR OrthoDB; EOG661H5V; -. DR PhylomeDB; P43702; -. DR Proteomes; UP000000579; 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:0009295; C:nucleoid; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.90.199.10; -; 2. DR HAMAP; MF_00936; ParC_type1; 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; IPR005742; TopoIV_A_Gneg. DR Pfam; PF03989; DNA_gyraseA_C; 2. DR Pfam; PF00521; DNA_topoisoIV; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF56719; SSF56719; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; DNA-binding; Isomerase; Membrane; KW Reference proteome; Topoisomerase. FT CHAIN 1 747 DNA topoisomerase 4 subunit A. FT /FTId=PRO_0000145400. FT ACT_SITE 124 124 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00936}. FT SITE 43 43 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00936}. FT SITE 79 79 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00936}. FT SITE 81 81 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00936}. FT SITE 123 123 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_00936}. SQ SEQUENCE 747 AA; 83367 MW; 433038EA479C8D01 CRC64; MTNINYEGIE QMPLRTFTEK AYLNYSMYVI MDRALPFIGD GLKPVQRRIV YAMSELGLNA TAKYKKSART VGDVLGKFHP HGDSACYEAM VLMAQPFSYR YPLVDGQGNW GAPDDPKSFA AMRYTESRLS KISEILLNEL GQGTVDYQPN FDGTLAEPQY LPARLPHILL NGTTGIAVGM ATDIPPHNIN EIADAAVMLL DNPKAGLDDV LEIVQGPDFP TEAEIISPKS EIRKIYEQGR GSIKMRATWK KEDGEIIISA LPHQSSPSKV IAQIAEQMTA KKLPMLEDIR DEADHENPIR IVLVPRSNRV DTDALMAHLF ATTDLEKSYR VNMNMIGLDH KPAVKGLLEI LNEWLDFRRT TVTRRLQYRL DKVLSRLHIL EGLMIAFLNI DEVIEIIRHE DDPKAELMAR FNLSDEQADA ILNLRLRHLA KLEENQLKAE QDELEKERLN LEAILGSERR LNTLIKKEIQ EDAKKYANPR MSQLVEREEA KMISESDMTP AEPVTVILSE MGWVRCAKGH DIDPKSLSYK AGDSYLAHAC GKSNQAVVFI DSTGRSYALD PLSLPSARSQ GEPLTGKLNL PTGATIEYVV MASEQQELLM ASDAGYGFIC KFEDLIARNK AGKALISLPE NAKVLKPKTL INSTALVVAI TSAGRMLIFP AQDLPVLSKG KGNKMITIPA ANAKDRSELL TKLLLISDQA SLEFYSGKRK IVLKPEDLQK FRAERGRKGS TLPRGLHTNL EIMVIEP // ID PBP2_HAEIN Reviewed; 651 AA. AC P44469; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Penicillin-binding protein 2; DE Short=PBP-2; GN Name=mrdA; Synonyms=pbp2; OrderedLocusNames=HI_0032; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation; PBP-2 is responsible for the CC determination of the rod shape of the cell. Its synthesize cross- CC linked peptidoglycan from the lipid intermediates (By similarity). CC {ECO:0000250}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. CC -!- DOMAIN: Has a penicillin insensitive transglycosylase domain CC (formation of linear glycan strands) and a penicillin-sensitive CC transpeptidase domain (cross-linking of the peptide subunits). CC -!- SIMILARITY: Belongs to the transpeptidase 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; L42023; AAC21710.1; -; Genomic_DNA. DR PIR; C64044; C64044. DR RefSeq; NP_438205.1; NC_000907.1. DR RefSeq; WP_005649850.1; NC_000907.1. DR ProteinModelPortal; P44469; -. DR STRING; 71421.HI0032; -. DR DrugBank; DB00671; Cefixime. DR DrugBank; DB00303; Ertapenem. DR EnsemblBacteria; AAC21710; AAC21710; HI_0032. DR GeneID; 950929; -. DR KEGG; hin:HI0032; -. DR PATRIC; 20188515; VBIHaeInf48452_0032. DR eggNOG; ENOG4105CJN; Bacteria. DR eggNOG; COG0768; LUCA. DR KO; K05515; -. DR OMA; ARNYSAY; -. DR OrthoDB; EOG6N0HHV; -. DR PhylomeDB; P44469; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; 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:0003824; F:catalytic activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR005311; PBP_dimer. DR InterPro; IPR001460; PCN-bd_Tpept. DR InterPro; IPR017790; Penicillin-binding_protein_2. DR Pfam; PF03717; PBP_dimer; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF56519; SSF56519; 1. DR SUPFAM; SSF56601; SSF56601; 1. DR TIGRFAMs; TIGR03423; pbp2_mrdA; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; Membrane; KW Multifunctional enzyme; Peptidoglycan synthesis; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 651 Penicillin-binding protein 2. FT /FTId=PRO_0000195448. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT ACT_SITE 338 338 Acyl-ester intermediate. {ECO:0000250}. SQ SEQUENCE 651 AA; 73813 MW; 4BEB73290952AAB0 CRC64; MNLKKFFNTP THEPFRDKKA ERNLFARRTL VAFLGILLLT GVLFTNIYQL QIVNFDTYQT RSNGNRIKLL PLPPTRGLIY DRYGKLLAEN LTFFGLYIVP EKTENLDRTL DELRYIVGLT DNDIENFKKE RRRGTRYTPI LLKPNLTEEQ ISRFAVNGYQ YPSLEVRPYF KRHYLYGETM AHILGYVGKM NDKDVERLKR EDKFANYAGT NDIGKLGIER YYEDILQGTT GFEEVEINNR GKVIRTLRSR PAVAGKSIHL TIDLALQRYI TELLSGLKGA VVVLDPKDSS VLAMVSTPSY DNNLFVDGIS SEDYKRLLND LARPLYSRAT QGAYPPASTV KPFIAVAAQT ENVITPNTTI FDPGYWVLPN STKRFRDWKK TGHGDTDLNK AITESSDTYF YQVAYNMGID RLSNWMKDFG FGMPTGIEIQ EETAANIPTR EWKQKRYKRP WVQGDTISVG IGQGYWTATP LQVAKATTIL VNNGKVNTPH LMKAIEGAVL EPYEDPLLYP DINTPKVAAW EAAKRGMYNV VNAANGTGRK AFADANYRVA GKSGTAQVFS LKENEKYNTA GLKKELHDHA WFTAYAPYDN PKLVVTVILE NAGGGSSNAA PLARKVMDYY LNQRLPQVEK YNVPIQQKKD LSQESEQING R // ID PBPA_HAEIN Reviewed; 853 AA. AC P31776; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 122. DE RecName: Full=Penicillin-binding protein 1A; DE Short=PBP-1a; DE Short=PBP1a; DE AltName: Full=Penicillin-binding protein A; DE Includes: DE RecName: Full=Penicillin-insensitive transglycosylase; DE EC=2.4.2.-; DE AltName: Full=Peptidoglycan TGase; DE Includes: DE RecName: Full=Penicillin-sensitive transpeptidase; DE EC=3.4.-.-; DE AltName: Full=DD-transpeptidase; GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=HI_0440; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP CHARACTERIZATION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7592463; RA Sharma U.K., Dwarakanath P., Banerjee N., Town C., Balganesh T.S.; RT "Expression and characterization of the ponA (ORF I) gene of RT Haemophilus influenzae: functional complementation in a heterologous RT system."; RL J. Bacteriol. 177:6745-6750(1995). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked CC peptidoglycan from the lipid intermediates. The enzyme has a CC penicillin-insensitive transglycosylase N-terminal domain CC (formation of linear glycan strands) and a penicillin-sensitive CC transpeptidase C-terminal domain (cross-linking of the peptide CC subunits) (By similarity). {ECO:0000250}. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC glycosyltransferase 51 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC transpeptidase 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; M62809; AAA25007.1; -; Genomic_DNA. DR EMBL; L42023; AAC22099.1; -; Genomic_DNA. DR PIR; D64068; JH0438. DR RefSeq; NP_438601.1; NC_000907.1. DR RefSeq; WP_005693721.1; NC_000907.1. DR ProteinModelPortal; P31776; -. DR SMR; P31776; 50-235. DR STRING; 71421.HI0440; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; AAC22099; AAC22099; HI_0440. DR GeneID; 949537; -. DR KEGG; hin:HI0440; -. DR PATRIC; 20189433; VBIHaeInf48452_0460. DR eggNOG; ENOG4108JQC; Bacteria. DR eggNOG; COG5009; LUCA. DR KO; K05366; -. DR OMA; MIAIRAM; -. DR OrthoDB; EOG6HMXCD; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.710.10; -; 3. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR031376; PCB_OB. DR InterPro; IPR001460; PCN-bd_Tpept. DR Pfam; PF17092; PCB_OB; 1. DR Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF56601; SSF56601; 4. PE 1: Evidence at protein level; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme; KW Peptidoglycan synthesis; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 853 Penicillin-binding protein 1A. FT /FTId=PRO_0000083165. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 7 27 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 28 853 Periplasmic. {ECO:0000255}. FT REGION 37 205 Transglycosylase. FT REGION 387 681 Transpeptidase. FT ACT_SITE 441 441 Acyl-ester intermediate. {ECO:0000250}. FT CONFLICT 33 33 L -> LPSVETLKTVEL (in Ref. 1). FT {ECO:0000305}. SQ SEQUENCE 853 AA; 94221 MW; FC0846096CDB663B CRC64; MRIAKLILNT LLTLCILGLV AGGMLYFHLK SELQQPMQIY TADGKLIGEV GEQRRIPVKL ADVPQRLIDA FLATEDSRFY DHHGLDPIGI ARALFVAVSN GGASQGASTI TQQLARNFFL TSEKTIIRKA REAVLAVEIE NTLNKQEILE LYLNKIFLGY RSYGVAAAAQ TYFGKSLNEL TLSEMAIIAG LPKAPSTMNP LYSLKRSEER RNVVLSRMLD EKYISKEEYD AALKEPIVAS YHGAKFEFRA DYVTEMVRQE MVRRFGEENA YTSGYKVFTT VLSKDQAEAQ KAVRNNLIDY DMRHGYRGGA PLWQKNEAAW DNDRIVGFLR KLPDSEPFIP AAVIGIVKGG ADILLASGEK MTLSTNAMRW TGRSNPVKVG EQIWIHQRAN GEWQLGQIPA ANSALVSLNS DNGAIEAVVG GFSYEQSKFN RATQSLVQVG SSIKPFIYAA ALEKGLTLSS VLQDSPISIQ KPGQKMWQPK NSPDRYDGPM RLRVGLGQSK NIIAIRAIQT AGIDFTAEFL QRFGFKRDQY FASEALALGA ASFTPLEMAR AYAVFDNGGF LIEPYIIEKI QDNTGKDLFI ANPKIACIEC NDIPVIYGET KDKINGFANI PLGENALKPT DDSTNGEELD QQPETVPELP ELQSNMTALK EDAIDLMAAA KNASSKIEYA PRVISGELAF LIRSALNTAI YGEQGLDWKG TSWRIAQSIK RSDIGGKTGT TNSSKVAWYA GFGANLVTTT YVGFDDNKRV LGRGEAGAKT AMPAWITYMK TALSDKPERK LSLPPKIVEK NIDTLTGLLS PNGGRKEYFI AGTEPTRTYL SEMQERGYYV PTELQQRLNN EGNTPATQPQ ELF // ID PCP_HAEIN Reviewed; 155 AA. AC P10325; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 104. DE RecName: Full=Outer membrane lipoprotein pcp; DE AltName: Full=15 kDa lipoprotein; DE AltName: Full=PAL cross-reacting lipoprotein; DE Flags: Precursor; GN Name=pcp; Synonyms=lpp; OrderedLocusNames=HI_1579; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-19, AND RP PALMITOYLATION AT CYS-19. RX PubMed=2828309; RA Deich R.A., Metcalf B.J., Finn C.W., Farley J.E., Green B.A.; RT "Cloning of genes encoding a 15,000-dalton peptidoglycan-associated RT outer membrane lipoprotein and an antigenically related 15,000-dalton RT protein from Haemophilus influenzae."; RL J. Bacteriol. 170:489-498(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. CC -!- SIMILARITY: Belongs to the Pcp/SlyB lipoprotein 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; M18877; AAA24938.1; -; mRNA. DR EMBL; L42023; AAC23228.1; -; Genomic_DNA. DR PIR; I64130; I64130. DR RefSeq; NP_439725.1; NC_000907.1. DR RefSeq; WP_010869250.1; NC_000907.1. DR STRING; 71421.HI1579; -. DR PRIDE; P10325; -. DR EnsemblBacteria; AAC23228; AAC23228; HI_1579. DR GeneID; 950439; -. DR KEGG; hin:HI1579; -. DR PATRIC; 20191889; VBIHaeInf48452_1652. DR eggNOG; ENOG4108XTF; Bacteria. DR eggNOG; COG3133; LUCA. DR KO; K06077; -. DR OMA; GCAYNSS; -. DR OrthoDB; EOG60W7X5; -. DR PhylomeDB; P10325; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR008816; Gly_zipper_2TM_dom. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Signal. FT SIGNAL 1 18 FT CHAIN 19 155 Outer membrane lipoprotein pcp. FT /FTId=PRO_0000018159. FT LIPID 19 19 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:2828309}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:2828309}. FT CONFLICT 135 143 CSLVAEFVF -> VAGRRVRI (in Ref. 1; FT AAA24938). {ECO:0000305}. SQ SEQUENCE 155 AA; 15425 MW; D7880327FCF0C985 CRC64; MKKTNMALAL LVAFSVTGCA NTDIFSGDVY SASQAKEARS ITYGTIVSVR PVKIQADNQG VVGTLGGGAL GGIAGSTIGG GRGQAIAAVV GAIGGAIAGS KIEEKMSQVN GAELVIKKDD GQEIVVVQKA DSSFCSLVAE FVFVGGGSSL NVSVL // ID PEPE_HAEIN Reviewed; 218 AA. AC P44766; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 19-DEC-2001, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=Peptidase E {ECO:0000255|HAMAP-Rule:MF_00510}; DE EC=3.4.13.21 {ECO:0000255|HAMAP-Rule:MF_00510}; DE AltName: Full=Alpha-aspartyl dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510}; DE AltName: Full=Asp-specific dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510}; DE AltName: Full=Dipeptidase E {ECO:0000255|HAMAP-Rule:MF_00510}; GN Name=pepE {ECO:0000255|HAMAP-Rule:MF_00510}; GN OrderedLocusNames=HI_0587; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate CC residues. May play a role in allowing the cell to use peptide CC aspartate to spare carbon otherwise required for the synthesis of CC the aspartate family of amino acids. {ECO:0000255|HAMAP- CC Rule:MF_00510}. CC -!- CATALYTIC ACTIVITY: Dipeptidase E catalyzes the hydrolysis of CC dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal CC Glu, Asn or Gln, nor does it cleave isoaspartyl peptides. CC {ECO:0000255|HAMAP-Rule:MF_00510}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00510}. CC -!- SIMILARITY: Belongs to the peptidase S51 family. CC {ECO:0000255|HAMAP-Rule:MF_00510}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22244.1; -; Genomic_DNA. DR PIR; C64079; C64079. DR RefSeq; NP_438745.2; NC_000907.1. DR RefSeq; WP_010869014.1; NC_000907.1. DR ProteinModelPortal; P44766; -. DR STRING; 71421.HI0587; -. DR MEROPS; S51.001; -. DR EnsemblBacteria; AAC22244; AAC22244; HI_0587. DR GeneID; 949646; -. DR KEGG; hin:HI0587; -. DR PATRIC; 20189731; VBIHaeInf48452_0608. DR eggNOG; ENOG4105EQ6; Bacteria. DR eggNOG; COG3340; LUCA. DR KO; K05995; -. DR OMA; KYTATVR; -. DR OrthoDB; EOG6M6JST; -. DR PhylomeDB; P44766; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00510; Peptidase_E; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR005320; Peptidase_S51. DR InterPro; IPR023172; Peptidase_S51_dipeptidase-E. DR Pfam; PF03575; Peptidase_S51; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Dipeptidase; Hydrolase; Protease; KW Reference proteome; Serine protease. FT CHAIN 1 218 Peptidase E. FT /FTId=PRO_0000209958. FT ACT_SITE 123 123 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_00510}. FT ACT_SITE 138 138 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_00510}. FT ACT_SITE 160 160 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_00510}. SQ SEQUENCE 218 AA; 24420 MW; 6201B0A3AA1C31B9 CRC64; MKNMLLLSSS KYKNTGYLEH TIPWLQNFLA DYRGKTIAFV PYAGVSRTFD EYEKTVQNAL SDLGMNIVSV HRGKQHRDII EQADVIAIGG GNTFCLLKQL YEHNLIDIIR EKVNNGTPYF GWSAGANVAG SSIMTTNDMP ITYPPSFQAL QLFPHQINPH FISGKMQGHN GESREERLAE FLLVNPTALV YALPEGSALH IQNGMGNRIG RKSYFVLQ // ID PFLB_HAEIN Reviewed; 770 AA. AC P43753; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 99. DE RecName: Full=Formate acetyltransferase; DE EC=2.3.1.54; DE AltName: Full=Pyruvate formate-lyase; GN Name=pflB; Synonyms=pfl; OrderedLocusNames=HI_0180; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + formate = CoA + pyruvate. CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from CC pyruvate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Several mechanisms have been proposed based on CC complexes formed with substrate analogs. After activation by the CC glycine radical, the cysteine radical, Cys-420, can abstract CC hydrogen atoms from the other active site cysteine, Cys-419, and CC from coenzyme A, and it can also transfer hydrogen atoms to CC product radicals. The other active site cysteine can attack the CC central carbonyl of pyruvate and covalently bind the product CC acetyl group (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glycine radical domain. CC {ECO:0000255|PROSITE-ProRule:PRU00493}. CC -!- SIMILARITY: Contains 1 PFL domain. {ECO:0000255|PROSITE- CC ProRule:PRU00887}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21849.1; 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; L42023; AAC21849.1; ALT_INIT; Genomic_DNA. DR PIR; F64052; F64052. DR RefSeq; NP_438348.1; NC_000907.1. DR ProteinModelPortal; P43753; -. DR SMR; P43753; 2-770. DR STRING; 71421.HI0180; -. DR PRIDE; P43753; -. DR EnsemblBacteria; AAC21849; AAC21849; HI_0180. DR GeneID; 951083; -. DR KEGG; hin:HI0180; -. DR PATRIC; 20188855; VBIHaeInf48452_0184. DR eggNOG; ENOG4105C6N; Bacteria. DR eggNOG; COG1882; LUCA. DR KO; K00656; -. DR OMA; FLHTLYN; -. DR OrthoDB; EOG6Q8J0J; -. DR UniPathway; UPA00920; UER00891. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008861; F:formate C-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central. DR InterPro; IPR005949; Form_AcTrfase. DR InterPro; IPR019777; Form_AcTrfase_GR_CS. DR InterPro; IPR001150; Gly_radical. DR InterPro; IPR004184; PFL_dom. DR Pfam; PF01228; Gly_radical; 1. DR Pfam; PF02901; PFL-like; 1. DR PIRSF; PIRSF000379; For_Ac_trans_1; 1. DR TIGRFAMs; TIGR01255; pyr_form_ly_1; 1. DR PROSITE; PS00850; GLY_RADICAL_1; 1. DR PROSITE; PS51149; GLY_RADICAL_2; 1. DR PROSITE; PS51554; PFL; 1. PE 3: Inferred from homology; KW Acyltransferase; Carbohydrate metabolism; Complete proteome; KW Cytoplasm; Glucose metabolism; Organic radical; Reference proteome; KW Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 770 Formate acetyltransferase. FT /FTId=PRO_0000166688. FT DOMAIN 5 635 PFL. {ECO:0000255|PROSITE- FT ProRule:PRU00887}. FT DOMAIN 642 770 Glycine radical. {ECO:0000255|PROSITE- FT ProRule:PRU00493}. FT ACT_SITE 419 419 S-acetylcysteine intermediate. FT {ECO:0000250}. FT ACT_SITE 420 420 Cysteine radical intermediate. FT {ECO:0000250}. FT MOD_RES 745 745 Glycine radical. {ECO:0000255|PROSITE- FT ProRule:PRU00493}. SQ SEQUENCE 770 AA; 86299 MW; 194AE21FDFB5CFBB CRC64; MSELNEMQKL AWAGFAGGDW QENVNVRDFI QKNYTPYEGD DSFLAGPTEA TTKLWESVME GIKIENRTHA PLDFDEHTPS TIISHAPGYI NKDLEKIVGL QTDEPLKRAI MPFGGIKMVE GSCKVYGREL DPKVKKIFTE YRKTHNQGVF DVYTPDILRC RKSGVLTGLP DAYGRGRIIG DYRRVALYGV DFLMKDKYAQ FSSLQKDLED GVNLEATIRL REEIAEQHRA LGQLKQMAAS YGYDISNPAT NAQEAIQWMY FAYLAAIKSQ NGAAMSFGRT ATFIDVYIER DLKAGKITET EAQELVDHLV MKLRMVRFLR TPEYDQLFSG DPMWATETIA GMGLDGRTLV TKNTFRILHT LYNMGTSPEP NLTILWSEQL PENFKRFCAK VSIDTSSVQY ENDDLMRPDF NNDDYAIACC VSPMIVGKQM QFFGARANLA KTLLYAINGG IDEKLGMQVG PKTAPITDEV LDFDTVMTRM DSFMDWLAKQ YVTALNVIHY MHDKYSYEAA LMALHDRDVY RTMACGIAGL SVAADSLSAI KYAKVKPVRG DIKDKDGNVV ATNVAIDFEI EGEYPQYGNN DNRVDDIACD LVERFMKKIQ KLKTYRNAVP TQSVLTITSN VVYGKKTGNT PDGRRAGAPF GPGANPMHGR DQKGAVASLT SVAKLPFAYA KDGISYTFSI VPNALGKDAE AQRRNLAGLM DGYFHHEATV EGGQHLNVNV LNREMLLDAM ENPDKYPQLT IRVSGYAVRF NSLTKEQQQD VITRTFTESM // ID PBPB_HAEIN Reviewed; 781 AA. AC P45345; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 119. DE RecName: Full=Penicillin-binding protein 1B; DE Short=PBP-1b; DE Short=PBP1b; DE AltName: Full=Murein polymerase; DE Includes: DE RecName: Full=Penicillin-insensitive transglycosylase; DE EC=2.4.1.129; DE AltName: Full=Peptidoglycan TGase; DE AltName: Full=Peptidoglycan glycosyltransferase; DE Includes: DE RecName: Full=Penicillin-sensitive transpeptidase; DE EC=3.4.-.-; DE AltName: Full=DD-transpeptidase; GN Name=mrcB; Synonyms=ponB; OrderedLocusNames=HI_1725; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked CC peptidoglycan from the lipid intermediates. The enzyme has a CC penicillin-insensitive transglycosylase N-terminal domain CC (formation of linear glycan strands) and a penicillin-sensitive CC transpeptidase C-terminal domain (cross-linking of the peptide CC subunits) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L- CC Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)- CC Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl CC diphosphate. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC glycosyltransferase 51 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC transpeptidase 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; L42023; AAC23371.1; -; Genomic_DNA. DR PIR; D64138; D64138. DR RefSeq; NP_439866.1; NC_000907.1. DR RefSeq; WP_005694212.1; NC_000907.1. DR ProteinModelPortal; P45345; -. DR STRING; 71421.HI1725; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; AAC23371; AAC23371; HI_1725. DR GeneID; 950545; -. DR KEGG; hin:HI1725; -. DR PATRIC; 20192203; VBIHaeInf48452_1804. DR eggNOG; ENOG4105BZ4; Bacteria. DR eggNOG; COG0744; LUCA. DR KO; K05365; -. DR OMA; QIWQLPA; -. DR OrthoDB; EOG6HMXCD; -. DR PhylomeDB; P45345; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; -; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001264; Glyco_trans_51. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR011813; PBP_1b. DR InterPro; IPR001460; PCN-bd_Tpept. DR InterPro; IPR028166; UB2H. DR Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR Pfam; PF14814; UB2H; 1. DR PIRSF; PIRSF002799; PBP_1b; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF56601; SSF56601; 2. DR TIGRFAMs; TIGR02071; PBP_1b; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme; KW Peptidoglycan synthesis; Reference proteome; Transferase. FT CHAIN 1 781 Penicillin-binding protein 1B. FT /FTId=PRO_0000083184. FT REGION 151 322 Transglycosylase. FT REGION 415 702 Transpeptidase. FT ACT_SITE 188 188 Proton donor; for transglycosylase FT activity. {ECO:0000250}. FT ACT_SITE 466 466 Acyl-ester intermediate; for FT transpeptidase activity. {ECO:0000250}. SQ SEQUENCE 781 AA; 88257 MW; 769CD5DE9A6E488E CRC64; MTSQHSAKKS SKNTPKNNRT FKGFLLKFSF TALVLTIFYG GYLDWQIRSK MDGQIWHLPA EVYSRLESVK IADNLAFDEV IQILLDNEYR QTTMVAAPGD FKLEDDSIVV LRRAFPFPDK AEPQRVLRLR FSHNKLSRIE DLVTVKTVDE FRLAPKLIAM LQSDNEDRLA IPLQNYPRLL IDTLILTEDR RFYEHNGINP VGILRALIAN IRAGQTVQGG STLTQQLVKN LFLSRERTIT RKANEALMSL VLDWRYDKNR ILETYLNEIY LGQNGDTQIH GFELASQFYF GRSIREISLD QIALLVGMVK GPSLYNPWRN PQNALERRNI VLRLMLEHKM IGDELYQLLS QRPLGVQKKG QISRKYPAFI QTLQADLRRK LGEHKISSLL GARIFSTMDL KQQAQAENAV GNTVSQLQLK MKNPHLEGAM IITDYRTGEI RAVVGGLQTQ YAGFNRALMA KRQIGSLVKP SIYLTALSNP EQFRLNTPIN NQPITINVKG SPPWQPRNYD KKYSDSVMLM DALARSLNIP TVNIGMKVGL SKVIDTQKAM GWDNVEIPKV PAMLLGSYTI SPYDVTKLYQ TLANQGGRIA LTTVDSIADR QGNLIFQHDK SAKQVVPQEA AFQTLFAMQQ TVERGTARSL QKDYADLHLA GKTGTTNESR DTWFVGIDGK NISTVWLGRD DNGETKLTGA SGALQIYKDY LNRTNIEKLA ITPPTTVKWV GINQYGDWDC ESYRTIPIWL NNGQNFCGET SSPSLTPTTE TETPPQESLW DVLDNPNPPA Q // ID PCNB_HAEIN Reviewed; 452 AA. AC P44439; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 102. DE RecName: Full=Poly(A) polymerase I {ECO:0000255|HAMAP-Rule:MF_00957}; DE Short=PAP I {ECO:0000255|HAMAP-Rule:MF_00957}; DE EC=2.7.7.19 {ECO:0000255|HAMAP-Rule:MF_00957}; GN Name=pcnB {ECO:0000255|HAMAP-Rule:MF_00957}; GN OrderedLocusNames=HI_0063; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Adds poly(A) tail to the 3' end of many RNAs, which CC usually targets these RNAs for decay. Plays a significant role in CC the global control of gene expression, through influencing the CC rate of transcript degradation, and in the general RNA quality CC control. {ECO:0000255|HAMAP-Rule:MF_00957}. CC -!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1). CC {ECO:0000255|HAMAP-Rule:MF_00957}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. {ECO:0000255|HAMAP-Rule:MF_00957}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21741.1; -; Genomic_DNA. DR PIR; B64046; B64046. DR RefSeq; NP_438236.1; NC_000907.1. DR RefSeq; WP_010868929.1; NC_000907.1. DR ProteinModelPortal; P44439; -. DR STRING; 71421.HI0063; -. DR EnsemblBacteria; AAC21741; AAC21741; HI_0063. DR GeneID; 950961; -. DR KEGG; hin:HI0063; -. DR PATRIC; 20188581; VBIHaeInf48452_0064. DR eggNOG; ENOG4105DJ0; Bacteria. DR eggNOG; COG0617; LUCA. DR KO; K00970; -. DR OMA; RFMAKLD; -. DR OrthoDB; EOG6PZX7Q; -. DR PhylomeDB; P44439; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00957; PolyA_pol; 1. DR InterPro; IPR002646; PolA_pol_head_dom. DR InterPro; IPR010206; PolA_pol_I. DR InterPro; IPR025866; PolyA_pol_arg_C_dom. DR InterPro; IPR032828; PolyA_RNA-bd. DR Pfam; PF01743; PolyA_pol; 1. DR Pfam; PF12626; PolyA_pol_arg_C; 1. DR Pfam; PF12627; PolyA_pol_RNAbd; 1. DR TIGRFAMs; TIGR01942; pcnB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; mRNA processing; Nucleotide-binding; KW Reference proteome; RNA-binding; Transcription; Transferase. FT CHAIN 1 452 Poly(A) polymerase I. FT /FTId=PRO_0000139093. FT ACT_SITE 68 68 {ECO:0000255|HAMAP-Rule:MF_00957}. FT ACT_SITE 70 70 {ECO:0000255|HAMAP-Rule:MF_00957}. FT ACT_SITE 150 150 {ECO:0000255|HAMAP-Rule:MF_00957}. SQ SEQUENCE 452 AA; 52698 MW; 1B3A9F9E2286F349 CRC64; MPKARAKKSE QTRRYDKNVI KAAQFDISPR DFSRNALNVV EKLQRQGFEA YIVGGCIRDL LLGKKPKDFD VATNARPEQI QNIFQRQCRL VGRRFRLAHI MFGRDIIEVA TFRANHSDAR NENQAKQSNE GMLLRDNVYG TIEQDAARRD FTVNALYYNP QDNTLRDYFE GIKDLKAGKL RLIGDPVTRY QEDPVRMLRS IRFMAKLDMF LEKPSEQPIR ELAPLLKNIP PARLFDESLK LLQAGQGVKT YRLLRQYGLF EQLFPALSAY FTEKEDSFAE RMIVTALTST DERVADKLRI NPAFLFAAFF WYPLREKVEI LKNEGGLNNH DAYALAGNEV LDLFCRALAA PRRHTAVIRD IWFLQLQLLK RTGSAPMRTM EHPKFRAGFD LLAMRAEIEG GETIELAKWW HEYQFSNGEQ REQLIQEQQR LHPKPKKKYY RPRRRKTTCS AE // ID PDXH_HAEIN Reviewed; 210 AA. AC P44909; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 2. DT 16-MAR-2016, entry version 111. DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE EC=1.4.3.5 {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=PNP/PMP oxidase {ECO:0000255|HAMAP-Rule:MF_01629}; DE Short=PNPOx {ECO:0000255|HAMAP-Rule:MF_01629}; DE AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01629}; GN Name=pdxH {ECO:0000255|HAMAP-Rule:MF_01629}; GN OrderedLocusNames=HI_0863; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'- CC phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal CC 5'-phosphate (PLP). {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) = CC pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000255|HAMAP- CC Rule:MF_01629}. CC -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'- CC phosphate + H(2)O(2). {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01629}; CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01629}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase CC family. {ECO:0000255|HAMAP-Rule:MF_01629}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22522.1; 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; L42023; AAC22522.1; ALT_INIT; Genomic_DNA. DR PIR; H64098; H64098. DR RefSeq; NP_439023.2; NC_000907.1. DR RefSeq; WP_010869074.1; NC_000907.1. DR ProteinModelPortal; P44909; -. DR STRING; 71421.HI0863; -. DR EnsemblBacteria; AAC22522; AAC22522; HI_0863. DR GeneID; 949875; -. DR KEGG; hin:HI0863; -. DR PATRIC; 20190381; VBIHaeInf48452_0904. DR eggNOG; ENOG4108S7T; Bacteria. DR eggNOG; COG0259; LUCA. DR KO; K00275; -. DR OMA; PEHWGGY; -. DR OrthoDB; EOG60KN2Z; -. DR PhylomeDB; P44909; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IBA:GO_Central. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 2.30.110.10; -; 1. DR HAMAP; MF_01629; PdxH; 1. DR InterPro; IPR000659; Pyridox_Oxase. DR InterPro; IPR019740; Pyridox_Oxase_CS. DR InterPro; IPR011576; Pyridox_Oxase_FMN-bd. DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR PANTHER; PTHR10851:SF0; PTHR10851:SF0; 1. DR Pfam; PF10590; PNPOx_C; 1. DR Pfam; PF01243; Pyridox_oxidase; 1. DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR00558; pdxH; 1. DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Pyridoxine biosynthesis; Reference proteome. FT CHAIN 1 210 Pyridoxine/pyridoxamine 5'-phosphate FT oxidase. FT /FTId=PRO_0000167711. FT NP_BIND 60 65 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 75 76 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT NP_BIND 139 140 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT REGION 7 10 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT REGION 189 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 81 81 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 82 82 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 104 104 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 126 126 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 130 130 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01629}. FT BINDING 183 183 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. FT BINDING 193 193 FMN. {ECO:0000255|HAMAP-Rule:MF_01629}. SQ SEQUENCE 210 AA; 24500 MW; 46C60A0D0AF6B852 CRC64; MELHNIRDEY TKRVLSQHDC HENPISQFEQ WQKEAIHAQV NEPTAMNIAT VDEQGRPNSR MVLLKEVNEQ GFVFFTNYLS RKGGCIEHNP YVALTFFWPE LERQVRIEGK AVKIPAEQSD KYFATRPYTS RIGAWASEQS AVISNYKSLL AKAALVAAKH PLNVPRPDYW GGYLVVPETV EFWQGRPSRL HDRIRYRKES DNWIRERLSP // ID PEPB_HAEIN Reviewed; 434 AA. AC P58474; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Putative peptidase B; DE EC=3.4.11.23 {ECO:0000255|HAMAP-Rule:MF_00504}; DE AltName: Full=Aminopeptidase B {ECO:0000255|HAMAP-Rule:MF_00504}; GN Name=pepB {ECO:0000255|HAMAP-Rule:MF_00504}; GN OrderedLocusNames=HI_0875; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probably plays an important role in intracellular CC peptide degradation. {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa, from CC a peptide or arylamide. Xaa is preferably Glu or Asp but may be CC other amino acids, including Leu, Met, His, Cys and Gln. CC {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00504}; CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000255|HAMAP-Rule:MF_00504}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=340; Note=This may be a natural frameshift.; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P58474; -. DR OMA; CIADNMV; -. DR Proteomes; UP000000579; 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:InterPro. DR HAMAP; MF_00504; Aminopeptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR008330; Pept_M17_PepB. DR InterPro; IPR000819; Peptidase_M17_C. DR Pfam; PF12404; DUF3663; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 5: Uncertain; KW Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Manganese; KW Metal-binding; Protease; Reference proteome. FT CHAIN 1 434 Putative peptidase B. FT /FTId=PRO_0000165836. FT ACT_SITE 210 210 {ECO:0000255|HAMAP-Rule:MF_00504}. FT ACT_SITE 284 284 {ECO:0000255|HAMAP-Rule:MF_00504}. FT METAL 198 198 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 203 203 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 203 203 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 221 221 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 280 280 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 282 282 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_00504}. FT METAL 282 282 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_00504}. SQ SEQUENCE 434 AA; 47285 MW; A5A592E51EB18B58 CRC64; MQITLSNTLA NDAWGKNAIL SFDSNKAMIH LKNNGKTDRT LVQQAARKLR GQGIKEVELV GEKWDLEFCW AFYQGFYTAK QDYAIEFPHL DDEPQDELLA RIECGDFVRG IINEPAQSLT PVKLVERAAE FILNQADIYN EKSAVSFKII SGEELEQQGY HGIWTVGKGS ANLPAMLQLD FNPTQDSNAP VLACLVGKGI TFDSGGYSIK PSDGMSTMRT DMGGAALLTG ALGFAIARGL NQRVKLYLCC AENLVSNNAF KLGDIITYKN GVSAEVLNTD AEGRLVLADG LIEADNQNPG FIIDCATLTG AAKSAVGNDY HSVLSMDDEL VKNLFQSAQA ENEPFWRLPF EDFHRSQINS SFADIANIGS VPVGAGASTA TAFLSYFVKN YKQNWLHIDC SATYRKSGSD LWSVGATGIG VQTLANLMLS RSLK // ID PGPB_HAEIN Reviewed; 241 AA. AC P44570; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Phosphatidylglycerophosphatase B; DE EC=3.1.3.27; DE AltName: Full=Diacylglycerol pyrophosphate phosphatase; DE Short=DGPP phosphatase; DE EC=3.1.3.81; DE AltName: Full=Phosphatidate phosphatase; DE EC=3.1.3.4; DE AltName: Full=Undecaprenyl pyrophosphate phosphatase; DE EC=3.6.1.27; DE AltName: Full=Undecaprenyl-diphosphatase; GN Name=pgpB; OrderedLocusNames=HI_0211; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol CC diphosphate (DGPP) to phosphatidate (PA) and the subsequent CC dephosphorylation of PA to diacylglycerol (DAG). Also has CC undecaprenyl pyrophosphate phosphatase activity, required for the CC biosynthesis of the lipid carrier undecaprenyl phosphate. Can also CC use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate CC as substrates. The pattern of activities varies according to CC subcellular location, PGP phosphatase activity is higher in the CC cytoplasmic membrane, whereas PA and LPA phosphatase activities CC are higher in the outer membrane. Activity is independent of a CC divalent cation ion and insensitive to inhibition by N- CC ethylmaleimide (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphatidylglycerophosphate + H(2)O = CC phosphatidylglycerol + phosphate. CC -!- CATALYTIC ACTIVITY: 1,2-diacyl-sn-glycerol 3-diphosphate + H(2)O = CC 1,2-diacyl-sn-glycerol 3-phosphate + phosphate. CC -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a CC 1,2-diacyl-sn-glycerol + phosphate. CC -!- CATALYTIC ACTIVITY: Ditrans,octacis-undecaprenyl diphosphate + CC H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol CC biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step CC 2/2. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. Cell outer membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase 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; L42023; AAC21879.1; -; Genomic_DNA. DR PIR; I64054; I64054. DR RefSeq; NP_438379.1; NC_000907.1. DR RefSeq; WP_005694086.1; NC_000907.1. DR ProteinModelPortal; P44570; -. DR STRING; 71421.HI0211; -. DR EnsemblBacteria; AAC21879; AAC21879; HI_0211. DR GeneID; 951120; -. DR KEGG; hin:HI0211; -. DR PATRIC; 20188917; VBIHaeInf48452_0215. DR eggNOG; ENOG4105EYK; Bacteria. DR eggNOG; COG0671; LUCA. DR KO; K01096; -. DR OMA; AQRLCGP; -. DR OrthoDB; EOG60CWKV; -. DR PhylomeDB; P44570; -. DR UniPathway; UPA00084; UER00504. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0050380; F:undecaprenyl-diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.20.144.10; -; 1. DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase. DR Pfam; PF01569; PAP2; 1. DR SMART; SM00014; acidPPc; 1. DR SUPFAM; SSF48317; SSF48317; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cell outer membrane; KW Complete proteome; Hydrolase; Lipid degradation; Lipid metabolism; KW Membrane; Phospholipid degradation; Phospholipid metabolism; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 241 Phosphatidylglycerophosphatase B. FT /FTId=PRO_0000058363. FT TOPO_DOM 1 4 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TOPO_DOM 26 45 Periplasmic. {ECO:0000250}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TOPO_DOM 67 71 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TOPO_DOM 93 158 Periplasmic. {ECO:0000250}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TOPO_DOM 180 181 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TOPO_DOM 203 211 Periplasmic. {ECO:0000250}. FT TRANSMEM 212 232 Helical. {ECO:0000255}. FT TOPO_DOM 233 241 Cytoplasmic. {ECO:0000250}. FT REGION 94 102 Phosphatase sequence motif I. FT REGION 157 160 Phosphatase sequence motif II. FT REGION 202 213 Phosphatase sequence motif III. SQ SEQUENCE 241 AA; 27491 MW; 86896C8B066D2A41 CRC64; MFKRLSLYTL LLCLVPFFIW GISYQWHGNS QLTQADYWLY LLTETGSVPY ALITCVLFTL LFAFLFKNPK QWILGVIVMG ISVIATQAAK TGAKALFEEP RPFTVYLAEQ THSTPENFYK NDRTLRAEIA KNFYSMDAIT PAWLVHHYEN ETGYSFPSGH TIFAATWLML AVGFTQLLGN RSFKAKLLVV GIAVWGLLML ISRVRLGMHY PIDLLVATLL AWLINSIIFA FLKKKAIFVM K // ID PGK_HAEIN Reviewed; 386 AA. AC P43726; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 111. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=HI_0525; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 2-6. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22183.1; -; Genomic_DNA. DR PIR; D64074; D64074. DR RefSeq; NP_438683.1; NC_000907.1. DR RefSeq; WP_005694128.1; NC_000907.1. DR ProteinModelPortal; P43726; -. DR SMR; P43726; 2-385. DR STRING; 71421.HI0525; -. DR EnsemblBacteria; AAC22183; AAC22183; HI_0525. DR GeneID; 949587; -. DR KEGG; hin:HI0525; -. DR PATRIC; 20189603; VBIHaeInf48452_0544. DR eggNOG; ENOG4105BZA; Bacteria. DR eggNOG; COG0126; LUCA. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR OrthoDB; EOG64N9Z0; -. DR PhylomeDB; P43726; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000579; 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 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; KW Glycolysis; Kinase; Nucleotide-binding; Reference proteome; KW Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10675023}. FT CHAIN 2 386 Phosphoglycerate kinase. FT /FTId=PRO_0000145948. FT NP_BIND 339 342 ATP. {ECO:0000250}. FT REGION 21 23 Substrate binding. {ECO:0000250}. FT REGION 59 62 Substrate binding. {ECO:0000250}. FT BINDING 36 36 Substrate. {ECO:0000250}. FT BINDING 112 112 Substrate. {ECO:0000250}. FT BINDING 145 145 Substrate. {ECO:0000250}. FT BINDING 196 196 ATP. {ECO:0000250}. FT BINDING 313 313 ATP. {ECO:0000250}. SQ SEQUENCE 386 AA; 40983 MW; 9029D21368DEB66D CRC64; MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAT IPTLKLALEK GAKVMVTSHL GRPTEGEFKP EDSLQPVVDY LKNAGFNVRL EQDYLNGVDV KDGEIVVLEN VRVNKGEKKN DPELGKKYAA LCDVFVMDAF GTAHRAQAST YGVAEFAPIA CAGPLLAAEL DALGKALKEP ARPMVAIVGG SKVSTKLEVL NSLSKIADQI IVGGGIANTF IAAAGHNVGK SLYEADLIPV AKELAANTDI PVPVDVRVGL EFSETAAATE KVVNEVKDDE SIFDIGDKSA EQLAEIIKNA KTVLWNGPVG VFEFPHFRKG TEIISHAIAN SDAFSIAGGG DTLAAIDLFG IADKISYIST GGGAFLEFVE GKVLPAVEIL EKRAKN // ID PGSA_HAEIN Reviewed; 185 AA. AC P44528; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. 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=HI_0123; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21797.1; -; Genomic_DNA. DR PIR; F64049; F64049. DR RefSeq; NP_438295.1; NC_000907.1. DR RefSeq; WP_005694415.1; NC_000907.1. DR STRING; 71421.HI0123; -. DR EnsemblBacteria; AAC21797; AAC21797; HI_0123. DR GeneID; 951031; -. DR KEGG; hin:HI0123; -. DR PATRIC; 20188731; VBIHaeInf48452_0127. DR eggNOG; ENOG4105BZQ; Bacteria. DR eggNOG; COG0558; LUCA. DR KO; K00995; -. DR OMA; VQMVAIP; -. DR OrthoDB; EOG6WMJ3D; -. DR PhylomeDB; P44528; -. DR UniPathway; UPA00084; UER00503. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IBA:GO_Central. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central. 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 1 185 CDP-diacylglycerol--glycerol-3-phosphate FT 3-phosphatidyltransferase. FT /FTId=PRO_0000056776. FT TRANSMEM 7 26 Helical. {ECO:0000255}. FT TRANSMEM 33 52 Helical. {ECO:0000255}. FT TRANSMEM 89 108 Helical. {ECO:0000255}. FT TRANSMEM 151 172 Helical. {ECO:0000255}. SQ SEQUENCE 185 AA; 21331 MW; 5BA9C5B2BBFF577B CRC64; MKFNIPIFLT IFRVILIPFF VIAFYLPIES SPFITTLIFF IAGVTDWLDG YLARKWKQTT RFGAFLDPVA DKVMVVAALV LIVEHQHTFW ITIPAIIMIS REIIISALRE WMAELGERSK IAVSWWGKWK TTAQMLALGG LLWRYNNYME IAAIILLYIA AILTIWSMIQ YLQVAKGSLL DNIQL // ID PHEA_HAEIN Reviewed; 385 AA. AC P43900; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=P-protein; DE Includes: DE RecName: Full=Chorismate mutase; DE Short=CM; DE EC=5.4.99.5; DE Includes: DE RecName: Full=Prephenate dehydratase; DE Short=PDT; DE EC=4.2.1.51; GN Name=pheA; OrderedLocusNames=HI_1145; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Chorismate = prephenate. CC -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2). CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; CC phenylpyruvate from prephenate: step 1/1. CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate CC biosynthesis; prephenate from chorismate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC -!- SIMILARITY: Contains 1 chorismate mutase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00515}. CC -!- SIMILARITY: Contains 1 prephenate dehydratase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00517}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22800.1; -; Genomic_DNA. DR PIR; B64186; B64186. DR RefSeq; NP_439303.1; NC_000907.1. DR RefSeq; WP_005647570.1; NC_000907.1. DR ProteinModelPortal; P43900; -. DR STRING; 71421.HI1145; -. DR EnsemblBacteria; AAC22800; AAC22800; HI_1145. DR GeneID; 950108; -. DR KEGG; hin:HI1145; -. DR PATRIC; 20190965; VBIHaeInf48452_1195. DR eggNOG; ENOG4105CQC; Bacteria. DR eggNOG; COG0077; LUCA. DR eggNOG; COG1605; LUCA. DR KO; K14170; -. DR OMA; WREVMSA; -. DR OrthoDB; EOG6WHNT1; -. DR PhylomeDB; P43900; -. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.59.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase. DR InterPro; IPR002701; Chorismate_mutase. DR InterPro; IPR020822; Chorismate_mutase_type_II. DR InterPro; IPR010952; CM_P_1. DR InterPro; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR Pfam; PF01817; CM_2; 1. DR Pfam; PF00800; PDT; 1. DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR TIGRFAMs; TIGR01797; CM_P_1; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1. DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Isomerase; Lyase; KW Multifunctional enzyme; Phenylalanine biosynthesis; KW Reference proteome. FT CHAIN 1 385 P-protein. FT /FTId=PRO_0000119188. FT DOMAIN 1 92 Chorismate mutase. {ECO:0000255|PROSITE- FT ProRule:PRU00515}. FT DOMAIN 105 285 Prephenate dehydratase. FT {ECO:0000255|PROSITE-ProRule:PRU00517}. FT DOMAIN 299 376 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT REGION 286 385 Regulatory (Phe-binding). FT SITE 278 278 Essential for prephenate dehydratase FT activity. {ECO:0000255}. SQ SEQUENCE 385 AA; 44001 MW; 2289BC7FF73C44EC CRC64; MALELSDIRQ QITQIDRSLL KLLSERHRLA FDVVRSKEIS QKSLRDVERE QQLLQELVQF AENENYQLEA QYITSIFQKI IEDSVLTQQV YLQNKLNEQR NQNLHIAFLG KRGSYSNLAA RNYAARYQKQ FVELGCQSFE QVFEKVQTGE ADFGVLPLEN TTSGAINEVY DLLQHTDLSL VGELAYPIKH CVLVNDKTDL NQIDTLYSHP QVIQQCSQFI HSLDRVHIEY CESSSHAMQL VASLNKPNIA ALGNEDGGKL YGLSVLKTNI ANQENNITRF IVVAKEPREV SSQIPTKTLL LMTTSQQAGA LVDALLVFKK HQINMTKLES RPIYGKPWEE MFYLEIEANI HHPDTKQALE ELKNYSNYLK ILGCYPSEIV KPVSV // ID PHOR_HAEIN Reviewed; 425 AA. AC P71380; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 129. DE RecName: Full=Phosphate regulon sensor protein PhoR; DE EC=2.7.13.3; GN Name=phoR; OrderedLocusNames=HI_1378; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Member of the two-component regulatory system PhoR/PhoB CC involved in the phosphate regulon genes expression. PhoR may CC function as a membrane-associated protein kinase that CC phosphorylates PhoB in response to environmental signals (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00107}. CC -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) 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; L42023; AAC23024.1; -; Genomic_DNA. DR RefSeq; NP_439530.1; NC_000907.1. DR RefSeq; WP_010869197.1; NC_000907.1. DR STRING; 71421.HI1378; -. DR EnsemblBacteria; AAC23024; AAC23024; HI_1378. DR GeneID; 950291; -. DR KEGG; hin:HI1378; -. DR PATRIC; 20191445; VBIHaeInf48452_1433. DR eggNOG; ENOG4105BZU; Bacteria. DR eggNOG; ENOG410XNMH; LUCA. DR KO; K07636; -. DR OMA; AITKHAL; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P71380; -. DR BRENDA; 2.7.13.3; 2529. DR Proteomes; UP000000579; 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR000014; PAS. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR014310; Sig_transdc_His_kinase_PhoR. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55785; SSF55785; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR02966; phoR_proteo; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Membrane; Nucleotide-binding; Phosphate transport; KW Phosphoprotein; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix; Transport; Two-component regulatory system. FT CHAIN 1 425 Phosphate regulon sensor protein PhoR. FT /FTId=PRO_0000074847. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT DOMAIN 89 156 PAS. FT DOMAIN 201 415 Histidine kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00107}. FT MOD_RES 204 204 Phosphohistidine; by autocatalysis. FT {ECO:0000255|PROSITE-ProRule:PRU00107}. SQ SEQUENCE 425 AA; 49859 MW; 47220F1DD7F32941 CRC64; MKKILNFIVE INLAIIISLF TSDFILWFAI ILLLILAWHH INEYRLLKYL NLKQDNKFSL LQLGTFSQTE AYHRHQIYKE KCASLRLLSQ INKNIKYLPD AIIICQHNGN ISWCNSIAPQ MFDFCWDKKV QENIFDVIFY EQFKHYFFSP KKRRPLVLLT YNQRYIEVQS HAYNSHMILV IARDITDMIH LLNSRQKFLS NINHELRTPL TVLQGYLEIL ADNNIQNPLQ KKAIXAMQEQ SQRMEHLLQQ FNFLAKIETT SDKDFRKFDM SAMINSLRKD TDILNTYNHH IEFIIQPNII IFGNESQLRS AVSNLIYNAI KHSGKQCHIQ IQWETCEQGI KFNVIDNGVG ISPQHIPHLT ERFYRVDESR SHLTGGSGLG LAIVKHTLLQ YHSHLNIEST ETKGSSFSFI IPKRFVISKN NKEIQ // ID PDXT_HAEIN Reviewed; 192 AA. AC P45294; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 17-FEB-2016, entry version 91. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615}; GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; GN OrderedLocusNames=HI_1648; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and CC ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The CC resulting ammonia molecule is channeled to the active site of CC PdxS. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of CC heterodimers. Only shows activity in the heterodimer. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23295.1; 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; L42023; AAC23295.1; ALT_INIT; Genomic_DNA. DR PIR; G64173; G64173. DR RefSeq; NP_439790.2; NC_000907.1. DR RefSeq; WP_005687358.1; NC_000907.1. DR ProteinModelPortal; P45294; -. DR STRING; 71421.HI1648; -. DR MEROPS; C26.A32; -. DR EnsemblBacteria; AAC23295; AAC23295; HI_1648. DR GeneID; 950854; -. DR KEGG; hin:HI1648; -. DR PATRIC; 20192041; VBIHaeInf48452_1724. DR eggNOG; ENOG4108UHX; Bacteria. DR eggNOG; COG0311; LUCA. DR KO; K08681; -. DR OMA; VYGTCAG; -. DR OrthoDB; EOG66F0BW; -. DR PhylomeDB; P45294; -. DR UniPathway; UPA00245; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01615; PdxT; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002161; PdxT/SNO. DR InterPro; IPR021196; PdxT/SNO_CS. DR Pfam; PF01174; SNO; 1. DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1. DR PROSITE; PS01236; PDXT_SNO_1; 1. DR PROSITE; PS51130; PDXT_SNO_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Hydrolase; Lyase; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1 192 Pyridoxal 5'-phosphate synthase subunit FT PdxT. FT /FTId=PRO_0000135641. FT REGION 50 52 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT REGION 136 137 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 82 82 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 172 172 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 174 174 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT BINDING 109 109 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01615}. SQ SEQUENCE 192 AA; 21070 MW; 52297D26C0EE5579 CRC64; MKIGILALQG AFAEHARMLE KLGIESVELR NLKNFQQHYS DLSGLILPGG ESTAIGKLLR ELYMLEPIKQ AISSGFPVFG TCAGLILLAK EITSQKESHF GTMDIVVERN AYGRQLGSFY TEADCKGVGK IPMTFIRGPI ISSVGKKVNI LATVNNKIVA AQEKNMLVTS FHPELTNNLS LHKYFIDICK VA // ID PFKA_HAEIN Reviewed; 321 AA. AC P43863; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339}; DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339}; DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339}; GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; GN OrderedLocusNames=HI_0982; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-148. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7768823; RA Karudapuram S., Zhao X., Barcak G.J.; RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a RT gene required for chromosomal but not plasmid DNA transformation."; RL J. Bacteriol. 177:3235-3240(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:0000255|HAMAP-Rule:MF_00339}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339}; CC -!- ENZYME REGULATION: Allosterically activated by ADP and other CC diphosphonucleosides, and allosterically inhibited by CC phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. ATP-dependent PFK group I subfamily. Prokaryotic clade CC "B1" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22644.1; -; Genomic_DNA. DR EMBL; U18657; AAA70114.1; -; Genomic_DNA. DR PIR; C64106; C64106. DR RefSeq; NP_439145.1; NC_000907.1. DR RefSeq; WP_005664214.1; NC_000907.1. DR ProteinModelPortal; P43863; -. DR SMR; P43863; 1-320. DR STRING; 71421.HI0982; -. DR PRIDE; P43863; -. DR EnsemblBacteria; AAC22644; AAC22644; HI_0982. DR GeneID; 949556; -. DR KEGG; hin:HI0982; -. DR PATRIC; 20190625; VBIHaeInf48452_1025. DR eggNOG; ENOG4105CTQ; Bacteria. DR eggNOG; COG0205; LUCA. DR KO; K00850; -. DR OMA; CGDLALH; -. DR OrthoDB; EOG644ZRM; -. DR PhylomeDB; P43863; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_00339; Phosphofructokinase_I_B1; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR012828; PFKA_ATP_prok. DR InterPro; IPR015912; Phosphofructokinase_CS. DR InterPro; IPR000023; Phosphofructokinase_dom. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 1. DR TIGRFAMs; TIGR02482; PFKA_ATP; 1. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm; KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 321 ATP-dependent 6-phosphofructokinase. FT /FTId=PRO_0000111956. FT NP_BIND 73 74 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}. FT NP_BIND 103 106 ATP. {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 22 26 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 55 60 Allosteric activator ADP binding; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 127 129 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 171 173 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT REGION 187 189 Allosteric activator ADP binding. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 215 217 Allosteric activator ADP binding. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT REGION 251 254 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT ACT_SITE 129 129 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT METAL 104 104 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT BINDING 12 12 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 156 156 Allosteric activator ADP. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 164 164 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 213 213 Allosteric activator ADP. FT {ECO:0000255|HAMAP-Rule:MF_00339}. FT BINDING 224 224 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00339}. FT BINDING 245 245 Substrate; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00339}. SQ SEQUENCE 321 AA; 34922 MW; A26F285077951523 CRC64; MIKKIAVLTS GGDAPGMNAA IRGVVRSALA EGLEVFGIYD GYQGLYNNKI KQLNRYSVSD VINRGGTFLG SARFPEFKDP NIRAKCAEIL RSHGIDALVV IGGDGSYMGA KLLTEEHSFP CVGLPGTIDN DVAGTDYTIG YQTALQTAVD AIDRLRDTSS SHQRISIVEI MGRHCSDLTI SAGIAGGCEY IVASEIEFNR EELIQQIERS IIRGKRHAII AITELLTDVH SLAKEIEARV GHETRATVLG HIQRGGSPCA FDRILASRMG AYAVDLLLQG KGGYCVGIQN EQLVHHDIID AINNMQRVFK ADWLKVAKRL E // ID PHOB_HAEIN Reviewed; 231 AA. AC P45189; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 103. DE RecName: Full=Phosphate regulon transcriptional regulatory protein PhoB; GN Name=phoB; OrderedLocusNames=HI_1379; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is a positive regulator for the phosphate CC regulon. Transcription of this operon is positively regulated by CC PhoB and PhoR when phosphate is limited (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Phosphorylated by PhoR. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 OmpR/PhoB-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01091}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23025.1; -; Genomic_DNA. DR PIR; F64120; F64120. DR RefSeq; NP_439531.1; NC_000907.1. DR RefSeq; WP_005650606.1; NC_000907.1. DR ProteinModelPortal; P45189; -. DR STRING; 71421.HI1379; -. DR EnsemblBacteria; AAC23025; AAC23025; HI_1379. DR GeneID; 950671; -. DR KEGG; hin:HI1379; -. DR PATRIC; 20191447; VBIHaeInf48452_1434. DR eggNOG; ENOG4105CK6; Bacteria. DR eggNOG; COG0745; LUCA. DR KO; K07657; -. DR OMA; MAMRYEG; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P45189; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR011879; Sig_transdc_resp-reg_PhoB. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR TIGRFAMs; TIGR02154; PhoB; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; KW Phosphate transport; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Transport; KW Two-component regulatory system. FT CHAIN 1 231 Phosphate regulon transcriptional FT regulatory protein PhoB. FT /FTId=PRO_0000081188. FT DOMAIN 4 119 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DNA_BIND 127 225 OmpR/PhoB-type. {ECO:0000255|PROSITE- FT ProRule:PRU01091}. FT MOD_RES 52 52 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 231 AA; 27508 MW; B90BF5FDD6BF414B CRC64; MTRKILIVED ECAIREMIAL FLSQKYYDVI EASDFKTAIN KIKENPKLIL LDWMLPGRSG IQFIQYIKKQ ESYAAIPIIM LTAKSTEEDC IACLNAGADD YITKPFSPQI LLARIEAVWR RIYEQQSQFI QIDELSIDEN AQRVFFQQQE INLSSTEFKL LHFFMRHPEK VYSREQLLNR IWHNDLEVEY RTVDSYIRRL RRNLAPFQCE HYIQTVRGSG YRFSSYLRDK Q // ID PHSG_HAEIN Reviewed; 821 AA. AC P45180; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Glycogen phosphorylase; DE EC=2.4.1.1; GN Name=glgP; OrderedLocusNames=HI_1361; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Phosphorylase is an important allosteric enzyme in CC carbohydrate metabolism. Enzymes from different sources differ in CC their regulatory mechanisms and in their natural substrates. CC However, all known phosphorylases share catalytic and structural CC properties (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-glucosyl)(n) + phosphate = CC ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the glycogen phosphorylase 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; L42023; AAC23008.1; -; Genomic_DNA. DR PIR; D64119; D64119. DR RefSeq; NP_439512.1; NC_000907.1. DR RefSeq; WP_005693999.1; NC_000907.1. DR ProteinModelPortal; P45180; -. DR STRING; 71421.HI1361; -. DR CAZy; GT35; Glycosyltransferase Family 35. DR PRIDE; P45180; -. DR EnsemblBacteria; AAC23008; AAC23008; HI_1361. DR GeneID; 950286; -. DR KEGG; hin:HI1361; -. DR PATRIC; 20191409; VBIHaeInf48452_1415. DR eggNOG; ENOG4107QQN; Bacteria. DR eggNOG; COG0058; LUCA. DR KO; K00688; -. DR OMA; RMAWFSS; -. DR OrthoDB; EOG60SCHC; -. DR PhylomeDB; P45180; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central. DR InterPro; IPR011833; Glycg_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. DR PANTHER; PTHR11468; PTHR11468; 1. DR Pfam; PF00343; Phosphorylase; 1. DR PIRSF; PIRSF000460; Pprylas_GlgP; 1. DR TIGRFAMs; TIGR02093; P_ylase; 1. DR PROSITE; PS00102; PHOSPHORYLASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Carbohydrate metabolism; Complete proteome; KW Glycogen metabolism; Glycosyltransferase; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 821 Glycogen phosphorylase. FT /FTId=PRO_0000188554. FT MOD_RES 667 667 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 821 AA; 94441 MW; B28D751D587736A4 CRC64; MIMDNFDSPF QYNRPEMTVE AIKKSIVYKL IFLIGRSPRE ASQRDWLNAT LHAVRDLVTE GWITTARQTR AEDSRRVYYL SMEFLIGRTL SNAMIAEGIY GLAQEALSEL NVDLEEVLEK EVDPGLGNGG LGRLAACFMD SIATLGLPGM GYGIRYEYGM FRQKIENGQQ VERPDAWLEK GAPWEFIRPS KRFTVEFGGN IHFEGKKCIW QDTEKVTALA YDQMIPGYQN NSAATLRLWS AHAGEVFNLA DFNRGEHLAA LEEHSANKNL SRVLYPDDST WNGRELRLRQ EYFLVSASLQ DILRRHKRTH NSLENLADKV AIHLNDTHPA LAIPELMRIL VDDEGFEWKK AWEMTRNIFS YTCHTLMSEA LETWPVEMMA KILPRHLQMI FEINDHFLEY VRTYVTTDND FIRRVSLIEE GYQRKVRMGW LSVVGSHKIN GVAEIHSDLM VTSTFADFAR IFPERFTNVT NGITPRRWLA VANPQLAALF DKYIGSEWRC DLSQIEKLKP FAQEKAFKEA VADIKFANKV KLAEYVKSEL GVELDPHALF DVQVKRIHEY KRQMLNVLHI IARYNEMLTN PEKDWQPRVF ILAGKAASAY YAAKQTIHLI NDVANVINND ERLKGRLKVV FIPNYSVSLA QLIIPAADIS EQISLAGTEA SGTSNMKFAL NGALTLGTLD GANVEILENV GEDNIFIFGN TVEQVEQLRR EGYRSFEYYQ NDAQLRTVVD QIIEGKFSPE DPQRYHQLLQ GLQYHDYYQA FADFRSYVET QKAVDEKYKQ RDQWIESTIQ NIVNMGFFSS DRTIKEYAER IWKVEPVQLG D // ID PEPD_HAEIN Reviewed; 484 AA. AC P44817; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 103. DE RecName: Full=Cytosol non-specific dipeptidase; DE EC=3.4.13.18; DE AltName: Full=Aminoacyl-histidine dipeptidase; DE AltName: Full=Beta-alanyl-histidine dipeptidase; DE AltName: Full=Carnosinase; DE AltName: Full=Peptidase D; DE AltName: Full=Xaa-His dipeptidase; DE Short=X-His dipeptidase; GN Name=pepD; OrderedLocusNames=HI_0675; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Dipeptidase with broad substrate specificity. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of dipeptides, preferentially CC hydrophobic dipeptides including prolyl amino acids. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. Can also use Co(2+). CC {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M20C 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; L42023; AAC22335.1; -; Genomic_DNA. DR PIR; E64085; E64085. DR RefSeq; NP_438835.1; NC_000907.1. DR RefSeq; WP_005694602.1; NC_000907.1. DR ProteinModelPortal; P44817; -. DR SMR; P44817; 7-484. DR STRING; 71421.HI0675; -. DR MEROPS; M20.007; -. DR DNASU; 950737; -. DR EnsemblBacteria; AAC22335; AAC22335; HI_0675. DR GeneID; 950737; -. DR KEGG; hin:HI0675; -. DR PATRIC; 20189967; VBIHaeInf48452_0705. DR eggNOG; ENOG4105CIN; Bacteria. DR eggNOG; COG2195; LUCA. DR KO; K01270; -. DR OMA; KGGYPGW; -. DR OrthoDB; EOG6BCSRT; -. DR PhylomeDB; P44817; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016805; F:dipeptidase 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 InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR001160; Peptidase_M20C. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF016599; Xaa-His_dipept; 1. DR PRINTS; PR00934; XHISDIPTASE. DR TIGRFAMs; TIGR01893; aa-his-dipept; 1. PE 3: Inferred from homology; KW Cobalt; Complete proteome; Dipeptidase; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 484 Cytosol non-specific dipeptidase. FT /FTId=PRO_0000185355. FT ACT_SITE 78 78 {ECO:0000250}. FT ACT_SITE 145 145 Proton acceptor. {ECO:0000250}. FT METAL 76 76 Zinc 2. {ECO:0000250}. FT METAL 115 115 Zinc 1. {ECO:0000250}. FT METAL 115 115 Zinc 2. {ECO:0000250}. FT METAL 146 146 Zinc 1. {ECO:0000250}. FT METAL 169 169 Zinc 2. {ECO:0000250}. FT METAL 456 456 Zinc 1. {ECO:0000250}. SQ SEQUENCE 484 AA; 52888 MW; BA102E194DC96BA1 CRC64; MSEITTLQPS LLWKWFDQIC AIPHPSHYED TLANFIVNWA KEKHFFVERD EVGNVLIRKP ATKGMENHTP VVLQAHLDMV PQANEGNPHD FTKDPIQPYI DGEWVKARGT TLGSDNGIGL ASTLAVLESN DLAHPPLEVL LTMTEETGMD GAKGLRHNWL QSEILINTDT EEIGEIYIGC AGGINANFEI PVQYETNTFE HSAQITLKGL RGGHSGGDIH TGRANAIKVL ARVLAKLSQN QPHFALSEIR GGSIRNAIPR EAAAVLAFNG DVKTIESAVE NLAVVLKEEL AIAEPNFTLF VESAEKAPTV FTAQSTQTVI NALNVLPNGV IRNSDVVKNV VESSLSVGVL KTEGNVVKST ILVRSLIESG KYYVTEMLSS LAILANAKVE FSAPYPGWQP VNDSTILDVT RKHYAEVLGE QPVVKVIHAG LECGLLKEHY PNIEMISVGP TIRNAHSPDE KVEIATVQTY WDLLTRVLAD IPAK // ID PGPA_HAEIN Reviewed; 163 AA. AC P44157; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Phosphatidylglycerophosphatase A; DE EC=3.1.3.27; DE AltName: Full=Phosphatidylglycerolphosphate phosphatase A; DE Short=PGP phosphatase A; GN Name=pgpA; OrderedLocusNames=HI_1306; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Lipid phosphatase which dephosphorylates CC phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Phosphatidylglycerophosphate + H(2)O = CC phosphatidylglycerol + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol CC biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step CC 2/2. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {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; L42023; AAC22953.1; -; Genomic_DNA. DR PIR; D64025; D64025. DR RefSeq; NP_439457.1; NC_000907.1. DR RefSeq; WP_005694464.1; NC_000907.1. DR ProteinModelPortal; P44157; -. DR STRING; 71421.HI1306; -. DR EnsemblBacteria; AAC22953; AAC22953; HI_1306. DR GeneID; 950237; -. DR KEGG; hin:HI1306; -. DR PATRIC; 20191295; VBIHaeInf48452_1358. DR eggNOG; ENOG4108ZAI; Bacteria. DR eggNOG; COG1267; LUCA. DR KO; K01095; -. DR OMA; VWDEIAG; -. DR OrthoDB; EOG6P5ZM2; -. DR PhylomeDB; P44157; -. DR UniPathway; UPA00084; UER00504. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR026037; PgpA. DR InterPro; IPR007686; YutG/PgpA. DR Pfam; PF04608; PgpA; 1. DR PIRSF; PIRSF006162; PgpA; 1. DR SUPFAM; SSF101307; SSF101307; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Lipid degradation; Lipid metabolism; Magnesium; Membrane; KW Metal-binding; Phospholipid degradation; Phospholipid metabolism; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 163 Phosphatidylglycerophosphatase A. FT /FTId=PRO_0000058360. FT TRANSMEM 10 28 Helical. {ECO:0000255}. FT TRANSMEM 35 51 Helical. {ECO:0000255}. FT TRANSMEM 92 116 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. SQ SEQUENCE 163 AA; 18035 MW; 77CC4D4FC550937B CRC64; MTENNPLKKI SLLNPIHLLA VGFGSGLIHP APGTWGSLAG TILGVILLSL LGVKIFLIFT ALCFLLGCYL CQKTTADMGV HDHGSIVWDE FVGVFIVLAA IPSLSWQWIL AAFALFRFFD ILKPFPIRYF DEKLENGFGI MIDDVLAAIY AVIVVFAIQY WML // ID PDXY_HAEIN Reviewed; 288 AA. AC P44690; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=Pyridoxal kinase PdxY {ECO:0000255|HAMAP-Rule:MF_01639}; DE Short=PL kinase {ECO:0000255|HAMAP-Rule:MF_01639}; DE EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01639}; GN Name=pdxY {ECO:0000255|HAMAP-Rule:MF_01639}; GN OrderedLocusNames=HI_0405; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of CC pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of CC pyridoxal to PLP. {ECO:0000255|HAMAP-Rule:MF_01639}. CC -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_01639}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01639}; CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; CC pyridoxal 5'-phosphate from pyridoxal: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01639}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01639}. CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01639}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22064.1; -; Genomic_DNA. DR PIR; E64151; E64151. DR RefSeq; NP_438567.1; NC_000907.1. DR RefSeq; WP_005630043.1; NC_000907.1. DR ProteinModelPortal; P44690; -. DR SMR; P44690; 1-287. DR STRING; 71421.HI0405; -. DR EnsemblBacteria; AAC22064; AAC22064; HI_0405. DR GeneID; 949504; -. DR KEGG; hin:HI0405; -. DR PATRIC; 20189361; VBIHaeInf48452_0424. DR eggNOG; ENOG4107G57; Bacteria. DR eggNOG; COG2240; LUCA. DR KO; K00868; -. DR OMA; DGMWHIS; -. DR OrthoDB; EOG69PQ1X; -. DR PhylomeDB; P44690; -. DR UniPathway; UPA01068; UER00298. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008478; F:pyridoxal kinase activity; IBA:GO_Central. DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central. DR GO; GO:0042816; P:vitamin B6 metabolic process; IBA:GO_Central. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_01639; PdxY; 1. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR004625; PyrdxlKinase. DR InterPro; IPR023685; Pyridoxal_kinase_PdxY. DR InterPro; IPR029056; Ribokinase-like. DR PANTHER; PTHR10534; PTHR10534; 1. DR Pfam; PF08543; Phos_pyr_kin; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00687; pyridox_kin; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 288 Pyridoxal kinase PdxY. FT /FTId=PRO_0000213346. FT REGION 44 45 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01639}. FT BINDING 9 9 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01639}. FT BINDING 111 111 ATP. {ECO:0000255|HAMAP-Rule:MF_01639}. FT BINDING 148 148 ATP. {ECO:0000255|HAMAP-Rule:MF_01639}. FT BINDING 181 181 ATP. {ECO:0000255|HAMAP-Rule:MF_01639}. FT BINDING 224 224 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01639}. SQ SEQUENCE 288 AA; 31772 MW; A4711DE7C4B421B8 CRC64; MKNVLSIQSH VVYGFAGNKS ATFPMQLLGV DVWALNTVQF SNHTQYGKWT GMVIPQEQIR EIVTGLDNIE KLQECDALLS GYLGSAEQVD QILFALEQIK LRNPNALYLC DPVMPHPKKI CVVANGVREA LIEKAIPVAD IMTPNLHELR QLTEFPINTF DDVLKAVNAL IAKGVKKVLV KHLGSAGKIN DPDTFEIIMA TPEGVWHLSR PLYQFNFEPV GVGDLIAGTF LANLLNGKSD VEAFEAMNNE VAGVMKTTFE LGSYELQTIA ARFEILNPSS NYKAEKVA // ID PHNA_HAEIN Reviewed; 120 AA. AC P44479; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Protein PhnA homolog; GN Name=phnA; OrderedLocusNames=HI_0046; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21724.1; -; Genomic_DNA. DR PIR; I64044; I64044. DR RefSeq; NP_438219.2; NC_000907.1. DR ProteinModelPortal; P44479; -. DR SMR; P44479; 13-120. DR STRING; 71421.HI0046; -. DR EnsemblBacteria; AAC21724; AAC21724; HI_0046. DR GeneID; 950944; -. DR KEGG; hin:HI0046; -. DR PATRIC; 20188545; VBIHaeInf48452_0046. DR eggNOG; ENOG4108Z8G; Bacteria. DR eggNOG; COG2824; LUCA. DR KO; K06193; -. DR OMA; SCLYEWN; -. DR OrthoDB; EOG6J752H; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR004624; PhnA. DR InterPro; IPR013988; PhnA_C. DR InterPro; IPR013987; PhnA_N. DR Pfam; PF03831; PhnA; 1. DR Pfam; PF08274; PhnA_Zn_Ribbon; 1. DR TIGRFAMs; TIGR00686; phnA; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 120 Protein PhnA homolog. FT /FTId=PRO_0000058387. SQ SEQUENCE 120 AA; 13678 MW; 5553FE2ACC6C6245 CRC64; MRLLYVIKKE NPMDQMPNCP KCQSEYVYHD SINFVCPDCG NEWDNNEIQE SDDDQLIVKD SNGNLLAEGD NVLLIKDLKL KGSSEVLKKG TKFKNIRLVN GDHNVDCGKI MLKSEFLKKA // ID PFLA_HAEIN Reviewed; 246 AA. AC P43751; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-MAR-2016, entry version 109. DE RecName: Full=Pyruvate formate-lyase 1-activating enzyme; DE EC=1.97.1.4; DE AltName: Full=Formate-C-acetyltransferase-activating enzyme 1; DE AltName: Full=PFL-activating enzyme 1; GN Name=pflA; Synonyms=act; OrderedLocusNames=HI_0179; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activation of pyruvate formate-lyase 1 under anaerobic CC conditions by generation of an organic free radical, using S- CC adenosylmethionine and reduced flavodoxin as cosubstrates to CC produce 5'-deoxy-adenosine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + dihydroflavodoxin + CC [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L- CC methionine + flavodoxin semiquinone + [formate C- CC acetyltransferase]-glycin-2-yl radical. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes 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; L42023; AAC21848.1; -; Genomic_DNA. DR PIR; E64052; E64052. DR RefSeq; NP_438347.1; NC_000907.1. DR RefSeq; WP_005694108.1; NC_000907.1. DR ProteinModelPortal; P43751; -. DR STRING; 71421.HI0179; -. DR EnsemblBacteria; AAC21848; AAC21848; HI_0179. DR GeneID; 951086; -. DR KEGG; hin:HI0179; -. DR PATRIC; 20188853; VBIHaeInf48452_0183. DR eggNOG; ENOG4105F1A; Bacteria. DR eggNOG; COG1180; LUCA. DR KO; K04069; -. DR OMA; VHQNLIG; -. DR OrthoDB; EOG64FKHC; -. DR PhylomeDB; P43751; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR012838; PFL_activating. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR TIGRFAMs; TIGR02493; PFLA; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Glucose metabolism; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; KW Reference proteome; S-adenosyl-L-methionine. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 246 Pyruvate formate-lyase 1-activating FT enzyme. FT /FTId=PRO_0000200525. FT REGION 36 38 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT REGION 130 132 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 30 30 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 34 34 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 37 37 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 79 79 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 203 203 S-adenosyl-L-methionine; via carbonyl FT oxygen and amide nitrogen. FT {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 246 AA; 28235 MW; 884313BD5B84376F CRC64; MSVLGRIHSF ESCGTVDGPG IRFILFMQGC LMRCKYCHNR DTWDLEGGKE ISVEDLMKEV VTYRHFMNAT GGGVTASGGE AVLQAEFVRD WFRACKEEGI NTCLDTNGFV RHYDHIIDEL LDVTDLVLLD LKELNDQVHQ NLIGVPNKRT LEFAKYLQKR NQHTWIRYVV VPGYTDSDHD VHLLGQFIEG MTNIEKVELL PYHRLGVHKW KTLGLDYELE NVLPPTKESL EHIKTILEGY GHTVKF // ID PMBA_HAEIN Reviewed; 451 AA. AC P45077; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Metalloprotease PmbA homolog; DE EC=3.4.-.-; GN Name=pmbA; OrderedLocusNames=HI_1152; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable metalloprotease. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase U62 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; L42023; AAC22807.1; -; Genomic_DNA. DR PIR; C64186; C64186. DR RefSeq; NP_439310.1; NC_000907.1. DR RefSeq; WP_005693467.1; NC_000907.1. DR ProteinModelPortal; P45077; -. DR STRING; 71421.HI1152; -. DR MEROPS; U62.001; -. DR EnsemblBacteria; AAC22807; AAC22807; HI_1152. DR GeneID; 950115; -. DR KEGG; hin:HI1152; -. DR PATRIC; 20190979; VBIHaeInf48452_1202. DR eggNOG; ENOG4105CMS; Bacteria. DR eggNOG; COG0312; LUCA. DR KO; K03592; -. DR OMA; TCEVPVL; -. DR OrthoDB; EOG65J4ZF; -. DR PhylomeDB; P45077; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metalloprotease; Protease; KW Reference proteome. FT CHAIN 1 451 Metalloprotease PmbA homolog. FT /FTId=PRO_0000142353. SQ SEQUENCE 451 AA; 48498 MW; 8C8E080C0A297700 CRC64; MKPAENSTAL LKAQEQELRQ AVSFAVELAT KAGASAEVAV TKVSGLSVSA RLQEIENVEF TNDGALGISV YMGQQKGNAS TSDLSESAIK NAVEAALAIA KYTSPDDCTG LADKDLMAFD APDLELYHAA DIDVDKATEL ALQAEQAALQ ADERIINSNG ASFNSHTGVK VYGNSHGMLQ SYLSSRYSLS CSVIGGVEDA LENDYEYTIS REFDKLQSPI WVGENCAKKV VSRLNPQKLS TREVPVIFLN DVATGIISHF AAAISGGSLY RKSSFLLDHL GKQVLPDWFS ISERPHLLRR LASTPFDSEG VRTQDREIVE NGILQTYLVT SYSGKKLGMS STGHAGGIHN WLVKPNLTGG LTALLRQMGT GLLVTDVMGQ GVNIVTGDYS RGASGFWVEN GEIQYPVAEI TIAGQLQDML KNMLAVADDI EHRSNIQTGS ILLDKMKISG N // ID PLDB_HAEIN Reviewed; 313 AA. AC P44800; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Probable lysophospholipase L2; DE EC=3.1.1.5; DE AltName: Full=Lecithinase B; GN Name=pldB; OrderedLocusNames=HI_0645; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O = CC glycerophosphocholine + a carboxylate. CC -!- SUBCELLULAR LOCATION: Cell inner 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; L42023; AAC22305.1; -; Genomic_DNA. DR PIR; A64084; A64084. DR RefSeq; NP_438805.1; NC_000907.1. DR RefSeq; WP_005694498.1; NC_000907.1. DR ProteinModelPortal; P44800; -. DR STRING; 71421.HI0645; -. DR ESTHER; haein-pldb; Monoglyceridelipase_lysophospholip. DR EnsemblBacteria; AAC22305; AAC22305; HI_0645. DR GeneID; 949694; -. DR KEGG; hin:HI0645; -. DR PATRIC; 20189905; VBIHaeInf48452_0674. DR eggNOG; ENOG4108EUD; Bacteria. DR eggNOG; COG2267; LUCA. DR KO; K01048; -. DR OMA; VVLPDCP; -. DR OrthoDB; EOG6CCH34; -. DR PhylomeDB; P44800; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central. DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR022742; Hydrolase_4. DR Pfam; PF12146; Hydrolase_4; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome. FT CHAIN 1 313 Probable lysophospholipase L2. FT /FTId=PRO_0000058457. SQ SEQUENCE 313 AA; 36658 MW; 891E784FF7F77C2E CRC64; MIREPYFHQF ALAELLPFFE QFPTQYLSGK RNIKLAYRHL IQPESAVRKL MILVNGRAEN MLKWSELAYD FYHQGYDVLL FDHRGQGYSQ RIIPQKGHLD EFRFYVDDMA KIIEKVTALF SYSTQHLLAH SMGALIATYY LANYDHHINK AVLSSPFYGI LLKHPIRDEL IITLMNILGQ GERYVFGKGA YQQAHLEYNE LTFCKTRMKW MNRINRKNPA INLGGPTFRW VHLCLNAIKR LPKVIPKIEI PILILQAEKE KIVDNKNLEK LTALFPNARC EVILNAKHEV LFEKDNVRRN VLKSVNHFLN VQS // ID PLSY_HAEIN Reviewed; 199 AA. AC P44603; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 101. 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}; GN OrderedLocusNames=HI_0266; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149. RC STRAIN=E1a / Serotype B, HI1388, and HI689 / Serotype B; RA Morton D.J., Madore L.C., Stull T.L.; RT "Role of the Hxu operon in the acquisition of heme from heme-albumin RT complexes by Haemophilus influenzae."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of an acyl group from acyl- CC phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form CC lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate CC as fatty acyl donor, but not acyl-CoA or acyl-ACP. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- CATALYTIC ACTIVITY: Acyl-phosphate + sn-glycerol 3-phosphate = 1- CC acyl-sn-glycerol 3-phosphate + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. CC {ECO:0000255|HAMAP-Rule:MF_01043}. CC -!- SUBUNIT: Probably interacts with PlsX. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01043}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC -!- SIMILARITY: Belongs to the PlsY family. {ECO:0000255|HAMAP- CC Rule:MF_01043}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21932.1; -; Genomic_DNA. DR EMBL; AF536755; AAQ10748.1; -; Genomic_DNA. DR EMBL; AF545479; AAQ11963.1; -; Genomic_DNA. DR EMBL; AF536754; AAQ10742.1; -; Genomic_DNA. DR PIR; E64146; E64146. DR RefSeq; NP_438435.1; NC_000907.1. DR RefSeq; WP_005653382.1; NC_000907.1. DR STRING; 71421.HI0266; -. DR EnsemblBacteria; AAC21932; AAC21932; HI_0266. DR GeneID; 949419; -. DR KEGG; hin:HI0266; -. DR PATRIC; 20189059; VBIHaeInf48452_0281. DR eggNOG; ENOG4105K7Z; Bacteria. DR eggNOG; COG0344; LUCA. DR KO; K08591; -. DR OMA; HIWPVWL; -. DR OrthoDB; EOG6M6JSX; -. DR PhylomeDB; P44603; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043772; F:acyl-phosphate glycerol-3-phosphate acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01043; PlsY; 1. DR InterPro; IPR003811; G3P_acylTferase_PlsY. DR PANTHER; PTHR30309:SF0; PTHR30309:SF0; 1. DR Pfam; PF02660; G3P_acyltransf; 1. DR SMART; SM01207; G3P_acyltransf; 1. DR TIGRFAMs; TIGR00023; TIGR00023; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 199 Glycerol-3-phosphate acyltransferase. FT /FTId=PRO_0000188378. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 56 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 80 100 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 115 135 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT TRANSMEM 154 176 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. FT VARIANT 18 18 I -> V (in strain: HI1388). FT VARIANT 27 28 IA -> LT (in strain: E1a). FT VARIANT 54 54 S -> F (in strain: HI689). SQ SEQUENCE 199 AA; 22113 MW; F9506EC831916B30 CRC64; MSLFALFYML FAYLLGSISS AILICRIAGL PDPRQNGSHN PGATNVLRIG NRKSALAVLI FDMLKGMIPV WAGYYLGLTQ FELGMVALGA CLGHIFPIFF QFKGGKGVAT AFGAIAPISW AVAGSMFGTW IFVFLVSGYS SLSAVISALL VPFYVWWFKP EFTFPVALVC CLLIYRHHDN IQRLWRGQED KVWAKFKKK // ID PNP_HAEIN Reviewed; 709 AA. AC P44584; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595}; DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595}; DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595}; DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595}; GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=HI_0229; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the CC phosphorolysis of single-stranded polyribonucleotides processively CC in the 3'- to 5'-direction. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- CATALYTIC ACTIVITY: RNA(n+1) + phosphate = RNA(n) + a nucleoside CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595}; CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. CC {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Belongs to the polyribonucleotide CC nucleotidyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC Rule:MF_01595}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21898.1; -; Genomic_DNA. DR PIR; E64056; E64056. DR RefSeq; NP_438401.1; NC_000907.1. DR RefSeq; WP_010868964.1; NC_000907.1. DR ProteinModelPortal; P44584; -. DR SMR; P44584; 616-690. DR STRING; 71421.HI0229; -. DR PRIDE; P44584; -. DR EnsemblBacteria; AAC21898; AAC21898; HI_0229. DR GeneID; 951143; -. DR KEGG; hin:HI0229; -. DR PATRIC; 20188981; VBIHaeInf48452_0243. DR eggNOG; ENOG4105C62; Bacteria. DR eggNOG; COG1185; LUCA. DR KO; K00962; -. DR OMA; RFMFHYN; -. DR OrthoDB; EOG6WT8CC; -. DR PhylomeDB; P44584; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 1.10.10.400; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1370.10; -; 1. DR Gene3D; 3.30.230.70; -; 2. DR HAMAP; MF_01595; PNPase; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012162; PNPase. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR PANTHER; PTHR11252; PTHR11252; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF03726; PNPase; 1. DR Pfam; PF01138; RNase_PH; 2. DR Pfam; PF03725; RNase_PH_C; 2. DR Pfam; PF00575; S1; 1. DR PIRSF; PIRSF005499; PNPase; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR SUPFAM; SSF54791; SSF54791; 1. DR SUPFAM; SSF55666; SSF55666; 2. DR TIGRFAMs; TIGR03591; polynuc_phos; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase. FT CHAIN 1 709 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000197914. FT DOMAIN 552 622 KH. {ECO:0000255|HAMAP-Rule:MF_01595}. FT DOMAIN 621 689 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 485 485 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. FT METAL 491 491 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01595}. SQ SEQUENCE 709 AA; 77007 MW; BD9E08EA6236C860 CRC64; MNPIVKQFKY GQHTVTLETG AIARQATAAV MASMDDTTVF VTVVAKKDVK EGQDFFPLTV NYQERTYAAG KIPGGFFKRE GRPSEGETLI ARLIDRPIRP LFPEGFFNEI QVVATVVSVN PQISPDLVAM IGASAALTLS GVPFNGPIGA ARVGFIDNQF VLNPTMAEQK QSRLDLVVAG TDKAVLMVES EADILTEEQM LAAVVFGHQQ QQVVVEAIKE FAKEAGKPRW DWVAPQPNTD LINKVKAIAE ARLGDAYRIT EKQLRYEQID AIKADVIAQI TAEDEEXSEG KIVDIFTALE SQIVRGRIIA GEPRIDGRTV DTVRALDICT GVLPRTHGSA IFTRGETQAL AVATLGTERD AQIIDELTGE RQDHFLFHYN FPPYSVGETG MIGSPKRREI GHGRLAKRGV AAVMPSLAEF PYVVRVVSEI TESNGSSSMA SVCGASLALM DAGVPIKAAV AGIAMGLVKE EEKFVVLSDI LGDEDHLGDM DFKVAGTREG VTALQMDIKI EGITPEIMQI ALNQAKSARM HILGVMEQAI PAPRADISDY APRIYTMKID PKKIKDVIGK GGATIRSLTE ETGTSIDIDD DGTVKIAAVD SNAAKNVMGR IEEIVAEVEA GVIYKGKVTR LADFGAFVAI VGNKEGLVHI SQIAEERVEK VSDYLQVGQE VNVKVVEIDR QGRIRLTMKD LAPKQETEIN QEDSVEEQE // ID POTA_HAEIN Reviewed; 372 AA. AC P45171; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 11-NOV-2015, entry version 110. DE RecName: Full=Spermidine/putrescine import ATP-binding protein PotA {ECO:0000255|HAMAP-Rule:MF_01726}; DE EC=3.6.3.31 {ECO:0000255|HAMAP-Rule:MF_01726}; GN Name=potA {ECO:0000255|HAMAP-Rule:MF_01726}; GN OrderedLocusNames=HI_1347; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01726}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Spermidine/putrescine importer (TC 3.A.1.11.1) family. CC {ECO:0000255|HAMAP-Rule:MF_01726}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01726}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22991.1; 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; L42023; AAC22991.1; ALT_INIT; Genomic_DNA. DR PIR; B64118; B64118. DR RefSeq; NP_439498.2; NC_000907.1. DR ProteinModelPortal; P45171; -. DR STRING; 71421.HI1347; -. DR EnsemblBacteria; AAC22991; AAC22991; HI_1347. DR GeneID; 950268; -. DR KEGG; hin:HI1347; -. DR PATRIC; 20191377; VBIHaeInf48452_1399. DR eggNOG; ENOG4105C53; Bacteria. DR eggNOG; COG3842; LUCA. DR KO; K11072; -. DR OMA; VENQPQN; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015594; F:putrescine-importing ATPase activity; IEA:InterPro. DR GO; GO:0015595; F:spermidine-importing ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR017879; ABC_Sperm/Put_ATP-bd_PotA. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005893; Sp_pt_ABC_ATP-bd. DR InterPro; IPR013611; Transp-assoc_OB_typ2. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08402; TOBE_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF50331; SSF50331; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01187; potA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51305; POTA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 372 Spermidine/putrescine import ATP-binding FT protein PotA. FT /FTId=PRO_0000092749. FT DOMAIN 11 241 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01726}. FT NP_BIND 43 50 ATP. {ECO:0000255|HAMAP-Rule:MF_01726}. SQ SEQUENCE 372 AA; 42408 MW; 4C26E6E047564C09 CRC64; MENQLQNKPI IELRSIKKSY GSNTIINDFN LTINNGEFVT ILGPSGCGKT TVLRLLAGLE ELDSGSIILD GEDITNVPAE KRHINTVFQS YALFPHMTIF ENVAFGLRMQ KVPNEEIKPR VLEALRMVQL EEMADRKPTQ LSGGQQQRIA IARAVVNKPK VLLLDESLSA LDYKLRKQMQ QELKMLQRQL GITFIFVTHD QEEAITMSDR IVLLRKGKIA QDGSPREIYE DPANLFVARF IGEINVFEAT VIERKSEQVV LANVEGRICD IYTDMPVEKD QKLQVLLRPE DIVIEELDEN EHSKAIIGHI IDRTYKGMTL ESTVEFDHNG MRVLVSEFFN EDDPHMDHSI GQRVGITWHE GWEVVLNDED NQ // ID POTE_HAEIN Reviewed; 435 AA. AC P44768; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Putrescine-ornithine antiporter; DE AltName: Full=Putrescine transport protein; GN Name=potE; OrderedLocusNames=HI_0590; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable putrescine-ornithine antiporter. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22247.1; -; Genomic_DNA. DR PIR; E64079; E64079. DR RefSeq; NP_438748.1; NC_000907.1. DR RefSeq; WP_005694562.1; NC_000907.1. DR STRING; 71421.HI0590; -. DR EnsemblBacteria; AAC22247; AAC22247; HI_0590. DR GeneID; 950609; -. DR KEGG; hin:HI0590; -. DR PATRIC; 20189739; VBIHaeInf48452_0612. DR eggNOG; ENOG4105D5Q; Bacteria. DR eggNOG; COG0531; LUCA. DR KO; K03756; -. DR OMA; IFLIMAM; -. DR OrthoDB; EOG6N945X; -. DR PhylomeDB; P44768; -. DR Proteomes; UP000000579; 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; IBA:GO_Central. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015496; F:putrescine:ornithine antiporter activity; IEA:InterPro. DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IBA:GOC. DR GO; GO:0015807; P:L-amino acid transport; IBA:GOC. DR InterPro; IPR002293; AA/rel_permease1. DR InterPro; IPR004754; Amino_acid_antiprt. DR InterPro; IPR027566; Antiport_PotE. DR PANTHER; PTHR11785; PTHR11785; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR TIGRFAMs; TIGR00905; 2A0302; 1. DR TIGRFAMs; TIGR04299; antiport_PotE; 1. PE 3: Inferred from homology; KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 435 Putrescine-ornithine antiporter. FT /FTId=PRO_0000054252. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. FT TRANSMEM 386 406 Helical. {ECO:0000255}. FT TRANSMEM 409 429 Helical. {ECO:0000255}. SQ SEQUENCE 435 AA; 46349 MW; C4D992217975B5A8 CRC64; MSAKSNKIGV VQLTILTMVN MMGSGIIMLP TKLAEIGTIS IVSWLVTAVG STALAYAFAQ CGMFSKKSGG MGGYAEYSFG KAGNFMANYT YGVSLVIANT AIAISAVGYG SELFGTILSP LSIALWTIFT LWLATVLNFG GARITGNISS FTIWGVIIPV VGISIIGWKW FDGSMYVNSW NPHNVPTFEA IGVSISMTLW AFLGLESACA NADAVENPEK NVPIAVLGGT LGAAVIYIVS TNVIAGIVPN LELANSTAPF GLAFAHMFDE TVGKVIMGLM VMSCFGSLLG WQFTIAQVFK SSAEEGYFPA FFKKITSKDA PVVGMITITA LQTLLSLMTI SPSLNKQFNV LVDLAVVTNV IPYLLSMAAL AVLLKAENVA PQKYKTTVFV AFIGSLYSIY ALYAAGEQAM LYGSIVTFIG WTLYGFVSYK FDLKK // ID PLSB_HAEIN Reviewed; 810 AA. AC P44857; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Glycerol-3-phosphate acyltransferase; DE Short=GPAT; DE EC=2.3.1.15; GN Name=plsB; OrderedLocusNames=HI_0748; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1- CC acyl-sn-glycerol 3-phosphate. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. 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 GPAT/DAPAT 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; L42023; AAC22406.1; -; Genomic_DNA. DR PIR; D64090; D64090. DR RefSeq; NP_438907.1; NC_000907.1. DR RefSeq; WP_005693149.1; NC_000907.1. DR ProteinModelPortal; P44857; -. DR STRING; 71421.HI0748; -. DR DNASU; 949773; -. DR EnsemblBacteria; AAC22406; AAC22406; HI_0748. DR GeneID; 949773; -. DR KEGG; hin:HI0748; -. DR PATRIC; 20190139; VBIHaeInf48452_0785. DR eggNOG; ENOG4105E55; Bacteria. DR eggNOG; COG2937; LUCA. DR KO; K00631; -. DR OMA; EVIYVPC; -. DR OrthoDB; EOG6B625B; -. DR PhylomeDB; P44857; -. DR UniPathway; UPA00557; UER00612. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00393; Glyc3P_acyltrans; 1. DR InterPro; IPR022284; GPAT/DHAPAT. DR InterPro; IPR028354; GPAT_PlsB. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR PANTHER; PTHR12563; PTHR12563; 2. DR Pfam; PF01553; Acyltransferase; 1. DR PIRSF; PIRSF500064; GPAT; 1. DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1. DR SMART; SM00563; PlsC; 1. DR TIGRFAMs; TIGR03703; plsB; 1. PE 3: Inferred from homology; KW Acyltransferase; Cell inner membrane; Cell membrane; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 810 Glycerol-3-phosphate acyltransferase. FT /FTId=PRO_0000195222. FT MOTIF 306 311 HXXXXD motif. SQ SEQUENCE 810 AA; 92775 MW; DB8564BC3E2C370D CRC64; MANFINMYRQ LLSLPLSALV KNNPIPANPI EELSLNIHQP IVYVLPYTSQ TDFVIFRRNC LALGLPDPAE KNEINGVKLP RYVYLDEGRR IFKSKGAKDE TTTIFNKYLE LHRTSESLDV QLIPVSVLWG RSPGQEDKSD LPNLRLLNGI QKTFAAIWFG RDTFVRFSQA VSLRYMVVEH GSDEKIAQKL ARVAKMHFAK QRISATGPRL PNRQAMFNKL LQSEAIRRAI EDEAKSKNIS IEKAQKEAYK ILDEIAADVS HSSLRAVDRF LRWLWNKLYS GINVQNSNRV RKLALEGHEI VYVPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPI GRMFRSWGAF FIRRTFKGNR LYSAIFREYL SELFHRGYSV EYFIEGGRSR TGRLLAPKTG MMSMTLQALQ HSQTRPISIV PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIKKLR NLGQGFVNFG EPITLSNYLS QHFPDWKEQN HEEKPQWFTP AVNNISKQVM ININKAAAVN SMNLVGTALL SSRQRALSRE QLLEQLSSYQ QLLQNVPYST DVVLPNVTPQ AMLEHVLALD RIGVLIEKDN FGEIVRLERS SAVLMTYYRN NIQHLFVLPS LVASIILHYE AIQKDLLLDA IRKIYPFLQG ELFLHFNEDE LNVQIHQIIN EFARQSVINS NDNFLSINKS KVRILQLWSA GMLEILQRYY ITVTILQKQP AISRAELEKE SQLVAQRLSV LHGINAPEFF DKAVFSSFIA NLKEQRYFDE SGYTVLDKIE ELASTLSHLI STEICLTVKG TIEKSEDLSS // ID PNUC_HAEIN Reviewed; 226 AA. AC Q57425; P96338; Q8L2G5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 11-NOV-2015, entry version 80. DE RecName: Full=Nicotinamide riboside transporter PnuC; GN Name=pnuC; OrderedLocusNames=HI_1077.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=12446641; DOI=10.1128/JB.184.24.6906-6917.2002; RA Kurnasov O.V., Polanuyer B.M., Ananta S., Sloutsky R., Tam A., RA Gerdes S.Y., Osterman A.L.; RT "Ribosylnicotinamide kinase domain of NadR protein: identification and RT implications in NAD biosynthesis."; RL J. Bacteriol. 184:6906-6917(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15561822; DOI=10.1128/AAC.48.12.4532-4541.2004; RA Sauer E., Merdanovic M., Mortimer A.P., Bringmann G., Reidl J.; RT "PnuC and the utilization of the nicotinamide riboside analog 3- RT aminopyridine in Haemophilus influenzae."; RL Antimicrob. Agents Chemother. 48:4532-4541(2004). CC -!- FUNCTION: Required for nicotinamide riboside transport across the CC inner membrane. {ECO:0000269|PubMed:15561822}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:15561822}; Multi-pass membrane protein CC {ECO:0000269|PubMed:15561822}. CC -!- INDUCTION: Repressed by NadR. CC -!- SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake CC permease (TC 4.B.1) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22744.1; Type=Frameshift; Positions=21, 175; 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; AF503632; AAM27449.1; -; Genomic_DNA. DR EMBL; L42023; AAC22744.1; ALT_FRAME; Genomic_DNA. DR EnsemblBacteria; AAC22744; AAC22744; HI_1077.1. DR OMA; GGYAMSW; -. DR BRENDA; 2.7.1.22; 2529. DR Proteomes; UP000000579; 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:0034257; F:nicotinamide riboside transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR006419; NMN_transpt_PnuC. DR Pfam; PF04973; NMN_transporter; 1. DR TIGRFAMs; TIGR01528; NMN_trans_PnuC; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 226 Nicotinamide riboside transporter PnuC. FT /FTId=PRO_0000078000. FT TOPO_DOM 1 14 Cytoplasmic. FT {ECO:0000305|PubMed:15561822}. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TOPO_DOM 36 36 Periplasmic. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TOPO_DOM 58 65 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TOPO_DOM 87 90 Periplasmic. {ECO:0000255}. FT TRANSMEM 91 110 Helical. {ECO:0000255}. FT TOPO_DOM 111 123 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TOPO_DOM 145 153 Periplasmic. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TOPO_DOM 175 179 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TOPO_DOM 201 202 Periplasmic. {ECO:0000255}. FT TRANSMEM 203 223 Helical. {ECO:0000255}. FT TOPO_DOM 224 226 Cytoplasmic. FT {ECO:0000305|PubMed:15561822}. FT BINDING 183 183 Nicotinamide riboside. FT {ECO:0000250|UniProtKB:D2ZZC1}. FT BINDING 187 187 Nicotinamide riboside. FT {ECO:0000250|UniProtKB:D2ZZC1}. SQ SEQUENCE 226 AA; 25530 MW; 6870235BA9C06EE3 CRC64; MTLAARLKQE FVSGWKPFEV VWLALFIIAQ IWAYVQTPDS WLAMISGISG ILCVVLVSKG KISNYFFGLI FAYTYFYVAW GSNFLGEMNT VLYVYLPSQF IGYFMWKANM QNSDGGESVI AKALTVKGWM TLIVVTTVGT LLFVQALQAA GGSSTGLDGL TTIITVAAQI LMILRYREQW LLWIGLNILS IFLWAETPAI YLMYSAYLLN SLYGYYNWTK LVKRTN // ID PLSC_HAEIN Reviewed; 240 AA. AC P44848; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=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=HI_0734; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. 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; L42023; AAC22391.1; -; Genomic_DNA. DR PIR; D64089; D64089. DR RefSeq; NP_438893.1; NC_000907.1. DR RefSeq; WP_005689023.1; NC_000907.1. DR ProteinModelPortal; P44848; -. DR STRING; 71421.HI0734; -. DR EnsemblBacteria; AAC22391; AAC22391; HI_0734. DR GeneID; 950749; -. DR KEGG; hin:HI0734; -. DR PATRIC; 20190105; VBIHaeInf48452_0768. DR eggNOG; ENOG4107S7E; Bacteria. DR eggNOG; COG0204; LUCA. DR KO; K00655; -. DR OMA; VCSTTHN; -. DR OrthoDB; EOG6ZWJDH; -. DR PhylomeDB; P44848; -. DR UniPathway; UPA00557; UER00613. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central. 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; Cell inner membrane; Cell membrane; KW Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 240 1-acyl-sn-glycerol-3-phosphate FT acyltransferase. FT /FTId=PRO_0000208169. FT MOTIF 73 78 HXXXXD motif. SQ SEQUENCE 240 AA; 27502 MW; 2333CE2618FF97BB CRC64; MLKLLRIFLV LICCILICVL GTIYSFIRFK NPSNVGIVAR WFGRLYPLFG LKVEHRIPQD QKQISRAIYI GNHQNNYDMV TISYMVQPRT VSVGKKSLIW IPFFGILYWV TGNIFLDREN RTKAHNTMSQ LARRINEDNL SIWMFPEGTR NRGRGLLPFK TGAFHAAISA GVPIIPVVCS STHNKINLNR WDNGKVICEI MDPIDVSGYT KDNVRDLAAY CHDLMEKRIA ELDEEIAKGN // ID PNTA_HAEIN Reviewed; 512 AA. AC P43842; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=NAD(P) transhydrogenase subunit alpha; DE EC=1.6.1.2; DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha; DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha; GN Name=pntA; OrderedLocusNames=HI_1362; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC -!- SUBUNIT: Heterodimer of an alpha (PntA) and a beta (PntB) chain. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AlaDH/PNT 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; L42023; AAC23009.1; -; Genomic_DNA. DR PIR; E64119; E64119. DR RefSeq; NP_439513.1; NC_000907.1. DR RefSeq; WP_005693998.1; NC_000907.1. DR ProteinModelPortal; P43842; -. DR SMR; P43842; 3-375. DR STRING; 71421.HI1362; -. DR EnsemblBacteria; AAC23009; AAC23009; HI_1362. DR GeneID; 950278; -. DR KEGG; hin:HI1362; -. DR PATRIC; 20191411; VBIHaeInf48452_1416. DR eggNOG; ENOG4108IIE; Bacteria. DR eggNOG; COG3288; LUCA. DR KO; K00324; -. DR OMA; NVAPKEF; -. DR OrthoDB; EOG61P6S9; -. DR PhylomeDB; P43842; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB. DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IBA:GO_Central. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central. DR GO; GO:0015992; P:proton transport; IBA:GO_Central. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR008142; AlaDH/PNT_CS1. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR026255; NADP_transhyd_a. DR InterPro; IPR024605; NADP_transhyd_a_C. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR Pfam; PF12769; PNTB_4TM; 1. DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00561; pntA; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 512 NAD(P) transhydrogenase subunit alpha. FT /FTId=PRO_0000199018. FT TOPO_DOM 1 400 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. FT TRANSMEM 422 442 Helical. {ECO:0000255}. FT TOPO_DOM 443 451 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 452 472 Helical. {ECO:0000255}. FT TOPO_DOM 473 478 Periplasmic. {ECO:0000255}. FT TRANSMEM 479 499 Helical. {ECO:0000255}. FT TOPO_DOM 500 512 Cytoplasmic. {ECO:0000255}. FT NP_BIND 125 128 NAD. {ECO:0000250}. FT NP_BIND 195 197 NAD. {ECO:0000250}. FT BINDING 175 175 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 225 225 NAD; via carbonyl oxygen. {ECO:0000250}. SQ SEQUENCE 512 AA; 54973 MW; 50D63AD536E837EF CRC64; MLIGVPRELL ENESRVAATP KTVQQILKLG FDVIVEHDAG FKASFEDQAF LEAGAKIGTS AEIWQSDIIF KVNAPTDEEI AQMKEGAALV SFIWRMQNPE LMKKLTAKKI NVLAMDAVPR ISRAQALDAL SSMANISGYR AVIEAAHEFG SFFTGQITAA GKVPPAKVLV IGAGVAGLAA IGAANSLGAI VRAFDSRPEV KEQVQSMGAS FLEIDFKEEG GSGDGYAKVM SEEFNRRAME LYAEQAKEVD IIITTAAIPG KPAPRLITKE MVDSMKPGSV IVDLAAATGG NCEYTQAGKV VTTENQVKVI GYTDFPSRLP TQSSQLYGTN LVNLLKLLCK EKDGNINIDF EDVVLRGVTV VRDGEEIPPA QIQVSAQPKQ ETKAAPVAEK KESKPTDPRV KYGVMAGVGV LFLWLASVAP AAFLSHFTVF VLACVVGYYV VWNVSHALHT PLMAVTNAIS GIIIVGALLQ IRQPTGNLFI DALAFVAILV ASINIFGGFR VTQRMLAMFR KG // ID POTD2_HAEIN Reviewed; 350 AA. AC P44731; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Spermidine/putrescine-binding periplasmic protein 2; DE Short=SPBP; DE Flags: Precursor; GN Name=potD-A; OrderedLocusNames=HI_0498; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine and spermidine. Polyamine binding CC protein (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein CC PotD/PotF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22155.1; 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; L42023; AAC22155.1; ALT_INIT; Genomic_DNA. DR PIR; E64072; E64072. DR RefSeq; NP_438656.2; NC_000907.1. DR RefSeq; WP_005666442.1; NC_000907.1. DR ProteinModelPortal; P44731; -. DR SMR; P44731; 27-349. DR STRING; 71421.HI0498; -. DR EnsemblBacteria; AAC22155; AAC22155; HI_0498. DR GeneID; 950055; -. DR KEGG; hin:HI0498; -. DR PATRIC; 20189547; VBIHaeInf48452_0516. DR eggNOG; ENOG4107RUE; Bacteria. DR eggNOG; COG0687; LUCA. DR KO; K11069; -. DR OMA; MAMAGAM; -. DR OrthoDB; EOG66XBH9; -. DR PhylomeDB; P44731; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1. DR PRINTS; PR00909; SPERMDNBNDNG. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 350 Spermidine/putrescine-binding periplasmic FT protein 2. FT /FTId=PRO_0000031841. SQ SEQUENCE 350 AA; 39647 MW; D764F90754618A47 CRC64; MKKFFAHSLK NLFLSTTALF AASAFANNKL YVYNWTDYVP SDLVAQFSKE TGIEVIYSTF ESNEEMYAKL KLTQNTGSGY DLVFPSSYYV NKMIKEKMLQ PIDQSKLTNI HQIPKHLLNK EFDPENKYSL PYVYGLTGIE VNADEIDPKT ITSWADLWKP EFKGKVLMTS DAREVFHVAL LLDGKSPNTT NEEDIKTAYE RLEKLLPNVA TFNSDSPEVP YVQGEVAIGM IWNGSAYLAQ KENQSLQFVY PKEGAIFWMD NYAIPTTAKN VEGAHKFIDF LLRPENAKIV IERMGFSMPN NGAKTLLSAE VANDPKLFPP AEEVEKGIMQ GDVGEAVDIY EKYWGKLKTN // ID PPDD_HAEIN Reviewed; 149 AA. AC P44623; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Prepilin peptidase-dependent protein D homolog; DE Flags: Precursor; GN Name=ppdD; OrderedLocusNames=HI_0299; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Fimbrium. CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin 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; L42023; AAC21963.1; -; Genomic_DNA. DR PIR; C64147; C64147. DR RefSeq; NP_438466.1; NC_000907.1. DR RefSeq; WP_005694367.1; NC_000907.1. DR ProteinModelPortal; P44623; -. DR STRING; 71421.HI0299; -. DR EnsemblBacteria; AAC21963; AAC21963; HI_0299. DR GeneID; 949521; -. DR KEGG; hin:HI0299; -. DR PATRIC; 20189137; VBIHaeInf48452_0315. DR eggNOG; COG4969; LUCA. DR KO; K02682; -. DR OMA; IPAYQGY; -. DR OrthoDB; EOG6D5G5G; -. DR PhylomeDB; P44623; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell. DR InterPro; IPR012902; N_methyl_site. DR Pfam; PF13633; N_methyl_3; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1. PE 3: Inferred from homology; KW Complete proteome; Fimbrium; Methylation; Reference proteome. FT PROPEP 1 12 {ECO:0000250}. FT /FTId=PRO_0000024282. FT CHAIN 13 149 Prepilin peptidase-dependent protein D FT homolog. FT /FTId=PRO_0000024283. FT MOD_RES 13 13 N-methylphenylalanine. FT {ECO:0000255|PROSITE-ProRule:PRU01070}. SQ SEQUENCE 149 AA; 15509 MW; 5056C8C0BE74F662 CRC64; MKLTTLQTLK KGFTLIELMI VIAIIAILAT IAIPSYQNYT KKAAVSELLQ ASAPYKADVE LCVYSTNETT SCTGGKNGIA ADIKTAKGYV ASVITQSGGI TVKGNGTLAN MEYILQAKGN AAAGVTWTTT CKGTDASLFP ANFCGSVTK // ID PPIB_HAEIN Reviewed; 169 AA. AC P44499; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B; DE Short=PPIase B; DE EC=5.2.1.8; DE AltName: Full=Rotamase B; GN Name=ppiB; OrderedLocusNames=HI_0079; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00156}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21754.1; -; Genomic_DNA. DR PIR; D64047; D64047. DR RefSeq; NP_438252.1; NC_000907.1. DR RefSeq; WP_005693842.1; NC_000907.1. DR ProteinModelPortal; P44499; -. DR SMR; P44499; 1-168. DR STRING; 71421.HI0079; -. DR EnsemblBacteria; AAC21754; AAC21754; HI_0079. DR GeneID; 950978; -. DR KEGG; hin:HI0079; -. DR PATRIC; 20188613; VBIHaeInf48452_0080. DR eggNOG; ENOG4108R5K; Bacteria. DR eggNOG; COG0652; LUCA. DR KO; K03768; -. DR OMA; GMDENFK; -. DR OrthoDB; EOG6S26C3; -. DR PhylomeDB; P44499; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR PANTHER; PTHR11071; PTHR11071; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; SSF50891; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isomerase; Reference proteome; Rotamase. FT CHAIN 1 169 Peptidyl-prolyl cis-trans isomerase B. FT /FTId=PRO_0000064203. FT DOMAIN 1 168 PPIase cyclophilin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00156}. SQ SEQUENCE 169 AA; 18965 MW; 2A600AEA0C259516 CRC64; MVTLHTNFGD IKIKLDFDKA PVTAENFLNY CKDGFYNNTI FHRVIDGFMI QGGGMESGMR EKATKAPIQN EANNRLSNKR GTIAMARTSD PHSATAQFFI NVADNDFLNY RSKEMFGREV VQEWGYAVFG EVVEGMDVVD KIKKVKTGNK GFHQDVPTED VVITSVSIE // ID POTC_HAEIN Reviewed; 257 AA. AC P45169; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Spermidine/putrescine transport system permease protein PotC; GN Name=potC; OrderedLocusNames=HI_1345; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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 -!- SEQUENCE CAUTION: CC Sequence=AAC22989.1; Type=Frameshift; Positions=5; 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; L42023; AAC22989.1; ALT_FRAME; Genomic_DNA. DR PIR; I64117; I64117. DR RefSeq; NP_439496.1; NC_000907.1. DR ProteinModelPortal; P45169; -. DR STRING; 71421.HI1345; -. DR EnsemblBacteria; AAC22989; AAC22989; HI_1345. DR GeneID; 950267; -. DR KEGG; hin:HI1345; -. DR PATRIC; 20191373; VBIHaeInf48452_1397. DR eggNOG; ENOG4105D38; Bacteria. DR eggNOG; COG1177; LUCA. DR KO; K11070; -. DR OrthoDB; EOG66XBH9; -. DR Proteomes; UP000000579; 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 inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 257 Spermidine/putrescine transport system FT permease protein PotC. FT /FTId=PRO_0000060184. FT TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 27 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 28 65 Periplasmic. {ECO:0000255}. FT TRANSMEM 66 85 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 86 100 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 101 120 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 121 128 Periplasmic. {ECO:0000255}. FT TRANSMEM 129 148 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 149 176 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 177 196 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 197 231 Periplasmic. {ECO:0000255}. FT TRANSMEM 232 251 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 252 257 Cytoplasmic. {ECO:0000255}. FT DOMAIN 60 248 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 257 AA; 28614 MW; 0A2C81CF154102D5 CRC64; MSRFFLRNAF MFVVYAYLYI PIIILVTNSF NKDRYGLSWK GFSWNWYERL FNNDTLIQAA IHSVTIAFFA ATLATIVGGL TAIALYRYRF RGKQAVSGML FIVMMSPDIV MAVSLLALFM VVGISLGFWS LLLAHVTFCL PYVTVTIFSR LNGFDSRMLE AAKDLGASEV TILRKIILPL ALPAVVSGWL LSFTISLDDV VVSSFVSGVS YEILPLRIFS LVKTGVTPEV NALATIMIVL SLALVVLSQL ITRKNNH // ID PRMA_HAEIN Reviewed; 296 AA. AC P44402; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Ribosomal protein L11 methyltransferase; DE Short=L11 Mtase; DE EC=2.1.1.-; GN Name=prmA; OrderedLocusNames=HI_0978; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Methylates ribosomal protein L11. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA 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; L42023; AAC22638.1; -; Genomic_DNA. DR PIR; I64105; I64105. DR RefSeq; NP_439141.1; NC_000907.1. DR RefSeq; WP_010869100.1; NC_000907.1. DR ProteinModelPortal; P44402; -. DR STRING; 71421.HI0978; -. DR EnsemblBacteria; AAC22638; AAC22638; HI_0978. DR GeneID; 949962; -. DR KEGG; hin:HI0978; -. DR PATRIC; 20190617; VBIHaeInf48452_1021. DR eggNOG; ENOG4105F59; Bacteria. DR eggNOG; COG2264; LUCA. DR KO; K02687; -. DR OMA; FVHKIEQ; -. DR OrthoDB; EOG6N684G; -. DR PhylomeDB; P44402; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00735; Methyltr_PrmA; 1. DR InterPro; IPR004498; Ribosomal_PrmA_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF000401; RPL11_MTase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00406; prmA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 296 Ribosomal protein L11 methyltransferase. FT /FTId=PRO_0000192266. SQ SEQUENCE 296 AA; 32764 MW; 3B771D669ED9DCC9 CRC64; MAWIQIRLNS TNEKAEQMSD FLEEIGSVSV TFMDSQDTPI FEPLPGETRL WGNTDVIALF DAETDMAEIV RLLKEAKHLD SNTAYKIGTN RRLKNWEREW MDNFHPMQFG KRLWICPSWR DVPDENAVNV MLDPGLAFGT GTHPTTALCL EWLDGLDLKD KSVIDFGCGS GILAIAALKL GAKSAVGIDI DPQAILASRN NAEQNGVTDR LQLFLSDEKP SDLKADVVVA NILAGPLKEL YPIISQLVKP NGDLGLSGIL ETQAQSVCDT YTQTFALEPV AAREEWCRIT GKLKTL // ID POTB_HAEIN Reviewed; 286 AA. AC P45170; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Spermidine/putrescine transport system permease protein PotB; GN Name=potB; OrderedLocusNames=HI_1346; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine and spermidine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC22990.1; -; Genomic_DNA. DR PIR; A64118; A64118. DR RefSeq; NP_439497.1; NC_000907.1. DR RefSeq; WP_005694014.1; NC_000907.1. DR ProteinModelPortal; P45170; -. DR STRING; 71421.HI1346; -. DR EnsemblBacteria; AAC22990; AAC22990; HI_1346. DR GeneID; 950272; -. DR KEGG; hin:HI1346; -. DR PATRIC; 20191375; VBIHaeInf48452_1398. DR eggNOG; ENOG4105F38; Bacteria. DR eggNOG; COG1176; LUCA. DR KO; K11071; -. DR OMA; KFFTPVY; -. DR OrthoDB; EOG6HMXBZ; -. DR PhylomeDB; P45170; -. DR Proteomes; UP000000579; 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 inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 286 Spermidine/putrescine transport system FT permease protein PotB. FT /FTId=PRO_0000060178. FT TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 14 33 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 34 71 Periplasmic. {ECO:0000255}. FT TRANSMEM 72 91 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 92 100 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 101 120 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 121 151 Periplasmic. {ECO:0000255}. FT TRANSMEM 152 171 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 172 199 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 200 219 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 220 252 Periplasmic. {ECO:0000255}. FT TRANSMEM 253 272 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 273 286 Cytoplasmic. {ECO:0000255}. FT DOMAIN 66 274 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 286 AA; 32210 MW; C8CC2F1A5866920B CRC64; MKIINNKFQK ITVAIIFSWL IFFVLIPNLL VLAVSFLTRD GSNFYAFPIT IENYTNLFNP LYAQVVWNSL SMSGIATIIC LLIGYPFAFM MSKIHPKYRP LLLFLVVLPF WTNSLIRIYG MKVFLGVKGI LNTMLIDMGI LSAPIRILNT EIAVIIGLVY LLLPFMILPL YSAIEKLDNR LLEAARDLGA NTFQRFFRVI LPLTMPGIIA GCLLVLLPAM GMFYVADLLG GAKVLLVGNV IKSEFLISRN WPFGSAVSIG LTVLMALLIF VYYRANKLLN RKVELE // ID PPID_HAEIN Reviewed; 622 AA. AC P44092; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-NOV-2015, entry version 107. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D; DE Short=PPIase D; DE EC=5.2.1.8; DE AltName: Full=Rotamase D; GN Name=ppiD; OrderedLocusNames=HI_1004; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: PPIases accelerate the folding of proteins. Seems to be CC involved in the folding of outer membrane proteins (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC type II membrane protein {ECO:0000305}; Periplasmic side CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00278}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22665.1; Type=Frameshift; Positions=43; 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; L42023; AAC22665.1; ALT_FRAME; Genomic_DNA. DR PIR; B64018; B64018. DR RefSeq; NP_439165.2; NC_000907.1. DR RefSeq; WP_010869104.1; NC_000907.1. DR ProteinModelPortal; P44092; -. DR STRING; 71421.HI1004; -. DR DNASU; 950512; -. DR EnsemblBacteria; AAC22665; AAC22665; HI_1004. DR GeneID; 950512; -. DR KEGG; hin:HI1004; -. DR PATRIC; 20190669; VBIHaeInf48452_1047. DR eggNOG; ENOG4105EIN; Bacteria. DR eggNOG; COG0760; LUCA. DR KO; K03770; -. DR OMA; QTDWFTR; -. DR OrthoDB; EOG6M9DS4; -. DR PhylomeDB; P44092; -. DR Proteomes; UP000000579; 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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR023058; PPIase_PpiC_CS. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF13145; Rotamase_2; 1. DR SUPFAM; SSF109998; SSF109998; 2. DR PROSITE; PS01096; PPIC_PPIASE_1; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Isomerase; Membrane; KW Reference proteome; Rotamase; Transmembrane; Transmembrane helix. FT CHAIN 1 622 Peptidyl-prolyl cis-trans isomerase D. FT /FTId=PRO_0000193426. FT TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TOPO_DOM 38 622 Periplasmic. {ECO:0000255}. FT DOMAIN 270 356 PpiC. {ECO:0000255|PROSITE- FT ProRule:PRU00278}. SQ SEQUENCE 622 AA; 69590 MW; EE5900A5381C4EB4 CRC64; MLIEKMHNLT NSKISKFILG LIAVSFLVGG MSGYLFSSND TYAAKVNGEV ISQQDFLNRY NQEFEIRAQR EGEAFVAQSD SPEFVTALRQ NIVNLMIDQE LLRQYVKELK LGVSDEMIKR AIVTDPNFQV KGKFDNAVYQ RILQQNHLTS DGYASILRAS LPLEQIQNGV ANSEFIVPAQ VKNSAEVFFQ KRLARLATLS LADEMAKQSV SDDEIKTYYE ANQKSFVQPE QVKVQYIDLS ADNISRNLQV TDVEIAQYYQ DNKAQFMTQH LAHIQFANEQ DAKVAYEELQ KGANFADVAK AKSLDKISGE NGGDLGWVNE NELPKAFEDA AAALQVGQYS QPINVDGNYH IVLVQERKAQ SLENVKAQIA DLVRKSLMES RYFSLEKQAS DKAFEDSKSL NTAAQAAGVK VQESDYFSRQ NVPAGLNFPN VIYTIFESDT TNVGMNSEPI NVGDYHTIIV RVLDRKAEGV KSLEEAKIDI ETFLKRQKAE NALNGKAQQA VKKLSENPES KVDGINFSSE QTFTLSENKD PILTNGIFSI AKPESSKALY QVVHNSNGDV VVVALNKVEQ GSLSEKELSQ FAMQLLRSHQ SELQVQLIQG LRERAKIEVN DSFINQDDEA QQ // ID PPX_HAEIN Reviewed; 323 AA. AC P44828; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative exopolyphosphatase; DE EC=3.6.1.11; DE AltName: Full=Metaphosphatase; GN Name=ppx; OrderedLocusNames=HI_0695; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Degradation of inorganic polyphosphates. Orthophosphate CC is released progressively from the ends of polyphosphate. CC -!- CATALYTIC ACTIVITY: (Polyphosphate)(n) + H(2)O = CC (polyphosphate)(n-1) + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GppA/Ppx family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. Compared with other CC ppx it lacks 200 residues at the C-terminal region. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22355.1; -; Genomic_DNA. DR PIR; C64087; C64087. DR RefSeq; NP_438855.1; NC_000907.1. DR RefSeq; WP_005694580.1; NC_000907.1. DR ProteinModelPortal; P44828; -. DR SMR; P44828; 16-321. DR STRING; 71421.HI0695; -. DR EnsemblBacteria; AAC22355; AAC22355; HI_0695. DR GeneID; 950213; -. DR KEGG; hin:HI0695; -. DR PATRIC; 20190011; VBIHaeInf48452_0727. DR eggNOG; ENOG4105C9X; Bacteria. DR eggNOG; COG0248; LUCA. DR KO; K01524; -. DR OMA; TERCFAS; -. DR OrthoDB; EOG6M6JN6; -. DR PhylomeDB; P44828; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro. DR InterPro; IPR022371; Exopolyphosphatase. DR InterPro; IPR003695; Ppx_GppA. DR Pfam; PF02541; Ppx-GppA; 1. DR TIGRFAMs; TIGR03706; exo_poly_only; 1. PE 5: Uncertain; KW Cell membrane; Complete proteome; Hydrolase; Magnesium; Membrane; KW Reference proteome. FT CHAIN 1 323 Putative exopolyphosphatase. FT /FTId=PRO_0000194302. SQ SEQUENCE 323 AA; 35566 MW; 5B7E9BBEFE780FB6 CRC64; MNDSILEPKH RGNVREIAAI DLGSNSFHMI VARIVNGSIQ VLSRLKQKVK LAEGLDENAV LNQEAITRGV NCLALFAERL QGFPMENVNV VGTYTLRRAV NNDEFLRQAA KVFPYPINII SGQTEAKTIY AGVCHTQPEK GRKLVIDIGG GSTEMIIGDD FTPLMAESRH MGCVSFATQF FTDGIISPEN FQRARQSAVN KIEDLGLEYR KLGWQSVLGS SGTIKTVAQV IATNLDPNGT ITAERLNALI EQTLQAKHFT ELNINGLNQD RVDVFVPGLA ILSAVFDVFH IQQMRYSDGA LREGVIYSLE KNFQVADIRA STA // ID PQQL_HAEIN Reviewed; 926 AA. AC P45181; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Probable zinc protease PqqL; DE EC=3.4.24.-; GN Name=pqqL; OrderedLocusNames=HI_1368; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M16 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; L42023; AAC23015.1; -; Genomic_DNA. DR PIR; E64171; E64171. DR RefSeq; NP_439519.1; NC_000907.1. DR RefSeq; WP_005693992.1; NC_000907.1. DR ProteinModelPortal; P45181; -. DR STRING; 71421.HI1368; -. DR MEROPS; M16.A05; -. DR EnsemblBacteria; AAC23015; AAC23015; HI_1368. DR GeneID; 950673; -. DR KEGG; hin:HI1368; -. DR PATRIC; 20191423; VBIHaeInf48452_1422. DR eggNOG; ENOG4107RAN; Bacteria. DR eggNOG; COG0612; LUCA. DR KO; K07263; -. DR OMA; RDINAFT; -. DR OrthoDB; EOG6QRW4S; -. DR PhylomeDB; P45181; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 3.30.830.10; -; 3. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR011237; Pept_M16_dom. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR001431; Pept_M16_Zn_BS. DR InterPro; IPR007863; Peptidase_M16_C. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 2. DR SUPFAM; SSF63411; SSF63411; 3. DR PROSITE; PS00143; INSULINASE; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1 926 Probable zinc protease PqqL. FT /FTId=PRO_0000074416. FT ACT_SITE 82 82 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10096}. FT METAL 79 79 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10096}. FT METAL 83 83 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10096}. FT METAL 159 159 Zinc. {ECO:0000255|PROSITE- FT ProRule:PRU10096}. SQ SEQUENCE 926 AA; 107024 MW; 450BBD8C24720002 CRC64; MKKTTALFLL IFSLIACQSL ELSPNNNLPF DPNIQHGKLS NGLQYFVLKN TEPKERVYIR LVINAGSMHE DDDQKGIAHL VEHMAFNGSK KYPENQIINA LEKLGMKFAR DINAFTDFEN TVYTLNLDSN NQQKLELAFD VINEWMNNIT FLPKDVDGER GVVQEEWRRR LSPMLRIGNK KSAIEMAGSR YVLRDPIGDM DIIKTISAKR VADFYHKWYR PDNMSVIIVG DIDTKQVVKL LKQNLSQENP ITKTTLEKID FNIPLINKWR LDSISEQGTT IPSIELSFFE NTIETNTLAS YKQELIQQIT TRLLNLRLQQ WEKETENGVD SANFYRTHLG KETLQSIFSL QLIDTQYSKT IDKLFAFIAS IKQQGFTQNE LSGEIKRLTQ LNEKQLNIRS GSLKIADDLI TSVANKQVVL SVNDRYELNK RFLSQITLAD LQRTLNQTLA LKAKLLLITQ PLPQKALPFD VAEIETRWNN VMEMQQHQWD EKKQIEKLPH LTFNTGSLSQ EKYWDRGDIY EFRLSNGSKL IYHYSDKTPN QVHFRAVTQG GLRSIPNKDY HLLRAAVSVV DETGVGELSL SAVNQIFSRD PLVIATVIDD DKQGFTGVSK PKDLENLLTL FRLKLRSSPI SDLALEKYRR ETRDYFKQID LETQFMQAVS KLRFPNIETV YTQKQAQQLS FDKNQLNNAY QHYILDKTDF TYFIIGDIEL NQVKKLAERY LASIESKTQI RHFVPTIIHT PTQSFIMNGL KEPRADVEIY LTADNTWRTE QKYLFNILAD IVQEKLRLIL REKVSGIYSV NSWFMQDVYA PQIEGKIEFS CDPKRVEELT YLTNQVLDDI IKNGIDENLL RKKLAEQHTQ IRREFDSLVS IASIIEESYW QQDNPDAIYT YQHLDQLATK ATIDALAQKA LKKSGRFVSI LKAASY // ID PROB_HAEIN Reviewed; 368 AA. AC P43763; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Glutamate 5-kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456}; DE AltName: Full=Gamma-glutamyl kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00456}; GN Name=proB {ECO:0000255|HAMAP-Rule:MF_00456}; GN OrderedLocusNames=HI_0900; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate CC to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22560.1; -; Genomic_DNA. DR PIR; D64101; D64101. DR RefSeq; NP_439061.1; NC_000907.1. DR RefSeq; WP_005693251.1; NC_000907.1. DR ProteinModelPortal; P43763; -. DR SMR; P43763; 2-365. DR STRING; 71421.HI0900; -. DR EnsemblBacteria; AAC22560; AAC22560; HI_0900. DR GeneID; 949633; -. DR KEGG; hin:HI0900; -. DR PATRIC; 20190457; VBIHaeInf48452_0942. DR eggNOG; ENOG4105CGT; Bacteria. DR eggNOG; COG0263; LUCA. DR KO; K00931; -. DR OMA; KMNKQWI; -. DR OrthoDB; EOG6PGK7G; -. DR PhylomeDB; P43763; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00456; ProB; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR011529; Glu_5kinase. DR InterPro; IPR005715; Glu_5kinase/COase_Synthase. DR InterPro; IPR019797; Glutamate_5-kinase_CS. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR01027; proB; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 368 Glutamate 5-kinase. FT /FTId=PRO_0000109678. FT DOMAIN 275 353 PUA. {ECO:0000255|HAMAP-Rule:MF_00456}. FT NP_BIND 168 169 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT NP_BIND 210 216 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 9 9 ATP. {ECO:0000255|HAMAP-Rule:MF_00456}. FT BINDING 49 49 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 136 136 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00456}. FT BINDING 148 148 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00456}. SQ SEQUENCE 368 AA; 40134 MW; E32B684A23709831 CRC64; MNKKTIVVKF GTSTLTQGSP KLNSPHMMEI VRQIAQLHND GFRIVIVTSG AIAAGRHYLN HPQLPPTIAS KQLLAAVGQS QLIQAWEKLF AIYDIHIGQL LLTRADIEDR ERFLNARDTL YALLDNHIIP VINENDAVAT AEIKVGDNDN LSALVAILVQ AEQLYLLTDQ QGLFDSDPRK NPEAKLIPVV EQITDHIRSI AGGSGTNLGT GGMMTKIIAA DVATRSGIET IIAPGNRPNV IADLAYEQNI GTKFIAHQSD RLESRKQWLF AAPSAGIITI DNGAQNAILE QNKSLLPAGI INVEGRFSRG EVVKIRTQSG KDIALGMPRY NSDALQLIKG RKSADIENVL GYEYGAVAMH RDDMIILS // ID PNTB_HAEIN Reviewed; 474 AA. AC P43010; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=NAD(P) transhydrogenase subunit beta; DE EC=1.6.1.2; DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta; DE AltName: Full=Pyridine nucleotide transhydrogenase subunit beta; GN Name=pntB; OrderedLocusNames=HI_1363; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-474. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6; RA Chandler M.S., Smith R.A.; RT "Characterization of the Haemophilus influenzae topA locus: DNA RT topoisomerase I is required for genetic competence."; RL Gene 169:25-31(1996). CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled CC to respiration and ATP hydrolysis and functions as a proton pump CC across the membrane. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PNT beta subunit 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; L42023; AAC23010.1; -; Genomic_DNA. DR EMBL; U20964; AAC43725.1; -; Genomic_DNA. DR PIR; F64119; F64119. DR RefSeq; NP_439514.1; NC_000907.1. DR RefSeq; WP_005693997.1; NC_000907.1. DR ProteinModelPortal; P43010; -. DR SMR; P43010; 308-474. DR STRING; 71421.HI1363; -. DR DNASU; 950280; -. DR EnsemblBacteria; AAC23010; AAC23010; HI_1363. DR GeneID; 950280; -. DR KEGG; hin:HI1363; -. DR PATRIC; 20191413; VBIHaeInf48452_1417. DR eggNOG; ENOG4105C15; Bacteria. DR eggNOG; COG1282; LUCA. DR KO; K00325; -. DR OMA; HHAEVFI; -. DR OrthoDB; EOG6WDSHK; -. DR PhylomeDB; P43010; -. DR Proteomes; UP000000579; 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:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR012136; NADH_DH_b. DR Pfam; PF02233; PNTB; 1. DR PIRSF; PIRSF000204; PNTB; 1. DR SUPFAM; SSF52467; SSF52467; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW NADP; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 474 NAD(P) transhydrogenase subunit beta. FT /FTId=PRO_0000199026. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 181 200 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. FT TRANSMEM 253 273 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT CONFLICT 343 343 A -> P (in Ref. 2; AAC43725). FT {ECO:0000305}. SQ SEQUENCE 474 AA; 50163 MW; 5F914630211FF844 CRC64; MSEGLVQAAY ILAALLFIMS LAGLSKHETA KAGCWFGIVG MTIALIATIF GPHSEGTFWI IIAMIIGGAI GVQRALKVEM TEMPELVAIL HSFVGLAAVL VGFNSYGLHH EALMPEGLDA AAQAAFVAEQ AVLTNIHNVE VFLGIFIGAV TFTGSVVAFG KLSGKINSKA LMLPHRHKLN LAALVVSALL MVAFLNNPES IFPVLLMTAI ALAFGWHLVA SIGGADMPVV VSMLNSYSGW AAAAAGFILN NDLLIVTGAL VGSSGAILSY IMCKAMNRSF VSVIAGGFGN DVQVSSSEEQ GEHRETTAEE VAELLKNASS VIITPGYGMA VAQAQYPVAD ITAKLRERGV NVRFGIHPVA GRLPGHMNVL LAEAKVPYDV VLEMDEINDD FADTDVVLVI GANDTVNPAA MEDPNSPIAG MPVLEVWKAQ NVIVFKRSMA VGYAGVQNPL FFKENTQMLF GDAKDRVEDI LKAL // ID PRIB_HAEIN Reviewed; 108 AA. AC P44748; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 24-OCT-2003, sequence version 3. DT 11-NOV-2015, entry version 91. DE RecName: Full=Primosomal replication protein n; GN Name=priB; OrderedLocusNames=HI_0546; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site CC (PAS). {ECO:0000250}. CC -!- SUBUNIT: Component of the preprimosomal complex composed of PriA, CC PriB, PriC, DnaB and DnaT. Upon transient interaction with DnaG it CC forms the primosome (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PriB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22204.1; 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; L42023; AAC22204.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_438704.2; NC_000907.1. DR RefSeq; WP_005694144.1; NC_000907.1. DR ProteinModelPortal; P44748; -. DR SMR; P44748; 8-107. DR STRING; 71421.HI0546; -. DR EnsemblBacteria; AAC22204; AAC22204; HI_0546. DR GeneID; 949533; -. DR KEGG; hin:HI0546; -. DR PATRIC; 20189645; VBIHaeInf48452_0565. DR eggNOG; ENOG4108VDV; Bacteria. DR eggNOG; COG2965; LUCA. DR KO; K02686; -. DR OMA; CQMPVII; -. DR OrthoDB; EOG6KMB8F; -. DR PhylomeDB; P44748; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00720; PriB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR023646; Prisomal_replication_PriB. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF003135; Primosomal_n; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR04418; PriB_gamma; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; Primosome; KW Reference proteome. FT CHAIN 1 108 Primosomal replication protein n. FT /FTId=PRO_0000199053. FT DOMAIN 8 108 SSB. SQ SEQUENCE 108 AA; 12107 MW; 93CC8E71BFE6948E CRC64; MLKSNLKIDN SFSVMGVVSR LPKRLKSPSG IEHCKFLLEH RSDQIESGFT RQAWLKMPVQ ISGNQLIEKT QSITVGSKIL VVGFITSHKT QSGLCQLVLH AEQIEFID // ID PRMC_HAEIN Reviewed; 292 AA. AC P45253; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126}; DE Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126}; DE EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=M.HindHemKP; DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; GN Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; Synonyms=hemK; GN OrderedLocusNames=HI_1559; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Methylates the class 1 translation termination release CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the CC universally conserved GGQ motif. {ECO:0000255|HAMAP- CC Rule:MF_02126}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [peptide chain CC release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + CC [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine. CC {ECO:0000255|HAMAP-Rule:MF_02126}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmC subfamily. {ECO:0000255|HAMAP-Rule:MF_02126}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23208.1; -; Genomic_DNA. DR PIR; H64129; H64129. DR RefSeq; NP_439708.1; NC_000907.1. DR RefSeq; WP_005693587.1; NC_000907.1. DR ProteinModelPortal; P45253; -. DR SMR; P45253; 2-290. DR STRING; 71421.HI1559; -. DR EnsemblBacteria; AAC23208; AAC23208; HI_1559. DR GeneID; 950419; -. DR KEGG; hin:HI1559; -. DR PATRIC; 20191843; VBIHaeInf48452_1630. DR eggNOG; ENOG4105EQY; Bacteria. DR eggNOG; COG2890; LUCA. DR KO; K02493; -. DR OMA; TYLFTWP; -. DR OrthoDB; EOG68Q0SZ; -. DR PhylomeDB; P45253; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02126; RF_methyltr_PrmC; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR025714; Methyltranfer_dom. DR InterPro; IPR004556; Modification_methylase_HemK. DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF13847; Methyltransf_31; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 292 Release factor glutamine FT methyltransferase. FT /FTId=PRO_0000157164. FT REGION 126 130 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT REGION 198 201 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_02126}. FT BINDING 157 157 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT BINDING 184 184 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT BINDING 198 198 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. SQ SEQUENCE 292 AA; 33055 MW; 3035B1A4423DB198 CRC64; MNYKEWLAQA IADLAKKNPT ENSKIDALVL LQHATGKSRT QILAFDDTEI DEKVRLKLTA LLDRRLKGEP IAYILGEKEF WSLPLNVSKG TLIPRPDTEI LVEKALQIAL EKLEENPPHF RILDLGTGTG AIALALASEL APICQKRHIP LEIIGVDLMS DVVALAQSNA ERNQLNVEFL QSRWFDNITG KFDLIVSNPP YIDAQDEHLH QGDVRFEPLS ALVANDEGYA DLRHIIELAS SYLNSNGVLL LEHGWQQGEK VRSIFQENHW EMVETVRDYS DNERVTLGFW KK // ID POTD1_HAEIN Reviewed; 360 AA. AC P45168; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Spermidine/putrescine-binding periplasmic protein 1; DE Short=SPBP; DE Flags: Precursor; GN Name=potD-B; OrderedLocusNames=HI_1344; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the activity of the bacterial periplasmic CC transport system of putrescine and spermidine. Polyamine binding CC protein (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein CC PotD/PotF family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22988.1; 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; L42023; AAC22988.1; ALT_INIT; Genomic_DNA. DR PIR; H64117; H64117. DR RefSeq; NP_439495.1; NC_000907.1. DR ProteinModelPortal; P45168; -. DR SMR; P45168; 37-359. DR STRING; 71421.HI1344; -. DR EnsemblBacteria; AAC22988; AAC22988; HI_1344. DR GeneID; 950266; -. DR KEGG; hin:HI1344; -. DR PATRIC; 20191371; VBIHaeInf48452_1396. DR eggNOG; ENOG4107RUE; Bacteria. DR eggNOG; COG0687; LUCA. DR KO; K11069; -. DR OMA; NHANIAP; -. DR OrthoDB; EOG66XBH9; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0019808; F:polyamine binding; IEA:InterPro. DR GO; GO:0015846; P:polyamine transport; IEA:InterPro. DR InterPro; IPR001188; Sperm_putr-bd. DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1. DR PRINTS; PR00909; SPERMDNBNDNG. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 16 {ECO:0000255}. FT CHAIN 17 360 Spermidine/putrescine-binding periplasmic FT protein 1. FT /FTId=PRO_0000031840. SQ SEQUENCE 360 AA; 39990 MW; 166CCC976D0579C0 CRC64; MKKFAGLITA SFVAATLTAC NDKDAKQETA KATAAANDTV YLYTWTEYVP DGLLDEFTKE TGIKVIVSSL ESNETMYAKL KTQGESGGYD VIAPSNYFVS KMAREGMLKE LDHSKLPVLK ELDPDWLNKP YDKGNKYSLP QLLGAPGIAF NTNTYKGEQF TSWADLWKPE FANKVQLLDD AREVFNIALL KIGQDPNTQD PAIIKQAYEE LLKLRPNVLS FNSDNPANSF ISGEVEVGQL WNGSVRIAKK EKAPLNMVFP KEGPVLWVDT LAIPATAKNS EGAHKLINYM LGKKTAEKLT LAIGYPTSNI EAKKALPKEI TEDPAIYPSA DILKNSHWQD DVGDAIQFYE QYYQELKAAK // ID PRC_HAEIN Reviewed; 695 AA. AC P45306; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Tail-specific protease; DE EC=3.4.21.102; DE AltName: Full=C-terminal-processing peptidase; DE AltName: Full=Protease Re; DE Flags: Precursor; GN Name=prc; OrderedLocusNames=HI_1668; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the cleavage of a C-terminal peptide of 11 CC residues from the precursor form of penicillin-binding protein 3 CC (PBP3). May be involved in protection of the bacterium from CC thermal and osmotic stresses (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: The enzyme shows specific recognition of a C- CC terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala CC or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, CC but then cleaves at a variable distance from the C-terminus. A CC typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala- CC Leu-Ala-Ala. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein; Periplasmic side. CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23314.1; -; Genomic_DNA. DR PIR; F64135; F64135. DR RefSeq; NP_439810.1; NC_000907.1. DR RefSeq; WP_005694393.1; NC_000907.1. DR ProteinModelPortal; P45306; -. DR STRING; 71421.HI1668; -. DR MEROPS; S41.001; -. DR EnsemblBacteria; AAC23314; AAC23314; HI_1668. DR GeneID; 950859; -. DR KEGG; hin:HI1668; -. DR PATRIC; 20192085; VBIHaeInf48452_1746. DR eggNOG; ENOG4105CN1; Bacteria. DR eggNOG; COG0793; LUCA. DR KO; K03797; -. DR OMA; IGWRLDE; -. DR OrthoDB; EOG6D5FZF; -. DR PhylomeDB; P45306; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.90.226.10; -; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004447; Peptidase_S41A. DR InterPro; IPR005151; Tail-specific_protease. DR InterPro; IPR020992; Tail_Prtase_C. DR Pfam; PF11818; DUF3340; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF03572; Peptidase_S41; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00245; TSPc; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR TIGRFAMs; TIGR00225; prc; 1. DR PROSITE; PS50106; PDZ; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Serine protease; Signal. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 695 Tail-specific protease. FT /FTId=PRO_0000027333. FT DOMAIN 256 316 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT ACT_SITE 459 459 Charge relay system. {ECO:0000250}. FT ACT_SITE 470 470 Charge relay system. {ECO:0000250}. FT ACT_SITE 484 484 Charge relay system. {ECO:0000250}. SQ SEQUENCE 695 AA; 78870 MW; 3FB5DECC7E62AC1E CRC64; MVMKFKMSKN VICYTWLSVC LSSAIPAFAV QPTLKPSDIS IPAISEESQL ATKRATTRLT QSHYRKIKLD DDFSEKIFDR YIKNLDFNHN TFLQSDIDEL RQKYGTKLDE QLNQGDLSAA FDIYDVMMKR RYERYTYALS LLDKEPDLNG QDQIEIDREK AAAPQTEADA NKLWDARVKN DIINLKLKDK KWSEIKAKLT KRYNLAIRRL TQTKADDIVQ IYLNAFAREI DPHTSYLSPR TAKSFNESIN LSLEGIGTTL QSEDDEISIK SLVPGAPAER SKKLHPGDKI IGVGQATGDI EDVVGWRLED LVEKIKGKKG TKVRLEIEPA KGGKSRIITL VRDKVRIEDQ AAKLTFEKVS GKNIAVIKIP SFYIGLTEDV KKLLVKLENQ KAEALIVDLR ENGGGALTEA VALSGLFITD GPVVQVRDAY QRIRVHEDDD ATQQYKGLLF VMINRYSASA SEIFAAAMQD YRRGIIIGQN TFGKGTVQQS RSLNFIYDLD QSPLGVLQYT IQKFYRVNGG STQLKGVAAD INFPEIIDAK EYGEDKEDNA LAWDKIPSAS YMEVGNINYI DNAVNILNEK HLARIAKDPE FVALNEELKV RNERRDRKFL SLNYKMRKAE NDKDDARRLK DLNERFKREG KKALKDIDDL PKDYEAPDFF LKEAEKIAAD FVIFNSDQKI NQANGLSEAK TESKK // ID PRX5_HAEIN Reviewed; 241 AA. AC P44758; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Hybrid peroxiredoxin hyPrx5; DE EC=1.11.1.15; DE AltName: Full=Thioredoxin reductase; GN OrderedLocusNames=HI_0572; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=12529327; DOI=10.1074/jbc.M209553200; RA Kim S.J., Woo J.R., Hwang Y.S., Jeong D.G., Shin D.H., Kim K., RA Ryu S.E.; RT "The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals RT interactions between electron donor and acceptor proteins."; RL J. Biol. Chem. 278:10790-10798(2003). CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22230.1; -; Genomic_DNA. DR PIR; I64154; I64154. DR RefSeq; NP_438729.1; NC_000907.1. DR RefSeq; WP_005694168.1; NC_000907.1. DR PDB; 1NM3; X-ray; 2.80 A; A/B=1-241. DR PDBsum; 1NM3; -. DR ProteinModelPortal; P44758; -. DR SMR; P44758; 3-241. DR STRING; 71421.HI0572; -. DR PeroxiBase; 4786; HinPrxGrx_KW20. DR EnsemblBacteria; AAC22230; AAC22230; HI_0572. DR GeneID; 950101; -. DR KEGG; hin:HI0572; -. DR PATRIC; 20189699; VBIHaeInf48452_0592. DR eggNOG; ENOG4105EHV; Bacteria. DR eggNOG; COG0678; LUCA. DR eggNOG; COG0695; LUCA. DR KO; K03386; -. DR OMA; DKMFIEP; -. DR OrthoDB; EOG6PKFB5; -. DR PhylomeDB; P44758; -. DR EvolutionaryTrace; P44758; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 2. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR011906; Glutaredoxin_dom. DR InterPro; IPR014025; Glutaredoxin_subgr. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00462; Glutaredoxin; 1. DR Pfam; PF08534; Redoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR02190; GlrX-dom; 1. DR PROSITE; PS00195; GLUTAREDOXIN_1; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Electron transport; KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome; KW Transport. FT CHAIN 1 241 Hybrid peroxiredoxin hyPrx5. FT /FTId=PRO_0000056612. FT DOMAIN 170 241 Glutaredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT REGION 1 169 Peroxiredoxin-like. FT ACT_SITE 49 49 Cysteine sulfenic acid (-SOH) FT intermediate. {ECO:0000250}. FT DISULFID 180 183 Redox-active. FT STRAND 13 18 {ECO:0000244|PDB:1NM3}. FT STRAND 21 26 {ECO:0000244|PDB:1NM3}. FT HELIX 27 31 {ECO:0000244|PDB:1NM3}. FT STRAND 34 42 {ECO:0000244|PDB:1NM3}. FT HELIX 47 51 {ECO:0000244|PDB:1NM3}. FT HELIX 53 66 {ECO:0000244|PDB:1NM3}. FT STRAND 71 78 {ECO:0000244|PDB:1NM3}. FT HELIX 80 89 {ECO:0000244|PDB:1NM3}. FT STRAND 95 99 {ECO:0000244|PDB:1NM3}. FT HELIX 104 108 {ECO:0000244|PDB:1NM3}. FT STRAND 112 114 {ECO:0000244|PDB:1NM3}. FT TURN 116 119 {ECO:0000244|PDB:1NM3}. FT STRAND 122 124 {ECO:0000244|PDB:1NM3}. FT STRAND 127 132 {ECO:0000244|PDB:1NM3}. FT STRAND 135 141 {ECO:0000244|PDB:1NM3}. FT STRAND 151 154 {ECO:0000244|PDB:1NM3}. FT HELIX 155 162 {ECO:0000244|PDB:1NM3}. FT STRAND 172 176 {ECO:0000244|PDB:1NM3}. FT HELIX 181 193 {ECO:0000244|PDB:1NM3}. FT STRAND 198 201 {ECO:0000244|PDB:1NM3}. FT TURN 202 205 {ECO:0000244|PDB:1NM3}. FT HELIX 208 214 {ECO:0000244|PDB:1NM3}. FT STRAND 218 220 {ECO:0000244|PDB:1NM3}. FT STRAND 222 225 {ECO:0000244|PDB:1NM3}. FT STRAND 228 232 {ECO:0000244|PDB:1NM3}. FT HELIX 233 238 {ECO:0000244|PDB:1NM3}. SQ SEQUENCE 241 AA; 26743 MW; D2FD230D20BE63F0 CRC64; MSSMEGKKVP QVTFRTRQGD KWVDVTTSEL FDNKTVIVFS LPGAFTPTCS SSHLPRYNEL APVFKKYGVD DILVVSVNDT FVMNAWKEDE KSENISFIPD GNGEFTEGMG MLVGKEDLGF GKRSWRYSML VKNGVVEKMF IEPNEPGDPF KVSDADTMLK YLAPQHQVQE SISIFTKPGC PFCAKAKQLL HDKGLSFEEI ILGHDATIVS VRAVSGRTTV PQVFIGGKHI GGSDDLEKYF A // ID PRIA_HAEIN Reviewed; 730 AA. AC P44647; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983}; DE AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983}; GN Name=priA {ECO:0000255|HAMAP-Rule:MF_00983}; GN OrderedLocusNames=HI_0339; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the restart of stalled replication forks. CC Recognizes and binds the arrested nascent DNA chain at stalled CC replication forks. It can open the DNA duplex, via its helicase CC activity, and promote assembly of the primosome and loading of the CC major replicative helicase DnaB onto DNA. {ECO:0000255|HAMAP- CC Rule:MF_00983}. CC -!- SUBUNIT: Component of the primosome. {ECO:0000255|HAMAP- CC Rule:MF_00983}. CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00983}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22001.1; -; Genomic_DNA. DR PIR; G64062; G64062. DR RefSeq; NP_438503.1; NC_000907.1. DR RefSeq; WP_005694336.1; NC_000907.1. DR ProteinModelPortal; P44647; -. DR STRING; 71421.HI0339; -. DR EnsemblBacteria; AAC22001; AAC22001; HI_0339. DR GeneID; 950761; -. DR KEGG; hin:HI0339; -. DR PATRIC; 20189221; VBIHaeInf48452_0356. DR eggNOG; ENOG4105C25; Bacteria. DR eggNOG; COG1198; LUCA. DR KO; K04066; -. DR OMA; RMTVHQR; -. DR OrthoDB; EOG6KT2K4; -. DR PhylomeDB; P44647; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00983; PriA; 1. 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; IPR005259; PriA. 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; 2. DR TIGRFAMs; TIGR00595; priA; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; DNA-binding; KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Primosome; KW Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 730 Primosomal protein N'. FT /FTId=PRO_0000102124. FT DOMAIN 212 378 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT DOMAIN 472 640 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT NP_BIND 225 232 ATP. {ECO:0000255|HAMAP-Rule:MF_00983}. FT ZN_FING 437 449 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT ZN_FING 464 480 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00983}. FT MOTIF 321 324 DEAH box. SQ SEQUENCE 730 AA; 82336 MW; 5DB1D638426C4714 CRC64; MKIVRVALAV PLPRLFDYFV PDDVSLQIGM RVLVPFGTQK RVAIVADFPT KSDVPEDKLK AILQPLDLAP LFTPIYWDWL HWAANYYQAG LGDVLFQALP VKLRNGESAV KNDRTFWRIT DAGKNALKQG ELKRSKKQAE ALQYLSETDL EKGNNDFSSA IWSALKAKGF IEEITIQTNP LSWQQRLGNN PIVNAENRLT LNKQQALAFS QLLFHSGFNV WLLDGVTGSG KTEIYLQYIE EILKSGKQVL VLVPEIGLTP QTVQRFKVRF NVEIDVLHSN LTDTQRLYVW DRARSGQSAI VIGTRSALFT QFSNLGAIIL DEEHDSSYKQ QDSWRYHARD LAIVLAQKLN ISVLMGSATP SLESINNVQN GKYQHLVLSK RAGNSTALRH FVIDLKNQNI QNGLSKPLLE RMKAHLEKGN QVLLFLNRRG FAPVLLCHEC GWIAQCPHCE KPYTYHQHQN VLRCHHCGAQ KTIPRQCGDC GSTHLVTTGL GTEQLEETLK TLFPHYSVAR IDRDSTSRKG KLEGYLEDIQ QGKSQILIGT QMLAKGHHFP NVTLVALVNV DSALFSLDFR AEERLAQLYI QVAGRAGRAD KQGEVVLQTH YPDHPLLTTL LANGYQAFAK ETLQLRHSMG LPPFTFQALI KAQARHSDLA ENCLSQIADF FQSKQITGLQ MLGPMPAPFS KKAGQYRWQL LLQHPSRMTL QKALREYQQA ELEKNSQVRL ILDVDPQDLS // ID PRMB_HAEIN Reviewed; 314 AA. AC P45106; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=50S ribosomal protein L3 glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02125}; DE Short=L3 MTase {ECO:0000255|HAMAP-Rule:MF_02125}; DE EC=2.1.1.298 {ECO:0000255|HAMAP-Rule:MF_02125}; DE AltName: Full=N5-glutamine methyltransferase PrmB {ECO:0000255|HAMAP-Rule:MF_02125}; GN Name=prmB {ECO:0000255|HAMAP-Rule:MF_02125}; GN OrderedLocusNames=HI_1201; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the 50S ribosomal protein L3 on CC a specific glutamine residue. {ECO:0000255|HAMAP-Rule:MF_02125}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [ribosomal protein CC L3]-L-glutamine = S-adenosyl-L-homocysteine + [ribosomal protein CC L3]-N(5)-methyl-L-glutamine. {ECO:0000255|HAMAP-Rule:MF_02125}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmB subfamily. {ECO:0000255|HAMAP-Rule:MF_02125}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22855.1; -; Genomic_DNA. DR PIR; F64189; F64189. DR RefSeq; NP_439357.1; NC_000907.1. DR RefSeq; WP_005694243.1; NC_000907.1. DR ProteinModelPortal; P45106; -. DR STRING; 71421.HI1201; -. DR EnsemblBacteria; AAC22855; AAC22855; HI_1201. DR GeneID; 950156; -. DR KEGG; hin:HI1201; -. DR PATRIC; 20191081; VBIHaeInf48452_1253. DR eggNOG; ENOG4105C76; Bacteria. DR eggNOG; COG2890; LUCA. DR KO; K07320; -. DR OMA; VLVCEVG; -. DR OrthoDB; EOG68Q0SZ; -. DR PhylomeDB; P45106; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro. DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_02125; L3_methyltr_PrmB; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004556; Modification_methylase_HemK. DR InterPro; IPR017127; Ribosome_L3_Gln-N5_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR PIRSF; PIRSF037167; Mtase_YfcB_prd; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00536; hemK_fam; 1. DR TIGRFAMs; TIGR03533; L3_gln_methyl; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 314 50S ribosomal protein L3 glutamine FT methyltransferase. FT /FTId=PRO_0000088006. SQ SEQUENCE 314 AA; 35590 MW; 2AC862003FE05301 CRC64; METSHNQELV ATILEDNVAN ELQTIQDFLR WTYSILNRSD IYFGQGHDNP WDESLQLVLS SLHLPIDLPT ELFNSRLTPS EKETLVQLVL TRIEQRVPVA YLTNSAWFCG HEFYVDERTI IPRSPISALI QDRFEDLISQ EPNHILDLCT GSGCIAIACA YAFPNAEVDA VDLSVDALNV AEINISRHQL EHRVFPIQSN LFENILGQKY DLIVTNPPYV DEEDLADMPE EFHFEPELAL GSGSDGLNIT KQILKQAPDY LTENGVLVCE VGNSMISLIE QYPDVPFEWV ELKNGGLGVF AIQRKDLVKY HDLF // ID PROA_HAEIN Reviewed; 417 AA. AC P45121; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 120. DE RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412}; DE EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; DE Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412}; GN Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; GN OrderedLocusNames=HI_1239; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate CC 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The CC product spontaneously undergoes cyclization to form 1-pyrroline-5- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + CC NADP(+) = L-glutamyl 5-phosphate + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00412}. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}. CC -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase CC family. {ECO:0000255|HAMAP-Rule:MF_00412}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22892.1; -; Genomic_DNA. DR PIR; D64112; D64112. DR RefSeq; NP_439395.1; NC_000907.1. DR RefSeq; WP_005694299.1; NC_000907.1. DR ProteinModelPortal; P45121; -. DR STRING; 71421.HI1239; -. DR EnsemblBacteria; AAC22892; AAC22892; HI_1239. DR GeneID; 950691; -. DR KEGG; hin:HI1239; -. DR PATRIC; 20191157; VBIHaeInf48452_1291. DR eggNOG; ENOG4105C2S; Bacteria. DR eggNOG; COG0014; LUCA. DR KO; K00147; -. DR OMA; CNAIETL; -. DR OrthoDB; EOG6FFSCX; -. DR PhylomeDB; P45121; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 2. DR HAMAP; MF_00412; ProA; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR012134; Glu-5-SA_DH. DR InterPro; IPR000965; GPR_dom. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00407; proA; 1. DR PROSITE; PS01223; PROA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP; KW Oxidoreductase; Proline biosynthesis; Reference proteome. FT CHAIN 1 417 Gamma-glutamyl phosphate reductase. FT /FTId=PRO_0000189732. SQ SEQUENCE 417 AA; 45396 MW; 30472E8ECFAB4D09 CRC64; MLEQMGKQAK DAAFILAQLT TAEKNCALSI IAEQLEQQAP LILAENAKDI ELAKQNGLSD ALIDRLLLTQ ERLQGIANDV RHVISLADPV GKIIDGGTLD SGLKIERVRT PLGVIGTIYE ARPNVTIDVA SLCLKTGNAV ILRGGKETQF SNKILIEVVQ NALEQAGLPK FAVQAITDPN RELVMQLLKL DRYVDMIIPR GGSGLHELCK QHSTIPVIVG GVGVCHTFVE KSADQNKAIF VIDNAKTQRP STCNTLETLL VQHSIAEEFL PKLVSHLSAK NVKYHAKSTA LNILKQAGAN VCEVTEKELR KEWGSLDLNV VVVEDIHAAI EHIRQYGTQH SESILTSSQS LARQFINQVD AAAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTSYKWVCE GEYTVRK // ID PSD_HAEIN Reviewed; 290 AA. AC P43789; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 105. DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00662}; DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00662}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00662}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00662}; GN Name=psd {ECO:0000255|HAMAP-Rule:MF_00662}; OrderedLocusNames=HI_0160; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine CC (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP- CC Rule:MF_00662}. CC -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine = CC phosphatidylethanolamine + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00662}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00662}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00662}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: CC step 2/2. {ECO:0000255|HAMAP-Rule:MF_00662}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit CC and a small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP- CC Rule:MF_00662}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00662}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00662}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The autoendoproteolytic cleavage occurs by a CC canonical serine protease mechanism, in which the side chain CC hydroxyl group of the serine supplies its oxygen atom to form the CC C-terminus of the beta chain, while the remainder of the serine CC residue undergoes an oxidative deamination to produce ammonia and CC the pyruvoyl prosthetic group on the alpha chain. During this CC reaction, the Ser that is part of the protease active site of the CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes CC an essential element of the active site of the mature CC decarboxylase. {ECO:0000255|HAMAP-Rule:MF_00662}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase CC family. PSD-B subfamily. Prokaryotic type I sub-subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00662}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20229; AAA62138.1; -; Genomic_DNA. DR EMBL; L42023; AAC21829.1; -; Genomic_DNA. DR PIR; I64051; I64051. DR RefSeq; NP_438330.1; NC_000907.1. DR RefSeq; WP_005694118.1; NC_000907.1. DR STRING; 71421.HI0160; -. DR EnsemblBacteria; AAC21829; AAC21829; HI_0160. DR GeneID; 951070; -. DR KEGG; hin:HI0160; -. DR PATRIC; 20188819; VBIHaeInf48452_0166. DR eggNOG; ENOG4105DJ4; Bacteria. DR eggNOG; COG0688; LUCA. DR KO; K01613; -. DR OMA; SMATVWH; -. DR OrthoDB; EOG6B8XK4; -. DR PhylomeDB; P43789; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00662; PS_decarb_PSD_B_type1; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033177; PSD. DR InterPro; IPR033178; PSD_type1_pro. DR PANTHER; PTHR10067; PTHR10067; 1. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR TIGRFAMs; TIGR00163; PS_decarb; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Decarboxylase; Lipid biosynthesis; KW Lipid metabolism; Lyase; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Pyruvate; Reference proteome; Zymogen. FT CHAIN 1 256 Phosphatidylserine decarboxylase beta FT chain. {ECO:0000255|HAMAP-Rule:MF_00662}. FT /FTId=PRO_0000029663. FT CHAIN 257 290 Phosphatidylserine decarboxylase alpha FT chain. {ECO:0000255|HAMAP-Rule:MF_00662}. FT /FTId=PRO_0000029664. FT ACT_SITE 96 96 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00662}. FT ACT_SITE 153 153 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00662}. FT ACT_SITE 257 257 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000255|HAMAP-Rule:MF_00662}. FT ACT_SITE 257 257 Schiff-base intermediate with substrate; FT via pyruvic acid; for decarboxylase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_00662}. FT SITE 256 257 Cleavage (non-hydrolytic); by FT autocatalysis. {ECO:0000255|HAMAP- FT Rule:MF_00662}. FT MOD_RES 257 257 Pyruvic acid (Ser); by autocatalysis. FT {ECO:0000255|HAMAP-Rule:MF_00662}. SQ SEQUENCE 290 AA; 33197 MW; 66766BC16AC82B2D CRC64; MMTSNSYWQR LKVAFQYVMP QIYLTQIAGW FAKQKWGKIT HFVIKAFAKK YNIDMSIAQK EQFSDYASFN EFFIRPLKEN ARPINQNPTA LCLPADGRIS ECGHIDDNLL LQAKGHFFSL EDLLAEDKEL VETFKNGEFV TTYLSPRDYH RVHMPCDATL RKMIYVPGDL FSVNPFLAQH VPNLFARNER VICVFDTEFG TMVQILVGAT ITASIGTTWA GVINPPRHNE VKTWTYEGES AVKLLKGQEM GWFQLGSTVI NLFQANQVRL ADHLSVNEPV RMGEILAYKK // ID PSS_HAEIN Reviewed; 455 AA. AC P44704; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase; DE EC=2.7.8.8; DE AltName: Full=Phosphatidylserine synthase; GN Name=pssA; OrderedLocusNames=HI_0425; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: CDP-diacylglycerol + L-serine = CMP + (3-sn- CC phosphatidyl)-L-serine. CC -!- SUBUNIT: Multimeric. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-II family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains. CC {ECO:0000255|PROSITE-ProRule:PRU00153}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22084.1; -; Genomic_DNA. DR PIR; I64066; I64066. DR RefSeq; NP_438586.1; NC_000907.1. DR RefSeq; WP_005693739.1; NC_000907.1. DR PDB; 3HSI; X-ray; 2.20 A; A/B/C=1-455. DR PDBsum; 3HSI; -. DR ProteinModelPortal; P44704; -. DR STRING; 71421.HI0425; -. DR DNASU; 950510; -. DR EnsemblBacteria; AAC22084; AAC22084; HI_0425. DR GeneID; 950510; -. DR KEGG; hin:HI0425; -. DR PATRIC; 20189403; VBIHaeInf48452_0445. DR eggNOG; ENOG4105JIM; Bacteria. DR eggNOG; COG1502; LUCA. DR KO; K00998; -. DR OMA; HLKGFVI; -. DR OrthoDB; EOG6M3P98; -. DR PhylomeDB; P44704; -. DR EvolutionaryTrace; P44704; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR025202; PLD-like_dom. DR InterPro; IPR016270; PLipase-D_PtdSer-synthase-type. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR PANTHER; PTHR12586; PTHR12586; 1. DR Pfam; PF13091; PLDc_2; 1. DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 1. DR SMART; SM00155; PLDc; 2. DR PROSITE; PS50035; PLD; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Membrane; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Repeat; Transferase. FT CHAIN 1 455 CDP-diacylglycerol--serine O- FT phosphatidyltransferase. FT /FTId=PRO_0000056825. FT DOMAIN 134 160 PLD phosphodiesterase 1. FT {ECO:0000255|PROSITE-ProRule:PRU00153}. FT DOMAIN 356 383 PLD phosphodiesterase 2. FT {ECO:0000255|PROSITE-ProRule:PRU00153}. FT HELIX 5 14 {ECO:0000244|PDB:3HSI}. FT STRAND 18 20 {ECO:0000244|PDB:3HSI}. FT HELIX 23 25 {ECO:0000244|PDB:3HSI}. FT STRAND 26 28 {ECO:0000244|PDB:3HSI}. FT HELIX 32 44 {ECO:0000244|PDB:3HSI}. FT STRAND 47 55 {ECO:0000244|PDB:3HSI}. FT HELIX 61 76 {ECO:0000244|PDB:3HSI}. FT STRAND 81 87 {ECO:0000244|PDB:3HSI}. FT HELIX 90 92 {ECO:0000244|PDB:3HSI}. FT HELIX 104 115 {ECO:0000244|PDB:3HSI}. FT STRAND 124 127 {ECO:0000244|PDB:3HSI}. FT STRAND 129 132 {ECO:0000244|PDB:3HSI}. FT HELIX 133 135 {ECO:0000244|PDB:3HSI}. FT STRAND 142 145 {ECO:0000244|PDB:3HSI}. FT STRAND 148 153 {ECO:0000244|PDB:3HSI}. FT TURN 158 162 {ECO:0000244|PDB:3HSI}. FT STRAND 172 176 {ECO:0000244|PDB:3HSI}. FT HELIX 178 190 {ECO:0000244|PDB:3HSI}. FT TURN 195 197 {ECO:0000244|PDB:3HSI}. FT STRAND 199 204 {ECO:0000244|PDB:3HSI}. FT HELIX 209 211 {ECO:0000244|PDB:3HSI}. FT HELIX 213 226 {ECO:0000244|PDB:3HSI}. FT STRAND 235 237 {ECO:0000244|PDB:3HSI}. FT STRAND 242 253 {ECO:0000244|PDB:3HSI}. FT HELIX 255 265 {ECO:0000244|PDB:3HSI}. FT STRAND 268 274 {ECO:0000244|PDB:3HSI}. FT STRAND 276 278 {ECO:0000244|PDB:3HSI}. FT HELIX 282 292 {ECO:0000244|PDB:3HSI}. FT TURN 293 295 {ECO:0000244|PDB:3HSI}. FT STRAND 297 303 {ECO:0000244|PDB:3HSI}. FT HELIX 305 307 {ECO:0000244|PDB:3HSI}. FT HELIX 320 323 {ECO:0000244|PDB:3HSI}. FT HELIX 324 338 {ECO:0000244|PDB:3HSI}. FT HELIX 340 345 {ECO:0000244|PDB:3HSI}. FT STRAND 346 353 {ECO:0000244|PDB:3HSI}. FT STRAND 358 360 {ECO:0000244|PDB:3HSI}. FT STRAND 364 367 {ECO:0000244|PDB:3HSI}. FT TURN 368 370 {ECO:0000244|PDB:3HSI}. FT STRAND 371 375 {ECO:0000244|PDB:3HSI}. FT HELIX 381 385 {ECO:0000244|PDB:3HSI}. FT STRAND 388 395 {ECO:0000244|PDB:3HSI}. FT HELIX 402 413 {ECO:0000244|PDB:3HSI}. FT STRAND 416 418 {ECO:0000244|PDB:3HSI}. FT HELIX 422 424 {ECO:0000244|PDB:3HSI}. FT HELIX 428 430 {ECO:0000244|PDB:3HSI}. FT HELIX 433 444 {ECO:0000244|PDB:3HSI}. FT HELIX 447 454 {ECO:0000244|PDB:3HSI}. SQ SEQUENCE 455 AA; 53080 MW; 255CA66C1C45B9EB CRC64; MLINKTKRAE QNLNNLPFLA LQAEQIEFLG SSAEFKTQII ELIRNAKKRI YVTALYWQKD EAGQEILDEI YRVKQENPHL DVKVLIDWHR AQRNLLGAEK SATNADWYCE QRQTYQLPDD PNMFFGVPIN TREVFGVLHV KGFVFDDTVL YSGASINNVY LHQFEKYRYD RYQKITHAEL ADSMVNFIND YLLDFSAVYP LDVTNRPRTK EIRGNIRAYR KDLAQNGEYS LKSAVKLPNV LSVSPLFGLG ASGNELNQVI EDLFLQVQKK LVICTPYFNF PRTLQHKIAT LLENGKRVEI IVGDKVANDF YIPPEQPFKM AGALPYLYES NLRRFCEKFE TQIESGQLVV RLWRDGDNTY HLKGVWVDDR YILLTGNNLN PRAWRLDAEN GLLIYDPQQQ LLAQVEKEQN QIRQHTKVLK HYTELEELNQ YPEPVQKLLK KFARIKADKL VKMIL // ID PSTA_HAEIN Reviewed; 282 AA. AC P45190; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Phosphate transport system permease protein PstA; GN Name=pstA; OrderedLocusNames=HI_1381; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for phosphate; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC23026.1; -; Genomic_DNA. DR PIR; G64120; G64120. DR RefSeq; NP_439533.1; NC_000907.1. DR RefSeq; WP_005650601.1; NC_000907.1. DR ProteinModelPortal; P45190; -. DR STRING; 71421.HI1381; -. DR EnsemblBacteria; AAC23026; AAC23026; HI_1381. DR GeneID; 950294; -. DR KEGG; hin:HI1381; -. DR PATRIC; 20191453; VBIHaeInf48452_1437. DR eggNOG; ENOG4105E2Z; Bacteria. DR eggNOG; COG0581; LUCA. DR KO; K02038; -. DR OMA; MAGTFVM; -. DR OrthoDB; EOG6TJ81W; -. DR PhylomeDB; P45190; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005672; Phosphate_PstA. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR00974; 3a0107s02c; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Phosphate transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 282 Phosphate transport system permease FT protein PstA. FT /FTId=PRO_0000060194. FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 71 91 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 111 131 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 198 218 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 254 274 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 71 274 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 282 AA; 31194 MW; 16D9907FB1256112 CRC64; MKTNQNLRFY WRKTHNKLML GLSYISVIIG LFWLCWILFT LITKGIPALS IDLFTQSTPA PNEKGGLLNA LIGSFFIVGA GTLIGTPIGV LAGTYLAEYG RYSRFAQITR FLNDILLSAP SIIIGLFVYS LYVSKIEHFS GWAGAFALAL LLIPIVVRTT DNMLLLVPNN LREAAAALGC SQWQVIMMIC YRAAKSGILT GVLLAVARIS GETAPLLFTA LSNQFLSWNM NEPIANLPVV IYQYAASPFT DWNNLAWAGA ALITLFVLCL NIFTRLFFQH KK // ID PT1_HAEIN Reviewed; 575 AA. AC P43922; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 110. DE RecName: Full=Phosphoenolpyruvate-protein phosphotransferase; DE EC=2.7.3.9; DE AltName: Full=Phosphotransferase system, enzyme I; GN Name=ptsI; OrderedLocusNames=HI_1712; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23357.1; -; Genomic_DNA. DR PIR; H64137; H64137. DR RefSeq; NP_439854.1; NC_000907.1. DR RefSeq; WP_005649967.1; NC_000907.1. DR ProteinModelPortal; P43922; -. DR SMR; P43922; 2-573. DR STRING; 71421.HI1712; -. DR PRIDE; P43922; -. DR EnsemblBacteria; AAC23357; AAC23357; HI_1712. DR GeneID; 950872; -. DR KEGG; hin:HI1712; -. DR PATRIC; 20192175; VBIHaeInf48452_1791. DR eggNOG; ENOG4105BZ3; Bacteria. DR eggNOG; COG1080; LUCA. DR KO; K08483; -. DR OMA; DYVLGFA; -. DR OrthoDB; EOG657JBQ; -. DR PhylomeDB; P43922; -. DR Proteomes; UP000000579; 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 1 575 Phosphoenolpyruvate-protein FT phosphotransferase. FT /FTId=PRO_0000147069. FT ACT_SITE 189 189 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 502 502 Proton donor. {ECO:0000250}. FT METAL 431 431 Magnesium. {ECO:0000250}. FT METAL 455 455 Magnesium. {ECO:0000250}. FT BINDING 296 296 Substrate. {ECO:0000250}. FT BINDING 332 332 Substrate. {ECO:0000250}. FT BINDING 431 431 Substrate. {ECO:0000250}. FT BINDING 452 452 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 453 453 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 454 454 Substrate. {ECO:0000250}. FT BINDING 455 455 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 575 AA; 63691 MW; DAC2B7909C38CE73 CRC64; MISGILASPG IAFGKALVLK EEKIVLDTQK ITDDQIDAEV ARFYEGRNAA VEQLNSIRER ALISLGEEKA AIFEGHLMIL EDEELEEEIL DYLRSNKVNA GVAASKILDQ QVTMLSEIDD EYLKERAGDI RDIANRLVKN ILGMYIVDLG DIQEESILVA YDLTPSETAQ LNLEKVLGVV TDIGGRTSHT SIMARSLELP AIVGTNKVTK LVNTGDYLIL DAINNQVYIN PTASQIDELK ALEAKISEEK AELAKLKDLP AITLDGHKVD VVANIGTIRD CDGAERNGAE GIGLYRTEFL FMDREQLPTE EEQFIAYKQV VEAMNGRLTV IRTMDIGGDK ELSYLDLPKE MNPFLGWRAI RIALDRREIL NAQLRAVLRA SAFGKLAVMF PMIISVEEIR ELKAVIETLK AELREEGRLF DNNIQVGVMV ETPSAAVNAK FLAKEVDFFS IGTNDLTQYT LAVDRGNEFI SHLYNPMHPS VLGLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISV PRIKKLIRNV NFQDAKVLAD TALQKPTAAE IDQLIEEFLL ENSLN // ID PROQ_HAEIN Reviewed; 197 AA. AC P44286; O05079; Q57119; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-FEB-2004, sequence version 3. DT 13-APR-2016, entry version 96. DE RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749}; GN Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749}; GN OrderedLocusNames=HI_1669/HI_1670; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: RNA chaperone with significant RNA binding, RNA strand CC exchange and RNA duplexing activities. {ECO:0000255|HAMAP- CC Rule:MF_00749}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00749}. CC -!- SIMILARITY: Belongs to the ProQ family. {ECO:0000255|HAMAP- CC Rule:MF_00749}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23315.1; Type=Frameshift; Positions=116; Note=Produces two separate ORFs.; 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; L42023; AAC23323.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC23315.1; ALT_FRAME; Genomic_DNA. DR PIR; G64135; G64135. DR PIR; H64039; H64039. DR RefSeq; NP_439812.1; NC_000907.1. DR ProteinModelPortal; P44286; -. DR STRING; 71421.HI1670; -. DR EnsemblBacteria; AAC23315; AAC23315; HI_1669. DR EnsemblBacteria; AAC23323; AAC23323; HI_1670. DR GeneID; 950501; -. DR KEGG; hin:HI1670; -. DR PATRIC; 20192089; VBIHaeInf48452_1748. DR eggNOG; ENOG41073DY; Bacteria. DR eggNOG; COG3109; LUCA. DR KO; K03607; -. DR OrthoDB; EOG6T1WWT; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033592; F:RNA strand annealing activity; IEA:UniProtKB-HAMAP. DR GO; GO:0034057; F:RNA strand-exchange activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010608; P:posttranscriptional regulation of gene expression; IEA:InterPro. DR Gene3D; 1.10.1710.10; -; 1. DR HAMAP; MF_00749; ProQ; 1. DR InterPro; IPR023529; ProQ. DR InterPro; IPR016103; ProQ/FinO. DR Pfam; PF04352; ProQ; 1. DR SMART; SM00945; ProQ; 1. DR SUPFAM; SSF48657; SSF48657; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome; KW RNA-binding. FT CHAIN 1 197 RNA chaperone ProQ. FT /FTId=PRO_0000214618. SQ SEQUENCE 197 AA; 21729 MW; 4B8DE7A74130B36C CRC64; MQTEVQKLTN AKAIITYLAE KFPLCFVLEG EAKPLKIGLF QDLAEALQDD ERVSKTQLRQ ALRQYTSNWR YLYGCREGAV RVDLQGNPAG VLDAEHVAHA AQQLAEAKAR FAEKRAAAKK AQQKKHPRKP ANKNLKKESK LSLSAVDFSQ ISVGSVVKVK AGDNAKKATV VEVLKDSARV ELENGLIMNV AADRLFA // ID PTGA_HAEIN Reviewed; 166 AA. AC P45338; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 108. DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component; DE EC=2.7.1.-; DE AltName: Full=EIIA-Glc; DE AltName: Full=EIII-Glc; DE AltName: Full=PTS system glucose-specific EIIA component; GN Name=crr; OrderedLocusNames=HI_1711; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 2-10. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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 (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine + CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L- CC histidine/cysteine. {ECO:0000255|PROSITE-ProRule:PRU00416}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23356.1; -; Genomic_DNA. DR PIR; G64137; G64137. DR RefSeq; NP_439853.1; NC_000907.1. DR RefSeq; WP_010869278.1; NC_000907.1. DR ProteinModelPortal; P45338; -. DR SMR; P45338; 2-166. DR STRING; 71421.HI1711; -. DR EnsemblBacteria; AAC23356; AAC23356; HI_1711. DR GeneID; 950531; -. DR KEGG; hin:HI1711; -. DR PATRIC; 20192173; VBIHaeInf48452_1790. DR eggNOG; ENOG4105C5Y; Bacteria. DR eggNOG; COG2190; LUCA. DR KO; K02777; -. DR OMA; KDSTVMV; -. DR OrthoDB; EOG6ND0GQ; -. DR PhylomeDB; P45338; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central. DR GO; GO:0034219; P:carbohydrate transmembrane transport; IBA:GO_Central. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central. DR GO; GO:0043610; P:regulation of carbohydrate utilization; IBA:GO_Central. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR001127; PTS_EIIA_1_perm. DR Pfam; PF00358; PTS_EIIA_1; 1. DR SUPFAM; SSF51261; SSF51261; 1. DR TIGRFAMs; TIGR00830; PTBA; 1. DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1. DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10675023}. FT CHAIN 2 166 Glucose-specific phosphotransferase FT enzyme IIA component. FT /FTId=PRO_0000186541. FT DOMAIN 36 140 PTS EIIA type-1. {ECO:0000255|PROSITE- FT ProRule:PRU00416}. FT ACT_SITE 88 88 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT SITE 73 73 Important for phospho-donor activity. FT {ECO:0000250}. SQ SEQUENCE 166 AA; 17911 MW; 2347E5FB81EC9DB8 CRC64; MGLFDKLFGS KENKSVEVEI YARISGEIVN IEDVPDVVFS EKIVGDGVAV RPIGNKIVAP VDGVIGKIFE TNHAFSMESK EGVELFVHFG IDTVELKGEG FTRIAQEGQS VKRGDTVIEF DLALLESKAK SVLTPIVISN MDEISCIVKK SGEVVAGESV VLALKK // ID PUR4_HAEIN Reviewed; 1297 AA. AC P43847; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 123. DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; GN OrderedLocusNames=HI_0752; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in CC the purines biosynthetic pathway. Catalyzes the ATP-dependent CC conversion of formylglycinamide ribonucleotide (FGAR) and CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00419}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS CC family. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22411.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22411.1; ALT_INIT; Genomic_DNA. DR PIR; H64090; H64090. DR RefSeq; NP_438911.1; NC_000907.1. DR ProteinModelPortal; P43847; -. DR STRING; 71421.HI0752; -. DR PRIDE; P43847; -. DR EnsemblBacteria; AAC22411; AAC22411; HI_0752. DR GeneID; 949775; -. DR KEGG; hin:HI0752; -. DR PATRIC; 20190149; VBIHaeInf48452_0790. DR eggNOG; ENOG4107QIK; Bacteria. DR eggNOG; COG0046; LUCA. DR eggNOG; COG0047; LUCA. DR KO; K01952; -. DR OMA; LSANWMW; -. DR OrthoDB; EOG6FNHHR; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.1330.10; -; 2. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00419; PurL_1; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010073; PRibForGlyAmidine_synth. DR InterPro; IPR016188; PurM-like_N. DR Pfam; PF02769; AIRS_C; 2. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF56042; SSF56042; 2. DR TIGRFAMs; TIGR01735; FGAM_synt; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 1297 Phosphoribosylformylglycinamidine FT synthase. FT /FTId=PRO_0000100409. FT DOMAIN 1045 1297 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00419}. FT NP_BIND 308 319 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1138 1138 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT ACT_SITE 1263 1263 {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1265 1265 {ECO:0000255|HAMAP-Rule:MF_00419}. FT METAL 680 680 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 719 719 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 723 723 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 887 887 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT BINDING 889 889 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. SQ SEQUENCE 1297 AA; 142747 MW; DCD23A9DA666E393 CRC64; MTVKTFRGSP ALSEFRLTQL QQKCQQYQLP ITSVYAEYLH FVEQKTSLVE DEIVKLQALL HYGSMFSELK PAGYCLIVTP RVGTISSWSS KATDIAHNCG LSKVNRIERG IAYYFNIERD LTEAELATLK DLLHDRMLET VLNHETEAAL LFTQQEPKAL TTIDILNGGR QALEQANIAL GLALADDEMD YLVESFTALK RNPQDVELYM FAQANSEHCR HKIFNADWII DGKKQDKSLF KMIKNTFEQT PDFVLSAYKD NAAVMEGSKV GRWFPDPDGQ YRVHQEDVHI LMKVETHNHP TAISPFPGAA TGSGGEIRDE GATGRGAKPK AGLTGFSVSN LVIPNFEQPW ENPLSKPNRI ASALDIMIDA PLGSAAFNNE FGRPALLGYF RTYEEKVNSF AGKEVRGYHK PIMLAGGIGN IRGEQVQKGE IPIGAKLIVL GGAAMNIGLG GGAASSMDSG KSKEDLDFAS VQRENPEMER RCQEVIDRCW QLGEENPILF IHDVGAGGLS NAMPELVHDG KRGGKFDLRS ILCDEKGMSP LEIWCNESQE RYVLAVAPEN LELFTALCER ERAPFAVIGE ATQAEHLILH DSHFDNNPID LPMNVLLGKT PKMTREVLSK TVENQSLKIE SIQLKEAFHR VLRLPVVAEK TFLITIGDRS VTGMVARDQM VGPWQIPVSD VAVTTASLDS YHGEAMAIGE RSPVALLDFS ASARLAVAEA ITNIAGTLIG EMKRIKLSAN WMSAAGHTGE DAGLYEAVKA VGEELCPALG LTIPVGKDSM SMKTTWIDNG EQKSVTAPLS LVISAFARVE DVRKTLTPQL RTDKGFSSLL LIDLGEGHNR LGATALAQVY KQLGDKPADV VKVQRLKDFY NAMQTLVAED KLLAYHDRSD GGLITTLAEM AFAGHCGVEV DISALGDNDL AVLFNEELGA VIQVADSQLE SVREVLKAHN LLGIIHQLGT VTADDRFEIS RGSHKLFSEK RSELRSIWAE LTYQMQRLRD NPECAEQEFE AKKNPDDKGL SAFLTYDVNE DITAPFINKG VKPTIAILRE QGVNSHYEMA AAFDRAGFNA IDVHMSDLMI GRRNLAEFNA MVACGGFSYG DVLGAGGGWA KSILFNPKLH EQFSQFFINP NTLTLGVCNG CQMISNLAEI IPGTENWPHF VRNKSERFEA RVSLVKINEV DSVWFAGMAG SHMPIAVSHG EGQVKFKSVE QFAGLKAQGI IAAQYIDNNG SPTELYPANP NGSSEGITAI TNLDGRVAIM MPHPERVFRA VSNSWHPENW TEDGAWMRLF RNARMVF // ID PTFBC_HAEIN Reviewed; 556 AA. AC P44714; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 113. DE RecName: Full=PTS system fructose-specific EIIBC component; DE AltName: Full=EIIBC-Fru; 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=HI_0446; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 inner membrane {ECO:0000255|PROSITE- CC ProRule:PRU00427}; Multi-pass membrane protein CC {ECO:0000255|PROSITE-ProRule:PRU00427}. 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 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; L42023; AAC22105.1; -; Genomic_DNA. DR PIR; I64068; I64068. DR RefSeq; NP_438607.1; NC_000907.1. DR RefSeq; WP_005693715.1; NC_000907.1. DR ProteinModelPortal; P44714; -. DR STRING; 71421.HI0446; -. DR EnsemblBacteria; AAC22105; AAC22105; HI_0446. DR GeneID; 949670; -. DR KEGG; hin:HI0446; -. DR PATRIC; 20189447; VBIHaeInf48452_0466. DR eggNOG; ENOG4105DM4; Bacteria. DR eggNOG; COG1299; LUCA. DR eggNOG; COG1445; LUCA. DR eggNOG; COG3925; LUCA. DR KO; K02769; -. DR KO; K02770; -. DR OMA; IPFVSEP; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P44714; -. DR Proteomes; UP000000579; 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 InterPro; IPR013011; PTS_EIIB_2. DR InterPro; IPR003501; PTS_EIIB_2/3. DR InterPro; IPR013014; PTS_EIIC_2. DR InterPro; IPR003353; PTS_IIB_fruc. DR InterPro; IPR006327; PTS_IIC_fruc. DR Pfam; PF02302; PTS_IIB; 1. DR SUPFAM; SSF52794; SSF52794; 1. DR TIGRFAMs; TIGR00829; FRU; 1. DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1. DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1. DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Kinase; KW Membrane; Phosphotransferase system; Reference proteome; Repeat; KW Sugar transport; Transferase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 556 PTS system fructose-specific EIIBC FT component. FT /FTId=PRO_0000186509. FT TRANSMEM 237 257 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 275 295 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 302 322 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 324 344 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 349 369 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 390 410 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 431 451 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 468 488 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 490 510 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT TRANSMEM 529 549 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT DOMAIN 106 201 PTS EIIB type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00422}. FT DOMAIN 224 556 PTS EIIC type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00427}. FT ACT_SITE 112 112 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000250}. SQ SEQUENCE 556 AA; 57706 MW; 31D8E77BFDBA7E42 CRC64; MKLFLTQSAN VGDVKAYLLH EVFRAAAQKA NVSIVGTPAE ADLVLVFGSV LPNNPDLVGK KVFIIGEAIA MISPEVTLAN ALANGADYVA PKSAVSFTGV SGVKNIVAVT ACPTGVAHTF MSAEAIEAYA KKQGWNVKVE TRGQVGAGNE ITVEEVAAAD LVFVAADIDV PLDKFKGKPM YRTSTGLALK KTEQEFDKAF KEAKIFDGGN NAGTKEESRE KKGVYKHLMT GVSHMLPLVV AGGLLIAISF MFSFNVIENT GVFQDLPNML INIGSGVAFK LMIAVFAGYV AFSIADRPGL AVGLIAGMLA SEAGAGILGG IIAGFLAGYV VKGLNVIIRL PASLTSLKPI LILPLLGSMI VGLTMIYLIN PPVAEIMKEL SNWLTSMGEV NAIVLGAIIG AMMCIDMGGP VNKAAYTFSV GLIASQVYTP MAAAMAAGMV PPIGMTVATW IARNKFTVSQ CDAGKASFVL GLCFISEGAL PFVAADPIRV IISSVIGGAV AGAISMGLNI TLQAPHGGLF VIPFVSEPLK YLGAIAIGAL STGVVYAIIK SKNNAE // ID PUR5_HAEIN Reviewed; 344 AA. AC P43848; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; DE EC=6.3.3.1; DE AltName: Full=AIR synthase; DE AltName: Full=AIRS; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; GN Name=purM; OrderedLocusNames=HI_1429; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AIR 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; L42023; AAC23076.1; -; Genomic_DNA. DR PIR; G64122; G64122. DR RefSeq; NP_439578.1; NC_000907.1. DR RefSeq; WP_005693936.1; NC_000907.1. DR ProteinModelPortal; P43848; -. DR SMR; P43848; 4-344. DR STRING; 71421.HI1429; -. DR EnsemblBacteria; AAC23076; AAC23076; HI_1429. DR GeneID; 950335; -. DR KEGG; hin:HI1429; -. DR PATRIC; 20191553; VBIHaeInf48452_1486. DR eggNOG; ENOG4105CXB; Bacteria. DR eggNOG; COG0150; LUCA. DR KO; K01933; -. DR OMA; NHCVNDI; -. DR OrthoDB; EOG61CM1V; -. DR PhylomeDB; P43848; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR004733; PurM_cligase. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00878; purM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 344 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_0000148215. SQ SEQUENCE 344 AA; 37066 MW; 06EF6784D42A3936 CRC64; MSNTQLSYKD AGVDIHTGNE LVERIKGDVK RTRRSEVMGG LGGFGALCAL PTKYKEPILV SGTDGVGTKL RLAIDLKKHD TIGQDLVAMC VNDLIVQGAE PLFFLDYYAT GKLDVDVAAS VIKGIADGCE MSGCALVGGE TAEMPGMYHE GDYDLAGFCV GVVEKSEIID GTAVKTGDTL IALGSSGAHS NGYSLIRKVL EVSGANPTDL LEGKPLSEHL LAPTKIYVKS ILQLIKQTEV HAIAHLTGGG FWENIPRVLP DNTKAVIDES SWQWPAIFNW LQEKGNISRY EMYRTFNCGV GMVIALPEKE VETALALLEQ SGEKAWVIGK IEHLGESEAQ VEIQ // ID PUR9_HAEIN Reviewed; 532 AA. AC P43852; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Bifunctional purine biosynthesis protein PurH; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase; DE EC=2.1.2.3; DE AltName: Full=AICAR transformylase; DE Includes: DE RecName: Full=IMP cyclohydrolase; DE EC=3.5.4.10; DE AltName: Full=ATIC; DE AltName: Full=IMP synthase; DE AltName: Full=Inosinicase; GN Name=purH; OrderedLocusNames=HI_0887; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl CC THF route): step 1/1. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22544.1; -; Genomic_DNA. DR PIR; B64100; B64100. DR RefSeq; NP_439048.1; NC_000907.1. DR RefSeq; WP_005693238.1; NC_000907.1. DR ProteinModelPortal; P43852; -. DR STRING; 71421.HI0887; -. DR PRIDE; P43852; -. DR EnsemblBacteria; AAC22544; AAC22544; HI_0887. DR GeneID; 949891; -. DR KEGG; hin:HI0887; -. DR PATRIC; 20190431; VBIHaeInf48452_0929. DR eggNOG; ENOG4105DC1; Bacteria. DR eggNOG; COG0138; LUCA. DR KO; K00602; -. DR OMA; PCGVAEG; -. DR OrthoDB; EOG6QCDFF; -. DR PhylomeDB; P43852; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dom. DR InterPro; IPR002695; AICARFT_IMPCHas. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR PANTHER; PTHR11692; PTHR11692; 2. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00355; purH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Multifunctional enzyme; KW Purine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 532 Bifunctional purine biosynthesis protein FT PurH. FT /FTId=PRO_0000192095. SQ SEQUENCE 532 AA; 58350 MW; 9DE1E241DD238E87 CRC64; MADRPIRQAL LSVSDKTGIV EFAQGLVKRG VKLLSTGGTA KLLAQNALPV IEVSDYTGFP EMMDGRVKTL HPKVHGGILG RRGTDDAIMQ QHGIEGIDMV VVNLYPFAAT VAKPDCTLAD AVENIDIGGP TMVRSAAKNH KDVAIVVNNH DFNAILAEMD QHQNSLTFET RFDLAIKAFE HTAQYDSMIA NYFGQLVKPY HIAEEEEANA KCGQFPRTLN LNFVRKQAMR YGENSHQNAA FYVDLNVKEA SVATANQLQG KALSYNNIAD TDAALECVKE FDDPACVIVK HANPCGVALG KDILDAYNRA YQTDPTSAFG GIIAFNRELD EKTANEIVER QFVEVIIAPK VSAEAQEVMK RKKNVRLLEC GEWTSRSERL DFKRVNGGLL VQDADLGMVG VDDLKVVSKR QPTEQELKDL LFCWKVAKFV KSNAIVYAKD NQTIGIGAGQ MSRVYSAKIA GIKAQDEGLE VAGCVMASDA FFPFRDGIDA AAKVGIQCVI HPGGSMRDQE VIDAADEHNM VMVLTGMRHF RH // ID PTFAH_HAEIN Reviewed; 499 AA. AC P44715; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 124. DE RecName: Full=Multiphosphoryl transfer protein; DE Short=MTP; DE AltName: Full=Fructose PTS diphosphoryl transfer protein; DE AltName: Full=Phosphotransferase FPr protein; DE AltName: Full=Pseudo-HPr; DE Includes: DE RecName: Full=Phosphocarrier protein HPr; DE Short=Protein H; DE Includes: DE RecName: Full=Fructose-specific phosphotransferase enzyme IIA component; DE EC=2.7.1.-; DE AltName: Full=EIIA-Fru; DE AltName: Full=EIII-Fru; DE AltName: Full=PTS system fructose-specific EIIA component; GN Name=fruB; OrderedLocusNames=HI_0448; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP DOMAIN STRUCTURE. RX PubMed=8763608; DOI=10.1016/0923-2508(96)81381-7; RA Reizer J., Reizer A., Saier M.H. Jr.; RT "Novel PTS proteins revealed by bacterial genome sequencing: a unique RT fructose-specific phosphoryl transfer protein with two HPr-like RT domains in Haemophilus influenzae."; RL Res. Microbiol. 147:209-215(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 (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine + CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L- CC histidine/cysteine. {ECO:0000255|PROSITE-ProRule:PRU00417}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: In contrast to classical PTS systems, the fructose PTS has CC no requirement for HPr; FPr combines a IIA domain with two HPr CC domains. {ECO:0000269|PubMed:8763608}. 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. {ECO:0000255|PROSITE-ProRule:PRU00417, CC ECO:0000269|PubMed:8763608}. CC -!- SIMILARITY: Contains 2 HPr domains. {ECO:0000255|PROSITE- CC ProRule:PRU00681}. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22107.1; -; Genomic_DNA. DR PIR; B64069; B64069. DR RefSeq; NP_438609.1; NC_000907.1. DR RefSeq; WP_005693713.1; NC_000907.1. DR ProteinModelPortal; P44715; -. DR STRING; 71421.HI0448; -. DR DNASU; 950651; -. DR EnsemblBacteria; AAC22107; AAC22107; HI_0448. DR GeneID; 950651; -. DR KEGG; hin:HI0448; -. DR PATRIC; 20189451; VBIHaeInf48452_0468. DR eggNOG; ENOG4105DTZ; Bacteria. DR eggNOG; COG1925; LUCA. DR eggNOG; COG4668; LUCA. DR KO; K02768; -. DR KO; K11183; -. DR OMA; QGIEWGE; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P44715; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW. DR Gene3D; 3.30.1340.10; -; 2. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR016258; FruB. DR InterPro; IPR000032; HPr_prot-like. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR InterPro; IPR002178; PTS_EIIA_type-2_dom. DR InterPro; IPR001020; PTS_HPr_His_P_site. DR InterPro; IPR002114; PTS_HPr_Ser_P_site. DR Pfam; PF00381; PTS-HPr; 2. DR Pfam; PF00359; PTS_EIIA_2; 1. DR PIRSF; PIRSF000690; Fruc_PTS_diPryltransf; 1. DR PRINTS; PR00107; PHOSPHOCPHPR. DR SUPFAM; SSF55594; SSF55594; 2. DR SUPFAM; SSF55804; SSF55804; 2. DR TIGRFAMs; TIGR01003; PTS_HPr_family; 2. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1. DR PROSITE; PS51350; PTS_HPR_DOM; 2. DR PROSITE; PS00369; PTS_HPR_HIS; 2. DR PROSITE; PS00589; PTS_HPR_SER; 2. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Phosphotransferase system; KW Reference proteome; Repeat; Sugar transport; Transferase; Transport. FT CHAIN 1 499 Multiphosphoryl transfer protein. FT /FTId=PRO_0000186520. FT DOMAIN 2 142 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT DOMAIN 286 376 HPr 1. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT DOMAIN 410 499 HPr 2. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT REGION 155 285 M domain. FT REGION 378 409 Linker. FT ACT_SITE 62 62 Tele-phosphohistidine intermediate; for FT EIIA activity. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. FT ACT_SITE 300 300 Pros-phosphohistidine intermediate; for FT HPr activity. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT ACT_SITE 424 424 Pros-phosphohistidine intermediate; for FT HPr activity. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. SQ SEQUENCE 499 AA; 53007 MW; D6DDC99884A58C63 CRC64; MLELSESNIH LNANAIDKQQ AIEMAVSALV QAGNVENGYL QGMLARELQT STFLGNGIAI PHGTLDTRLM VKKTGVQVFQ FPQGIEWGEG NIAYVVIGIA ARSDEHLSLL RQLTHVLSDE DTAAKLAKIT DVAEFCAILM GETIDPFEIP AANISLDVNT QSLLTLVAIN AGQLQVQSAV ENRFISEVIN NAALPLGKGL WVTDSVVGNV KNALAFSRAK TIFSHNGKAV KGVITVSAVG DQINPTLVRL LDDDVQTTLL NGNSTEILTA LLGSSSDVET QSVEGAVVGT FTIRNEHGLH ARPSANLVNE VKKFTSKITM QNLTRESEVV SAKSLMKIVA LGVTQGHRLR FVAEGEDAKQ AIESLGKAIA NGLGENVSAV PPSEPDTIEI MGDQIHTPAV TEDDNLPANA IEAVFVIKNE QGLHARPSAI LVNEVKKYNA SVAVQNLDRN SQLVSAKSLM KIVALGVVKG TRLRFVATGE EAQQAIDGIG AVIESGLGE // ID PUR1_HAEIN Reviewed; 505 AA. AC P43854; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 116. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931}; GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; GN OrderedLocusNames=HI_1207; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate + CC L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate CC + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01931}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC purine/pyrimidine phosphoribosyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22861.1; -; Genomic_DNA. DR PIR; I64189; I64189. DR RefSeq; NP_439363.1; NC_000907.1. DR RefSeq; WP_005694238.1; NC_000907.1. DR ProteinModelPortal; P43854; -. DR SMR; P43854; 2-489. DR STRING; 71421.HI1207; -. DR MEROPS; C44.001; -. DR PRIDE; P43854; -. DR EnsemblBacteria; AAC22861; AAC22861; HI_1207. DR GeneID; 950171; -. DR KEGG; hin:HI1207; -. DR PATRIC; 20191093; VBIHaeInf48452_1259. DR eggNOG; ENOG4105CBA; Bacteria. DR eggNOG; COG0034; LUCA. DR KO; K00764; -. DR OMA; AARVHMG; -. DR OrthoDB; EOG6KT2Q1; -. DR PhylomeDB; P43854; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_01931; PurF; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005854; PurF. DR Pfam; PF00156; Pribosyltran; 1. DR PIRSF; PIRSF000485; Amd_phspho_trans; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01134; purF; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Glycosyltransferase; KW Magnesium; Metal-binding; Purine biosynthesis; Reference proteome; KW Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 505 Amidophosphoribosyltransferase. FT /FTId=PRO_0000139639. FT DOMAIN 2 235 Glutamine amidotransferase type-2. FT {ECO:0000255|HAMAP-Rule:MF_01931}. FT ACT_SITE 2 2 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 306 306 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 368 368 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 369 369 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. SQ SEQUENCE 505 AA; 56206 MW; CD665BB22EB88E22 CRC64; MCGIVGIVSQ SPVNESIYAA LTLLQHRGQD AAGIVTVDDE NRFRLRKANG LVSDVFHQEH MLRLQGNAGL GHVRYPTAGS SSVSEAQPFY VNSPYGVTLV HNGNLTNSVE LKEKVFKTAR RHVNTNSDSE LLLNILANHL DHIPQDHLDP QDIFYAVRKT HKDVRGAYAC LAMIIGHGMV AFRDPFGIRP LVLGKREENG KTDYMFASET VALDIVGFEF VRDIAAGEAV YVTFDGELYS QQCAESAVLN PCIFEYVYFA RPDSTIDGVS VYAARVHMGE KLGQKIAKEW ADEIDNIDVV IPVPETSTDI ALQIARVLGK PYRQGFVKNR YVGRTFIMPG QAQRISSVRR KLNTIKAEFK DKNVLLVDDS IVRGTTSEQI VEMARSAGAK KIYFASAAPE IRYPNVYGID MPSRDELIAY GRNVDEIAEL IGVDKLIFQD LTALTESVQL ENPAIQGFDC SVFTGEYITG DISPEYLEKI ATQRNDNAKK KREKQASNLE IYNEQ // ID PUR3_HAEIN Reviewed; 212 AA. AC P43846; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01930}; DE EC=2.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01930}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000255|HAMAP-Rule:MF_01930}; DE AltName: Full=GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01930}; DE Short=GART {ECO:0000255|HAMAP-Rule:MF_01930}; GN Name=purN {ECO:0000255|HAMAP-Rule:MF_01930}; GN OrderedLocusNames=HI_1428; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10- CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and CC tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + N(1)-(5-phospho-D- CC ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide. {ECO:0000255|HAMAP-Rule:MF_01930}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5- CC phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000255|HAMAP- CC Rule:MF_01930}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23075.1; -; Genomic_DNA. DR PIR; F64122; F64122. DR RefSeq; NP_439577.1; NC_000907.1. DR RefSeq; WP_005693938.1; NC_000907.1. DR ProteinModelPortal; P43846; -. DR SMR; P43846; 3-210. DR STRING; 71421.HI1428; -. DR EnsemblBacteria; AAC23075; AAC23075; HI_1428. DR GeneID; 950331; -. DR KEGG; hin:HI1428; -. DR PATRIC; 20191551; VBIHaeInf48452_1485. DR eggNOG; ENOG4108V3E; Bacteria. DR eggNOG; COG0299; LUCA. DR KO; K11175; -. DR OMA; GDSEHGT; -. DR OrthoDB; EOG615VP4; -. DR PhylomeDB; P43846; -. DR UniPathway; UPA00074; UER00126. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR004607; PurN_trans. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW Complete proteome; Purine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 212 Phosphoribosylglycinamide FT formyltransferase. FT /FTId=PRO_0000074944. FT REGION 12 14 5'-phosphoribosylglycinamide binding. FT {ECO:0000255|HAMAP-Rule:MF_01930}. FT REGION 90 93 10-formyltetrahydrofolate binding. FT {ECO:0000255|HAMAP-Rule:MF_01930}. FT ACT_SITE 109 109 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01930}. FT BINDING 107 107 10-formyltetrahydrofolate. FT {ECO:0000255|HAMAP-Rule:MF_01930}. FT SITE 145 145 Raises pKa of active site His. FT {ECO:0000255|HAMAP-Rule:MF_01930}. SQ SEQUENCE 212 AA; 23463 MW; D1AE249CDDB879C4 CRC64; MKKIAVLISG QGTNLQTIID ACHSGDIPAK IACVISNKAD AYGLVRAKQA QIPQAVFLRK NFSNNLEMDD AIGDYLQSLA VDLIVLAGYM KILTPKFTQR FAGKILNIHP SLLPKYAGLN TYQRAIEAGD NEHGTTVHFV NEEVDGGAIV LQAKVPIFPE DSIEEVEART REQEYQIYPL VIKWFTEGRL RLKDNLAYLD GKALPKSGYA NE // ID PTSN_HAEIN Reviewed; 164 AA. AC P45072; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Nitrogen regulatory protein homolog; DE Includes: DE RecName: Full=Putative phosphotransferase enzyme IIA component; DE EC=2.7.1.-; DE AltName: Full=Putative PTS system EIIA component; GN Name=ptsN; OrderedLocusNames=HI_1147; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Not known; lacks the phosphorylation site found in other CC PtsN proteins. CC -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00417}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22802.1; -; Genomic_DNA. DR PIR; H64167; H64167. DR RefSeq; NP_439305.1; NC_000907.1. DR RefSeq; WP_005693461.1; NC_000907.1. DR ProteinModelPortal; P45072; -. DR STRING; 71421.HI1147; -. DR EnsemblBacteria; AAC22802; AAC22802; HI_1147. DR GeneID; 950111; -. DR KEGG; hin:HI1147; -. DR PATRIC; 20190969; VBIHaeInf48452_1197. DR eggNOG; ENOG4107RM2; Bacteria. DR eggNOG; COG1762; LUCA. DR KO; K02806; -. DR OMA; QSETTFE; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P45072; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase 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; IPR006320; PTS_Nitro_regul. DR Pfam; PF00359; PTS_EIIA_2; 1. DR SUPFAM; SSF55804; SSF55804; 1. DR TIGRFAMs; TIGR01419; nitro_reg_IIA; 1. DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Phosphotransferase system; Reference proteome. FT CHAIN 1 164 Nitrogen regulatory protein homolog. FT /FTId=PRO_0000186698. FT DOMAIN 5 152 PTS EIIA type-2. {ECO:0000255|PROSITE- FT ProRule:PRU00417}. SQ SEQUENCE 164 AA; 18444 MW; A71EBDD5C2738611 CRC64; MKITELLSPE NIRQGVSFSS KKRLFESIAH FVEEQILAEK GEQACFECLF EREKLGNSGL GNGIAMPKAK IPVTVSDKAI AVFMQLDNPI DYDAFDGKPV DLIFALLIPE NQCETYIPVL ASLIEKLTDK NVLKQLRSAK SADEIWQVFE ITDQSETTFE EVKE // ID PUTP_HAEIN Reviewed; 504 AA. AC P45174; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Sodium/proline symporter; DE AltName: Full=Proline permease; GN Name=putP; OrderedLocusNames=HI_1352; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular CC L-proline. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) CC (TC 2.A.21) 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; L42023; AAC22999.1; -; Genomic_DNA. DR PIR; E64118; E64118. DR RefSeq; NP_439503.1; NC_000907.1. DR RefSeq; WP_010869188.1; NC_000907.1. DR STRING; 71421.HI1352; -. DR EnsemblBacteria; AAC22999; AAC22999; HI_1352. DR GeneID; 950133; -. DR KEGG; hin:HI1352; -. DR PATRIC; 20191389; VBIHaeInf48452_1405. DR eggNOG; ENOG4105CK7; Bacteria. DR eggNOG; COG0591; LUCA. DR KO; K11928; -. DR OMA; EYSTALW; -. DR OrthoDB; EOG6HB9QC; -. DR PhylomeDB; P45174; -. DR Proteomes; UP000000579; 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:0005298; F:proline:sodium symporter activity; IEA:InterPro. DR GO; GO:0031402; F:sodium ion binding; IEA:InterPro. DR InterPro; IPR011851; Na/Pro_symporter. DR InterPro; IPR001734; Na/solute_symporter. DR InterPro; IPR018212; Na/solute_symporter_CS. DR PANTHER; PTHR11819; PTHR11819; 1. DR Pfam; PF00474; SSF; 1. DR TIGRFAMs; TIGR02121; Na_Pro_sym; 1. DR TIGRFAMs; TIGR00813; sss; 1. DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1. DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1. DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Ion transport; Membrane; Reference proteome; KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 504 Sodium/proline symporter. FT /FTId=PRO_0000105399. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 127 147 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TRANSMEM 324 344 Helical. {ECO:0000255}. FT TRANSMEM 374 394 Helical. {ECO:0000255}. FT TRANSMEM 405 425 Helical. {ECO:0000255}. FT TRANSMEM 434 454 Helical. {ECO:0000255}. FT TRANSMEM 461 481 Helical. {ECO:0000255}. SQ SEQUENCE 504 AA; 54899 MW; 61ED0A52A142A7F0 CRC64; MFGFDPSLIT FTIYIFGMLL IGVLAYYYTN NLSDYILGGR RLGSFVTAMS AGASDMSGWL LMGLPGAVYL SGLVEGWIAI GLTIGAYFNW LLVAGRLRVY TELNNNALTL PEYFHNRFGS SHKLLKLVSA TIILVFLTIY CASGVVAGAK LFQNIFSVEY STALWYGAAA TIAYTFIGGF LAVSWTDTIQ ATLMIFALIL TPVFVLLSFA DTAQFSAVLE QAEAAVNKDF TDLFTSTTPL GLLSLAAWGL GYFGQPHILA RFMAADSVKS LIKARRISMG WMVLCLAGAI GIGLFAIPYF FANPAIAGTV NREPEQVFIE LAKLLFNPWI AGILLSAILA AVMSTLSAQL LISSSSITED FYKGFIRPNA SEKELVWLGR IMVLVIAALA IWIAQDENSK VLKLVEFAWA GFGSAFGPVV LFSLFWKRMT SSGAMAGMLV GAVTVFAWKE VVPADTDWFK VYEMIPGFAF ASLAIIVISL LSNKPEQDIL NTFDKAEKAY KEAK // ID PSTC_HAEIN Reviewed; 315 AA. AC P45191; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Phosphate transport system permease protein PstC; GN Name=pstC; OrderedLocusNames=HI_1382; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for phosphate; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC23027.1; -; Genomic_DNA. DR PIR; H64120; H64120. DR RefSeq; NP_439534.1; NC_000907.1. DR RefSeq; WP_005656744.1; NC_000907.1. DR STRING; 71421.HI1382; -. DR EnsemblBacteria; AAC23027; AAC23027; HI_1382. DR GeneID; 950295; -. DR KEGG; hin:HI1382; -. DR PATRIC; 20191455; VBIHaeInf48452_1438. DR eggNOG; ENOG4105C8U; Bacteria. DR eggNOG; COG0573; LUCA. DR KO; K02037; -. DR OMA; TAIFITE; -. DR OrthoDB; EOG6TJ81W; -. DR PhylomeDB; P45191; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR011864; Phosphate_PstC. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR02138; phosphate_pstC; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Phosphate transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 315 Phosphate transport system permease FT protein PstC. FT /FTId=PRO_0000060209. FT TOPO_DOM 1 22 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 23 43 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 44 77 Periplasmic. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 99 117 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 139 164 Periplasmic. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 186 223 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 245 281 Periplasmic. {ECO:0000255}. FT TRANSMEM 282 302 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 303 315 Cytoplasmic. {ECO:0000255}. FT DOMAIN 74 302 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 315 AA; 34343 MW; 8FF6FD702A885F0B CRC64; MLTKSRKYFN QTWIESLFKQ TTALFALLVF ILLAAILISL VIGSWESIKR FGGSFLLETY WDPVQEQYGA IIPILGTLIT AGIALFIAVP ISFGIAIFLT ELAPNWLKRP ISIAIEMLAA IPSIIYGMWG LFVFVPLFQE HIQPVLIDNL GNLPGLELFF SGVPFGVGLF TAGLVLAIMI IPFIASVMRD VFSIVPPMLK EGAYGLGATT WEVVRQVIVP HTRIGLVGSV MLGLGRALGE TMAITFIIGN SFQLPNSLFS PSTSIASAIA NEFNEAGGLQ KSALMELGLL LFVITTMVLI LSRLMITKMQ QTKGK // ID PSTS_HAEIN Reviewed; 334 AA. AC P45192; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Phosphate-binding protein PstS; DE Short=PBP; DE Flags: Precursor; GN Name=pstS; OrderedLocusNames=HI_1383; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. {ECO:0000250}. 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:0000305}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23028.1; Type=Frameshift; Positions=2; 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; L42023; AAC23028.1; ALT_FRAME; Genomic_DNA. DR PIR; I64120; I64120. DR RefSeq; NP_439535.1; NC_000907.1. DR RefSeq; WP_010869198.1; NC_000907.1. DR ProteinModelPortal; P45192; -. DR SMR; P45192; 21-333. DR STRING; 71421.HI1383m; -. DR EnsemblBacteria; AAC23028; AAC23028; HI_1383. DR GeneID; 950702; -. DR KEGG; hin:HI1383m; -. DR PATRIC; 20191457; VBIHaeInf48452_1439. DR eggNOG; ENOG4107QMV; Bacteria. DR eggNOG; COG0226; LUCA. DR KO; K02040; -. DR OMA; GKNAWPI; -. DR OrthoDB; EOG6Z99XR; -. DR PhylomeDB; P45192; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042301; F:phosphate ion binding; IBA:GO_Central. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central. DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central. DR InterPro; IPR005673; ABC_phos-bd_PstS. DR InterPro; IPR024370; PBP_domain. DR Pfam; PF12849; PBP_like_2; 1. DR PIRSF; PIRSF002756; PstS; 1. DR TIGRFAMs; TIGR00975; 3a0107s03; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Phosphate transport; Reference proteome; KW Signal; Transport. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 334 Phosphate-binding protein PstS. FT /FTId=PRO_0000031849. FT REGION 27 29 Phosphate binding. FT {ECO:0000250|UniProtKB:P9WGT7}. FT REGION 157 159 Phosphate binding. FT {ECO:0000250|UniProtKB:P9WGT7}. FT BINDING 56 56 Phosphate. FT {ECO:0000250|UniProtKB:P9WGT7}. FT BINDING 74 74 Phosphate. FT {ECO:0000250|UniProtKB:P9WGT7}. SQ SEQUENCE 334 AA; 36665 MW; FFC44EE853FE6B62 CRC64; MKKKSYYVLT LGTLPFAQAN SITGAGASFP YPIYAKWASL YEKETGNKVN YQSIGSGGGQ QQIIAKTVDF GASDDPMKSE LLQQHQLVQF PAVIGGIVPV VNLPEIKPGK LKLSGKLLAE IFLGKIKKWN DPDLVALNPT LPLPNKNIIV IHRSDGSGTT FGFTNYLSKI SNDWKNQVGE GKSVKWLTGQ GGKGNEGVAS YVRQMKYSIG YVEYAYAKQN QLAWISLQNQ AGQFVQPSNE SFMAAASHAK WHEKAGMGVI LTNETGEKSW PITAASFILL NKYSDNPETT KNVLAFFDWA FSRGQDAATE LDYVPIPADV VSTIKSQWKT ELKQ // ID PTA_HAEIN Reviewed; 711 AA. AC P45107; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 107. DE RecName: Full=Phosphate acetyltransferase; DE EC=2.3.1.8; DE AltName: Full=Phosphotransacetylase; GN Name=pta; OrderedLocusNames=HI_1203; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}. 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 -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The N-terminal region seems to be important for proper CC quaternary structure. The C-terminal region contains the CC substrate-binding site (By similarity). {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphate CC acetyltransferase and 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; L42023; AAC22857.1; -; Genomic_DNA. DR PIR; B64169; B64169. DR RefSeq; NP_439359.1; NC_000907.1. DR RefSeq; WP_005694242.1; NC_000907.1. DR ProteinModelPortal; P45107; -. DR STRING; 71421.HI1203; -. DR PRIDE; P45107; -. DR DNASU; 950151; -. DR EnsemblBacteria; AAC22857; AAC22857; HI_1203. DR GeneID; 950151; -. DR KEGG; hin:HI1203; -. DR PATRIC; 20191085; VBIHaeInf48452_1255. DR eggNOG; ENOG4108DNC; Bacteria. DR eggNOG; COG0280; LUCA. DR eggNOG; COG0857; LUCA. DR KO; K13788; -. DR OMA; KPIAQPH; -. DR OrthoDB; EOG6BKJ5W; -. DR PhylomeDB; P45107; -. DR UniPathway; UPA00340; UER00459. DR Proteomes; UP000000579; 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 Gene3D; 3.40.1390.20; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR010766; DRTGG. DR InterPro; IPR016475; P-Actrans_bac. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004614; P_AcTrfase. DR InterPro; IPR002505; PTA_PTB. DR InterPro; IPR028979; Ser_kin/Pase_Hpr_N-like. DR Pfam; PF07085; DRTGG; 1. DR Pfam; PF01515; PTA_PTB; 1. DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF75138; SSF75138; 1. DR TIGRFAMs; TIGR00651; pta; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 711 Phosphate acetyltransferase. FT /FTId=PRO_0000179130. FT REGION 390 711 Phosphate acetyltransferase. SQ SEQUENCE 711 AA; 76517 MW; 4C684C943E2870CB CRC64; MSRTIILIPV STGVGLTSIS LGLIHSLEQK GTKVAFMKPV SQPSTGEDKL DRTTSIIRTS TSLETAEPFM LSVAESLIGQ NQSDVLLEKI VANHQQLTKN NDIVVVEGLI PTRKHGYANS INYEIAQALD AEIVLVAAPA TETPTELKDR VEAAASLFGG KNNPNLLGVV VNKFNAPVDE SGRTRPDLAE IFDSFQHNHI SETEVNKLFA GSAIKLLACV PWNANLIATR AIDLVKHLGA SIINEGEINR RIRGITFCAR SLPNMVEHFR AGSLLVASAD RPDVLVAAAL AASNGIEIGG ILLTGGYKID AQINKLCRPT FEKAKLPIFR IEGNTWQTAL SLQSFNLEVP VDDKERIENI KQYISQHFNA DFINNLVADS SRLPRLSPPA FRFQLTELAR AAKKRIVLPE GDEPRTIKAA VLCAERGIAE CVLLADPASV QRVAEAQGVK LGKGITIINP ADVRENYVDR LVELRKAKGM TETAAREQLE DTVVLGTMML EANEVDGLVS GAVHTTANTI RPPMQIIKTA PGSSIVSSIF FMLLPDQVLV YGDCAVNPDP TAEQLAEIAI QSADSAKAFG IDPKVAMISY STGTSGSGAD VEKVKEATRI AKEKRPDLLI DGPLQYDAAV MEDVARSKAP NSPVAGKATV FVFPDLNTGN TTYKAVQRSA DLVSIGPMLQ GMRKPVNDLS RGALVDDIVY TIALTAIQAT Q // ID PTHP_HAEIN Reviewed; 85 AA. AC P43921; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Phosphocarrier protein HPr; DE EC=2.7.11.-; DE AltName: Full=Histidine-containing protein; GN Name=ptsH; OrderedLocusNames=HI_1713; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- CATALYTIC ACTIVITY: Protein HPr N(pi)-phospho-L-histidine + CC protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L- CC histidine. 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; L42023; AAC23358.1; -; Genomic_DNA. DR PIR; I64137; I64137. DR RefSeq; NP_439855.1; NC_000907.1. DR RefSeq; WP_005649965.1; NC_000907.1. DR ProteinModelPortal; P43921; -. DR SMR; P43921; 1-85. DR STRING; 71421.HI1713; -. DR EnsemblBacteria; AAC23358; AAC23358; HI_1713. DR GeneID; 950527; -. DR KEGG; hin:HI1713; -. DR PATRIC; 20192177; VBIHaeInf48452_1792. DR eggNOG; ENOG4105KZ7; Bacteria. DR eggNOG; COG1925; LUCA. DR KO; K02784; -. DR OMA; YQGKDVN; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P43921; -. DR Proteomes; UP000000579; 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 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; Phosphotransferase system; KW Reference proteome; Serine/threonine-protein kinase; Sugar transport; KW Transferase; Transport. FT CHAIN 1 85 Phosphocarrier protein HPr. FT /FTId=PRO_0000107854. FT DOMAIN 1 85 HPr. {ECO:0000255|PROSITE- FT ProRule:PRU00681}. FT ACT_SITE 15 15 Pros-phosphohistidine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00681}. SQ SEQUENCE 85 AA; 9004 MW; 3D8D599742311830 CRC64; MYSKDVEIIA SNGLHTRPAA QFVKEAKAFS SEITVTSGGK SASAKSLFKL QTLALTQGTI LTISADGEDE QQAVEHLVAL IPTLE // ID PTH_HAEIN Reviewed; 194 AA. AC P44682; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. 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=HI_0394; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22053.1; -; Genomic_DNA. DR PIR; C64065; C64065. DR RefSeq; NP_438556.1; NC_000907.1. DR RefSeq; WP_005693775.1; NC_000907.1. DR ProteinModelPortal; P44682; -. DR SMR; P44682; 4-193. DR STRING; 71421.HI0394; -. DR EnsemblBacteria; AAC22053; AAC22053; HI_0394. DR GeneID; 949493; -. DR KEGG; hin:HI0394; -. DR PATRIC; 20189339; VBIHaeInf48452_0413. DR eggNOG; ENOG4108ZPD; Bacteria. DR eggNOG; COG0193; LUCA. DR KO; K01056; -. DR OMA; FMNRSGL; -. DR OrthoDB; EOG6C5RTR; -. DR PhylomeDB; P44682; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1470; -; 1. DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1. DR InterPro; IPR001328; Pept_tRNA_hydro. DR InterPro; IPR018171; Pept_tRNA_hydro_CS. DR PANTHER; PTHR17224; PTHR17224; 1. DR Pfam; PF01195; Pept_tRNA_hydro; 1. DR SUPFAM; SSF53178; SSF53178; 1. DR TIGRFAMs; TIGR00447; pth; 1. DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1. DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 194 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000187747. SQ SEQUENCE 194 AA; 21389 MW; 638E5590EEFCC4FE CRC64; MSEIKLIVGL GNPGDKYTDT RHNAGEWLIE RLARRFNVSL NPESKFFGKT ARTLVNGKEV RLLVPTTFMN LSGKAVGALA SFYRIKPEEI LVIHDELDLP PGTAKLKQGG GHGGHNGLKD IVAQLGNNNN FYRLRIGIGH PGHRDLVAGY VLNKPSPADR DALEKVLDEA TDCVEMIFRD GMVKATNRLN SFKI // ID PUR7_HAEIN Reviewed; 290 AA. AC P43851; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 26-JUL-2002, sequence version 2. DT 17-FEB-2016, entry version 104. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; GN Name=purC; OrderedLocusNames=HI_1726; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23372.1; 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; L42023; AAC23372.1; ALT_INIT; Genomic_DNA. DR PIR; E64138; E64138. DR RefSeq; NP_439867.2; NC_000907.1. DR RefSeq; WP_005649949.1; NC_000907.1. DR ProteinModelPortal; P43851; -. DR STRING; 71421.HI1726; -. DR EnsemblBacteria; AAC23372; AAC23372; HI_1726. DR GeneID; 950883; -. DR KEGG; hin:HI1726; -. DR PATRIC; 20192205; VBIHaeInf48452_1805. DR eggNOG; ENOG4105C8V; Bacteria. DR eggNOG; COG0152; LUCA. DR KO; K01923; -. DR OMA; WNKQPPA; -. DR OrthoDB; EOG69SKD1; -. DR PhylomeDB; P43851; -. DR UniPathway; UPA00074; UER00131. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.470.20; -; 1. DR HAMAP; MF_00137; SAICAR_synth; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR028923; SAICAR_synt/ADE2_N. DR InterPro; IPR001636; SAICAR_synth. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Pfam; PF01259; SAICAR_synt; 1. DR TIGRFAMs; TIGR00081; purC; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 290 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_0000100831. SQ SEQUENCE 290 AA; 32581 MW; 517F3EEDE9F3442E CRC64; MTQQLPILSL KKIYSGKVRD LYEIDDKRML MVTSDRLSAF DVILDDPIPR KGEILTQISN FWFNKLAHIM PNHFTGDSVY DVLPKEEADL IRDRAVVCKR LNPIKIESIV RGYLTGSGLK DYKQTGTICG LKLPEGLVEA SKLPEAIFTP SSKEEVGNHD INISYAECEK LIGADLAAQV KEKAIALYTV AAEYALTKGI IICDTKFEFG LDENGTLTLM DEVLTPDSSR FWSVDTYQAG TNPPSFDKQF VRDWLENSGW NKQAPAPKVP ENIIQKTVDK YQEALDLLTK // ID PYRR_HAEIN Reviewed; 179 AA. AC P44722; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Bifunctional protein PyrR; DE Includes: DE RecName: Full=Pyrimidine operon regulatory protein; DE Includes: DE RecName: Full=Uracil phosphoribosyltransferase; DE Short=UPRTase; DE EC=2.4.2.9; GN Name=pyrR; OrderedLocusNames=HI_0459; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Regulates the transcription of the pyrimidine nucleotide CC (pyr) operon in response to exogenous pyrimidines. {ECO:0000250}. CC -!- FUNCTION: Also displays a weak uracil phosphoribosyltransferase CC activity which is not physiologically significant. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UMP + diphosphate = uracil + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrR 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; L42023; AAC22117.1; -; Genomic_DNA. DR PIR; G64069; G64069. DR RefSeq; NP_438620.1; NC_000907.1. DR RefSeq; WP_005649361.1; NC_000907.1. DR ProteinModelPortal; P44722; -. DR STRING; 71421.HI0459; -. DR EnsemblBacteria; AAC22117; AAC22117; HI_0459. DR GeneID; 949777; -. DR KEGG; hin:HI0459; -. DR PATRIC; 20189473; VBIHaeInf48452_0479. DR eggNOG; ENOG4108UK1; Bacteria. DR eggNOG; COG2065; LUCA. DR KO; K02825; -. DR OMA; VPTSRKE; -. DR OrthoDB; EOG61VZD8; -. DR PhylomeDB; P44722; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. 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; 3.40.50.2020; -; 1. DR HAMAP; MF_01219; PyrR; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR023050; PyrR. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transcription; Transcription regulation; Transferase. FT CHAIN 1 179 Bifunctional protein PyrR. FT /FTId=PRO_0000183038. FT REGION 39 40 Substrate-binding. {ECO:0000250}. FT REGION 104 112 Substrate binding. {ECO:0000250}. FT MOTIF 100 112 PRPP-binding. {ECO:0000250}. FT BINDING 137 137 Substrate. {ECO:0000250}. FT BINDING 161 161 Substrate. {ECO:0000250}. SQ SEQUENCE 179 AA; 20528 MW; 1E96972790C0A9E9 CRC64; MEKIIIDHDR FLRTISRISH EIIEKHQTLD DLVIVGIKRR GAEIAELLQR RVEELSSINL PSMELDITFY RDDLTLVDQE DKMPVYSGSS QYLNIQDKTV ILVDDVLFTG RTIRAAMDAL TDFGRAAKIE LVIFVDRGHR ELPIRADYVG KNVPTSRDEL VQVRTEKQDG CYEVAILGK // ID PUR2_HAEIN Reviewed; 429 AA. AC P43845; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; GN OrderedLocusNames=HI_0888; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22545.1; -; Genomic_DNA. DR PIR; C64100; C64100. DR RefSeq; NP_439049.1; NC_000907.1. DR RefSeq; WP_005693239.1; NC_000907.1. DR ProteinModelPortal; P43845; -. DR SMR; P43845; 1-425. DR STRING; 71421.HI0888; -. DR PRIDE; P43845; -. DR EnsemblBacteria; AAC22545; AAC22545; HI_0888. DR GeneID; 949893; -. DR KEGG; hin:HI0888; -. DR PATRIC; 20190433; VBIHaeInf48452_0930. DR eggNOG; ENOG4105C12; Bacteria. DR eggNOG; COG0151; LUCA. DR KO; K01945; -. DR OMA; DYQNFTE; -. DR OrthoDB; EOG69SKD1; -. DR PhylomeDB; P43845; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 429 Phosphoribosylamine--glycine ligase. FT /FTId=PRO_0000151452. FT DOMAIN 109 316 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00138}. FT NP_BIND 135 196 ATP. {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 286 286 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 288 288 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00138}. SQ SEQUENCE 429 AA; 46248 MW; 3F31BC3B5B9D373B CRC64; MNILIIGNGG REHALAWKVA QSPLADKVFV APGNAGTALE HKVENVNISA TDIPALVKFA QDKQIGLTIV GPEAPLVIGV VDAFREAGLK IFGPAKAAAQ LEGSKAFTKD FLARHKIPTA EYQNFTEVEP ALTYLREKGT PIVVKADGLA AGKGVIVAMT LQEAEDAVRD MLSGNAFGEA GSRVVIEEFL DGEEASFIVM VDGKNVEPMA SSQDHKRVGE NDTGLNTGGM GAYSPAPVIT PEIHSRIMKE VIYPTVNGMA AEGNVYTGFL YAGLMIMPNG QPKVIEFNCR FGDPETQPIM LRLKSDLVEL CLKACDGKLD EVISQWDLRA SLGIVLAAEG YPKDYRKGDE ISGLPKSAVK NEKVFLAGVA EQEGKLVTNG GRVLCVTALG ESVFEAQQKA LKLAEQIQWS GRFYRRDIGY RAVERELQK // ID PUR8_HAEIN Reviewed; 456 AA. AC P44797; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Adenylosuccinate lyase; DE Short=ASL; DE EC=4.3.2.2; DE AltName: Full=Adenylosuccinase; DE Short=ASase; GN Name=purB; OrderedLocusNames=HI_0639; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. CC -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- CC (5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits CC contribute catalytic and substrate-binding residues to each active CC site (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22299.1; -; Genomic_DNA. DR RefSeq; NP_438799.1; NC_000907.1. DR RefSeq; WP_010869024.1; NC_000907.1. DR ProteinModelPortal; P44797; -. DR SMR; P44797; 1-455. DR STRING; 71421.HI0639; -. DR PRIDE; P44797; -. DR EnsemblBacteria; AAC22299; AAC22299; HI_0639. DR GeneID; 949686; -. DR KEGG; hin:HI0639; -. DR PATRIC; 20189885; VBIHaeInf48452_0667. DR eggNOG; ENOG4107QTF; Bacteria. DR eggNOG; COG0015; LUCA. DR KO; K01756; -. DR OMA; TFGKEMA; -. DR OrthoDB; EOG686NDB; -. DR PhylomeDB; P44797; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR GO; GO:0006163; P:purine nucleotide metabolic process; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR InterPro; IPR013539; PurB_C. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF08328; ASL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00928; purB; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Purine biosynthesis; Reference proteome. FT CHAIN 1 456 Adenylosuccinate lyase. FT /FTId=PRO_0000137880. FT REGION 15 16 Substrate binding. {ECO:0000250}. FT REGION 90 92 Substrate binding. {ECO:0000250}. FT REGION 122 123 Substrate binding. {ECO:0000250}. FT REGION 301 303 Substrate binding. {ECO:0000250}. FT REGION 340 344 Substrate binding. {ECO:0000250}. FT ACT_SITE 171 171 Proton donor/acceptor. {ECO:0000250}. FT ACT_SITE 295 295 Proton donor/acceptor. {ECO:0000250}. FT BINDING 247 247 Substrate. {ECO:0000250}. FT BINDING 309 309 Substrate. {ECO:0000250}. FT BINDING 335 335 Substrate. {ECO:0000250}. FT BINDING 340 340 Substrate. {ECO:0000250}. SQ SEQUENCE 456 AA; 51993 MW; 9C3021D612A3CAC8 CRC64; MQLSTLTALS PLDGRYQDKV TPLRAIFSEF GLMKFRVAVE VRWLQKLAST ADITEVPPFS TQANAFLDGI VANFNEADAA RIKEIERTTN HDVKAVEYFL KEKIQNEVEL VKVSEFIHFA CTSEDINNLS HALMLSTARD EVILPEWQKL IDEITRLAEE YKTIPLLSRT HGQPASPSTV GKEMANVVYR LKRQFKQLQN AEILGKINGA VGNYNAHLSA YPNIDWHKFS EEFVTSLGIQ WNPYTTQIEP HDYITEFFDA VVRFNTIIID FDRDLWGYIA LNHFKQRTIA GEIGSSTMPH KVNPIDFENS EGNLGLANAV MTHLGQKLPI SRWQRDLTDS TVLRNLGVGL GYCLIAYAST RKGISKLEVN QPHLLEELNQ NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVTEQAMR EFIDKLDIPQ EEKLRLQKLT PATYIGAAVE LVEKLS // ID PURA_HAEIN Reviewed; 432 AA. AC P45283; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 13-APR-2016, entry version 122. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; GN OrderedLocusNames=HI_1633; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. Catalyzes the first committed step in the CC biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + CC N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23278.1; -; Genomic_DNA. DR PIR; G64133; G64133. DR RefSeq; NP_439775.1; NC_000907.1. DR RefSeq; WP_010869263.1; NC_000907.1. DR ProteinModelPortal; P45283; -. DR SMR; P45283; 2-432. DR STRING; 71421.HI1633; -. DR EnsemblBacteria; AAC23278; AAC23278; HI_1633. DR GeneID; 950476; -. DR KEGG; hin:HI1633; -. DR PATRIC; 20192009; VBIHaeInf48452_1708. DR eggNOG; ENOG4105C91; Bacteria. DR eggNOG; COG0104; LUCA. DR KO; K01939; -. DR OMA; FHHAKPI; -. DR OrthoDB; EOG68Q0QG; -. DR PhylomeDB; P45283; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 432 Adenylosuccinate synthetase. FT /FTId=PRO_0000095183. FT NP_BIND 13 19 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 41 43 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 332 334 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 415 417 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT REGION 14 17 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 39 42 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 300 306 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 14 14 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 42 42 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 14 14 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 41 41 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 130 130 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 144 144 IMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 225 225 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 240 240 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 304 304 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 306 306 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. SQ SEQUENCE 432 AA; 47367 MW; A106DD2BD5A5D91D CRC64; MGKSVVILGA QWGDEGKGKI VDLLTDRVKY VVRYQGGHNA GHTLIINGEK TVLRLIPSGM LHPNVTCLIG NGVVVSPEAL MKEMGELESR GIKVRERLLI SEACPLILPY HVAMDHAREA ALGKKAIGTT GRGIGPAYED KVARRGLRVG DLFNKEAFAE KLKNILEYYN FQLVNYYKVE PVDYQKTLDD VMAIADVITG MVADITTILD TARKNGEHIL FEGAQGTMLD IDHGTYPYVT SSNTTAGGVA TGSGFGPRNL DYVLGIIKAY CTRVGGGPFT TELFDDVGAE IARKGNEFGA VTGRPRRCGW FDAVAIRRAI QLNSISGFCM TKLDVLDGFD EVKICVAYKM PNGEIVEYAP LAAKDWEGVE PIYETLPGWK ENTFRITDVN KLPQNCINYI KRIEEVTGVP IDILSTGPDR VETMILREPF AA // ID PURK_HAEIN Reviewed; 362 AA. AC P43850; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928}; DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928}; DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928}; GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928}; GN OrderedLocusNames=HI_1616; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5- CC aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5- CC carboxyaminoimidazole ribonucleotide (N5-CAIR). CC {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole CC + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole. {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP- CC Rule:MF_01928}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_01928}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23264.1; -; Genomic_DNA. DR PIR; H64132; H64132. DR RefSeq; NP_439758.1; NC_000907.1. DR RefSeq; WP_005693629.1; NC_000907.1. DR ProteinModelPortal; P43850; -. DR STRING; 71421.HI1616; -. DR EnsemblBacteria; AAC23264; AAC23264; HI_1616. DR GeneID; 950468; -. DR KEGG; hin:HI1616; -. DR PATRIC; 20191963; VBIHaeInf48452_1689. DR eggNOG; ENOG4105CY8; Bacteria. DR eggNOG; COG0026; LUCA. DR KO; K01589; -. DR OMA; CHIHWYG; -. DR OrthoDB; EOG6QZMX7; -. DR PhylomeDB; P43850; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01928; PurK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR005875; PurK. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01161; purK; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 362 N5-carboxyaminoimidazole ribonucleotide FT synthase. FT /FTId=PRO_0000074998. FT DOMAIN 89 274 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_01928}. FT NP_BIND 130 136 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. FT NP_BIND 158 161 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. FT NP_BIND 244 245 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. FT BINDING 85 85 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. FT BINDING 125 125 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. FT BINDING 166 166 ATP. {ECO:0000255|HAMAP-Rule:MF_01928}. SQ SEQUENCE 362 AA; 41273 MW; 90CE70504784B452 CRC64; MQNSTLYPTV YVLGNGQLGR MLRYAGAPLD IYVEPLAFNA PVFDLPENAI ITAEIERWEK TPLTELLGNH KNFVNQHIFG LLADRFTQKS LLDELNLSTS PWCLLKDKNQ WNDLFQTVGE KVVVKRRTGG YDGRGQWIIR DENRADITDD LFGEVIAEKF IPFDYEVSIV GARFKNGEKR FYPVTHNLQQ NGILRYSVVD CAFPQQSVQQ KQAETMLGKI MDKLGYVGVM AMECFVVGDK LLINELAPRV HNSGHWTQLG CSISQFELHL RALLNLPTPE LQTFAPSVMI NLIGTNHNPK WLNIPFAQLH WYGKEVRIGR KVGHINLSHP NKAVIIQQLE KLCTELPEDY QSGLNWAIEK LK // ID PURR_HAEIN Reviewed; 336 AA. AC P46456; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 111. DE RecName: Full=HTH-type transcriptional repressor PurR {ECO:0000255|HAMAP-Rule:MF_01277}; DE AltName: Full=Pur regulon repressor {ECO:0000255|HAMAP-Rule:MF_01277}; DE AltName: Full=Purine nucleotide synthesis repressor {ECO:0000255|HAMAP-Rule:MF_01277}; GN Name=purR {ECO:0000255|HAMAP-Rule:MF_01277}; GN OrderedLocusNames=HI_1635; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is the main repressor of the genes involved in the de CC novo synthesis of purine nucleotides, regulating purB, purC, CC purEK, purF, purHD, purL, purMN and guaBA expression. PurR is CC allosterically activated to bind its cognate DNA by binding the CC purine corepressors, hypoxanthine or guanine, thereby effecting CC transcription repression. {ECO:0000255|HAMAP-Rule:MF_01277}. CC -!- PATHWAY: Purine metabolism; purine nucleotide biosynthesis CC [regulation]. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01277}. CC -!- DOMAIN: Consists of two structural and functional domains: an N- CC terminal DNA-binding domain, approximately the first 60 residues, CC and a larger C-terminal domain, approximately 280 residues, which CC imparts the function of corepressor binding and oligomerization. CC {ECO:0000255|HAMAP-Rule:MF_01277}. CC -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23280.1; -; Genomic_DNA. DR RefSeq; NP_439777.1; NC_000907.1. DR RefSeq; WP_010869264.1; NC_000907.1. DR ProteinModelPortal; P46456; -. DR SMR; P46456; 1-333. DR STRING; 71421.HI1635; -. DR EnsemblBacteria; AAC23280; AAC23280; HI_1635. DR GeneID; 950319; -. DR KEGG; hin:HI1635; -. DR PATRIC; 20192015; VBIHaeInf48452_1711. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K03604; -. DR OMA; WIMEGFF; -. DR OrthoDB; EOG6SJJMM; -. DR PhylomeDB; P46456; -. DR UniPathway; UPA00488; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR HAMAP; MF_01277; HTH_type_PurR; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR InterPro; IPR023588; Tscrpt_reg_HTH_PurR. DR Pfam; PF00356; LacI; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Purine biosynthesis; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 336 HTH-type transcriptional repressor PurR. FT /FTId=PRO_0000107979. FT DOMAIN 2 56 HTH lacI-type. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT DNA_BIND 4 23 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT DNA_BIND 48 56 {ECO:0000255|HAMAP-Rule:MF_01277}. FT BINDING 73 73 Corepressor. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT BINDING 188 188 Corepressor. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT BINDING 190 190 Corepressor. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT BINDING 219 219 Corepressor. {ECO:0000255|HAMAP- FT Rule:MF_01277}. FT BINDING 273 273 Corepressor. {ECO:0000255|HAMAP- FT Rule:MF_01277}. SQ SEQUENCE 336 AA; 37508 MW; 75084FF974EDAE31 CRC64; MATIKDVAKM AGVSTTTVSH VINKTRFVAK DTEEAVLSAI KQLNYSPSAV ARSLKVNTTK SIGMIVTTSE APYFAEIIHS VEEHCYRQGY SLFCVTHKMD PEKVKNHLEM LAKKRVDGLL VMCSEYTQDS LDLLSSFSTI PMVVMDWGPN ANTDVIDDHS FDGGYLATKH LIECGHKKIG IICGELNKTT ARTRYEGFEK AMEEAKLTIN PSWVLEGAFE PEDGYECMNR LLTQEKLPTA LFCCNDVMAL GAISALTEKG LRVPEDMSII GYDDIHASRF YAPPLTTIHQ SKLRLGRQAI NILLERITHK DEGVQQYSRI DITPELIIRK SVKSIL // ID PURU_HAEIN Reviewed; 278 AA. AC Q03432; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 115. DE RecName: Full=Formyltetrahydrofolate deformylase {ECO:0000255|HAMAP-Rule:MF_01927}; DE EC=3.5.1.10 {ECO:0000255|HAMAP-Rule:MF_01927}; DE AltName: Full=Formyl-FH(4) hydrolase {ECO:0000255|HAMAP-Rule:MF_01927}; GN Name=purU {ECO:0000255|HAMAP-Rule:MF_01927}; GN OrderedLocusNames=HI_1588; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-278. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8335255; DOI=10.1016/0378-1119(93)90713-D; RA Maskell D.J.; RT "Cloning and sequencing of the Haemophilus influenzae aroA gene."; RL Gene 129:155-156(1993). CC -!- FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate CC (formyl-FH4) to formate and tetrahydrofolate (FH4). CC {ECO:0000255|HAMAP-Rule:MF_01927}. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + H(2)O = formate + CC tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01927}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC formate from 10-formyl-5,6,7,8-tetrahydrofolate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01927}. CC -!- SIMILARITY: Belongs to the PurU family. {ECO:0000255|HAMAP- CC Rule:MF_01927}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|HAMAP- CC Rule:MF_01927}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23236.1; -; Genomic_DNA. DR EMBL; L04686; AAA24942.1; -; Genomic_DNA. DR PIR; E64131; E64131. DR RefSeq; NP_439733.1; NC_000907.1. DR RefSeq; WP_005693604.1; NC_000907.1. DR ProteinModelPortal; Q03432; -. DR STRING; 71421.HI1588; -. DR PRIDE; Q03432; -. DR EnsemblBacteria; AAC23236; AAC23236; HI_1588. DR GeneID; 950306; -. DR KEGG; hin:HI1588; -. DR PATRIC; 20191909; VBIHaeInf48452_1662. DR eggNOG; ENOG4105CIY; Bacteria. DR eggNOG; COG0788; LUCA. DR KO; K01433; -. DR OMA; TLCEAMS; -. DR OrthoDB; EOG615VP4; -. DR PhylomeDB; Q03432; -. DR UniPathway; UPA00074; UER00170. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008864; F:formyltetrahydrofolate deformylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.170; -; 1. DR HAMAP; MF_01927; PurU; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR004810; PurU. DR PANTHER; PTHR10520:SF7; PTHR10520:SF7; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR PRINTS; PR01575; FFH4HYDRLASE. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00655; PurU; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; One-carbon metabolism; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 278 Formyltetrahydrofolate deformylase. FT /FTId=PRO_0000074963. FT DOMAIN 6 85 ACT. {ECO:0000255|HAMAP-Rule:MF_01927}. FT ACT_SITE 223 223 {ECO:0000255|HAMAP-Rule:MF_01927}. FT CONFLICT 115 117 VIG -> RNR (in Ref. 2; AAA24942). FT {ECO:0000305}. FT CONFLICT 138 140 HEN -> PK (in Ref. 2; AAA24942). FT {ECO:0000305}. FT CONFLICT 205 205 K -> E (in Ref. 2; AAA24942). FT {ECO:0000305}. SQ SEQUENCE 278 AA; 32173 MW; 7F375AB3C422EC4B CRC64; MIEKKILLTD CPDDKGLIAK ITNICYKHQL NILHNNEFVD FETKHFFMRT ELEGIFNEAT LLEDLKYSLP EETNCRLIGT QRKRIVILVT KEAHCLGDIL MKNYYGALDV EIAAVIGNHD NLRELVERFN IPFHLVSHEN LTRVEHDKLL AEKIDEYTPD YIVLAKYMRV LNPEFVARYP NRVINIHHSF LPAFIGAKPY QQAYKRGVKI IGATAHFINN ELDQGPIIMQ NVINVDHTYN AEAMMRAGRD VEKTVLSRAL DLALHDRIFV YKNKTVVL // ID PYRH_HAEIN Reviewed; 237 AA. AC P43890; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Uridylate kinase; DE Short=UK; DE EC=2.7.4.22; DE AltName: Full=Uridine monophosphate kinase; DE Short=UMP kinase; DE Short=UMPK; GN Name=pyrH; Synonyms=smbA; OrderedLocusNames=HI_1065; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, ENZYME REGULATION, KINETIC PARAMETERS, IDENTIFICATION BY RP MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=17210578; DOI=10.1074/jbc.M606963200; RA Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., RA Assairi L., Ionescu M., Palibroda N., Barzu O., Gilles A.-M.; RT "Regulatory mechanisms differ in UMP kinases from Gram-negative and RT Gram-positive bacteria."; RL J. Biol. Chem. 282:7242-7253(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-237. RG New York structural genomics research consortium (NYSGRC); RT "Crystal structure of uridylate kinase."; RL Submitted (JUN-2005) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000269|PubMed:17210578}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. CC -!- ENZYME REGULATION: Allosterically activated by GTP. Inhibited by CC UTP. {ECO:0000269|PubMed:17210578}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.57 mM for ATP (in the absence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=0.46 mM for ATP (in the presence of GTP) CC {ECO:0000269|PubMed:17210578}; CC KM=40 uM for UMP {ECO:0000269|PubMed:17210578}; CC Vmax=57 umol/min/mg enzyme {ECO:0000269|PubMed:17210578}; CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:17210578}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UMP 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; L42023; AAC22719.1; -; Genomic_DNA. DR PIR; H64180; H64180. DR RefSeq; NP_439223.1; NC_000907.1. DR RefSeq; WP_005693391.1; NC_000907.1. DR PDB; 2A1F; X-ray; 2.10 A; A/B/C/D/E/F=2-237. DR PDBsum; 2A1F; -. DR ProteinModelPortal; P43890; -. DR SMR; P43890; 2-237. DR STRING; 71421.HI1065; -. DR DNASU; 950042; -. DR EnsemblBacteria; AAC22719; AAC22719; HI_1065. DR GeneID; 950042; -. DR KEGG; hin:HI1065; -. DR PATRIC; 20190793; VBIHaeInf48452_1109. DR eggNOG; ENOG4105C41; Bacteria. DR eggNOG; COG0528; LUCA. DR KO; K09903; -. DR OMA; IIVFDMN; -. DR OrthoDB; EOG6M0T8S; -. DR PhylomeDB; P43890; -. DR SABIO-RK; P43890; -. DR UniPathway; UPA00159; UER00275. DR EvolutionaryTrace; P43890; -. DR Proteomes; UP000000579; 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 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; ATP-binding; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Pyrimidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 237 Uridylate kinase. FT /FTId=PRO_0000143847. FT NP_BIND 12 15 ATP. {ECO:0000250}. FT NP_BIND 135 142 UMP. {ECO:0000250}. FT REGION 20 25 Involved in allosteric activation by GTP. FT {ECO:0000255}. FT BINDING 54 54 UMP; via amide nitrogen. {ECO:0000250}. FT BINDING 55 55 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 59 59 ATP. {ECO:0000250}. FT BINDING 74 74 UMP. {ECO:0000250}. FT BINDING 162 162 ATP. {ECO:0000250}. FT BINDING 168 168 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 171 171 ATP. {ECO:0000250}. FT STRAND 7 13 {ECO:0000244|PDB:2A1F}. FT HELIX 15 18 {ECO:0000244|PDB:2A1F}. FT STRAND 23 25 {ECO:0000244|PDB:2A1F}. FT HELIX 28 42 {ECO:0000244|PDB:2A1F}. FT TURN 43 45 {ECO:0000244|PDB:2A1F}. FT STRAND 47 52 {ECO:0000244|PDB:2A1F}. FT TURN 55 57 {ECO:0000244|PDB:2A1F}. FT HELIX 61 65 {ECO:0000244|PDB:2A1F}. FT HELIX 70 94 {ECO:0000244|PDB:2A1F}. FT STRAND 99 105 {ECO:0000244|PDB:2A1F}. FT TURN 108 110 {ECO:0000244|PDB:2A1F}. FT STRAND 111 113 {ECO:0000244|PDB:2A1F}. FT HELIX 116 124 {ECO:0000244|PDB:2A1F}. FT STRAND 128 133 {ECO:0000244|PDB:2A1F}. FT HELIX 142 152 {ECO:0000244|PDB:2A1F}. FT STRAND 156 166 {ECO:0000244|PDB:2A1F}. FT STRAND 182 184 {ECO:0000244|PDB:2A1F}. FT HELIX 186 191 {ECO:0000244|PDB:2A1F}. FT HELIX 199 208 {ECO:0000244|PDB:2A1F}. FT STRAND 212 216 {ECO:0000244|PDB:2A1F}. FT HELIX 222 227 {ECO:0000244|PDB:2A1F}. FT STRAND 232 236 {ECO:0000244|PDB:2A1F}. SQ SEQUENCE 237 AA; 25726 MW; FDB0D6CE2CBCDCE3 CRC64; MSQPIYKRIL LKLSGEALQG EDGLGIDPAI LDRMAVEIKE LVEMGVEVSV VLGGGNLFRG AKLAKAGMNR VVGDHMGMLA TVMNGLAMRD SLFRADVNAK LMSAFQLNGI CDTYNWSEAI KMLREKRVVI FSAGTGNPFF TTDSTACLRG IEIEADVVLK ATKVDGVYDC DPAKNPDAKL YKNLSYAEVI DKELKVMDLS AFTLARDHGM PIRVFNMGKP GALRQVVTGT EEGTTIC // ID QUEC_HAEIN Reviewed; 228 AA. AC P44124; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 17-FEB-2016, entry version 97. DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633}; GN Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; GN OrderedLocusNames=HI_1191; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- CATALYTIC ACTIVITY: 7-carboxy-7-carbaguanine + NH(3) + ATP = 7- CC cyano-7-carbaguanine + ADP + phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01633}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP- CC Rule:MF_01633}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22844.1; Type=Frameshift; Positions=182; 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; L42023; AAC22844.1; ALT_FRAME; Genomic_DNA. DR PIR; G64021; G64021. DR ProteinModelPortal; P44124; -. DR STRING; 71421.HI1191; -. DR EnsemblBacteria; AAC22844; AAC22844; HI_1191. DR PATRIC; 20191061; VBIHaeInf48452_1243. DR eggNOG; ENOG4105FD2; Bacteria. DR eggNOG; COG0603; LUCA. DR OMA; VFIKSMN; -. DR OrthoDB; EOG6091HB; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000579; Chromosome. 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:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01633; QueC; 1. DR InterPro; IPR018317; QueC. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF06508; QueC; 1. DR PIRSF; PIRSF006293; ExsB; 1. DR TIGRFAMs; TIGR00364; TIGR00364; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Metal-binding; KW Nucleotide-binding; Queuosine biosynthesis; Reference proteome; Zinc. FT CHAIN 1 228 7-cyano-7-deazaguanine synthase. FT /FTId=PRO_0000168632. FT NP_BIND 16 26 ATP. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 195 195 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 203 203 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 206 206 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 209 209 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. SQ SEQUENCE 228 AA; 25659 MW; D393B4449B4ECB57 CRC64; MNIFNPNHDR KAIVIFSGGQ DSTTCLFQAI AEYGKENIEA ITFQYGQRHA IELEKARTIA QDLGIKQTLI DTSVMKAITH NALMDEQAHI EQKENELPNT FVDGRNALFL LYAAIYAKGQ GIQDIITGVC ETDFSGYPDC RDVFIKSMNV TLNLAMDYPI PISKTPLMYL TKAQTWQLAD ELGVLDYVQK HTHTCYEGIE GGCRKCPSCI LRNKGLKKYL TQKGRKNV // ID RARA_HAEIN Reviewed; 446 AA. AC P45262; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Replication-associated recombination protein A; GN Name=rarA; OrderedLocusNames=HI_1590; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DNA-dependent ATPase that plays important roles in CC cellular responses to stalled DNA replication processes. CC {ECO:0000250|UniProtKB:P0AAZ4}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 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; L42023; AAC23238.1; -; Genomic_DNA. DR PIR; F64172; F64172. DR RefSeq; NP_439735.1; NC_000907.1. DR RefSeq; WP_010869253.1; NC_000907.1. DR ProteinModelPortal; P45262; -. DR SMR; P45262; 251-434. DR STRING; 71421.HI1590; -. DR DNASU; 950837; -. DR EnsemblBacteria; AAC23238; AAC23238; HI_1590. DR GeneID; 950837; -. DR KEGG; hin:HI1590; -. DR PATRIC; 20191913; VBIHaeInf48452_1664. DR eggNOG; ENOG4105D1H; Bacteria. DR eggNOG; COG2256; LUCA. DR KO; K07478; -. DR OMA; YRYDHDE; -. DR OrthoDB; EOG64FKG0; -. DR PhylomeDB; P45262; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032423; AAA_assoc_2. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR021886; MgsA_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR Pfam; PF16193; AAA_assoc_2; 1. DR Pfam; PF12002; MgsA_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA replication; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 446 Replication-associated recombination FT protein A. FT /FTId=PRO_0000168758. FT NP_BIND 57 64 ATP. {ECO:0000250|UniProtKB:P0AAZ4}. SQ SEQUENCE 446 AA; 50217 MW; 0F943B7A3736A4F7 CRC64; MSNFNFDFAE NDFGPLAAKM RPTSLEQYFG QSHLIGEGKP LRKAIQAGHI YSMIFWGPPG TGKTTLAEII AQRINAEVER ISAVTSGIKE IREAIDRAKQ NRLADRKTIL FVDEVHRFNK SQQDAFLPHI EDGTVIFIGA TTENPSFELN NALLSRARVY VLKSLTTAEI EQVLQQAVED PKRGLGKERL ILEENLLQVL AEYVNGDARL ALNCLELMVD MADETENGKK IDRTLLKEVL GERQARFDKQ GDRFYDLISA LHKSVRGSAP DAALYWYARI LTAGGDPLYV ARRLLAIASE DVGNADPRAM QVALAAWDCF SRVGAYEGER AIAQAIIYLS VAPKSNAVYT AFNTAKQQAK DLPDYDVPPH LRNAPTNLMK ELGYGTEYRY AHDEPNAYAA GENYFPPELK DTQYYFPTNR GMEIQIKEKL ERLREQDKSA VKKRYK // ID PURE_HAEIN Reviewed; 164 AA. AC P43849; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; GN OrderedLocusNames=HI_1615; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161. RC STRAIN=AM30 (770235) / Serotype B; RX PubMed=7997179; DOI=10.1111/j.1365-2958.1994.tb00461.x; RA van Ham M.S., van Alphen L., Mooi F.R., van Putten J.P.M.; RT "The fimbrial gene cluster of Haemophilus influenzae type b."; RL Mol. Microbiol. 13:673-684(1994). CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole CC ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01929}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23263.1; -; Genomic_DNA. DR EMBL; Z33502; CAA83909.1; -; Genomic_DNA. DR PIR; G64132; G64132. DR PIR; S54434; S54434. DR RefSeq; NP_439757.1; NC_000907.1. DR RefSeq; WP_005693627.1; NC_000907.1. DR ProteinModelPortal; P43849; -. DR SMR; P43849; 5-163. DR STRING; 71421.HI1615; -. DR EnsemblBacteria; AAC23263; AAC23263; HI_1615. DR GeneID; 949616; -. DR KEGG; hin:HI1615; -. DR PATRIC; 20191961; VBIHaeInf48452_1688. DR eggNOG; ENOG4108UM6; Bacteria. DR eggNOG; COG0041; LUCA. DR KO; K01588; -. DR OMA; SDWATMR; -. DR OrthoDB; EOG6Z0QH2; -. DR PhylomeDB; P43849; -. DR UniPathway; UPA00074; UER00943. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.7700; -; 1. DR HAMAP; MF_01929; PurE_classI; 1. DR InterPro; IPR024694; N5-CAIR_mutase_PurE. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR PIRSF; PIRSF001338; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. DR TIGRFAMs; TIGR01162; purE; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Purine biosynthesis; Reference proteome. FT CHAIN 1 164 N5-carboxyaminoimidazole ribonucleotide FT mutase. FT /FTId=PRO_0000074975. FT BINDING 13 13 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 16 16 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 43 43 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT CONFLICT 139 143 DALFT -> AELLS (in Ref. 2; CAA83909). FT {ECO:0000305}. FT CONFLICT 147 147 A -> S (in Ref. 2; CAA83909). FT {ECO:0000305}. FT CONFLICT 151 151 N -> S (in Ref. 2; CAA83909). FT {ECO:0000305}. FT CONFLICT 154 155 NM -> RA (in Ref. 2; CAA83909). FT {ECO:0000305}. SQ SEQUENCE 164 AA; 17269 MW; 60A03B0D4DD85412 CRC64; MSKTAQIAVV MGSKSDWATM QEATQILDEL NVPYHVEVVS AHRTPDKLFE FAENAQKNGY KVIIAGAGGA AHLPGMIAAK TLVPVLGVPV KSSMLSGVDS LYSIVQMPKG IPVGTLAIGP AGAANAGLLA AQILAGWDDA LFTRLQAFRE NQTNMVLDNP DPRT // ID PYRE_HAEIN Reviewed; 213 AA. AC P43855; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; GN OrderedLocusNames=HI_0272; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation CC of orotidine monophosphate (OMP). {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate CC + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21938.1; -; Genomic_DNA. DR PIR; I64058; I64058. DR RefSeq; NP_438441.1; NC_000907.1. DR RefSeq; WP_005686697.1; NC_000907.1. DR ProteinModelPortal; P43855; -. DR SMR; P43855; 1-213. DR STRING; 71421.HI0272; -. DR EnsemblBacteria; AAC21938; AAC21938; HI_0272. DR GeneID; 949395; -. DR KEGG; hin:HI0272; -. DR PATRIC; 20189071; VBIHaeInf48452_0287. DR eggNOG; ENOG4107QP2; Bacteria. DR eggNOG; COG0461; LUCA. DR KO; K00762; -. DR OMA; MKAYQRQ; -. DR OrthoDB; EOG6091H8; -. DR PhylomeDB; P43855; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01208; PyrE; 1. DR InterPro; IPR023031; OPRT. DR InterPro; IPR004467; Or_phspho_trans_dom. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Magnesium; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 213 Orotate phosphoribosyltransferase. FT /FTId=PRO_0000110700. FT REGION 34 35 Orotate binding. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT REGION 72 73 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT REGION 124 132 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 26 26 5-phosphoribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 99 99 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 100 100 5-phosphoribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 103 103 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 105 105 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 128 128 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 156 156 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. SQ SEQUENCE 213 AA; 23643 MW; A5D0B40CD490547E CRC64; MEQYKRDFIE FALSRNVLKF GEFTLKSGRK SPYFFNAGLF NTGADLARLG EFYAAAIQAS AVDFDVVFGP AYKGIPIGTS VSVALFNRYG IDKPVCFNRK EVKDHGEGGN LIGSPLQGKI LLVDDVITAG TAIRESMELI SANQAELAAV LIALNRKERG KGELSAIQEV ERDYQCQVLS IIDLDDLMQF IEQDPRYSSH LPEMRAYRAE FGV // ID PYRG_HAEIN Reviewed; 545 AA. AC P44341; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=CTP synthase; DE EC=6.3.4.2; DE AltName: Full=CTP synthetase; DE AltName: Full=UTP--ammonia ligase; GN Name=pyrG; OrderedLocusNames=HI_1077; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP (By similarity). {ECO:0000250}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22733.1; -; Genomic_DNA. DR PIR; F64181; F64181. DR RefSeq; NP_439233.1; NC_000907.1. DR RefSeq; WP_005693400.1; NC_000907.1. DR ProteinModelPortal; P44341; -. DR SMR; P44341; 1-542. DR STRING; 71421.HI1077; -. DR EnsemblBacteria; AAC22733; AAC22733; HI_1077. DR GeneID; 950052; -. DR KEGG; hin:HI1077; -. DR PATRIC; 20190813; VBIHaeInf48452_1119. DR eggNOG; ENOG4105C8D; Bacteria. DR eggNOG; COG0504; LUCA. DR KO; K01937; -. DR OMA; MRLGEYE; -. DR OrthoDB; EOG6RC3NR; -. DR PhylomeDB; P44341; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 545 CTP synthase. FT /FTId=PRO_0000138188. FT DOMAIN 291 542 Glutamine amidotransferase type-1. FT REGION 1 253 Aminator domain. FT ACT_SITE 379 379 Nucleophile. {ECO:0000250}. FT ACT_SITE 515 515 {ECO:0000250}. FT ACT_SITE 517 517 {ECO:0000250}. SQ SEQUENCE 545 AA; 60253 MW; 9DBBA18AF811ECA8 CRC64; MATNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPTQHGEV FVTQDGAETD LDLGHYERFI RTKMTKRNNF TTGKIYSEVL RKERRGDYLG ATIQVIPHIT NEIKDRVIAG AQGHDVVIVE VGGTVGDIES LPFLEALRQL AVQVGREHTL FMHLTLVPYI PTAGEVKTKP TQHSVKELLS IGIQPDVLIC RSDRMIPPNE RAKIALFCNV AERAVISLKD VNSIYQIPAL LKSQGLDDFV CERFRLTCPE ADLTEWEQVL YKQANPVGEV TIGMVGKYTE LPDAYKSVNE ALKHAGLTNR LSVNIKYIDS QDVETKGVEV LKGIDGILVP GGFGYRGVEG KIRTAQYARE NKIPYLGICL GMQIALIEYA RNVAGLTKAN SSEFDKDCEQ PVVALITEWQ DAEGNTEVRT DESDLGGTMR LGAQQCHLVS GSRARELYGK ETIEERHRHR YEVNNTLLPQ IEKAGLKVTG LSADKKLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAAYENH KKSVK // ID QSEB_HAEIN Reviewed; 221 AA. AC P45337; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 102. DE RecName: Full=Transcriptional regulatory protein QseB; GN Name=qseB; OrderedLocusNames=HI_1708; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Member of a two-component regulatory system QseB/QseC. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- PTM: Phosphorylated by QseC. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 OmpR/PhoB-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01091}. CC -!- SIMILARITY: Contains 1 response regulatory domain. CC {ECO:0000255|PROSITE-ProRule:PRU00169}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23354.1; -; Genomic_DNA. DR PIR; F64137; F64137. DR RefSeq; NP_439850.1; NC_000907.1. DR RefSeq; WP_005649974.1; NC_000907.1. DR ProteinModelPortal; P45337; -. DR STRING; 71421.HI1708; -. DR EnsemblBacteria; AAC23354; AAC23354; HI_1708. DR GeneID; 950525; -. DR KEGG; hin:HI1708; -. DR PATRIC; 20192167; VBIHaeInf48452_1787. DR eggNOG; ENOG4105XJC; Bacteria. DR eggNOG; ENOG4111FPD; LUCA. DR KO; K07666; -. DR OMA; RREYSIL; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P45337; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Two-component regulatory system. FT CHAIN 1 221 Transcriptional regulatory protein QseB. FT /FTId=PRO_0000081027. FT DOMAIN 2 116 Response regulatory. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. FT DNA_BIND 124 218 OmpR/PhoB-type. {ECO:0000255|PROSITE- FT ProRule:PRU01091}. FT MOD_RES 51 51 4-aspartylphosphate. FT {ECO:0000255|PROSITE-ProRule:PRU00169}. SQ SEQUENCE 221 AA; 24903 MW; 1CA898668BD68A23 CRC64; MRILLIEDDN LIGNGLQIGL TKLGFAVDWF TDGKTGMAAL TSAPYDAVVL DLTLPKLDGL EVLQQWRSNH QDVPVLILTA RDTLDERVKG LQSGADDYLC KPFALAEVAA RLQALIRRRY GYHHSVIEQA GVKLDQNQRS VWLNNQPISL TSREYKLLEL FMLNKDRVLS RSSIEEKLSS WDEEISSGAL DVHIYNLRQK LGKQFIRTVH GVGYALGQVE K // ID QUEE_HAEIN Reviewed; 211 AA. AC P45097; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917}; DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917}; GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917}; GN OrderedLocusNames=HI_1189; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- CC carboxy-7-deazaguanine (CDG), a step common to the biosynthetic CC pathways of all 7-deazapurine-containing compounds. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7- CC carboxy-7-carbaguanine + NH(3). {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- CC deazaguanine synthase family. {ECO:0000255|HAMAP-Rule:MF_00917}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22842.1; -; Genomic_DNA. DR PIR; I64188; I64188. DR RefSeq; NP_439345.1; NC_000907.1. DR RefSeq; WP_005686506.1; NC_000907.1. DR ProteinModelPortal; P45097; -. DR STRING; 71421.HI1189; -. DR DNASU; 950138; -. DR EnsemblBacteria; AAC22842; AAC22842; HI_1189. DR GeneID; 950138; -. DR KEGG; hin:HI1189; -. DR PATRIC; 20191057; VBIHaeInf48452_1241. DR eggNOG; ENOG4105EIZ; Bacteria. DR eggNOG; COG0602; LUCA. DR OMA; RYYLSPC; -. DR OrthoDB; EOG6RJV40; -. DR PhylomeDB; P45097; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00917; QueE; 1. DR InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF000370; QueE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium; KW Metal-binding; Queuosine biosynthesis; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 211 7-carboxy-7-deazaguanine synthase. FT /FTId=PRO_0000169319. FT REGION 22 24 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT REGION 122 124 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 48 48 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 50 50 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 37 37 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 78 78 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 80 80 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00917}. SQ SEQUENCE 211 AA; 24337 MW; FBA0B4106432A99E CRC64; MLMEKYHDFE PNFNIVEIFE SLQGEGFNTG MPSVFVRFGK CNLDCPWCDT PYNNFKRWSV SQILEKVRSF SSKNIIITGG EPTIVPKIEY LLEQFKSDGY FLAIETNGLK AIPAQIDYIA TSPKSLYAHK YEKRCIPFAN EVRIVMDSNM PSFCELIEQK IKAKNYYLSP CEIDGKMNLL ETITLLGQLN QRSNKPKWQL SLQTHKLIGI E // ID QUEF_HAEIN Reviewed; 279 AA. AC P44153; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 110. DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00817}; DE EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00817}; DE AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00817}; DE AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00817}; DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00817}; GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00817}; GN OrderedLocusNames=HI_1291; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). CC {ECO:0000255|HAMAP-Rule:MF_00817}. CC -!- CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7- CC cyano-7-carbaguanine + 2 NADPH. {ECO:0000255|HAMAP-Rule:MF_00817}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00817}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00817}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00817}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type CC 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00817}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22940.1; -; Genomic_DNA. DR PIR; I64024; I64024. DR RefSeq; NP_439443.1; NC_000907.1. DR RefSeq; WP_005694533.1; NC_000907.1. DR ProteinModelPortal; P44153; -. DR SMR; P44153; 19-279. DR STRING; 71421.HI1291; -. DR EnsemblBacteria; AAC22940; AAC22940; HI_1291. DR GeneID; 949405; -. DR KEGG; hin:HI1291; -. DR PATRIC; 20191265; VBIHaeInf48452_1343. DR eggNOG; ENOG4107R1K; Bacteria. DR eggNOG; COG0780; LUCA. DR eggNOG; COG2904; LUCA. DR KO; K06879; -. DR OMA; QCVERIY; -. DR OrthoDB; EOG6D5G0M; -. DR PhylomeDB; P44153; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046857; F:oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00817; QueF_type2; 1. DR InterPro; IPR029500; QueF. DR InterPro; IPR029139; QueF_N. DR InterPro; IPR016428; QueF_type2. DR Pfam; PF14489; QueF; 1. DR Pfam; PF14819; QueF_N; 1. DR PIRSF; PIRSF004750; Nitrile_oxidored_YqcD_prd; 1. DR TIGRFAMs; TIGR03138; QueF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Queuosine biosynthesis; Reference proteome. FT CHAIN 1 279 NADPH-dependent 7-cyano-7-deazaguanine FT reductase. FT /FTId=PRO_0000163035. FT NP_BIND 88 89 NADPH. {ECO:0000255|HAMAP-Rule:MF_00817}. FT NP_BIND 255 256 NADPH. {ECO:0000255|HAMAP-Rule:MF_00817}. FT REGION 86 88 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00817}. FT REGION 226 227 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00817}. FT ACT_SITE 187 187 Thioimide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00817}. FT ACT_SITE 194 194 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00817}. SQ SEQUENCE 279 AA; 32543 MW; 56CB934C2A8DBE22 CRC64; MNYQDNSLKS LKLGQKTEYA SQYDRTLLQP VPRALNRDGL GITQNQPFTI GADIWTAYEI SWLNEKGLPQ VAIADIYLDY QSQNLIESKS FKLYLNSFNQ SKFADFNAVQ QTMQRDLSEC AQGDVKVRLN PMAVYDSQKI DHLQGDCIDE QDIEITSYEF NANWLKDCVS DEIVEEKLVS HLLKSNCLIT NQPDWGTLHI HYVGKKINQE KLLRYVVSFR QHNEFHEQCV ERIFCDLMHY AKPEKLTVYA RYTRRGGLDI NPFRSNFENL PENLRLARQ // ID RADA_HAEIN Reviewed; 458 AA. AC P45266; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498}; DE AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498}; GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; GN OrderedLocusNames=HI_1597; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DNA-dependent ATPase involved in processing of CC recombination intermediates, plays a role in repairing DNA breaks. CC Stimulates the branch migration of RecA-mediated strand transfer CC reactions, allowing the 3' invading strand to extend heteroduplex CC DNA faster. Binds ssDNA in the presence of ADP but not other CC nucleotides, has ATPase activity that is stimulated by ssDNA and CC various branched DNA structures, but inhibited by SSB. Does not CC have RecA's homology-searching function. {ECO:0000255|HAMAP- CC Rule:MF_01498}. CC -!- DOMAIN: Has a putative N-terminal zinc-finger, a middle region CC with homology to RecA with ATPase motifs including the RadA KNRFG CC motif, while the C-terminus is homologous to Lon protease. CC {ECO:0000255|HAMAP-Rule:MF_01498}. CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01498}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23242.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23242.1; ALT_INIT; Genomic_DNA. DR PIR; I64131; I64131. DR RefSeq; NP_439739.2; NC_000907.1. DR RefSeq; WP_005693612.1; NC_000907.1. DR ProteinModelPortal; P45266; -. DR STRING; 71421.HI1597; -. DR MEROPS; S16.004; -. DR DNASU; 950453; -. DR EnsemblBacteria; AAC23242; AAC23242; HI_1597. DR GeneID; 950453; -. DR KEGG; hin:HI1597; -. DR PATRIC; 20191925; VBIHaeInf48452_1670. DR eggNOG; ENOG4105DNJ; Bacteria. DR eggNOG; COG1066; LUCA. DR KO; K04485; -. DR OMA; FEGERGH; -. DR OrthoDB; EOG6DRPHC; -. DR PhylomeDB; P45266; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01498; RadA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PRINTS; PR01874; DNAREPAIRADA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR TIGRFAMs; TIGR00416; sms; 1. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome; KW Stress response; Zinc; Zinc-finger. FT CHAIN 1 458 DNA repair protein RadA. FT /FTId=PRO_0000187927. FT ZN_FING 11 28 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_01498}. FT NP_BIND 100 107 ATP. {ECO:0000255|HAMAP-Rule:MF_01498}. FT REGION 355 458 Lon-protease-like. {ECO:0000255|HAMAP- FT Rule:MF_01498}. FT MOTIF 256 260 RadA KNRFG motif. {ECO:0000255|HAMAP- FT Rule:MF_01498}. SQ SEQUENCE 458 AA; 49371 MW; 5AA547FCD17630B2 CRC64; MAKAPKTAYV CNDCGAEFSR WQGQCSACKA WNTITEVRLI STAKSKNDRF SGYAGETQAK IQTLSEISLQ ETPRFSSGFS ELDRVLGGGI VPGSAILIGG HPGAGKSTLL LQVMCGLAKN MTALYVTGEE SLQQVAMRAS RLGLPSDQLK MLSETSVEQI CNLADQLKPQ IIVVDSIQVM HLADIQSSPG SVAQVRECAS FLTRYAKTRQ VAIIMVGHVT KDGTLAGPKV LEHAIDCSLL LEGEADSRYR TLRSHKNRFG AVNELGVFGM TEQGLREVKN PSAIFLSRGD EITSGSSVMV LWEGTRPLLV EIQALVDHSM LANPRRVAVG LEQNRLALLL AVLHRHGGLQ MADQDVFVNV VGGVKVSETS ADLALLLALI SSFRNRPLPQ DLVIFGEVGL AGEIRPVPSG QERISEAAKH GFKRAIVPFG NKPKSAVENM QVFTVKKLTD ALAVLDNL // ID PYRD_HAEIN Reviewed; 339 AA. AC P45477; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 123. DE RecName: Full=Dihydroorotate dehydrogenase (quinone); DE EC=1.3.5.2; DE AltName: Full=DHOdehase; DE Short=DHOD; DE Short=DHODase; DE AltName: Full=Dihydroorotate oxidase; GN Name=pyrD; OrderedLocusNames=HI_1401; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate CC with quinone as electron acceptor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a CC quinol. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (quinone route): step CC 1/1. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC Type 2 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; L42023; AAC23047.1; -; Genomic_DNA. DR PIR; A64122; A64122. DR RefSeq; NP_439554.1; NC_000907.1. DR RefSeq; WP_005693962.1; NC_000907.1. DR ProteinModelPortal; P45477; -. DR SMR; P45477; 2-338. DR STRING; 71421.HI1401; -. DR EnsemblBacteria; AAC23047; AAC23047; HI_1401. DR GeneID; 950325; -. DR KEGG; hin:HI1401; -. DR PATRIC; 20191501; VBIHaeInf48452_1461. DR eggNOG; ENOG4107QYT; Bacteria. DR eggNOG; COG0167; LUCA. DR KO; K00254; -. DR OMA; TLVRHKM; -. DR OrthoDB; EOG65BDN8; -. DR PhylomeDB; P45477; -. DR UniPathway; UPA00070; UER00946. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00225; DHO_dh_type2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR005719; Dihydroorotate_DH_2. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR TIGRFAMs; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane; KW Oxidoreductase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 339 Dihydroorotate dehydrogenase (quinone). FT /FTId=PRO_0000148444. FT NP_BIND 64 68 FMN. {ECO:0000250}. FT NP_BIND 320 321 FMN. {ECO:0000250}. FT REGION 113 117 Substrate binding. {ECO:0000250}. FT REGION 248 249 Substrate binding. {ECO:0000250}. FT ACT_SITE 177 177 Nucleophile. {ECO:0000250}. FT BINDING 68 68 Substrate. {ECO:0000250}. FT BINDING 88 88 FMN; via amide nitrogen. {ECO:0000250}. FT BINDING 141 141 FMN. {ECO:0000250}. FT BINDING 174 174 FMN. {ECO:0000250}. FT BINDING 174 174 Substrate. {ECO:0000250}. FT BINDING 179 179 Substrate. {ECO:0000250}. FT BINDING 219 219 FMN. {ECO:0000250}. FT BINDING 247 247 FMN; via carbonyl oxygen. {ECO:0000250}. FT BINDING 270 270 FMN; via amide nitrogen. {ECO:0000250}. FT BINDING 299 299 FMN; via amide nitrogen. {ECO:0000250}. SQ SEQUENCE 339 AA; 37271 MW; FC1C327F12F2A47F CRC64; MYQLFRHGIF QMDAEKAHNF TIQCLKLAGN PLFQPILKSL IHAPKGFPKT VMGVNFPNPI GLAAGADKNG DAIDGFGALG FGFLELGTVT PVAQDGNAKP RQFRLIEAEG IINRNGFNNN GIDYLIENVK NARYKGVIGI NIGKNKFTSL EQGKDDYIFC LNKAYNYAGY ITVNISSPNT PDLRQLQYGD YFDDLLRSIK DRQAILANQY NKYVPIAVKI APDLTESELV QIADTLVRHK MDGVIATNTT ISRDTVTGMK NAEQQGGLSG KPLQHKSTEI IKRLHQELKG QIPIIGSGGI DGLQNAQEKI EAGAELLQVY SGLIYHGPKL VKELVKNIK // ID RBFA_HAEIN Reviewed; 128 AA. AC P45141; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; GN OrderedLocusNames=HI_1288; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22937.1; -; Genomic_DNA. DR PIR; A64170; A64170. DR RefSeq; NP_439440.1; NC_000907.1. DR RefSeq; WP_005694530.1; NC_000907.1. DR PDB; 1JOS; X-ray; 1.70 A; A=1-128. DR PDBsum; 1JOS; -. DR ProteinModelPortal; P45141; -. DR SMR; P45141; 7-106. DR STRING; 71421.HI1288; -. DR EnsemblBacteria; AAC22937; AAC22937; HI_1288. DR GeneID; 950218; -. DR KEGG; hin:HI1288; -. DR PATRIC; 20191259; VBIHaeInf48452_1340. DR eggNOG; ENOG4105KG7; Bacteria. DR eggNOG; COG0858; LUCA. DR KO; K02834; -. DR OMA; GFIRSEV; -. DR OrthoDB; EOG6XQ3TJ; -. DR PhylomeDB; P45141; -. DR EvolutionaryTrace; P45141; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_00003; RbfA; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR000238; Ribosome-bd_facA. DR InterPro; IPR023799; Ribosome-bd_facA_dom. DR InterPro; IPR020053; Ribosome-bd_factorA_CS. DR Pfam; PF02033; RBFA; 1. DR ProDom; PD007327; Rib_bd_factA; 1. DR SUPFAM; SSF89919; SSF89919; 1. DR TIGRFAMs; TIGR00082; rbfA; 1. DR PROSITE; PS01319; RBFA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW rRNA processing. FT CHAIN 1 128 Ribosome-binding factor A. FT /FTId=PRO_0000102670. FT HELIX 8 26 {ECO:0000244|PDB:1JOS}. FT TURN 30 32 {ECO:0000244|PDB:1JOS}. FT STRAND 35 42 {ECO:0000244|PDB:1JOS}. FT STRAND 48 56 {ECO:0000244|PDB:1JOS}. FT HELIX 61 73 {ECO:0000244|PDB:1JOS}. FT HELIX 75 86 {ECO:0000244|PDB:1JOS}. FT STRAND 93 98 {ECO:0000244|PDB:1JOS}. SQ SEQUENCE 128 AA; 14805 MW; 9E274DC1240D64DF CRC64; MAREFKRSDR VAQEIQKEIA VILQREVKDP RIGMVTVSDV EVSSDLSYAK IFVTFLFDHD EMAIEQGMKG LEKASPYIRS LLGKAMRLRI VPEIRFIYDQ SLVEGMRMSN LVTNVVREDE KKHVEESN // ID PYRF_HAEIN Reviewed; 230 AA. AC P43812; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; GN OrderedLocusNames=HI_1224; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'- CC monophosphate (OMP) to uridine 5'-monophosphate (UMP). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01200}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22877.1; -; Genomic_DNA. DR PIR; B64111; B64111. DR RefSeq; NP_439380.1; NC_000907.1. DR RefSeq; WP_005667227.1; NC_000907.1. DR ProteinModelPortal; P43812; -. DR SMR; P43812; 3-229. DR STRING; 71421.HI1224; -. DR EnsemblBacteria; AAC22877; AAC22877; HI_1224. DR GeneID; 950791; -. DR KEGG; hin:HI1224; -. DR PATRIC; 20191127; VBIHaeInf48452_1276. DR eggNOG; ENOG4106EG9; Bacteria. DR eggNOG; COG0284; LUCA. DR KO; K01591; -. DR OMA; NFKIFLD; -. DR OrthoDB; EOG6N6815; -. DR PhylomeDB; P43812; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01200_B; OMPdecase_type1_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis; KW Reference proteome. FT CHAIN 1 230 Orotidine 5'-phosphate decarboxylase. FT /FTId=PRO_0000134546. FT REGION 59 68 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT ACT_SITE 61 61 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 10 10 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 32 32 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 119 119 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 180 180 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 189 189 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 209 209 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01200}. FT BINDING 210 210 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. SQ SEQUENCE 230 AA; 25192 MW; 14E8E825DBC767D9 CRC64; MTSKIIVALD FEKEAEALAL VDQIDPSLCR LKVGKEMFTT LGINFVKQLH QRNFDVFLDL KYHDIPNTVA RAVRSAADLG VWMVDLHASG GLRMMEDAKK ILEPYGKDAP LLIAVTVLTS MEDLDLLQIG INASPMEQVL RLAHLTQRAG LDGVVCSPQE VEILRNACGE DFKLVTPGIR PIGTDFGDQR RVMTPTAAIR AGSDYLVIGR PITQADNPAE VLRSINVSIG // ID QUEA_HAEIN Reviewed; 363 AA. AC P44595; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113}; DE EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113}; DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113}; GN Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; GN OrderedLocusNames=HI_0245; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet CC to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give CC epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 7-aminomethyl-7- CC carbaguanosine(34) in tRNA = L-methionine + adenine + CC epoxyqueuosine(34) in tRNA. {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}. CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|HAMAP- CC Rule:MF_00113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21912.1; -; Genomic_DNA. DR PIR; B64057; B64057. DR RefSeq; NP_438415.1; NC_000907.1. DR RefSeq; WP_005694057.1; NC_000907.1. DR ProteinModelPortal; P44595; -. DR STRING; 71421.HI0245; -. DR EnsemblBacteria; AAC21912; AAC21912; HI_0245. DR GeneID; 949371; -. DR KEGG; hin:HI0245; -. DR PATRIC; 20189015; VBIHaeInf48452_0260. DR eggNOG; ENOG4105E2N; Bacteria. DR eggNOG; COG0809; LUCA. DR KO; K07568; -. DR OMA; YGDAMFL; -. DR OrthoDB; EOG6X6RBB; -. DR PhylomeDB; P44595; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central. DR HAMAP; MF_00113; QueA; 1. DR InterPro; IPR003699; QueA. DR Pfam; PF02547; Queuosine_synth; 1. DR SUPFAM; SSF111337; SSF111337; 1. DR TIGRFAMs; TIGR00113; queA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Queuosine biosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 363 S-adenosylmethionine:tRNA FT ribosyltransferase-isomerase. FT /FTId=PRO_0000165407. SQ SEQUENCE 363 AA; 40629 MW; 225D526C5F046863 CRC64; MRVSDFNFDL PDELIARYPK TDRVSCRLLQ LNGENGEIFH RTFSDVLDLI DEGDLLIFNN TRVIPARMFG RKASGGKIEV LVERMLDEHR FLAHIRSSKS PKEGAELFLG EDKLGENNGI KAVMKARHGA LFEVELSDKS TALLDVLQTI GHMPLPPYID RPDEEADQEC YQTVYSKVPG AVAAPTAGLH FDENLLEKLK AKGVNFEFVT LHVGAGTFQP VRVENIEDHV MHAEYVEVSQ EVCNAIIATK KAGKRVIAVG TTSVRSIESA ALSAEEFGNP DLIEPYFSDT SIFIYPGKKF RVVDCLITNF HLPESTLIML VSAFAGYKNT MNAYKHAVKE KYRFFSYGDA MFINKNSNVR GLE // ID RBSB_HAEIN Reviewed; 292 AA. AC P44737; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 105. DE RecName: Full=Ribose import binding protein RbsB {ECO:0000250|UniProtKB:P02925}; DE Flags: Precursor; GN Name=rbsB; OrderedLocusNames=HI_0504; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 24-30. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in CC ribose import. Binds ribose. {ECO:0000250|UniProtKB:P02925}. CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), CC two transmembrane proteins (RbsC) and a solute-binding protein CC (RbsB). {ECO:0000250|UniProtKB:P02925}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P02925}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 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; L42023; AAC22162.1; -; Genomic_DNA. DR PIR; A64073; A64073. DR RefSeq; NP_438662.1; NC_000907.1. DR RefSeq; WP_005693669.1; NC_000907.1. DR ProteinModelPortal; P44737; -. DR SMR; P44737; 24-290. DR STRING; 71421.HI0504; -. DR EnsemblBacteria; AAC22162; AAC22162; HI_0504. DR GeneID; 949573; -. DR KEGG; hin:HI0504; -. DR PATRIC; 20189561; VBIHaeInf48452_0523. DR eggNOG; ENOG4105E9V; Bacteria. DR eggNOG; COG1879; LUCA. DR KO; K10439; -. DR OMA; MENILQS; -. DR OrthoDB; EOG61P6T8; -. DR PhylomeDB; P44737; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Periplasm; KW Reference proteome; Signal; Sugar transport; Transport. FT SIGNAL 1 23 {ECO:0000269|PubMed:10675023}. FT CHAIN 24 292 Ribose import binding protein RbsB. FT /FTId=PRO_0000031735. SQ SEQUENCE 292 AA; 30315 MW; 4DD3F259BF3F95A6 CRC64; MKKLTALTSA VLLGLAVSSS ASAQDTIALA VSTLDNPFFV TLKDGAQKKA DELGYKLVVL DSQNDPAKEL ANIEDLTVRG AKILLINPTA SEAVGNAVAI ANRKHIPVIT LDRGAAKGNV VSHIASDNIA GGKMAGDFIA QKLGDNAKVI QLEGIAGTSA ARERGEGFKQ AIDAHKFNVL ASQPADFDRT KGLNVTENLL ASKGDVQAIF AQNDEMALGA LRAVKAANKK VLIVGFDGTD DGVKAVKSGK MAATIAQQPE LIGSLGVVTA DKILKGEKVE AKIPVDLKVI SE // ID QSEC_HAEIN Reviewed; 451 AA. AC P45336; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 124. DE RecName: Full=Sensor protein QseC; DE EC=2.7.13.3; GN Name=qseC; OrderedLocusNames=HI_1707; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Member of a two-component regulatory system QseB/QseC. CC May activate QseB by phosphorylation (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00102}. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23353.1; -; Genomic_DNA. DR PIR; E64137; E64137. DR RefSeq; NP_439849.1; NC_000907.1. DR RefSeq; WP_005694197.1; NC_000907.1. DR ProteinModelPortal; P45336; -. DR STRING; 71421.HI1707; -. DR EnsemblBacteria; AAC23353; AAC23353; HI_1707. DR GeneID; 950868; -. DR KEGG; hin:HI1707; -. DR PATRIC; 20192165; VBIHaeInf48452_1786. DR eggNOG; ENOG4105DHQ; Bacteria. DR eggNOG; ENOG410XS4R; LUCA. DR KO; K07645; -. DR OMA; FGQMWIW; -. DR OrthoDB; EOG6G4VQG; -. DR PhylomeDB; P45336; -. DR BRENDA; 2.7.13.3; 2529. DR Proteomes; UP000000579; 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR013727; 2CSK_N. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF08521; 2CSK_N; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; KW Two-component regulatory system. FT CHAIN 1 451 Sensor protein QseC. FT /FTId=PRO_0000074705. FT TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 10 31 Helical. {ECO:0000255}. FT TOPO_DOM 32 162 Periplasmic. {ECO:0000255}. FT TRANSMEM 163 180 Helical. {ECO:0000255}. FT TOPO_DOM 181 451 Cytoplasmic. {ECO:0000255}. FT DOMAIN 181 233 HAMP. {ECO:0000255|PROSITE- FT ProRule:PRU00102}. FT DOMAIN 241 451 Histidine kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00107}. FT MOD_RES 244 244 Phosphohistidine; by autocatalysis. FT {ECO:0000255|PROSITE-ProRule:PRU00107}. SQ SEQUENCE 451 AA; 51271 MW; 00C86B648128D383 CRC64; MKNRSLTLRL ISVLCLTALF VWLGSTLVAW WQVRHDVNKV FDAQQVLFAE RLANSDLSTI LLESSTTLNK NSQSVLKKSY DDDALAFAIF SKTGKLLFSD GRNGKDFIFN YKTGFYNANI YDDDDKWRIF WRMAANGELV IAVGQELDYR EDLIEEMILG QMWIWFASLP ILIIVLGWLI HKELRPIKRL SQEVQTRKSG DVSLLNTEGL PVEILPLVKN LNQFFDRTSA MLQRERRFTS DAAHELRSPL AALRIQIEVA QLAGDDVALR EQALLHLTQG IDRASQLIEQ LLTLSRLDNL QALETLQLLD WEAIVQSLIS ERYFVAEKRK ITLVFEKESE PKQKQGQSIL VSLMLRNLLD NAIKYCPEDT IVSVKISSSQ IIIEDNGGGV EPEDLKKLGQ RFYRPAGQNE KGSGLGLSIV MRIAELHGFK VRLENVVKEG RRIGLKAIIS L // ID QUED_HAEIN Reviewed; 141 AA. AC P44123; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase; DE Short=CPH4 synthase; DE EC=4.1.2.50; DE AltName: Full=Queuosine biosynthesis protein QueD; GN Name=queD; OrderedLocusNames=HI_1190; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin CC triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) CC and acetaldehyde. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O = CC 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC -!- MISCELLANEOUS: The active site is at the interface between 2 CC subunits. The proton acceptor Cys is on one subunit, and the CC charge relay system is on the other subunit (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PTPS family. QueD 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; L42023; AAC22843.1; -; Genomic_DNA. DR PIR; F64021; F64021. DR RefSeq; NP_439346.1; NC_000907.1. DR RefSeq; WP_005663812.1; NC_000907.1. DR ProteinModelPortal; P44123; -. DR STRING; 71421.HI1190; -. DR EnsemblBacteria; AAC22843; AAC22843; HI_1190. DR GeneID; 950142; -. DR KEGG; hin:HI1190; -. DR PATRIC; 20191059; VBIHaeInf48452_1242. DR eggNOG; ENOG4107ZIF; Bacteria. DR eggNOG; COG0720; LUCA. DR KO; K01737; -. DR OMA; MVVWIFE; -. DR OrthoDB; EOG6FFSCJ; -. DR PhylomeDB; P44123; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR PANTHER; PTHR12589; PTHR12589; 1. DR Pfam; PF01242; PTPS; 1. DR TIGRFAMs; TIGR00039; 6PTHBS; 1. DR TIGRFAMs; TIGR03367; queuosine_QueD; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Queuosine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 141 6-carboxy-5,6,7,8-tetrahydropterin FT synthase. FT /FTId=PRO_0000057925. FT ACT_SITE 23 23 Proton acceptor. {ECO:0000250}. FT ACT_SITE 71 71 Charge relay system. {ECO:0000250}. FT ACT_SITE 131 131 Charge relay system. {ECO:0000250}. FT METAL 14 14 Zinc. {ECO:0000250}. FT METAL 27 27 Zinc. {ECO:0000250}. FT METAL 29 29 Zinc. {ECO:0000250}. SQ SEQUENCE 141 AA; 16322 MW; 6843517DEA5A7C3E CRC64; MFKISKEFSF DMAHLLDGHD GKCQNLHGHT YKLQVEISGD LYKSGAKKAM VIDFSDLKSI VKKVILDPMD HAFIYDQTNE RESQIATLLQ KLNSKTFGVP FRTTAEEIAR FIFNRLKHDE QLSISSIRLW ETPTSFCEYQ E // ID RBSA_HAEIN Reviewed; 493 AA. AC P44735; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 114. DE RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716}; DE EC=3.6.3.17 {ECO:0000255|HAMAP-Rule:MF_01716}; GN Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716}; GN OrderedLocusNames=HI_0502; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in CC ribose import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + monosaccharide(Out) = ADP + CC phosphate + monosaccharide(In). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), CC two transmembrane proteins (RbsC) and a solute-binding protein CC (RbsB). {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01716}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose CC importer (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_01716}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22160.1; -; Genomic_DNA. DR PIR; H64072; H64072. DR RefSeq; NP_438660.1; NC_000907.1. DR RefSeq; WP_005693671.1; NC_000907.1. DR ProteinModelPortal; P44735; -. DR STRING; 71421.HI0502; -. DR DNASU; 950602; -. DR EnsemblBacteria; AAC22160; AAC22160; HI_0502. DR GeneID; 950602; -. DR KEGG; hin:HI0502; -. DR PATRIC; 20189557; VBIHaeInf48452_0521. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR KO; K10441; -. DR OMA; TEVMRTI; -. DR OrthoDB; EOG6QK4RR; -. DR PhylomeDB; P44735; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015591; F:D-ribose transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015407; F:monosaccharide-transporting ATPase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015861; ABC_transpr_RbsA. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS51254; RBSA; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Sugar transport; Transport. FT CHAIN 1 493 Ribose import ATP-binding protein RbsA. FT /FTId=PRO_0000092957. FT DOMAIN 5 241 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT DOMAIN 252 491 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_01716}. FT NP_BIND 37 44 ATP. {ECO:0000255|HAMAP-Rule:MF_01716}. SQ SEQUENCE 493 AA; 54157 MW; 9C686A9FA0B79126 CRC64; METLLKISGV DKSFPGVKAL NNACLSVYAG RVMALMGENG AGKSTLMKVL TGIYSKDAGT IEYLNRSVNF NGPKASQEAG ISIIHQELNL VGNLTIAENI FLGREFKTSW GAINWQKMHQ EADKLLARLG VTHSSKQLCA ELSIGEQQMV EIAKALSFES KVIIMDEPTD ALTDTETEAL FNVIRELKAE NRGIVYISHR LKEIFQICDD VTVLRDGQFI GERVMAEITE DDLIEMMVGR RLDEQYPHLS QEKGECVLDV KHVSGSGIDD VSFKLHAGEI VGVSGLMGAG RTELGKLLYG ALPKTAGKVR LKNQEIENRS PQDGLDNGIV YISEDRKGDG LVLGMSVKEN MSLTSLDHFS QKGGIRHQAE KMAVDDFILM FNIKTPNRDQ QVGLLSGGNQ QKVAIARGLM TRPNVLILDE PTRGVDVGAK KEIYQLINEF KKEGLSILMI SSDMPEVLGM SDRVLVMREG KISAEFSREE ATQEKLLAAA IGK // ID RBSC_HAEIN Reviewed; 323 AA. AC P44736; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Ribose import permease protein RbsC {ECO:0000250|UniProtKB:P0AGI1}; GN Name=rbsC; OrderedLocusNames=HI_0503; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in CC ribose import. Probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250|UniProtKB:P0AGI1}. CC -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), CC two transmembrane proteins (RbsC) and a solute-binding protein CC (RbsB). {ECO:0000250|UniProtKB:P0AGI1}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000250|UniProtKB:P0AGI1}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. AraH/RbsC 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; L42023; AAC22161.1; -; Genomic_DNA. DR PIR; I64072; I64072. DR RefSeq; NP_438661.1; NC_000907.1. DR RefSeq; WP_005693670.1; NC_000907.1. DR STRING; 71421.HI0503; -. DR EnsemblBacteria; AAC22161; AAC22161; HI_0503. DR GeneID; 949666; -. DR KEGG; hin:HI0503; -. DR PATRIC; 20189559; VBIHaeInf48452_0522. DR eggNOG; ENOG4105CNN; Bacteria. DR eggNOG; COG1172; LUCA. DR KO; K10440; -. DR OMA; LAVMIDN; -. DR OrthoDB; EOG61P6T8; -. DR PhylomeDB; P44736; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 323 Ribose import permease protein RbsC. FT /FTId=PRO_0000060226. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. SQ SEQUENCE 323 AA; 33969 MW; BB033CB7A7971A6F CRC64; MMKNETSNFQ IGRFLIEQRS FIALIILIAI VSMINPDFFS VDNILNILRQ TSVNAIIAVG MTFVILIAGI DLSVGSVLAL TGAIAASMVS IELPIFLVIP VVLLIGTLLG GISGVIVAKG KVQAFIATLV TMTLLRGITM VYTDGRPITT GFSDNADLFA SIGTGYVLGI PVPIWIMSIV FAVAWYILKD TPIGRYIYAL GGNEAATQLS GINVNKIKVF VFAVSGFLSA LAGLIVTSRL SSAQPTAGVS YELDAIAAVV VGGTSLMGGK GRVMGTLIGA LIIGFLNNAL NLLDISSYYQ MIAKALVILV AVLADNYLGT KKL // ID REC2_HAEIN Reviewed; 788 AA. AC P44408; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=Recombination protein 2; GN Name=rec2; Synonyms=rec-2; OrderedLocusNames=HI_0061; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BC200; RX PubMed=8063112; DOI=10.1016/0378-1119(94)90840-0; RA Clifton S.W., McCarthy D., Roe B.A.; RT "Sequence of the rec-2 locus of Haemophilus influenzae: homologies to RT comE-ORF3 of Bacillus subtilis and msbA of Escherichia coli."; RL Gene 146:95-100(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Might contribute to transformation as a member of a CC membrane-bound pore complex at the base of the transformasome. It CC could directly interact with transforming DNA during translocation CC indirectly by participating in the assembly of the pore. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L20805; AAC13733.1; -; Genomic_DNA. DR EMBL; L42023; AAC21739.1; -; Genomic_DNA. DR PIR; I64045; I64045. DR RefSeq; NP_438234.1; NC_000907.1. DR RefSeq; WP_005693861.1; NC_000907.1. DR ProteinModelPortal; P44408; -. DR STRING; 71421.HI0061; -. DR TCDB; 3.A.11.2.2; the bacterial competence-related dna transformation transporter (dna-t) family. DR EnsemblBacteria; AAC21739; AAC21739; HI_0061. DR GeneID; 950960; -. DR KEGG; hin:HI0061; -. DR PATRIC; 20188575; VBIHaeInf48452_0061. DR eggNOG; ENOG4108EQH; Bacteria. DR eggNOG; COG0658; LUCA. DR eggNOG; COG2333; LUCA. DR KO; K02238; -. DR OMA; GFDYEAW; -. DR OrthoDB; EOG647TTM; -. DR PhylomeDB; P44408; -. DR Proteomes; UP000000579; 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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR004477; ComEC_N. DR InterPro; IPR004797; Competence_ComEC/Rec2. DR InterPro; IPR025405; DUF4131. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF03772; Competence; 1. DR Pfam; PF13567; DUF4131; 1. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00360; ComEC_N-term; 1. DR TIGRFAMs; TIGR00361; ComEC_Rec2; 1. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Competence; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 788 Recombination protein 2. FT /FTId=PRO_0000097224. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 313 333 Helical. {ECO:0000255}. FT TRANSMEM 367 387 Helical. {ECO:0000255}. FT TRANSMEM 401 421 Helical. {ECO:0000255}. FT TRANSMEM 434 454 Helical. {ECO:0000255}. FT TRANSMEM 456 476 Helical. {ECO:0000255}. FT TRANSMEM 508 528 Helical. {ECO:0000255}. FT CONFLICT 748 788 VENTAVSGQVRVNFFQDRLEIQQARTKFSPWYARVIGLSKE FT -> GRKYRCFGASAGKFFSRPIRNPASSHKIFPLVCACNWI FT IKGIKGTMRAIFTIR (in Ref. 1; AAC13733). FT {ECO:0000305}. SQ SEQUENCE 788 AA; 89356 MW; F31104595CB4E47A CRC64; MKLNLITLVV LLIVADLTLL FLPQPLLLPW QVALVIALVL IFLFIFLRRN FLVSLAFFVA SLGYFHYSAL SLSQQAQNIT AQKQVVTFKI QEILHQQDYQ TLIATATLEN NLQEQRIFLN WKAKEVPQLS EIWQAEISLR SLSARLNFGG FDRQQWYFSK GITAVGTVKS AVKIADVSSL RAEKLQQVKK QTEGLSLQGL LIALAFGERA WLDKTTWSIY QQTNTAHLIA ISGLHIGLAM GIGFCLARVV QVFFPTRFIH PYFPLVFGVL FALIYAYLAG FSVPTFRAIS ALVFVLFIQI MRRHYSPIQF FTLVVGFLLF CDPLMPLSVS FWLSCGAVGC LLLWYRYVPF SLFQWKNRPF SPKVRWIFSL FHLQFGLLLF FTPLQLFLFN GLSLSGFLAN FMAVPIYSFL LVPLILFAVF TNGTMFSWQL ANKLAEGITG LISVFQGNWL TVSFNLALGL TALCAGIFML IIWNIYREPE ISSSNWQIKR AKFFTLNLSK PLLKNERINV LRCSFGIILL CFTILLFKQL SKPTWQVDTL DVGQGLATLI VKNGKGILYD TGSSWRGGSM AELEILPYLQ REGIVLEKLI LSHDDNDHAG GASTILKAYP NVELITPSRK NYGENYRTFC TAGRDWHWQG LHFQILSPHN VVTRADNSHS CVILVDDGKN SVLLTGDAEA KNEQIFARTL GKIDVLQVGH HGSKTSTSEY LLSQVRPDVA IISSGRWNPW KFPHYSVMER LHRYKSAVEN TAVSGQVRVN FFQDRLEIQQ ARTKFSPWYA RVIGLSKE // ID RECA_HAEIN Reviewed; 354 AA. AC P43705; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268}; DE AltName: Full=Recombinase 1; DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268}; GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; Synonyms=rec-1, rec1; GN OrderedLocusNames=HI_0600; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8226674; RA Zulty J.J., Barcak G.J.; RT "Structural organization, nucleotide sequence, and regulation of the RT Haemophilus influenzae rec-1+ gene."; RL J. Bacteriol. 175:7269-7281(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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. Plays a CC central role in DNA metabolism, participating in general CC homologous recombination, recombinational (postreplication) DNA CC repair, and prophage induction. 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; L07529; AAC36817.1; -; Unassigned_DNA. DR EMBL; L42023; AAC22257.1; -; Genomic_DNA. DR PIR; A49929; A49929. DR RefSeq; NP_438757.1; NC_000907.1. DR RefSeq; WP_005654959.1; NC_000907.1. DR ProteinModelPortal; P43705; -. DR STRING; 71421.HI0600; -. DR PRIDE; P43705; -. DR EnsemblBacteria; AAC22257; AAC22257; HI_0600. DR GeneID; 949644; -. DR KEGG; hin:HI0600; -. DR PATRIC; 20189757; VBIHaeInf48452_0621. DR eggNOG; ENOG4105C68; Bacteria. DR eggNOG; COG0468; LUCA. DR KO; K03553; -. DR OMA; TRKGAWY; -. DR OrthoDB; EOG6ZKXNZ; -. DR PhylomeDB; P43705; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.30.250.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00268; RecA; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013765; DNA_recomb/repair_RecA. DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR023400; RecA_C. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR PANTHER; PTHR22942:SF1; PTHR22942:SF1; 1. DR Pfam; PF00154; RecA; 1. DR PRINTS; PR00142; RECA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54752; SSF54752; 1. DR TIGRFAMs; TIGR02012; tigrfam_recA; 1. DR PROSITE; PS00321; RECA_1; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. PE 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 1 354 Protein RecA. FT /FTId=PRO_0000122722. FT NP_BIND 67 74 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. SQ SEQUENCE 354 AA; 38133 MW; C25C01D2FD4AF7C5 CRC64; MATQEEKQKA LAAALGQIEK QFGKGSIMKL GDTKTLDVES ISTGSLGLDV ALGIGGLPMG RIVEIFGPES SGKTTLTLSV IAQAQKAGKT CAFIDAEHAL DPIYAAKLGV DVKELFVSQP DNGEQALEIC DALVRSGAID VIIVDSVAAL TPKAEIEGDM GDSHMGLQAR LMSQALRKLT GQIKNANCLV VFINQIRMKI GVMFGNPETT TGGNALKFYS SVRLDIRRTG SVKDGENIIG NETRVKVVKN KLAAPFRQVD FQILYGEGIS KAGELLELGV KHKLVEKSGA WYSYNGEKIG QGKANSMKWL NENIEKSDEL EARLRAELVA NPEQALMADI EQSENNTESE SDFE // ID REP_HAEIN Reviewed; 670 AA. AC P44804; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000255|HAMAP-Rule:MF_01920}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01920}; GN Name=rep {ECO:0000255|HAMAP-Rule:MF_01920}; OrderedLocusNames=HI_0649; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase CC involved in DNA replication; it can initiate unwinding at a nick CC in the DNA. It binds to the single-stranded DNA and acts in a CC progressive fashion along the DNA in the 3' to 5' direction. CC {ECO:0000255|HAMAP-Rule:MF_01920}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01920}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01920}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01920}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01920}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22309.1; -; Genomic_DNA. DR RefSeq; NP_438809.1; NC_000907.1. DR RefSeq; WP_010869028.1; NC_000907.1. DR ProteinModelPortal; P44804; -. DR SMR; P44804; 2-641. DR STRING; 71421.HI0649; -. DR EnsemblBacteria; AAC22309; AAC22309; HI_0649. DR GeneID; 949695; -. DR KEGG; hin:HI0649; -. DR PATRIC; 20189913; VBIHaeInf48452_0678. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR KO; K03656; -. DR OMA; EKVLMQN; -. DR OrthoDB; EOG64N9TW; -. DR PhylomeDB; P44804; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 4. DR HAMAP; MF_01920; Helicase_Rep; 1. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR005752; Helicase_Rep. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01074; rep; 1. 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 replication; DNA-binding; KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome. FT CHAIN 1 670 ATP-dependent DNA helicase Rep. FT /FTId=PRO_0000102069. FT DOMAIN 1 280 UvrD-like helicase ATP-binding. FT {ECO:0000255|HAMAP-Rule:MF_01920}. FT DOMAIN 281 563 UvrD-like helicase C-terminal. FT {ECO:0000255|HAMAP-Rule:MF_01920}. FT NP_BIND 22 29 ATP. {ECO:0000255|HAMAP-Rule:MF_01920}. FT BINDING 278 278 ATP. {ECO:0000255|HAMAP-Rule:MF_01920}. SQ SEQUENCE 670 AA; 77746 MW; 802A131251ED4E24 CRC64; MKLNPQQQQA VEYVTGPCLV LAGAGSGKTR VIINKIAHLI EKCGYSPKQI AAVTFTNKAA REMKERVAHS IGKEQSKGLL VSTFHTLGFD ILKREYKALG FKSNMTLFDE HDQFALLKEL TADVLKEDKD LLRELISVIS NWKNDLISPK QAFALARDAK YQTFAKCYER YATQIRTYNA LDFDDLIMLP TLLFKQNEEV RSKWQAKIRY LLVDEYQDTN TSQYELIKLL VGDRACFTVV GDDDQSIYSW RGARPENMVR LRDDFPRLNV IKLEQNYRST QRILHCANIL IDNNEHVFDK KLFSTIGKGE KLLVIEAKNE EHEAERIVAE LIAHRFSRKT KYKDYAILYR GNHQSRLLEK VLMQNRIPYK ISGGTSFFSR AEIKDMMAYL RLVVNQDDDA AFLRIVNTPK REIGTATLQK LGELAQEKHI SLFEAIFEFE LIQRITPKAY DSLQKFGRWI VELNDEIQRS EPERAVRSML SAIHYEEYLY EYATSPKAAE MQSKNVATLF DWVADMLKGD ETNEPMNLNQ VVTRLTLRDM LERGEDDDDS DQVQLMTLHA SKGLEFPYVY LIGMEEGILP HQTSIDEDNV EEERRLAYVG ITRAQKELTF SLCRERRQYG ELVRPEPSRF LAELPNDDVL WERDKPKLTT EQKQEKTQNQ LDRLRAILKS // ID RAPA_HAEIN Reviewed; 923 AA. AC P44781; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=RNA polymerase-associated protein RapA {ECO:0000255|HAMAP-Rule:MF_01821}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01821}; DE AltName: Full=ATP-dependent helicase HepA {ECO:0000255|HAMAP-Rule:MF_01821}; GN Name=rapA {ECO:0000255|HAMAP-Rule:MF_01821}; Synonyms=hepA; GN OrderedLocusNames=HI_0616; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transcription regulator that activates transcription by CC stimulating RNA polymerase (RNAP) recycling in case of stress CC conditions such as supercoiled DNA or high salt concentrations. CC Probably acts by releasing the RNAP, when it is trapped or CC immobilized on tightly supercoiled DNA. Does not activate CC transcription on linear DNA. Probably not involved in DNA repair. CC {ECO:0000255|HAMAP-Rule:MF_01821}. CC -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the CC core RNAP than for the holoenzyme. Its ATPase activity is CC stimulated by binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01821}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01821}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01821}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22275.1; -; Genomic_DNA. DR PIR; H64081; H64081. DR RefSeq; NP_438774.1; NC_000907.1. DR RefSeq; WP_005692755.1; NC_000907.1. DR ProteinModelPortal; P44781; -. DR STRING; 71421.HI0616; -. DR EnsemblBacteria; AAC22275; AAC22275; HI_0616. DR GeneID; 949665; -. DR KEGG; hin:HI0616; -. DR PATRIC; 20189815; VBIHaeInf48452_0640. DR eggNOG; ENOG4105BZK; Bacteria. DR eggNOG; COG0553; LUCA. DR KO; K03580; -. DR OMA; HHLVLFD; -. DR OrthoDB; EOG6D2KQT; -. DR PhylomeDB; P44781; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01821; Helicase_RapA; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR023949; Helicase_RapA. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022737; RapA_C. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF12137; RapA_C; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW Activator; ATP-binding; Complete proteome; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 923 RNA polymerase-associated protein RapA. FT /FTId=PRO_0000207177. FT DOMAIN 162 332 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_01821}. FT DOMAIN 443 597 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_01821}. FT NP_BIND 175 182 ATP. {ECO:0000255|HAMAP-Rule:MF_01821}. FT MOTIF 278 281 DEAH box. SQ SEQUENCE 923 AA; 104405 MW; 8022403581DAADBD CRC64; MPFAIGQRWL SESENALGLG VITALDQRTV TIYFPAADET RIYAMAQAPL SRIVFSKGET LSHQAGWQGE ILDVQNMNGL LFYLVKNPQD EDVIVQERDI SPIISFSQAK DRLFSAQIDR STHFALRYRT LCHQQAQFKS PLRGLRGTRA SLIPHQLHIA AEVGNRVNPR VLLADEVGLG KTIEAGMILQ NQLFAEKVQR VLIIVPETLQ HQWLVEMLRR FNLHFALFDE ERCNDFDLDA VNPFTTESLI ICSLNWLETH PNRVELVLNA QFDCLIVDEA HHLVWSETSP STAYLLVEQL ARIIPSVLLL TATPEQLGQE SHFARLRLLD PERFFDYQTF VKEQEHYQPV VNAVESLLAN KALSAVEKNH ISDLLLEQDV EPLFKAIASN NDEEQQRARQ ELIQALIDRH GTGRMLFRNT RQGVKGFPHR VYHQITLSEE NDKIDWLIDF LKLHRNEKIF VICQTAATAI QLEQILRERE AIRAAVFHEK MSIIERDRAA AYFADLENGA QVLLSSSIGS EGRNFQFAAN LVLFDLPTNP DLLEQCIGRL DRIGQKRDVQ VYVPCAKDSP QSRLARWYNE GLNAFEQTCP MGMALFSQFA DELEKVRSNS TALSENEFSG LLKQTKTARE KLKIELEKGR DRLLELNSHG GEQAQALADQ IADEDNSPEL VNFALKLFDI IGVEQEDLGA NSIVISPTGT MLVPDFPGLK EEGVTVTFDR ELALAREEME FLTWDHPMIR QGIDLVASGD IGKAAMALLV NKQLPAGTLL IELIYVVESQ SPKGLQLNRF LPPTPIRLLL DNKGNNIGEQ VAFETLHSKL KPLGKNITNQ MVKMARSNIE SLIMRGDQLV KSLAEPIIAE AKNQADQQLS AEINRLQALR AVNKNIRQSE IDILEQQRTQ SLDELSKANW RLDCLRVIVT NKE // ID RBSK_HAEIN Reviewed; 306 AA. AC P44331; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_01987}; DE Short=RK {ECO:0000255|HAMAP-Rule:MF_01987}; DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_01987}; GN Name=rbsK {ECO:0000255|HAMAP-Rule:MF_01987}; GN OrderedLocusNames=HI_0505; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a CC reaction requiring ATP and magnesium. The resulting D-ribose-5- CC phosphate can then be used either for sythesis of nucleotides, CC histidine, and tryptophan, or as a component of the pentose CC phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_01987}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose = ADP + D-ribose 5-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01987}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01987}; CC Note=Requires a divalent cation, most likely magnesium in vivo, as CC an electrophilic catalyst to aid phosphoryl group transfer. It is CC the chelate of the metal and the nucleotide that is the actual CC substrate. {ECO:0000255|HAMAP-Rule:MF_01987}; CC -!- ENZYME REGULATION: Activated by a monovalent cation that binds CC near, but not in, the active site. The most likely occupant of the CC site in vivo is potassium. Ion binding induces a conformational CC change that may alter substrate affinity. {ECO:0000255|HAMAP- CC Rule:MF_01987}. CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose CC 5-phosphate from beta-D-ribopyranose: step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01987}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01987}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01987}. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC Ribokinase subfamily. {ECO:0000255|HAMAP-Rule:MF_01987}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22163.1; -; Genomic_DNA. DR PIR; B64073; B64073. DR RefSeq; NP_438663.1; NC_000907.1. DR RefSeq; WP_005693668.1; NC_000907.1. DR ProteinModelPortal; P44331; -. DR SMR; P44331; 4-305. DR STRING; 71421.HI0505; -. DR EnsemblBacteria; AAC22163; AAC22163; HI_0505. DR GeneID; 949575; -. DR KEGG; hin:HI0505; -. DR PATRIC; 20189563; VBIHaeInf48452_0524. DR eggNOG; ENOG4108RVA; Bacteria. DR eggNOG; COG0524; LUCA. DR KO; K00852; -. DR OMA; NADHVIS; -. DR OrthoDB; EOG64JFMD; -. DR PhylomeDB; P44331; -. DR UniPathway; UPA00916; UER00889. DR Proteomes; UP000000579; 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:0004747; F:ribokinase activity; IEA:UniProtKB-EC. DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_01987; Ribokinase; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011877; D_ribokin_bac. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR002139; Ribokinase. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00990; RIBOKINASE. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Potassium; KW Reference proteome; Transferase. FT CHAIN 1 306 Ribokinase. FT /FTId=PRO_0000080099. FT NP_BIND 221 226 ATP. {ECO:0000255|HAMAP-Rule:MF_01987}. FT NP_BIND 252 253 ATP. {ECO:0000255|HAMAP-Rule:MF_01987}. FT REGION 12 14 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT REGION 40 44 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT ACT_SITE 253 253 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT METAL 247 247 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT METAL 249 249 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01987}. FT METAL 283 283 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01987}. FT METAL 286 286 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01987}. FT METAL 288 288 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01987}. FT METAL 292 292 Potassium. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT BINDING 141 141 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01987}. FT BINDING 185 185 ATP. {ECO:0000255|HAMAP-Rule:MF_01987}. FT BINDING 253 253 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01987}. SQ SEQUENCE 306 AA; 32205 MW; 3DCE8810827C8E84 CRC64; MRKTLTVLGS INADHVISVP YFTKPGETLT GQNYQIAYGG KGANQAVAAA RLGAKVAFIS CIGSDSIGKT MKNAFAQEGI DTTHINTVSQ EMTGMAFIQV AKSSENSIVL ASGANSHLSE MVVRQSEAQI AQSDCLLMQL ETPLSGVELA AQIAKKNGVK VVLNPAPAQI LSDELLSLID IITPNETEAE ILTGVEVADE QSAVKAASVF HDKGIETVMI TLGAKGVFVS RKGKSRIIKG FCVQAIDTTA AGDTFNGGFV TALLEEKSFD EAIRFGQAAA AISVTKKGAQ SSIPTRQETL EFLEHA // ID RECB_HAEIN Reviewed; 1211 AA. AC P45157; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485}; DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485}; DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485}; DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485}; GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485}; GN OrderedLocusNames=HI_1321; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit contributes ATPase, CC 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. CC {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. Interacts with RecA. CC {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent CC ATPase and has ATP-dependent 3'-5' helicase function. This domain CC interacts with RecC. {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts CC with RecD. It interacts with RecA, facilitating its loading onto CC ssDNA. {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_01485}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22966.1; -; Genomic_DNA. DR PIR; D64116; D64116. DR RefSeq; NP_439472.1; NC_000907.1. DR RefSeq; WP_005694451.1; NC_000907.1. DR ProteinModelPortal; P45157; -. DR STRING; 71421.HI1321; -. DR EnsemblBacteria; AAC22966; AAC22966; HI_1321. DR GeneID; 950246; -. DR KEGG; hin:HI1321; -. DR PATRIC; 20191325; VBIHaeInf48452_1373. DR eggNOG; ENOG4107QKA; Bacteria. DR eggNOG; COG1074; LUCA. DR KO; K03582; -. DR OMA; IMIGDPK; -. DR OrthoDB; EOG6677M1; -. DR PhylomeDB; P45157; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 5. DR Gene3D; 3.90.320.10; -; 1. DR HAMAP; MF_01485; RecB; 1. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 4. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 2. DR SUPFAM; SSF52540; SSF52540; 5. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00609; recB; 1. 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; DNA-binding; KW Exonuclease; Helicase; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 1211 RecBCD enzyme subunit RecB. FT /FTId=PRO_0000102047. FT DOMAIN 1 485 UvrD-like helicase ATP-binding. FT {ECO:0000255|HAMAP-Rule:MF_01485}. FT DOMAIN 500 772 UvrD-like helicase C-terminal. FT {ECO:0000255|HAMAP-Rule:MF_01485}. FT NP_BIND 22 29 ATP. {ECO:0000255|HAMAP-Rule:MF_01485}. FT REGION 1 916 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000255|HAMAP- FT Rule:MF_01485}. FT REGION 927 1211 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000255|HAMAP- FT Rule:MF_01485}. FT ACT_SITE 1120 1120 For nuclease activity. FT {ECO:0000255|HAMAP-Rule:MF_01485}. FT METAL 997 997 Magnesium; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01485}. FT METAL 1107 1107 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01485}. FT METAL 1120 1120 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01485}. SQ SEQUENCE 1211 AA; 139858 MW; 37B76430651FAD68 CRC64; MAETIPLNPI TLPLNQISLI EASAGTGKTY TIGSLYLRLL LKAGENNFSR PLNVEEILVV TFTEMATEEL KKKIRERITD AINKLTAFAK TQDKSAFKND EFLTALCDNL NIFEAIHRLK LAEQNMDLAA IYTIHGFCRR MLMQYAFHSG IHFNLELIKD QSDLLVRFAN EFWREHFYPL DFESANFIAT ELVSPANVLS LLKADLGKDL QVEIENKQAL SVPIQIFLPQ YLGGYQKALN ELKAFWLESA DEISAIITNE LVKDYPKDQL KSLNRKKYQV KRLGDWINKI NQWSNNPRDY QINTTLKDYF LQSSIEKNCE ESTDKNKDKK PATPFYSPIF ADLEKRVNAL MTPDLLSKLT LYHYRQGLQQ KLLDYKLNHQ EKSFDDLLRL LCEALQDAQG DELAEMIRFQ YPFAMIDEFQ DTDSQQYAIF SKIYRDNPEK NTGFIMIGDP KQAIYRFRGA DIFTYLKASD EAQSRFELTK NYRSEKHLVD GVNALFDFPQ SPFIYQNIKF TAVDSRDDHL RFYLNGKVEP AYRFYLTESD KVNKTEMAKI CAISIQHWLK SAAENQAVFQ NEDTYKTLQA ANIAVLVRDK NEAALVKNEL QKLGIASVYL SDQNSVFDSN VAKELAWVLK ACLNVAERPI LNAIATALFG LNAADIHQIQ QNEADWQRWA DSFAQYQQTW QRQGILAMLH QILLEQGISE RLLSQATGER DLTDFLHLAE ILQQAATLHE SEAALLSWFE KQIQGEARQE AQIRLESERQ LVKIVTIHKS KGLEYDLVWL PFLAAPSKDP SKKYINIYYS KERDETLWDI ENRNLNALCE ETFAEELRLL YVALTRAKYQ MAFALPAQFD KKWNALHYVL SQGEIGKEIN LSDSKDTETL LQTFKEKMQD NVEICTKPNL EALPTLSINT KNDDFKASEF TGNIEQDWRI TSFTSIEQAH RRQNYFTESA GKKHAVFDDA KDYDSQNAIE ISTALLNENE SNILDLPRGK QVGTALHRHF ENCYFSDLAN TEEIDKLRQS LQLDETFTES LQNWLQQISH TPLSNEIGIA LADLANKDCI KEMPFYLAIR EHFDVEAFNH TLKAHHHLPS ESLQFEQIQG MVRGSIDLVF RHNGKYYLVD YKSNFLGSTL ADYNQEALKK EMLHSHYDWQ YLIYTLALHR YLQSVVPHYD YARDFGGVFY LFLRGMNGEP QSGVFYDRPS VELITELDGV F // ID RELA_HAEIN Reviewed; 743 AA. AC P44644; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=GTP pyrophosphokinase; DE EC=2.7.6.5; DE AltName: Full=(p)ppGpp synthase; DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase; DE AltName: Full=ppGpp synthase I; GN Name=relA; OrderedLocusNames=HI_0334; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 formation of pppGpp which is then hydrolyzed to form ppGpp (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + GTP = AMP + guanosine 3'-diphosphate 5'- CC triphosphate. CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: CC step 1/2. CC -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21996.1; -; Genomic_DNA. DR PIR; D64062; D64062. DR RefSeq; NP_438498.1; NC_000907.1. DR RefSeq; WP_005694339.1; NC_000907.1. DR ProteinModelPortal; P44644; -. DR STRING; 71421.HI0334; -. DR EnsemblBacteria; AAC21996; AAC21996; HI_0334. DR GeneID; 950822; -. DR KEGG; hin:HI0334; -. DR PATRIC; 20189211; VBIHaeInf48452_0351. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR KO; K00951; -. DR OMA; TEIGHNC; -. DR OrthoDB; EOG6SV551; -. DR PhylomeDB; P44644; -. DR UniPathway; UPA00908; UER00884. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005618; C:cell wall; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0008728; F:GTP diphosphokinase activity; IBA:GO_Central. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IBA:GO_Central. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; GTP-binding; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 743 GTP pyrophosphokinase. FT /FTId=PRO_0000166549. FT DOMAIN 670 743 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 743 AA; 84567 MW; 39B47619896AC211 CRC64; MVAVRGSHLL NPQDFVIEQW CTGLKLAEQT EKSLIDAWYY ARDLMNAYPD EMKNATLMLQ SGVEMVEILH ELNMDAETLL TAMLFPIVAN KLTDWESLKE KFGAKITKLL KGVLEMDNIR QLNASHSANA LQVDNVRRML LAMVDDFRCV IIKLAERITF LRDAEHRCAE EDKVLAVKEC SYIYAPLANR LGIGQLKWEL EDYCFRYLHP EQYRAIAKLL QERRLDREHY IADFVSELSG YLRENIEQVE VYGRPKHIYS IWRKMQKKHL EFSGLYDVRA VRIIVQKLQD CYTALGIVHT QFKHLPKEFD DYVANPKPNG YQSIHTVVLG KGGKPIEVQI RTQQMHDDAE LGMAAHWKYK EGNTGSMSAY EEKIAWLRKL LAWQDDITDS GEVLAELRSQ VFDDRVYVFT PKGEVVDLPT GSTPLDFAYA IHSEIGHRCI GAKVAGRIVP FTYQLQMGDQ IDIITQKNPN PSRDWLNPNL GFTHTAKSRA KIQAWFKKQD RDKNIPAGKE LLDNELALLN LSIKQVEPYA LPRYNLKNLD DLYAGIGSGD IRLNNLIHFL QSKLIKVTAE EADQEILRHV ANKSAVNSQQ KSEKNNGCVI VEGVDNLMHH IARCCQPIPG DAIVGYITMG RGISIHRADC EQFLDLQAAH PERVVESIWG ENYASGFHIN IRIVAGDRNG LLRDITTVLA NEKISVLGVS SRADTKKQLA TIDMEIELHN VESLSKILAR LAKLDDVIEA KRL // ID RAIA_HAEIN Reviewed; 107 AA. AC P71346; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 107. DE RecName: Full=Ribosome-associated inhibitor A; GN Name=raiA; OrderedLocusNames=HI_0257; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP STRUCTURE BY NMR, AND MASS SPECTROMETRY. RX PubMed=11551193; DOI=10.1021/bi011077i; RA Parsons L., Eisenstein E., Orban J.; RT "Solution structure of HI0257, a bacterial ribosome binding protein."; RL Biochemistry 40:10979-10986(2001). CC -!- FUNCTION: During stationary phase, prevents 70S dimer formation, CC probably in order to regulate translation efficiency during CC transition between the exponential and the stationary phases. In CC addition, during environmental stress such as cold shock or CC excessive cell density at stationary phase, stabilizes the 70S CC ribosome against dissociation, inhibits translation initiation and CC increase translation accuracy. When normal growth conditions are CC restored, is quickly released from the ribosome (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Associates mainly with 70S ribosomes. {ECO:0000250}. CC -!- INDUCTION: By environmental stress or during stationary phase. CC {ECO:0000250}. CC -!- MASS SPECTROMETRY: Mass=12473.3; Method=MALDI; Range=2-107; CC Evidence={ECO:0000269|PubMed:11551193}; CC -!- SIMILARITY: Belongs to the Hpf/RaiA ribosome-associated protein CC family. RaiA 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; L42023; AAC21923.1; -; Genomic_DNA. DR RefSeq; NP_438426.1; NC_000907.1. DR RefSeq; WP_005653397.1; NC_000907.1. DR PDB; 1IMU; NMR; -; A=1-107. DR PDBsum; 1IMU; -. DR ProteinModelPortal; P71346; -. DR SMR; P71346; 1-107. DR STRING; 71421.HI0257; -. DR EnsemblBacteria; AAC21923; AAC21923; HI_0257. DR GeneID; 949379; -. DR KEGG; hin:HI0257; -. DR PATRIC; 20189039; VBIHaeInf48452_0272. DR eggNOG; ENOG4108WPH; Bacteria. DR eggNOG; COG1544; LUCA. DR KO; K05809; -. DR OMA; TPAIRSH; -. DR OrthoDB; EOG618R0J; -. DR PhylomeDB; P71346; -. DR EvolutionaryTrace; P71346; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0044238; P:primary metabolic process; IEA:InterPro. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.100; -; 1. DR InterPro; IPR003489; Ribosomal_S30Ae/sigma54_mod. DR Pfam; PF02482; Ribosomal_S30AE; 1. DR SUPFAM; SSF69754; SSF69754; 1. DR TIGRFAMs; TIGR00741; yfiA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Stress response; KW Translation regulation. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 107 Ribosome-associated inhibitor A. FT /FTId=PRO_0000169265. FT STRAND 8 10 {ECO:0000244|PDB:1IMU}. FT HELIX 14 28 {ECO:0000244|PDB:1IMU}. FT STRAND 38 44 {ECO:0000244|PDB:1IMU}. FT STRAND 47 54 {ECO:0000244|PDB:1IMU}. FT STRAND 61 68 {ECO:0000244|PDB:1IMU}. FT HELIX 70 90 {ECO:0000244|PDB:1IMU}. SQ SEQUENCE 107 AA; 12191 MW; 60708BA29CA334E2 CRC64; MTLNITSKQM DITPAIREHL EERLAKLGKW QTQLISPHFV LNKVPNGFSV EASIGTPLGN LLASATSDDM YKAINEVEEK LERQLNKLQH KSESRRADER LKDSFEN // ID RBSD_HAEIN Reviewed; 139 AA. AC P44734; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=D-ribose pyranase; DE EC=5.4.99.62; GN Name=rbsD; OrderedLocusNames=HI_0501; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta- CC furan forms of D-ribose. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Beta-D-ribopyranose = beta-D-ribofuranose. CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose CC 5-phosphate from beta-D-ribopyranose: step 1/2. CC -!- SUBUNIT: Homodecamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD 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; L42023; AAC22159.1; -; Genomic_DNA. DR PIR; G64072; G64072. DR RefSeq; NP_438659.1; NC_000907.1. DR RefSeq; WP_005693672.1; NC_000907.1. DR ProteinModelPortal; P44734; -. DR SMR; P44734; 1-138. DR STRING; 71421.HI0501; -. DR DNASU; 949497; -. DR EnsemblBacteria; AAC22159; AAC22159; HI_0501. DR GeneID; 949497; -. DR KEGG; hin:HI0501; -. DR PATRIC; 20189555; VBIHaeInf48452_0520. DR eggNOG; ENOG4105MRB; Bacteria. DR eggNOG; COG1869; LUCA. DR KO; K06726; -. DR OMA; IIRTGEC; -. DR OrthoDB; EOG68SW4G; -. DR PhylomeDB; P44734; -. DR UniPathway; UPA00916; UER00888. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016872; F:intramolecular lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048029; F:monosaccharide binding; IEA:InterPro. DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1650.10; -; 1. DR HAMAP; MF_01661; D_rib_pyranase; 1. DR InterPro; IPR023064; D-ribose_pyranase. DR InterPro; IPR023750; RbsD-like. DR InterPro; IPR007721; RbsD_FucU. DR Pfam; PF05025; RbsD_FucU; 1. DR SUPFAM; SSF102546; SSF102546; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Reference proteome. FT CHAIN 1 139 D-ribose pyranase. FT /FTId=PRO_0000097193. FT REGION 128 130 Substrate binding. {ECO:0000250}. FT ACT_SITE 20 20 Proton donor. {ECO:0000250}. FT BINDING 28 28 Substrate. {ECO:0000250}. FT BINDING 106 106 Substrate. {ECO:0000250}. SQ SEQUENCE 139 AA; 15339 MW; C5E424FDDF7A2C67 CRC64; MKKTALLNAQ LSHCIATLGH TESLTICDAG LPIPLSVERI DLALTAGVPS FLQTLNVVTN EMYVERVVIA EEIKEKNPEI LTALLTQLQK LESHQGNQIQ VEFVSHETFK KFTLESKAIV RTGECSPYAN VILYSGVPF // ID RDGC_HAEIN Reviewed; 302 AA. AC P44628; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Recombination-associated protein RdgC; GN Name=rdgC; OrderedLocusNames=HI_0306; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: May be involved in recombination. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RdgC 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; L42023; AAC21971.1; -; Genomic_DNA. DR PIR; E64147; E64147. DR RefSeq; NP_438473.1; NC_000907.1. DR RefSeq; WP_005694359.1; NC_000907.1. DR ProteinModelPortal; P44628; -. DR SMR; P44628; 1-299. DR STRING; 71421.HI0306; -. DR DNASU; 949925; -. DR EnsemblBacteria; AAC21971; AAC21971; HI_0306. DR GeneID; 949925; -. DR KEGG; hin:HI0306; -. DR PATRIC; 20189153; VBIHaeInf48452_0323. DR eggNOG; ENOG4105DH7; Bacteria. DR eggNOG; COG2974; LUCA. DR KO; K03554; -. DR OMA; PCSSQDI; -. DR OrthoDB; EOG6WX4MD; -. DR PhylomeDB; P44628; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00194; RdgC; 1. DR InterPro; IPR007476; RdgC. DR Pfam; PF04381; RdgC; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; DNA recombination; Reference proteome. FT CHAIN 1 302 Recombination-associated protein RdgC. FT /FTId=PRO_0000211740. SQ SEQUENCE 302 AA; 34706 MW; ABE8471C9095A75C CRC64; MWFKNLMTYR LTKPLDWDLA QLQTQLEDCQ FHPCGTQDQS KFGWSAPLRG SDLLYFSVGK QILLIAKKEE KILPANVVKR ELDDRIESLE QKENRKLKKV EKQTLKDDVV MNLLPRAFSK NQHTALWIDT ENNLIHIDAA SSKRAEDALA LLRKSLGSLP VVPLAFANEP STILTNWILQ DNLPHWLLAL EEAELRGSQE DSVIRCKKQP LENEEILALL QDGKKVVSKL ALEWEDTLTF VFNEDCTIKR LKFADTVREK NDDILKEDFA QRFDADFVLM TGILAKLTEN LLDEFGGEKA RL // ID RF2_HAEIN Reviewed; 365 AA. AC P43918; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Peptide chain release factor 2; DE Short=RF-2; GN Name=prfB; OrderedLocusNames=HI_1212; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Peptide chain release factor 2 directs the termination CC of translation in response to the peptide chain termination codons CC UGA and UAA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Methylated by PrmC. Methylation increases the termination CC efficiency of RF2 (By similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: The gene for this protein contains a UGA in-frame CC termination codon after Leu-25; a naturally occurring frameshift CC enables complete translation of RF-2. This provides a mechanism CC for the protein to regulate its own production (By similarity). CC {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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A64190; A64190. DR ProteinModelPortal; P43918; -. DR SMR; P43918; 4-365. DR PRIDE; P43918; -. DR OMA; RLYEHEM; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00094; Rel_fac_2; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR020853; Peptide_chain_release_fac2_bac. DR InterPro; IPR004374; PrfB. DR PANTHER; PTHR11075:SF6; PTHR11075:SF6; 1. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00020; prfB; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome; Ribosomal frameshifting. FT CHAIN 1 365 Peptide chain release factor 2. FT /FTId=PRO_0000166820. FT MOD_RES 252 252 N5-methylglutamine. {ECO:0000250}. SQ SEQUENCE 365 AA; 41281 MW; 70C39621CCEFE312 CRC64; MFEINPVKNK IIDLSDRTSV LRGYLDFDAK VERLEEVNGE LEQPDVWNDP DKAQALGKER VSLEQVVNTI KNLEQGLEDV DGLLELAIEA EDEDTFNEAV AELDELEQQL EKLEFRRMFS GEHDACDCYV DLQAGSGGTE AQDWTEMLLR MYLRWAESKG FKTELMEVSD GDVAGLKSAT IKVSGEYAFG WLRTETGIHR LVRKSPFDSN NRRHTSFSAA FVYPEIDDDI DIEINPADLR IDVYRASGAG GQHVNKTESA VRITHMPSGI VVQCQNDRSQ HKNKDQAMKQ LKAKLYELEL QKKNADKQAM EDNKSDIGWG SQIRSYVLDD SRIKDLRTGV ENRNTQAVLD GDLDRFIEAS LKAGL // ID RBSR_HAEIN Reviewed; 332 AA. AC P44329; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=Ribose operon repressor; GN Name=rbsR; OrderedLocusNames=HI_0506; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transcriptional repressor for the ribose rbsDACBK CC operon. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22164.1; -; Genomic_DNA. DR PIR; C64073; C64073. DR RefSeq; NP_438664.1; NC_000907.1. DR RefSeq; WP_005693667.1; NC_000907.1. DR ProteinModelPortal; P44329; -. DR SMR; P44329; 1-56. DR STRING; 71421.HI0506; -. DR EnsemblBacteria; AAC22164; AAC22164; HI_0506. DR GeneID; 949576; -. DR KEGG; hin:HI0506; -. DR PATRIC; 20189565; VBIHaeInf48452_0525. DR eggNOG; ENOG4105ETE; Bacteria. DR eggNOG; COG1609; LUCA. DR KO; K02529; -. DR OMA; SHVINNS; -. DR OrthoDB; EOG6SJJMM; -. DR PhylomeDB; P44329; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. DR Pfam; PF00356; LacI; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 332 Ribose operon repressor. FT /FTId=PRO_0000107989. FT DOMAIN 2 56 HTH lacI-type. {ECO:0000255|PROSITE- FT ProRule:PRU00111}. FT DNA_BIND 4 23 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00111}. SQ SEQUENCE 332 AA; 36715 MW; E335C70E6030953F CRC64; MATMKDIARL AQVSTSTVSH VINGSRFVSD EIREKVMRIV AELNYTPSAV ARSLKVRETK TIGLLVTATN NPFFAEVMAG VEQYCQKNQY NLIIATTGGD AKRLQQNLQT LMHKQVDGLL LMCGDSRFQA DIELAISLPL VVMDWWFTEL NADKILENSA LGGYLATKAL IDAGHRKIGI ITGNLKKSVA QNRLQGYKNA LSEAKIALNP HWIVESHFDF EGGVLGIQSL LTQSSRPTAV FCCSDTIAVG AYQAIQQQGL RIPQDLSIMG YDDIELARYL SPPLSTICQP KAELGKLAVE TLLQRIKNPN ENYRTLVLEP TCVLRESIYS LK // ID RECC_HAEIN Reviewed; 1121 AA. AC P44945; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=RecBCD enzyme subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486}; DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01486}; DE AltName: Full=Exonuclease V subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486}; DE Short=ExoV subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000255|HAMAP-Rule:MF_01486}; GN Name=recC {ECO:0000255|HAMAP-Rule:MF_01486}; GN OrderedLocusNames=HI_0942; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit recognizes the wild- CC type Chi sequence, and when added to isolated RecB increases its CC ATP-dependent helicase processivity. {ECO:0000255|HAMAP- CC Rule:MF_01486}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000255|HAMAP-Rule:MF_01486}. CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01486}. CC -!- SIMILARITY: Belongs to the RecC family. {ECO:0000255|HAMAP- CC Rule:MF_01486}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22596.1; -; Genomic_DNA. DR PIR; G64103; G64103. DR RefSeq; NP_439102.1; NC_000907.1. DR RefSeq; WP_005693290.1; NC_000907.1. DR ProteinModelPortal; P44945; -. DR STRING; 71421.HI0942; -. DR EnsemblBacteria; AAC22596; AAC22596; HI_0942. DR GeneID; 950610; -. DR KEGG; hin:HI0942; -. DR PATRIC; 20190541; VBIHaeInf48452_0983. DR eggNOG; ENOG4105DSY; Bacteria. DR eggNOG; COG1330; LUCA. DR KO; K03583; -. DR OMA; SWMRRYP; -. DR OrthoDB; EOG61P6M4; -. DR PhylomeDB; P44945; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004519; F:endonuclease activity; IBA:GO_Central. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GOC. DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GOC. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01486; RecC; 1. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006697; RecC. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR PIRSF; PIRSF000980; RecC; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR01450; recC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 1121 RecBCD enzyme subunit RecC. FT /FTId=PRO_0000087121. SQ SEQUENCE 1121 AA; 129669 MW; E5070957296AE0D3 CRC64; MFIVYYSNQL EKQKEILSSL FKSLPPEDPF QQDIILVQSP NMAQWLQIEL AKETGISANL KFPMPASFIW QLYAQNLPAT ALENPFDKDS MMWRLMRLIP IFLEKENFSP LRNYLSSSPH SEQYKLYQLS SKIADLFDQY LVYRPEWIFA WEKGEDEQIT DQIQKQQPNL NATLFAQIQG NTKWQGELWR ALVVDVKSDV NEATHRAALH NQFLALLADK KAPKKLPSRI FIFGIPALPT AYLNILQAIS SEVDIHLFFN NPCQEYWGDI SDLRLDYLRS RQRYQFNKQD ENQPLFSEDQ LSQLENAQFD VTYQKENLQL GNPLLAAWGK MGRDFLYILV RDEEHIPTYP VNAYQEIESN SLLGQLQSQI LHLENKPLNI AKNDRTLTLH SCHSAMREVE VLHDYLLDLF NQDPSLTPKD VVVMVADINQ YTPYIQAVFG QKNGDVPQIP FSLSDNKLSE SDVLVSSYLT LLRLKESNFS AEDVLVLLDI PAMRERFNIS LADLPLVREW VTDSGIRFGL QKNQDGINFN SWQAGLERMI LGYAMREEQG IWQDSLGLNS SYGLKGELAG NLSHFFTALS ALHETLQQAH SIEKWQEILT ALLSDFFVRN EDTSDMIFYI QEKINELAEH LKTLHFNEEL QAEVIADVIT MQLEDAPNSL KFLAGKVNFC TLLPMRSVPF KVVCLLGMND ADYPRTQTPN SFDLMQYHYQ KGDRVRRDDD RYLFLEALLA ARDYCYISYV GRSITDNQPK EPSVLVSQLL DYINQGQKEN VLTVIEHPMT AFSPDNFKNN EKFTRSFATK WLPIAQFDAS SNNSEFAVTM TENLEKIEEV ELDALVSFVE NPVKFFFEKQ LGVYFRDKDE RIADSENFTL SGLDNYSLNN DLIYLDEQNF ADYFRQAEVK GVLPRAEFGK VYAENIRDNV LEFKKKIADL GEAKHASVDF NLSVDWQNEN QKIRLFGYMD ALFGDDSQVI HWHFAKYKDR YCIRPWIYYL IQCVTQENAV PAKLITQDKV LELPPIEREV ALAQLQIYVK DYLQSQIEIQ LVPTVRNISD FIVSDENSVS EKLQELTESN GFGPKADPYW SRVLAQTSRF KQPENIAKLL KQTKAWFGLL FAQKKTRKTQ S // ID RECD_HAEIN Reviewed; 640 AA. AC P45158; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 100. DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487}; DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01487}; DE AltName: Full=Exonuclease V subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487}; DE Short=ExoV subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487}; GN Name=recD {ECO:0000255|HAMAP-Rule:MF_01487}; GN OrderedLocusNames=HI_1322; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit has ssDNA-dependent CC ATPase and 5'-3' helicase activity. When added to pre-assembled CC RecBC greatly stimulates nuclease activity and augments holoenzyme CC processivity. Negatively regulates the RecA-loading ability of CC RecBCD. {ECO:0000255|HAMAP-Rule:MF_01487}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000255|HAMAP-Rule:MF_01487}. CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01487}. CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000255|HAMAP- CC Rule:MF_01487}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22967.1; -; Genomic_DNA. DR PIR; E64116; E64116. DR RefSeq; NP_439473.1; NC_000907.1. DR RefSeq; WP_005694450.1; NC_000907.1. DR ProteinModelPortal; P45158; -. DR STRING; 71421.HI1322; -. DR EnsemblBacteria; AAC22967; AAC22967; HI_1322. DR GeneID; 950249; -. DR KEGG; hin:HI1322; -. DR PATRIC; 20191327; VBIHaeInf48452_1374. DR eggNOG; ENOG4107QYX; Bacteria. DR eggNOG; COG0507; LUCA. DR KO; K03581; -. DR OMA; EVTTVHR; -. DR OrthoDB; EOG60GRSZ; -. DR PhylomeDB; P45158; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01487; RecD; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006344; RecD. DR InterPro; IPR027785; UvrD-like_helicase_C. DR Pfam; PF13538; UvrD_C_2; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR01447; recD; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 640 RecBCD enzyme subunit RecD. FT /FTId=PRO_0000087116. FT NP_BIND 194 201 ATP. {ECO:0000255|HAMAP-Rule:MF_01487}. SQ SEQUENCE 640 AA; 72864 MW; C3C530AC398B5DA0 CRC64; MLSVLHKLKE LRILSQGDYY FAKLIADKQC HTDYAEPVKN LAILLAALCS WRYTQGNTCS QLDRYLEHNL FGLAYRTTEE DYLAEIHEKI GYLPVEDWQN ALCGHMAFTQ DPVNQIAPMA FQFGALYFYR AWQDEYRIVQ YIKNTLKKYR TLAFSYDEIH QKLEKYFPEK QEKTDWQKVA VATAIKSPFS IITGGPGTGK TTTVTRLLLV LQELFDCKLH IKLVAPTGKA ASRLEESIKN ALGFMQEKMN VSHSLFNAIP QKASTLHSLL GVNAFNDYTR YNSHNPLQLD VLVVDETSMI DLPMMAKLIN ALKPETRLIL LGDQAQLASV EAGAVLGELA QFVTQPYSHE QAAYLLATTG YKVEGSDCSN PIRDCLCHLT ESRRFDKDSG IGKLSEFIQK GKADDSLELF DHYPQELHFN SLNDEGDAVN QVVKSAVENY RTFLKMLDDL RKQKIDPNAK NEQGISYAEA IQVQFNSVRF LTALRNNNLG VENLNKEIAL ALREQKLLWF RNEQDWYIGK PIMITENDHN VRLYNGDIGL CLANGKVWFG NREVLTNRIP AHEPAFMMTI HKSQGSEFKH TVMVLPTEVN PVLSRELVFT GVTRAKKELT VFADEKIWKT AIRQTVKRQS GLGKLLEDLN // ID RECG_HAEIN Reviewed; 693 AA. AC P43809; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=ATP-dependent DNA helicase RecG; DE EC=3.6.4.12; GN Name=recG; OrderedLocusNames=HI_1740; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Critical role in recombination and DNA repair. Helps CC process Holliday junction intermediates to mature products by CC catalyzing branch migration. Has a DNA unwinding activity CC characteristic of a DNA helicase with a 3'- to 5'- polarity. CC Unwinds branched duplex DNA (Y-DNA) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily. 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; L42023; AAC23387.1; -; Genomic_DNA. DR PIR; E64139; E64139. DR RefSeq; NP_439884.1; NC_000907.1. DR RefSeq; WP_005693902.1; NC_000907.1. DR ProteinModelPortal; P43809; -. DR STRING; 71421.HI1740; -. DR EnsemblBacteria; AAC23387; AAC23387; HI_1740. DR GeneID; 950549; -. DR KEGG; hin:HI1740; -. DR PATRIC; 20192251; VBIHaeInf48452_1823. DR eggNOG; ENOG4105CB5; Bacteria. DR eggNOG; COG1200; LUCA. DR KO; K03655; -. DR OMA; YEDETRI; -. DR OrthoDB; EOG6FNHKW; -. DR PhylomeDB; P43809; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR033454; RecG_wedge. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF17191; RecG_wedge; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00643; recG; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 693 ATP-dependent DNA helicase RecG. FT /FTId=PRO_0000102142. FT DOMAIN 283 448 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 482 628 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 296 303 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 397 400 DEQH box. SQ SEQUENCE 693 AA; 78086 MW; 12D1BC65F0259950 CRC64; MSLELLDAVP LTSLSGVGAA ISNKLAKIGI HNLQDLLFHL PIRYEDRTRI TLIANLRPEQ YFTIEGIVQT CEVAFGRRPI LSVSLSDGTS KIMLRFFNFN AGMRNSFQVG VRVKAFGEVK RGRHMPEIHH PEYQIVRDNA PIVLEETLTP IYSTTEGLKQ NSLRKLTDQA LALLDKVQIA EILPNEFNPH QYSLKEALRL LHRPPPDISL EMLEQGKHPA QQRLIFEELL AHNLAMQKVR LGTQQFSALP LHYQTDLKQR FLATLPFQPT NAQKRVVSDI EQDLIKDYPM MRLVQGDVGS GKTLVAALAA LTAIDNGKQV ALMAPTEILA EQHANNFRRW FKPFGIEVGW LAGKVKGKSR QAELEKIKTG AVQMVVGTHA LFQEEVEFSD LALVIIDEQH RFGVHQRLML REKGEKAGFY PHQLIMTATP IPRTLAMTVY ADLDTSIIDE LPPGRTPITT VVVSEERRAE IVMRVKNACV NEKRQAYWVC TLIDESEVLE AQAAEAIWED LTKALPMLNI GLVHGRMKPQ EKQDVMMRFK NAELDLLVAT TVIEVGVDVP NASLMIIENA ERLGLSQLHQ LRGRVGRGCT ASFCVLMYKP PLGKVSQKRL QVLRDSQDGF VISEKDLEIR GPGEVLGTKQ TGIAELRVAN LMRDRKMIPT VQHYAKSLIQ KYPDVAESLI RRWLNNKEIY SNA // ID RF1_HAEIN Reviewed; 360 AA. AC P43917; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 2. DT 17-FEB-2016, entry version 105. DE RecName: Full=Peptide chain release factor 1; DE Short=RF-1; GN Name=prfA; OrderedLocusNames=HI_1561; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC23209.1; 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; L42023; AAC23209.1; ALT_INIT; Genomic_DNA. DR PIR; I64129; I64129. DR RefSeq; NP_439710.1; NC_000907.1. DR RefSeq; WP_005637988.1; NC_000907.1. DR ProteinModelPortal; P43917; -. DR SMR; P43917; 7-354. DR STRING; 71421.HI1561; -. DR EnsemblBacteria; AAC23209; AAC23209; HI_1561. DR GeneID; 950421; -. DR KEGG; hin:HI1561; -. DR PATRIC; 20191847; VBIHaeInf48452_1632. DR eggNOG; ENOG4105C8K; Bacteria. DR eggNOG; COG0216; LUCA. DR KO; K02835; -. DR OMA; LRIDVFC; -. DR OrthoDB; EOG6TN48J; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00093; Rel_fac_1; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR005139; PCRF. DR InterPro; IPR000352; Pep_chain_release_fac_I_II. DR InterPro; IPR004373; PrfA. DR Pfam; PF03462; PCRF; 1. DR Pfam; PF00472; RF-1; 1. DR SMART; SM00937; PCRF; 1. DR TIGRFAMs; TIGR00019; prfA; 1. DR PROSITE; PS00745; RF_PROK_I; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methylation; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 360 Peptide chain release factor 1. FT /FTId=PRO_0000177679. FT MOD_RES 235 235 N5-methylglutamine. {ECO:0000250}. SQ SEQUENCE 360 AA; 40917 MW; 99A48CD372616488 CRC64; MKDSIIAKLE SLKERYEELE ALLGDVSVIS DQDKFRAYSK EYSQLEEVVK CFNRWTQLNQ NIEEAEILLD DPEMKEMAQM EIEESKAEIE EVEQQLQILL LPKDPNDEYN CYLEIRAGTG GDEAGIFAGD LFRMYSRYAE SKRWRVEMLS ANESEQGGYK EVIVKVTGEG VYGQLKFESG GHRVQRVPKT ESQGRIHTSA CTVAVMPELP ESEMPEINPA DLRIDTYRSS GAGGQHVNTT DSAVRITHIP TGIVVECQDE RSQHKNKAKA MSVLASRIVQ AEQERQAAEQ TDMRRNLLGS GDRSDKIRTY NYPQGRVTDH RINLTIYRLD EVMNGKIDEL IQPIITEYQA DQLAALSEQN // ID RF3_HAEIN Reviewed; 527 AA. AC P43928; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Peptide chain release factor 3; DE Short=RF-3; GN Name=prfC; OrderedLocusNames=HI_1735; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Increases the formation of ribosomal termination CC complexes and stimulates activities of RF-1 and RF-2. It binds CC guanine nucleotides and has strong preference for UGA stop codons. CC It may interact directly with the ribosome. The stimulation of RF- CC 1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP CC (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. PrfC 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; L42023; AAC23380.1; -; Genomic_DNA. DR PIR; C64139; C64139. DR RefSeq; NP_439877.1; NC_000907.1. DR RefSeq; WP_005694221.1; NC_000907.1. DR ProteinModelPortal; P43928; -. DR SMR; P43928; 5-527. DR STRING; 71421.HI1735; -. DR EnsemblBacteria; AAC23380; AAC23380; HI_1735. DR GeneID; 950874; -. DR KEGG; hin:HI1735; -. DR PATRIC; 20192227; VBIHaeInf48452_1816. DR eggNOG; ENOG4105C8A; Bacteria. DR eggNOG; COG4108; LUCA. DR KO; K02837; -. DR OMA; DFAEDTY; -. DR OrthoDB; EOG6677Q1; -. DR PhylomeDB; P43928; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; IBA:GO_Central. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. DR GO; GO:0006449; P:regulation of translational termination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00072; Rel_fac_3; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004548; PrfC. DR InterPro; IPR032090; RF3_C. 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; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF16658; RF3_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR00503; prfC; 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; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 527 Peptide chain release factor 3. FT /FTId=PRO_0000210944. FT DOMAIN 9 278 tr-type G. FT NP_BIND 18 25 GTP. {ECO:0000250}. FT NP_BIND 86 90 GTP. {ECO:0000250}. FT NP_BIND 140 143 GTP. {ECO:0000250}. SQ SEQUENCE 527 AA; 59174 MW; B36E235D242C35CA CRC64; MSYPLEEVNK RRTFAIISHP DAGKTTITEK VLLYGNAIQT AGSVKGKGSA AHAKSDWMEM EKQRGISITT SVMQFPYNDC LVNLLDTPGH EDFSEDTYRT LTAVDSCLMV IDSAKGVEER TIKLMEVTRL RDTPIITFMN KLDRDIRDPI ELLDEVENVL KIRCAPITWP IGCGKLFKGV YHLAKDETYL YQSGQGSTIQ AVRVVKGLNN PELDVAVGDD LAQQLREELE LVQGASNEFE QDAFIKGELT PVFFGTALGN FGVDHFLDGL TQWAPKPQSR QADTRTVESA EEKFSGFVFK IQANMDPKHR DRVAFMRVVS GKYEKGMKLK HVRIGKDVVI SDALTFMAGD RAHAEEAYAG DIIGLHNHGT IQIGDTFTQG ETLKFTGIPN FAPELFRRIR LKDPLKQKQL LKGLVQLSEE GAVQVFRPLL NNDLIVGAVG VLQFDVVVSR LKTEYNVEAI YENVNVATAR WVECADEKKF EEFKRKNEQN LALDGGDNLT YIAPTMVNLN LAQERYPDVV FYKTREH // ID RFAF_HAEIN Reviewed; 346 AA. AC P45042; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=ADP-heptose--LPS heptosyltransferase 2; DE EC=2.-.-.-; DE AltName: Full=ADP-heptose--LPS heptosyltransferase II; GN Name=rfaF; OrderedLocusNames=HI_1105; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core CC biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 9 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; L42023; AAC22760.1; -; Genomic_DNA. DR PIR; G64182; G64182. DR RefSeq; NP_439262.1; NC_000907.1. DR RefSeq; WP_005693429.1; NC_000907.1. DR ProteinModelPortal; P45042; -. DR SMR; P45042; 1-346. DR STRING; 71421.HI1105; -. DR CAZy; GT9; Glycosyltransferase Family 9. DR DNASU; 950079; -. DR EnsemblBacteria; AAC22760; AAC22760; HI_1105. DR GeneID; 950079; -. DR KEGG; hin:HI1105; -. DR PATRIC; 20190881; VBIHaeInf48452_1153. DR eggNOG; ENOG4105XA0; Bacteria. DR eggNOG; COG0859; LUCA. DR KO; K02843; -. DR OMA; CLKQRHP; -. DR OrthoDB; EOG64N9TX; -. DR PhylomeDB; P45042; -. DR UniPathway; UPA00958; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008713; F:ADP-heptose-lipopolysaccharide heptosyltransferase activity; IBA:GO_Central. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central. DR InterPro; IPR002201; Glyco_trans_9. DR InterPro; IPR011910; LipoPS_heptosylTferase-II. DR Pfam; PF01075; Glyco_transf_9; 1. DR TIGRFAMs; TIGR02195; heptsyl_trn_II; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 346 ADP-heptose--LPS heptosyltransferase 2. FT /FTId=PRO_0000207263. SQ SEQUENCE 346 AA; 38847 MW; 14D0E11C6773FCA9 CRC64; MNILIIGPSW VGDMMMSHSL YQQLKIQYPN CNIDVMAPNW CKPLLARMPE VRKAIEMPLG HGAFELGTRY RLGKSLREQY DMAIVLPNSL KSAFIPFFAK IVHRRGWKGE SRYILLNDLR ANKKDYPMMV QRYVALAFEK DVIPKADDIP VLKPYLTVEP AQQAETLKKF EKQTALLGER PIIGFCPGAE FGPAKRWPHY HYAKLAEMLI TQGYAVALFG SAKDEPVGEE IRQALPEELR EFCVNLAGKT NLNEAVDLIA NCTAVVTNDS GLMHIAAAVN RPLIALYGPT SPQYTPPLSD KATIIRLIEG ELIKVRKGDK EGGYHQSLID ITPEMALEKL NELLAK // ID RIBD_HAEIN Reviewed; 372 AA. AC P44326; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=Riboflavin biosynthesis protein RibD; DE Includes: DE RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase; DE Short=DRAP deaminase; DE EC=3.5.4.26; DE AltName: Full=Riboflavin-specific deaminase; DE Includes: DE RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase; DE EC=1.1.1.193; DE AltName: Full=HTP reductase; GN Name=ribD; Synonyms=ribG; OrderedLocusNames=HI_0944; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone CC 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- CC pyrimidinedione 5'-phosphate. CC -!- CATALYTIC ACTIVITY: 2,5-diamino-6-hydroxy-4-(5- CC phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5- CC phosphoribosylamino)uracil + NH(3). CC -!- CATALYTIC ACTIVITY: 5-amino-6-(5-phospho-D-ribitylamino)uracil + CC NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 2/4. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 3/4. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and CC deoxycytidylate deaminase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP CC reductase 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; L42023; AAC22598.1; -; Genomic_DNA. DR PIR; H64103; H64103. DR RefSeq; NP_439104.1; NC_000907.1. DR RefSeq; WP_005693291.1; NC_000907.1. DR ProteinModelPortal; P44326; -. DR SMR; P44326; 3-370. DR STRING; 71421.HI0944; -. DR EnsemblBacteria; AAC22598; AAC22598; HI_0944. DR GeneID; 949944; -. DR KEGG; hin:HI0944; -. DR PATRIC; 20190545; VBIHaeInf48452_0985. DR eggNOG; ENOG4105D1W; Bacteria. DR eggNOG; COG0117; LUCA. DR eggNOG; COG1985; LUCA. DR KO; K11752; -. DR OMA; YRAGEPH; -. DR OrthoDB; EOG66F07R; -. DR PhylomeDB; P44326; -. DR UniPathway; UPA00275; UER00401. DR UniPathway; UPA00275; UER00402. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IBA:GO_Central. DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central. DR GO; GO:0009451; P:RNA modification; IBA:GO_Central. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR004794; Eubact_RibD. DR InterPro; IPR011549; RibD_C. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF01872; RibD_C; 1. DR PIRSF; PIRSF006769; RibD; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00326; eubact_ribD; 1. DR TIGRFAMs; TIGR00227; ribD_Cterm; 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; Multifunctional enzyme; KW NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis; KW Zinc. FT CHAIN 1 372 Riboflavin biosynthesis protein RibD. FT /FTId=PRO_0000171722. FT DOMAIN 6 128 CMP/dCMP-type deaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT NP_BIND 166 169 NADP. {ECO:0000250}. FT NP_BIND 304 310 NADP. {ECO:0000250}. FT REGION 1 150 Deaminase. FT REGION 151 372 Reductase. FT ACT_SITE 57 57 Proton donor. {ECO:0000250}. FT METAL 55 55 Zinc; catalytic. {ECO:0000250}. FT METAL 80 80 Zinc; catalytic. {ECO:0000250}. FT METAL 89 89 Zinc; catalytic. {ECO:0000250}. FT BINDING 159 159 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 173 173 Substrate. {ECO:0000250}. FT BINDING 175 175 NADP. {ECO:0000250}. FT BINDING 189 189 Substrate. {ECO:0000250}. FT BINDING 201 201 NADP. {ECO:0000250}. FT BINDING 205 205 NADP. {ECO:0000250}. FT BINDING 209 209 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 212 212 Substrate. {ECO:0000250}. FT BINDING 239 239 NADP. {ECO:0000250}. FT BINDING 302 302 Substrate. {ECO:0000250}. SQ SEQUENCE 372 AA; 40931 MW; C7504EDD8B886F7D CRC64; MLEFSSQDCV FMQRALDLAA KGQYTTTPNP SVGCVLVKNG EIVGEGFHFK AGQPHAERVA LAQAGENAKG ATAYVTLEPC AHYGRTPPCA LGLIEAGVVK VIAAMQDPNP QVAGKGLKML SDAGIESTVN LLNDQAEKIN KGFLKRMRQG MPFVQLKLAM SLDGRTAMAS GESKWITGPD ARSDVQKMRA KSSALLSTST TVIADDPSLN VRWDEFPENL KTEYKKEWLR QPVRVILDSQ HRIQPTHKLF LTHSPVWLVS SEPRDLTGFP DFCEQIIFPK ENLLKELMRE LGKRQINTLW VEAGANLSGS LIDAKLVDEL IIYIAPKLLG DNARGLCQLP NLTKLADAPL WQLNELEQIG DDIKLTYTPK GV // ID RECJ_HAEIN Reviewed; 575 AA. AC P45112; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Single-stranded-DNA-specific exonuclease RecJ; DE EC=3.1.-.-; GN Name=recJ; OrderedLocusNames=HI_1214; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Single-stranded-DNA-specific exonuclease. Required for CC many types of recombinational events, although the stringency of CC the requirement for RecJ appears to vary with the type of CC recombinational event monitored and the other recombination gene CC products which are available (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecJ 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; L42023; AAC22867.1; -; Genomic_DNA. DR PIR; F64110; F64110. DR RefSeq; NP_439370.1; NC_000907.1. DR RefSeq; WP_005694232.1; NC_000907.1. DR ProteinModelPortal; P45112; -. DR STRING; 71421.HI1214; -. DR EnsemblBacteria; AAC22867; AAC22867; HI_1214. DR GeneID; 950889; -. DR KEGG; hin:HI1214; -. DR PATRIC; 20191107; VBIHaeInf48452_1266. DR eggNOG; ENOG4105C2R; Bacteria. DR eggNOG; COG0608; LUCA. DR KO; K07462; -. DR OMA; NRFDYGY; -. DR OrthoDB; EOG63C0P5; -. DR PhylomeDB; P45112; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR004610; RecJ. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. DR TIGRFAMs; TIGR00644; recJ; 1. PE 3: Inferred from homology; KW Complete proteome; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 575 Single-stranded-DNA-specific exonuclease FT RecJ. FT /FTId=PRO_0000097230. SQ SEQUENCE 575 AA; 64219 MW; B1CE80039BBEF208 CRC64; MKKLIKRREI PIGNSVSNHP LLDRLYRARH IQNTKELDRT LKSMLNPNQL YGIEQAVNLL VEAYQPQQKI VIVGDFDADG ATSTALSVLA LRQLGFSDVD YLVPNRFEQG YGLSIPVAEM AIEKGVQLLM TVDNGVSSFD GVAFLKEKGI RVLVTDHHLP PETLPPADAI VNPNLSQCGF PSKSLAGVGV AFYLMLAVRA KFRELGIFTA ETQPNFTDLL DLVALGTIAD VVPLDQNNRI LAYQGLMRIR ARHCRLGIIA LAEVANRNVE QFTSSDLGFC IGPRLNAAGR LDNMSIGVEL LLANEMSKAR ELALDLDQLN QTRKEIEAGM KLEAIKICQN LTALFKELPY GITLYQPDWH QGVLGIVSSR IKDQYHRPVI AFAQDSEGIL KGSARSIEGL HMRDVLERIH SQHPNMILKF GGHAMAAGLS IREEHFADFQ HIFNQTVADW LDEEHLQGVI WTDGELNSNE FNLETAELIK SVGTWGQGFP EPCFDGEFKI LDQRAIGQNK NHLKMLLEPK QGGVLLDAIA FNINTRLYPD LSIKQARLAY KLEINEFRGN RSLQLLVDYI EPIDE // ID RECQ_HAEIN Reviewed; 619 AA. AC P71359; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=ATP-dependent DNA helicase RecQ; DE EC=3.6.4.12; GN Name=recQ; OrderedLocusNames=HI_0728; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA helicase. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily. 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 HRDC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22387.1; -; Genomic_DNA. DR RefSeq; NP_438887.1; NC_000907.1. DR RefSeq; WP_005693132.1; NC_000907.1. DR ProteinModelPortal; P71359; -. DR SMR; P71359; 16-519, 536-608. DR STRING; 71421.HI0728; -. DR EnsemblBacteria; AAC22387; AAC22387; HI_0728. DR GeneID; 949757; -. DR KEGG; hin:HI0728; -. DR PATRIC; 20190093; VBIHaeInf48452_0762. DR eggNOG; ENOG4105C9U; Bacteria. DR eggNOG; COG0514; LUCA. DR KO; K03654; -. DR OMA; WDATEPA; -. DR OrthoDB; EOG6ZSPDC; -. DR PhylomeDB; P71359; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.150.80; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ. DR InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR010997; HRDC-like. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032284; RecQ_Zn-bd. DR InterPro; IPR018982; RQC_domain. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00570; HRDC; 1. DR Pfam; PF16124; RecQ_Zn_bind; 1. DR Pfam; PF09382; RQC; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00341; HRDC; 1. DR SMART; SM00956; RQC; 1. DR SUPFAM; SSF47819; SSF47819; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01389; recQ; 1. DR TIGRFAMs; TIGR00614; recQ_fam; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50967; HRDC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 619 ATP-dependent DNA helicase RecQ. FT /FTId=PRO_0000205036. FT DOMAIN 37 205 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 229 374 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT DOMAIN 535 615 HRDC. {ECO:0000255|PROSITE- FT ProRule:PRU00328}. FT NP_BIND 50 57 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 149 152 DEAH box. SQ SEQUENCE 619 AA; 70056 MW; 4785BD6E599337BB CRC64; MLDSPLLSKI IEKPTALSVL KSVFGYQSFR KGQEEVINAA LNGQDALVVM ATGNGKSLCY QIPALCFDGL TLVISPLISL MKDQVDQLQA NGIEADFLNS SQTLEQQQQV QNKLISGQLK LLYVSPEKVM TNSFFQLISY SKVCFIAIDE AHCISQWGHD FRPEYTQLGG LKASFPDAPI MALTATADYA TQQDILRHLN LKNLHKYIGS FDRPNIRYTL EEKYKPMEQL TRFVLAQKGK SGIIYCNSRN KVERIAESLR NKGVSAAAYH AGMETAIRER VQQDFQRDNV QVVVATIAFG MGINKSNVRF VAHFDLPRSI ESYYQETGRA GRDDLPAEAV LFYEPADYAW LQKILLEKPE TPQRQIEQHK LEAIGEFAES QTCRRLVLLN YFGEHRQTPC NNCDICLDPP KKYDGLVDAQ KVMSTIYRVG QCFGAHYVIA VLRGMHNQKI IERQHHKLSV YGIGKDKSKE HWQSVIRQLI HLGFVQQVIS ELNPTLQLTE SAKVILKGEE PLELAMPRIS AISKIAHNPQ RQGVANYDKD LFARLRFLRK QIADKENIPP YIVFNDATLQ EMAQYMPTSN IEMLQINGVG SIKLERFGQP FMALIQEHKA ILANAQNND // ID RECR_HAEIN Reviewed; 200 AA. AC P44712; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017}; GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; GN OrderedLocusNames=HI_0443; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May play a role in DNA repair. It seems to be involved CC in an RecBC-independent recombinational process of DNA repair. It CC may act with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}. CC -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP- CC Rule:MF_00017}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00017}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22102.1; -; Genomic_DNA. DR PIR; F64068; F64068. DR RefSeq; NP_438604.1; NC_000907.1. DR RefSeq; WP_005626527.1; NC_000907.1. DR ProteinModelPortal; P44712; -. DR STRING; 71421.HI0443; -. DR EnsemblBacteria; AAC22102; AAC22102; HI_0443. DR GeneID; 949512; -. DR KEGG; hin:HI0443; -. DR PATRIC; 20189439; VBIHaeInf48452_0463. DR eggNOG; ENOG4105F3K; Bacteria. DR eggNOG; COG0353; LUCA. DR KO; K06187; -. DR OMA; DVMAIEN; -. DR OrthoDB; EOG62NX85; -. DR PhylomeDB; P44712; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00017; RecR; 1. DR InterPro; IPR000093; DNA_Rcmb_RecR. DR InterPro; IPR023627; Rcmb_RecR. DR InterPro; IPR023628; Rcmb_RecR_C4-type_Zn. DR InterPro; IPR015967; Rcmb_RecR_CS. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF02132; RecR; 1. DR Pfam; PF13662; Toprim_4; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF111304; SSF111304; 1. DR TIGRFAMs; TIGR00615; recR; 1. DR PROSITE; PS01300; RECR; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Metal-binding; Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 200 Recombination protein RecR. FT /FTId=PRO_0000190328. FT DOMAIN 81 176 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00017}. FT ZN_FING 57 72 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00017}. SQ SEQUENCE 200 AA; 22107 MW; 77D417A4B234A90B CRC64; MQSSPLLEHL IENLRCLPGV GPKSAQRMAY HLLQRNRSGG MNLARALTEA MSKIGHCSQC RDFTEEDTCN ICNNPRRQNS GLLCVVEMPA DIQAIEQTGQ FSGRYFVLMG HLSPLDGIGP REIGLDLLQK RLVEESFHEV ILATNPTVEG DATANYIAEM CRQHNIKVSR IAHGIPVGGE LETVDGTTLT HSFLGRRQID // ID RECX_HAEIN Reviewed; 152 AA. AC P43706; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 21-NOV-2003, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Regulatory protein RecX; GN Name=recX; OrderedLocusNames=HI_0599; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Modulates RecA activity. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RecX family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22256.1; 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; L42023; AAC22256.1; ALT_INIT; Genomic_DNA. DR PIR; I64079; I64079. DR RefSeq; NP_438756.2; NC_000907.1. DR RefSeq; WP_005694572.1; NC_000907.1. DR ProteinModelPortal; P43706; -. DR STRING; 71421.HI0599; -. DR EnsemblBacteria; AAC22256; AAC22256; HI_0599. DR GeneID; 949641; -. DR KEGG; hin:HI0599; -. DR PATRIC; 20189755; VBIHaeInf48452_0620. DR eggNOG; ENOG4105Y3E; Bacteria. DR eggNOG; COG2137; LUCA. DR KO; K03565; -. DR OMA; CKMQEKA; -. DR OrthoDB; EOG693GQ0; -. DR PhylomeDB; P43706; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006282; P:regulation of DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 3. DR HAMAP; MF_01114; RecX; 1. DR InterPro; IPR003783; Regulatory_RecX. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02631; RecX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 152 Regulatory protein RecX. FT /FTId=PRO_0000162436. SQ SEQUENCE 152 AA; 18313 MW; 709CD6CAB02202D0 CRC64; MSSLAFNYIV NLLSRREYSE FELRNKMQEK NFSEEEIDDA LSRCQAKNWQ SDRRFSENYL NSRVQKGYGV GRIRQELRQL KGVSSDIIDE VLMESEIDWY EMAENLLRKK FPNYNEQQTP KMKQKIWQYM LSHGFRSDEF ADLIGQNQSE WD // ID RELB_HAEIN Reviewed; 98 AA. AC P71357; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Putative antitoxin RelB; GN Name=relB; OrderedLocusNames=HI_0710; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Its cognate toxin is RelE (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RelB/DinJ antitoxin 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; L42023; AAC22377.1; -; Genomic_DNA. DR PIR; A64088; A64088. DR RefSeq; NP_438868.1; NC_000907.1. DR RefSeq; WP_005661259.1; NC_000907.1. DR ProteinModelPortal; P71357; -. DR STRING; 71421.HI0710; -. DR EnsemblBacteria; AAC22377; AAC22377; HI_0710. DR GeneID; 950711; -. DR KEGG; hin:HI0710; -. DR PATRIC; 20190041; VBIHaeInf48452_0741. DR eggNOG; COG3077; LUCA. DR KO; K07473; -. DR OMA; INDAFSF; -. DR OrthoDB; EOG6JHRPR; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007337; RelB/DinJ. DR Pfam; PF04221; RelB; 1. DR TIGRFAMs; TIGR02384; RelB_DinJ; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Putative antitoxin RelB. FT /FTId=PRO_0000077949. SQ SEQUENCE 98 AA; 11015 MW; 9F972D5663423021 CRC64; MALTNSSISF RTVEKTKLEA YQVIEQYGLT PSQVFNMFLA QIAKTRSIPV DLNYLRPNKE TLAAIDELDS GNAESFFIEA SENYSAEEFT KRILNGGQ // ID RIBA_HAEIN Reviewed; 216 AA. AC P44571; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 95. DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_00179}; DE EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_00179}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_00179}; GN Name=ribA {ECO:0000255|HAMAP-Rule:MF_00179}; GN OrderedLocusNames=HI_0212; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00179}. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6- CC hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00179}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00179}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00179}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_00179}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. CC {ECO:0000255|HAMAP-Rule:MF_00179}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21880.1; 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; L42023; AAC21880.1; ALT_INIT; Genomic_DNA. DR PIR; A64055; A64055. DR RefSeq; NP_438380.2; NC_000907.1. DR RefSeq; WP_005629111.1; NC_000907.1. DR ProteinModelPortal; P44571; -. DR SMR; P44571; 3-175. DR STRING; 71421.HI0212; -. DR EnsemblBacteria; AAC21880; AAC21880; HI_0212. DR GeneID; 951119; -. DR KEGG; hin:HI0212; -. DR PATRIC; 20188919; VBIHaeInf48452_0216. DR eggNOG; ENOG4107T1C; Bacteria. DR eggNOG; COG0807; LUCA. DR KO; K01497; -. DR OMA; PTPFGVF; -. DR OrthoDB; EOG679TK8; -. DR PhylomeDB; P44571; -. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00179; RibA; 1. DR InterPro; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR TIGRFAMs; TIGR00505; ribA; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome; Riboflavin biosynthesis; Zinc. FT CHAIN 1 216 GTP cyclohydrolase-2. FT /FTId=PRO_0000151758. FT NP_BIND 51 55 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT NP_BIND 94 96 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT ACT_SITE 128 128 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT ACT_SITE 130 130 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 56 56 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 67 67 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT METAL 69 69 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00179}. FT BINDING 72 72 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 116 116 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 151 151 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. FT BINDING 156 156 GTP. {ECO:0000255|HAMAP-Rule:MF_00179}. SQ SEQUENCE 216 AA; 24320 MW; 98258355F47ED8F2 CRC64; MAKIQLVAQA NLPTEYGIFK MVGFEFPDTK KEHVALVMGD ISNADEPVLA RIHSECLTGD ALHSLKCDCG FQLATALKQI QEEGRGVLIY HREEGRGIGL INKIRAYSLQ DKGMDTIEAN LALGFKADER NFEVCADMFE LLGVKKVRLM TNNPEKVETM KKAGINVVER VPLNVGENRY NTKYLDTKAK KMGHYIVHNN DEQHLMTCPH CQEEII // ID RIMM_HAEIN Reviewed; 178 AA. AC P44568; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN OrderedLocusNames=HI_0203; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: An accessory protein needed during the final step in the CC assembly of 30S ribosomal subunit, possibly for assembly of the CC head region. Probably interacts with S19. Essential for efficient CC processing of 16S rRNA. May be needed both before and after RbfA CC during the maturation of 16S rRNA. It has affinity for free CC ribosomal 30S subunits but not for 70S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SUBUNIT: Binds ribosomal protein S19. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- DOMAIN: The PRC barrel domain binds ribosomal protein S19. CC {ECO:0000255|HAMAP-Rule:MF_00014}. CC -!- SIMILARITY: Belongs to the RimM family. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC -!- SIMILARITY: Contains 1 PRC barrel domain. {ECO:0000255|HAMAP- CC Rule:MF_00014}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21872.1; -; Genomic_DNA. DR PIR; D64145; D64145. DR RefSeq; NP_438372.2; NC_000907.1. DR PDB; 3H9N; X-ray; 2.70 A; A=8-178. DR PDBsum; 3H9N; -. DR ProteinModelPortal; P44568; -. DR STRING; 71421.HI0203; -. DR EnsemblBacteria; AAC21872; AAC21872; HI_0203. DR GeneID; 951115; -. DR KEGG; hin:HI0203; -. DR PATRIC; 20188903; VBIHaeInf48452_0208. DR eggNOG; ENOG4108ZR6; Bacteria. DR eggNOG; COG0806; LUCA. DR KO; K02860; -. DR OMA; QPWFIQR; -. DR OrthoDB; EOG6SBT2K; -. DR EvolutionaryTrace; P44568; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR Gene3D; 2.40.30.60; -; 1. DR HAMAP; MF_00014; Ribosome_mat_RimM; 1. DR InterPro; IPR011961; 16S_RimM. DR InterPro; IPR027275; PRC-brl_dom. DR InterPro; IPR011033; PRC_barrel-like. DR InterPro; IPR002676; RimM. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF05239; PRC; 1. DR Pfam; PF01782; RimM; 1. DR SUPFAM; SSF50346; SSF50346; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR02273; 16S_RimM; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Cytoplasm; KW Reference proteome; Ribosome biogenesis. FT CHAIN 1 178 Ribosome maturation factor RimM. FT /FTId=PRO_0000163297. FT DOMAIN 99 178 PRC barrel. {ECO:0000255|HAMAP- FT Rule:MF_00014}. FT STRAND 9 18 {ECO:0000244|PDB:3H9N}. FT STRAND 20 23 {ECO:0000244|PDB:3H9N}. FT STRAND 25 29 {ECO:0000244|PDB:3H9N}. FT STRAND 31 34 {ECO:0000244|PDB:3H9N}. FT HELIX 35 39 {ECO:0000244|PDB:3H9N}. FT STRAND 42 47 {ECO:0000244|PDB:3H9N}. FT STRAND 50 54 {ECO:0000244|PDB:3H9N}. FT STRAND 56 64 {ECO:0000244|PDB:3H9N}. FT STRAND 66 72 {ECO:0000244|PDB:3H9N}. FT HELIX 76 80 {ECO:0000244|PDB:3H9N}. FT TURN 81 84 {ECO:0000244|PDB:3H9N}. FT STRAND 86 90 {ECO:0000244|PDB:3H9N}. FT STRAND 98 100 {ECO:0000244|PDB:3H9N}. FT HELIX 102 106 {ECO:0000244|PDB:3H9N}. FT TURN 107 109 {ECO:0000244|PDB:3H9N}. FT STRAND 111 114 {ECO:0000244|PDB:3H9N}. FT STRAND 119 131 {ECO:0000244|PDB:3H9N}. FT STRAND 133 138 {ECO:0000244|PDB:3H9N}. FT STRAND 148 153 {ECO:0000244|PDB:3H9N}. FT TURN 157 159 {ECO:0000244|PDB:3H9N}. FT STRAND 160 164 {ECO:0000244|PDB:3H9N}. FT HELIX 165 167 {ECO:0000244|PDB:3H9N}. FT STRAND 169 172 {ECO:0000244|PDB:3H9N}. SQ SEQUENCE 178 AA; 20571 MW; 59A5B0F334F9EAE1 CRC64; MKNMEQQHIE VVGKLGSTYG IRGWLRIYSS TEQAESIFDY QPWFLKIKGE WQSIELENWR YHNHEIIVKL KGVDDREAAQ ILANVEIGVD LSVFPELEEG DYYWHDLIGC TVVNLEGYTM GTVTEMMETG SNDVLVVKAN TKDAFGKQER LIPFLYEQVV KRVDLTTKTI EVDWDAGF // ID RECF_HAEIN Reviewed; 359 AA. AC P43767; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 110. DE RecName: Full=DNA replication and repair protein RecF; GN Name=recF; OrderedLocusNames=HI_0991; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is CC required for DNA replication and normal SOS inducibility. RecF CC binds preferentially to single-stranded, linear DNA. It also seems CC to bind ATP (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecF 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; L42023; AAC22653.1; -; Genomic_DNA. DR RefSeq; NP_439154.1; NC_000907.1. DR RefSeq; WP_005693333.1; NC_000907.1. DR ProteinModelPortal; P43767; -. DR STRING; 71421.HI0991; -. DR DNASU; 949990; -. DR EnsemblBacteria; AAC22653; AAC22653; HI_0991. DR GeneID; 949990; -. DR KEGG; hin:HI0991; -. DR PATRIC; 20190643; VBIHaeInf48452_1034. DR eggNOG; ENOG4105C3X; Bacteria. DR eggNOG; COG1195; LUCA. DR KO; K03629; -. DR OMA; KVQTFIT; -. DR OrthoDB; EOG6HTP3X; -. DR PhylomeDB; P43767; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00365; RecF; 1. DR InterPro; IPR001238; DNA-binding_RecF. DR InterPro; IPR018078; DNA-binding_RecF_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1. DR Pfam; PF02463; SMC_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00611; recf; 1. DR PROSITE; PS00617; RECF_1; 1. DR PROSITE; PS00618; RECF_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair; KW DNA replication; DNA-binding; Nucleotide-binding; Reference proteome; KW SOS response. FT CHAIN 1 359 DNA replication and repair protein RecF. FT /FTId=PRO_0000196420. FT NP_BIND 30 37 ATP. {ECO:0000255}. SQ SEQUENCE 359 AA; 41194 MW; 269026C1B98583C1 CRC64; MAISRLLVEK FRNLTAVDLD FDPCFNFLIG NNGSGKTSLL EAIFYLGHGR SFKSAVTNRI ISYDEPHFTL FGQIQESQHQ WSIGLQKLRQ GNTLVKINGE DGNKISDLAH LLPMQLITPE GLTLLNGGPS YRRAFLDWGL FHHQTSFYSA WSNLNRLLKQ RNAALAQNQP YSAIKIWDVE LAKLAHQVSE WRAEYAEALS PEIEQTCQLF LPELEINVSF HQGWEKNADY YEILQQNFER DRALNYTFSG PQKADFRFKA QGLPVEDVLS RGQLKLLMCA LRLAQGEHLM KEKQRHCIFL IDDFASELDQ YKRALLAERL QQSGSQVFVT AITQRQLKEM QVENKKMFSV HNGIINALN // ID RECN_HAEIN Reviewed; 558 AA. AC P44496; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=DNA repair protein RecN; DE AltName: Full=Recombination protein N; GN Name=recN; OrderedLocusNames=HI_0070; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May be involved in recombinational repair of damaged CC DNA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecN 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; L42023; AAC21748.1; -; Genomic_DNA. DR PIR; H64046; H64046. DR RefSeq; NP_438243.1; NC_000907.1. DR RefSeq; WP_005693852.1; NC_000907.1. DR ProteinModelPortal; P44496; -. DR STRING; 71421.HI0070; -. DR EnsemblBacteria; AAC21748; AAC21748; HI_0070. DR GeneID; 950958; -. DR KEGG; hin:HI0070; -. DR PATRIC; 20188595; VBIHaeInf48452_0071. DR eggNOG; ENOG4105C4F; Bacteria. DR eggNOG; COG0497; LUCA. DR KO; K03631; -. DR OMA; QVICVTH; -. DR OrthoDB; EOG6WQD34; -. DR PhylomeDB; P44496; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR004604; DNA_recomb/repair_RecN. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR PANTHER; PTHR11059; PTHR11059; 1. DR Pfam; PF02463; SMC_N; 1. DR PIRSF; PIRSF003128; RecN; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00634; recN; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA repair; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 558 DNA repair protein RecN. FT /FTId=PRO_0000188018. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 558 AA; 62634 MW; 6C573A656FA72387 CRC64; MLTQLTINNF AIVRQLDIEL AKGMSVITGE TGAGKSIAID ALGLCFGQRV ETSMVREGQE RAEICATFQL ESQNPAYHWL SEQELQDPDN PTECILRRII NADGRSKAFI NSTPVSASQL KEIAQYLVHI NGQHASQLLL KNDYQLQLVD NFAAHPELLV KMREDYQTWK NLQNQVKTFQ QKVAENEARK QLLQYQVDEL DEFNLRPNEY LELEDEQRRL SSSEQLTQLS QSALQILSEN DTVNIDSLLY RATQYIDELA ELDPQYAEVQ NMLNDALIQV QEATSEVQNL SSNIEQDPQL LQEIEQRISQ TLQLARKHQV KPEDLVEQHK KLKAELTALL DFSESEEMLI EQEKRAFEQM QATATALTAS RQQSATRLAQ NVTQSIKQLA MENAEFYVEL NTDLDKVSAN GADNVIFTLR SNLGQQPQPL AKIASGGELS RISLAIQVLT SDQSAIPTLI FDEVDVGISG KTASVVGKLL RQLSERCQVL CVTHLPQVAC HGHHQFNVEK FTVDNKTETK MTALSQAERV PALARLLGGS EITELALANA QEMLDLVH // ID RECO_HAEIN Reviewed; 236 AA. AC P44642; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=DNA repair protein RecO; DE AltName: Full=Recombination protein O; GN Name=recO; OrderedLocusNames=HI_0332; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99. RC STRAIN=Rd / H175; RX PubMed=8559074; DOI=10.1111/j.1365-2958.1995.mmi_17030555.x; RA Weiser J.N., Chong S.T., Greenberg D., Fong W.; RT "Identification and characterization of a cell envelope protein of RT Haemophilus influenzae contributing to phase variation in colony RT opacity and nasopharyngeal colonization."; RL Mol. Microbiol. 17:555-564(1995). CC -!- FUNCTION: Involved in DNA repair and RecF pathway recombination. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RecO 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; L42023; AAC21994.1; -; Genomic_DNA. DR EMBL; U17037; AAA56763.1; -; Genomic_DNA. DR PIR; C64062; C64062. DR RefSeq; NP_438496.1; NC_000907.1. DR RefSeq; WP_005654053.1; NC_000907.1. DR ProteinModelPortal; P44642; -. DR STRING; 71421.HI0332; -. DR EnsemblBacteria; AAC21994; AAC21994; HI_0332. DR GeneID; 950611; -. DR KEGG; hin:HI0332; -. DR PATRIC; 20189207; VBIHaeInf48452_0349. DR eggNOG; ENOG41071DT; Bacteria. DR eggNOG; COG1381; LUCA. DR KO; K03584; -. DR OMA; YVLHSRA; -. DR OrthoDB; EOG6X10W9; -. DR PhylomeDB; P44642; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00201; RecO; 1. DR InterPro; IPR022572; DNA_rep/recomb_RecO_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR003717; RecO. DR Pfam; PF02565; RecO_C; 1. DR Pfam; PF11967; RecO_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00613; reco; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Reference proteome. FT CHAIN 1 236 DNA repair protein RecO. FT /FTId=PRO_0000204958. SQ SEQUENCE 236 AA; 26862 MW; 5687F6B77790B158 CRC64; MQSELQRGFV LHRRPYSETS LLVDLFTEES GRLTVIAKGA RAKRSSWKSV LQPFTPLLLR WTGKSTLKTL TKAEPAAITL PLQQIALYSG FYVNELLTRV IESETPNPAL FQHYLKCLTG LATETNIEPT LRLFEFQLLQ ILGYGVDFLH CAGSGEPVDF SMTYRYREEK GFIASLVKDN LTFYGRDLLA FEALDFSDDA VRQAAKRFTR IALKPYLGDK PLKSRELFTQ NILLLK // ID RELE_HAEIN Reviewed; 102 AA. AC P44041; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Putative toxin RelE; GN Name=relE; OrderedLocusNames=HI_0711; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Its CC cognate antitoxin is RelB (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RelE toxin 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; L42023; AAC22368.1; -; Genomic_DNA. DR PIR; E64012; E64012. DR RefSeq; NP_438869.1; NC_000907.1. DR RefSeq; WP_005694595.1; NC_000907.1. DR ProteinModelPortal; P44041; -. DR STRING; 71421.HI0711; -. DR EnsemblBacteria; AAC22368; AAC22368; HI_0711. DR GeneID; 949734; -. DR KEGG; hin:HI0711; -. DR PATRIC; 20190043; VBIHaeInf48452_0742. DR eggNOG; COG3041; LUCA. DR KO; K19157; -. DR OMA; SKQFVRD; -. DR OrthoDB; EOG68Q0X7; -. DR PhylomeDB; P44041; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007712; RelE/ParE_toxin. DR InterPro; IPR004386; Toxin_YafQ-like. DR Pfam; PF15738; YafQ_toxin; 1. DR PIRSF; PIRSF006156; YafQ; 1. DR TIGRFAMs; TIGR02385; RelE_StbE; 1. DR TIGRFAMs; TIGR00053; TIGR00053; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Toxin. FT CHAIN 1 102 Putative toxin RelE. FT /FTId=PRO_0000168541. SQ SEQUENCE 102 AA; 11908 MW; 410DBEAD23CD5892 CRC64; MSEEKPLKVS YSKQFVRDLT DLAKRSPNVL IGSKYITAIH CLLNRLPLPE NYQDHALVGE WKGYRDCHIQ GDLVLIYQYV IQDEFDELKF SRLNIHSQTA LK // ID RIMI_HAEIN Reviewed; 146 AA. AC P44305; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Ribosomal-protein-alanine acetyltransferase; DE EC=2.3.1.128; DE AltName: Full=Acetylating enzyme for N-terminal of ribosomal protein S18; GN Name=rimI; OrderedLocusNames=HI_0010; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This enzyme acetylates the N-terminal alanine of a CC ribosomal protein S18. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + ribosomal-protein L-alanine = CoA CC + ribosomal-protein N-acetyl-L-alanine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21688.1; -; Genomic_DNA. DR RefSeq; NP_438183.1; NC_000907.1. DR RefSeq; WP_010868917.1; NC_000907.1. DR ProteinModelPortal; P44305; -. DR SMR; P44305; 1-146. DR STRING; 71421.HI0010; -. DR EnsemblBacteria; AAC21688; AAC21688; HI_0010. DR GeneID; 950907; -. DR KEGG; hin:HI0010; -. DR PATRIC; 20188471; VBIHaeInf48452_0010. DR eggNOG; ENOG4105KEG; Bacteria. DR eggNOG; COG0456; LUCA. DR KO; K03789; -. DR OMA; FEGEQQV; -. DR OrthoDB; EOG6D8B8B; -. DR PhylomeDB; P44305; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0008999; F:ribosomal-protein-alanine N-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0017189; P:N-terminal peptidyl-alanine acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR006464; Rbsml_AcTrfase. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR01575; rimI; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 146 Ribosomal-protein-alanine FT acetyltransferase. FT /FTId=PRO_0000074565. FT DOMAIN 2 146 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 146 AA; 16745 MW; CA4B7DB5B9BADFD3 CRC64; MSIISQIEAC DFERLYEIEQ QAHLVPWSFG TLKNNQGERY LNLKLIENNQ IIGFAICQTV LDEATLFNIA ILPTYQGCGF GKLLLGKLIF QLKEKGVQTL WLEVRESNSA RFLYEKIGFN EVDIRKNYYP KPSGGRENAV VMACYL // ID RL11_HAEIN Reviewed; 142 AA. AC P44351; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 100. 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=HI_0517; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22175.1; -; Genomic_DNA. DR PIR; A64074; A64074. DR RefSeq; NP_438675.1; NC_000907.1. DR RefSeq; WP_005630840.1; NC_000907.1. DR ProteinModelPortal; P44351; -. DR SMR; P44351; 2-142. DR STRING; 71421.HI0517; -. DR EnsemblBacteria; AAC22175; AAC22175; HI_0517. DR GeneID; 949669; -. DR KEGG; hin:HI0517; -. DR PATRIC; 20189587; VBIHaeInf48452_0536. DR eggNOG; ENOG4108UIK; Bacteria. DR eggNOG; COG0080; LUCA. DR KO; K02867; -. DR OMA; CKQFNAK; -. DR OrthoDB; EOG69PQ9D; -. DR PhylomeDB; P44351; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.10.250; -; 1. DR Gene3D; 3.30.1550.10; -; 1. DR HAMAP; MF_00736; Ribosomal_L11; 1. DR InterPro; IPR000911; Ribosomal_L11/L12. DR InterPro; IPR006519; Ribosomal_L11_bac-typ. DR InterPro; IPR020783; Ribosomal_L11_C. DR InterPro; 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 2 142 50S ribosomal protein L11. FT /FTId=PRO_0000104294. SQ SEQUENCE 142 AA; 14904 MW; 837E3770A9F056A0 CRC64; MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNARTESLE KGLPIPVVIT VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK VTLDQVRQIA ETKAADMTGA TIETKMKSIA GTARSMGLVV EE // ID RHLB_HAEIN Reviewed; 415 AA. AC P44922; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2003, sequence version 2. DT 11-MAY-2016, entry version 107. DE RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000255|HAMAP-Rule:MF_00661}; DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00661}; GN Name=rhlB {ECO:0000255|HAMAP-Rule:MF_00661}; GN OrderedLocusNames=HI_0892; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has CC RNA-dependent ATPase activity and unwinds double-stranded RNA. CC {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. CC {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00661}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22552.1; 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; L42023; AAC22552.1; ALT_INIT; Genomic_DNA. DR PIR; E64100; E64100. DR RefSeq; NP_439053.1; NC_000907.1. DR ProteinModelPortal; P44922; -. DR STRING; 71421.HI0892; -. DR EnsemblBacteria; AAC22552; AAC22552; HI_0892. DR GeneID; 949895; -. DR KEGG; hin:HI0892; -. DR PATRIC; 20190441; VBIHaeInf48452_0934. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR KO; K03732; -. DR OMA; FIRDIRY; -. DR OrthoDB; EOG6GBMBM; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00661; DEAD_helicase_RhlB; 1. 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; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR023554; RNA_helicase_ATP-dep_RhlB. 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; PS00039; DEAD_ATP_HELICASE; 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; Cytoplasm; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 415 ATP-dependent RNA helicase RhlB. FT /FTId=PRO_0000200773. FT DOMAIN 40 218 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00661}. FT DOMAIN 241 389 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00661}. FT NP_BIND 53 60 ATP. {ECO:0000255|HAMAP-Rule:MF_00661}. FT MOTIF 9 37 Q motif. FT MOTIF 164 167 DEAD box. SQ SEQUENCE 415 AA; 46659 MW; E543BF942BA6530C CRC64; MQQDYLSQQR FSALPLHPIV RGALAKKGFD FCTPIQALSL PISLNGRDVA GQAQTGTGKT MAFLTATFHH LLTHQDPNLK YPHPRALILA PTRELAVQIS NDAEFLAKAS GLKTALAYGG DGYDKQLQAI ERGVDILIGT TGRVIDYVKQ GVIGLDEIQV VVLDEADRMF DLGFIRDIRY LLRKCPAPQA RLTMLFSATL SYKVRELAFE DMNEPEYIEI EPEQKTGHRI KEELFYPSNQ DKMALLLTLM EDEWPERCIV FANTKHRCEE IWGYLAADGH RVGLLTGDVA QKKRLSLLKQ FTDGDLDILV ATDVAARGLH ISDVTHVFNY DLPDDREDYV HRIGRTGRAG ESGVSISFAC EEYAMNLPAI EEYIGHSIPV SQYETEALLE LPKPYRLKRA VPPQGHTRHR SYHAK // ID RIBB_HAEIN Reviewed; 215 AA. AC P44866; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00180}; DE Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_00180}; DE EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_00180}; GN Name=ribB {ECO:0000255|HAMAP-Rule:MF_00180}; GN OrderedLocusNames=HI_0764; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00180}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00180}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00180}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00180}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000255|HAMAP-Rule:MF_00180}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00180}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00180}. CC -!- SIMILARITY: Belongs to the DHBP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22422.1; -; Genomic_DNA. DR PIR; E64091; E64091. DR RefSeq; NP_438923.1; NC_000907.1. DR RefSeq; WP_005652350.1; NC_000907.1. DR ProteinModelPortal; P44866; -. DR SMR; P44866; 1-213. DR STRING; 71421.HI0764; -. DR EnsemblBacteria; AAC22422; AAC22422; HI_0764. DR GeneID; 950808; -. DR KEGG; hin:HI0764; -. DR PATRIC; 20190179; VBIHaeInf48452_0803. DR eggNOG; ENOG4105C66; Bacteria. DR eggNOG; COG0108; LUCA. DR KO; K02858; -. DR OMA; QMAKLIR; -. DR OrthoDB; EOG679TK8; -. DR PhylomeDB; P44866; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00180; RibB; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR Pfam; PF00926; DHBP_synthase; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Magnesium; Manganese; Metal-binding; KW Reference proteome; Riboflavin biosynthesis. FT CHAIN 1 215 3,4-dihydroxy-2-butanone 4-phosphate FT synthase. FT /FTId=PRO_0000151800. FT REGION 38 39 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00180}. FT REGION 151 155 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00180}. FT METAL 39 39 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00180}. FT METAL 39 39 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00180}. FT METAL 154 154 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00180}. FT BINDING 43 43 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00180}. FT BINDING 175 175 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00180}. FT SITE 137 137 Essential for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00180}. FT SITE 175 175 Essential for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00180}. SQ SEQUENCE 215 AA; 23254 MW; 51E47507E25E63A9 CRC64; MNQSILSPFG NTAEERVLNA INAFKNGTGV LVLDDEDREN EGDLIFPAET ITPEQMAKLI RYGSGIVCLC ITDERCQQLD LPPMVEHNNS VNKTAFTVTI EAAKGVSTGV SAADRVTTIQ TAIADNAVLT DLHRPGHVFP LRAANGGVLT RRGHTEASVD LARLAGFKEA GVICEITNDD GTMARAPEIV EFAKKFGYSV LTIEDLVEYR LAHNI // ID RHO_HAEIN Reviewed; 420 AA. AC P44619; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Transcription termination factor Rho {ECO:0000255|HAMAP-Rule:MF_01884}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884}; DE AltName: Full=ATP-dependent helicase Rho {ECO:0000255|HAMAP-Rule:MF_01884}; GN Name=rho {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=HI_0295; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Facilitates transcription termination by a mechanism CC that involves Rho binding to the nascent RNA, activation of Rho's CC RNA-dependent ATPase activity, and release of the mRNA from the CC DNA template. {ECO:0000255|HAMAP-Rule:MF_01884}. CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring CC structure. {ECO:0000255|HAMAP-Rule:MF_01884}. CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP- CC Rule:MF_01884}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21959.1; -; Genomic_DNA. DR PIR; B64060; B64060. DR RefSeq; NP_438462.1; NC_000907.1. DR RefSeq; WP_005648966.1; NC_000907.1. DR ProteinModelPortal; P44619; -. DR SMR; P44619; 1-418. DR STRING; 71421.HI0295; -. DR PRIDE; P44619; -. DR EnsemblBacteria; AAC21959; AAC21959; HI_0295. DR GeneID; 949491; -. DR KEGG; hin:HI0295; -. DR PATRIC; 20189129; VBIHaeInf48452_0311. DR eggNOG; ENOG4105C4P; Bacteria. DR eggNOG; COG1158; LUCA. DR KO; K03628; -. DR OMA; FLRAPDY; -. DR OrthoDB; EOG6N681W; -. DR PhylomeDB; P44619; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01884; Rho; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011112; Rho_N. DR InterPro; IPR011113; Rho_RNA-bd. DR InterPro; IPR004665; Term_rho. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF07498; Rho_N; 1. DR Pfam; PF07497; Rho_RNA_bind; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00959; Rho_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF68912; SSF68912; 1. DR TIGRFAMs; TIGR00767; rho; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding; Transcription; KW Transcription regulation; Transcription termination. FT CHAIN 1 420 Transcription termination factor Rho. FT /FTId=PRO_0000188965. FT NP_BIND 170 175 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. FT NP_BIND 182 187 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. FT BINDING 213 213 ATP. {ECO:0000255|HAMAP-Rule:MF_01884}. SQ SEQUENCE 420 AA; 46978 MW; 73C486F4A92017BA CRC64; MHLTELKNTP VSDLVKLGEE QMGLENLARL RKQDIVFAIL KQHAKSGEDI FGGGVLEILP DGFGFLRSAD SSYLAGPDDI YVSPSQIRRF NLQTGDKIEG KIRPPKEGER YFALLKVDQV NDDKPEVSRS KILFENLTPL HANSRLRMER GNGSTEDLTA RILDLASPIG KGQRGLIVAP PKAGKTMLLQ NIAQSITHNY PDVELIVLLI DERPEEVTEM QRSVKGEVIA STFDEPATRH VQVAEMVIEK AKRSVEHKKD VVILLDSITR LARAYNTVTP ASGKILSGGV DANALHRPKR FFGAARNVEE GGSLTIIATA LVDTGSKMDE VIFEEFKGTG NMELHLSRKI AERRVFPAID FKRSGTRKED LLTTADELQK MWILRKILNP MDEVDAMEFL IDKLMMAKTN EEFFEVMKRS // ID RIR2_HAEIN Reviewed; 376 AA. AC P43755; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 120. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=nrdB; OrderedLocusNames=HI_1660; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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. {ECO:0000255|PROSITE-ProRule:PRU10014}. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23306.1; -; Genomic_DNA. DR PIR; C64135; C64135. DR RefSeq; NP_439802.1; NC_000907.1. DR RefSeq; WP_005650087.1; NC_000907.1. DR ProteinModelPortal; P43755; -. DR SMR; P43755; 2-342. DR STRING; 71421.HI1660; -. DR PRIDE; P43755; -. DR EnsemblBacteria; AAC23306; AAC23306; HI_1660. DR GeneID; 950858; -. DR KEGG; hin:HI1660; -. DR PATRIC; 20192069; VBIHaeInf48452_1738. DR eggNOG; ENOG4105E05; Bacteria. DR eggNOG; COG0208; LUCA. DR KO; K00526; -. DR OMA; LEPMFLG; -. DR OrthoDB; EOG6J48J7; -. DR PhylomeDB; P43755; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. 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; IPR000358; RNR_small. DR InterPro; IPR030475; RNR_small_AS. DR PANTHER; PTHR23409; PTHR23409; 2. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 376 Ribonucleoside-diphosphate reductase FT subunit beta. FT /FTId=PRO_0000190479. FT ACT_SITE 123 123 {ECO:0000255|PROSITE-ProRule:PRU10014}. FT METAL 85 85 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU10014}. FT METAL 116 116 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU10014}. FT METAL 116 116 Iron 2. {ECO:0000250}. FT METAL 119 119 Iron 1. {ECO:0000255|PROSITE- FT ProRule:PRU10014}. FT METAL 205 205 Iron 2. {ECO:0000250}. FT METAL 239 239 Iron 2. {ECO:0000250}. FT METAL 242 242 Iron 2. {ECO:0000250}. SQ SEQUENCE 376 AA; 43326 MW; F3B8FD9EAF9C7238 CRC64; MAYTTFSQNK NDQLKEPMFF GQNVNVARYD QQKYETFEKL IEKQLSFFWR PEEVDVSQDR IDYAALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLV SIPELETWIE TWTFSETIHS RSYTHIIRNI VNDPSIVFDD IVTNEEIIKR AQDISSYYDD LIRDSQLYGL YGEGTYTVDG KECVVTLRSL KKQLYLCLMS VNALEAIRFY VSFACSFAFA ERRLMEGNAK IIKFIARDEA LHLTGTQHIL NIMAAGQDDP EMAEIAEECK QEAYDLFVAA AEQEKAWADY LFKDGSMIGL NRDILVQYVE YITNIRMQAV GLPLPFQTRS NPIPWINAWL VSDNVQVAPQ EVEVSSYLVG QIDSKVDTND FDDFSL // ID RISA_HAEIN Reviewed; 204 AA. AC P45273; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Riboflavin synthase; DE Short=RS; DE EC=2.5.1.9; GN Name=ribE; Synonyms=ribC; OrderedLocusNames=HI_1613; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the dismutation of two molecules of 6,7- CC dimethyl-8-ribityllumazine, resulting in the formation of CC riboflavin and 5-amino-6-(D-ribitylamino)uracil. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = CC riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 2/2. CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SIMILARITY: Contains 2 lumazine-binding repeats. CC {ECO:0000255|PROSITE-ProRule:PRU00524}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23257.1; -; Genomic_DNA. DR PIR; E64132; E64132. DR RefSeq; NP_439755.1; NC_000907.1. DR RefSeq; WP_005693624.1; NC_000907.1. DR ProteinModelPortal; P45273; -. DR SMR; P45273; 1-202. DR STRING; 71421.HI1613; -. DR EnsemblBacteria; AAC23257; AAC23257; HI_1613. DR GeneID; 950465; -. DR KEGG; hin:HI1613; -. DR PATRIC; 20191957; VBIHaeInf48452_1686. DR eggNOG; ENOG4108R6K; Bacteria. DR eggNOG; COG0307; LUCA. DR KO; K00793; -. DR OMA; HILSGHV; -. DR OrthoDB; EOG6VMTQH; -. DR PhylomeDB; P45273; -. DR UniPathway; UPA00275; UER00405. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.40.30.20; -; 2. DR InterPro; IPR023366; ATPase_asu-like. DR InterPro; IPR001783; Lumazine-bd. DR InterPro; IPR026017; Lumazine-bd_dom. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR21098; PTHR21098; 1. DR Pfam; PF00677; Lum_binding; 2. DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1. DR SUPFAM; SSF63380; SSF63380; 2. DR TIGRFAMs; TIGR00187; ribE; 1. DR PROSITE; PS51177; LUMAZINE_BIND; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; KW Riboflavin biosynthesis; Transferase. FT CHAIN 1 204 Riboflavin synthase. FT /FTId=PRO_0000068167. FT REPEAT 1 97 Lumazine-binding 1. FT REPEAT 98 195 Lumazine-binding 2. FT REGION 4 6 Substrate 1 binding. FT {ECO:0000250|UniProtKB:Q2YN92}. FT REGION 48 50 Substrate 2 binding; shared with one FT trimeric partner. FT {ECO:0000250|UniProtKB:Q2YN92}. FT REGION 62 67 Substrate 2 binding; shared with one FT trimeric partner. FT {ECO:0000250|UniProtKB:P0AFU8}. FT REGION 101 103 Substrate 2 binding; shared with one FT trimeric partner. FT {ECO:0000250|UniProtKB:Q2YN92}. FT REGION 146 148 Substrate 1 binding. FT {ECO:0000250|UniProtKB:Q2YN92}. FT REGION 160 165 Substrate 1 binding. FT {ECO:0000250|UniProtKB:Q2YN92}. FT BINDING 137 137 Substrate 2 binding. FT {ECO:0000250|UniProtKB:Q2YN92}. SQ SEQUENCE 204 AA; 22590 MW; B7C2172F88BC1DA4 CRC64; MFTGIVQGTA PIHSIKEKAN FRTQVVKLLP EMRKDLEIGA SIANNGVCLT VTEINGDLVS FDLMQETLKI TNLGTVKVGD YVNIERAMQM GTEIGGHLLS GHIYCTAKIS DIIASENNRQ IWFELPSADV MKYILTKGFV AVDGISLTIG EVRDTQFCVN LIPETLQRTL MGRRKVGDIV NIEIDPQTQA IVDTVENYLQ SKNF // ID RL15_HAEIN Reviewed; 144 AA. AC P44353; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 91. 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=HI_0797; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22455.1; -; Genomic_DNA. DR PIR; F64094; F64094. DR RefSeq; NP_438956.1; NC_000907.1. DR RefSeq; WP_005648410.1; NC_000907.1. DR ProteinModelPortal; P44353; -. DR SMR; P44353; 1-144. DR STRING; 71421.HI0797; -. DR EnsemblBacteria; AAC22455; AAC22455; HI_0797. DR GeneID; 949815; -. DR KEGG; hin:HI0797; -. DR PATRIC; 20190245; VBIHaeInf48452_0836. DR eggNOG; ENOG4108UZ0; Bacteria. DR eggNOG; COG0200; LUCA. DR KO; K02876; -. DR OMA; HKGQWAR; -. DR OrthoDB; EOG6CGCM5; -. DR PhylomeDB; P44353; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01341; Ribosomal_L15; 1. DR InterPro; IPR030878; Ribosomal_L15. DR InterPro; IPR005749; Ribosomal_L15_bac-type. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR PANTHER; PTHR12934; PTHR12934; 1. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR TIGRFAMs; TIGR01071; rplO_bact; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 144 50S ribosomal protein L15. FT /FTId=PRO_0000104730. SQ SEQUENCE 144 AA; 15072 MW; F0CFC80684DC64C5 CRC64; MRLNTLSPAE GAKHSAKRLG RGIGSGLGKT GGRGHKGQKS RTGGGVRRGF EGGQMPLYRR LPKFGFTSMK SAVTAEVRLN ELTKVEGNVV TLETLKAANI LTKDIQFAKV ILAGEVKSAV TVRGLRVTKG AKAAIEAAGG SIEE // ID RIBF_HAEIN Reviewed; 308 AA. AC P44957; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=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=HI_0963; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC22622.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22622.1; ALT_INIT; Genomic_DNA. DR PIR; H64162; H64162. DR RefSeq; NP_439124.1; NC_000907.1. DR ProteinModelPortal; P44957; -. DR STRING; 71421.HI0963; -. DR EnsemblBacteria; AAC22622; AAC22622; HI_0963. DR GeneID; 949965; -. DR KEGG; hin:HI0963; -. DR PATRIC; 20190585; VBIHaeInf48452_1005. DR eggNOG; ENOG4105DTN; Bacteria. DR eggNOG; COG0196; LUCA. DR KO; K11753; -. DR OMA; FPTANMR; -. DR OrthoDB; EOG6QP0ZV; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000579; 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 1 308 Riboflavin biosynthesis protein RibF. FT /FTId=PRO_0000194140. SQ SEQUENCE 308 AA; 35121 MW; 5DA4EA0F5492923E CRC64; MQLIRGLHNA NRVLQGCALT IGNFDGVHLG HQTVLRHLRQ KADELNLPMA VLLFESQPRE YFMGKNAPAR LMRLRDKIYY LEKAKVDVVI VAKFDRTFAE QLADVFIEQT LVNHLHVKFL SIGDDFKFGS KRQGNFAMLQ AASKRFGFIV EDNRSFCLDA QRISSTAIRE ALANDDLQLA ENLLGKPYRI FGRVIHGNKL GRTIGFPTAN IRLHRQVNPI KGVYAVKVRL KSGEIFNGVA NMGKRPTING LMQLLEVHLF DFSQNIYGQM VEVEFCHKIR NEIKFPSFDD LKVQIEKDVE TAKAFFNS // ID RIMK_HAEIN Reviewed; 302 AA. AC P45241; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552}; DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552}; GN Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552}; GN OrderedLocusNames=HI_1531; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01552}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01552}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01552}; CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP- CC Rule:MF_01552}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_01552}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23177.1; -; Genomic_DNA. DR PIR; H64127; H64127. DR RefSeq; NP_439680.1; NC_000907.1. DR RefSeq; WP_005693559.1; NC_000907.1. DR ProteinModelPortal; P45241; -. DR STRING; 71421.HI1531; -. DR EnsemblBacteria; AAC23177; AAC23177; HI_1531. DR GeneID; 950393; -. DR KEGG; hin:HI1531; -. DR PATRIC; 20191787; VBIHaeInf48452_1602. DR eggNOG; ENOG4105D9I; Bacteria. DR eggNOG; COG0189; LUCA. DR KO; K05844; -. DR OMA; NYLRCYM; -. DR OrthoDB; EOG6DZDX8; -. DR PhylomeDB; P45241; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01552; RimK; 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 InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR023533; RimK. 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; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 302 Probable alpha-L-glutamate ligase. FT /FTId=PRO_0000205459. FT DOMAIN 112 294 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_01552}. FT NP_BIND 185 186 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}. FT NP_BIND 218 220 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}. FT METAL 255 255 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01552}. FT METAL 267 267 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01552}. FT METAL 267 267 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01552}. FT METAL 269 269 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01552}. FT BINDING 148 148 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}. FT BINDING 194 194 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}. SQ SEQUENCE 302 AA; 33262 MW; 318381BDFD4EAF9E CRC64; MKLLMLCREP RLYSCQRLKE AAKHQGHEMD ILDPNHCFLK LSQNPPHFQI FYQENSESKP YLLSDYDAVL PRFGTTSTQM GCSVLQHFEG KGTFCLNSSQ AFLNARDKWK SLQLLLKAGI PVPNSLLSGG EVQAQATIPH ISSPTILKTL NGSQGIGVIL AEKPQSAVSI MEAFKQTNIS MLQQDFIEEA GNADIRCFVI GDQVVATMQR IGQNGEFRAN CHRGGKTEKI TLSDEEKQIA IQATKAIGLD VAGVDLIRSK KGLLVLEVNA SPGLEMIEKT SGIDIAAEII DYIEINAFIN SR // ID RIMP_HAEIN Reviewed; 151 AA. AC P45138; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 17-FEB-2016, entry version 87. DE RecName: Full=Ribosome maturation factor RimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN Name=rimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN OrderedLocusNames=HI_1282; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for maturation of 30S ribosomal subunits. CC {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01077}. CC -!- SIMILARITY: Belongs to the RimP family. {ECO:0000255|HAMAP- CC Rule:MF_01077}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22931.1; 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; L42023; AAC22931.1; ALT_INIT; Genomic_DNA. DR PIR; I64169; I64169. DR RefSeq; NP_439434.2; NC_000907.1. DR RefSeq; WP_005657488.1; NC_000907.1. DR ProteinModelPortal; P45138; -. DR STRING; 71421.HI1282; -. DR EnsemblBacteria; AAC22931; AAC22931; HI_1282. DR GeneID; 950221; -. DR KEGG; hin:HI1282; -. DR PATRIC; 20191247; VBIHaeInf48452_1334. DR eggNOG; ENOG4105K7D; Bacteria. DR eggNOG; COG0779; LUCA. DR KO; K09748; -. DR OMA; NIQKANI; -. DR OrthoDB; EOG6NSGP3; -. DR PhylomeDB; P45138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.180; -; 1. DR Gene3D; 3.30.300.70; -; 1. DR HAMAP; MF_01077; RimP; 1. DR InterPro; IPR003728; Ribosome_maturation_RimP. DR InterPro; IPR028998; RimP_C. DR InterPro; IPR028989; RimP_N. DR Pfam; PF02576; DUF150; 1. DR SUPFAM; SSF74942; SSF74942; 1. DR SUPFAM; SSF75420; SSF75420; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Ribosome biogenesis. FT CHAIN 1 151 Ribosome maturation factor RimP. FT /FTId=PRO_0000181876. SQ SEQUENCE 151 AA; 17267 MW; 92A46B8A58BF6E01 CRC64; MATLEQNLQE MLQDAVEDLG CELWGIECQR VGRFMTVRLF IDKDGGVTVD DCADVSRQVS AILDVEDPIA DKYNLEVSSP GLDRPLFTLP QFERYIGQDI AVHLRIPVME RRKWQGKLER IEKDMITLIV DDQEQILVFG NIQKANVVAK F // ID RIR1_HAEIN Reviewed; 756 AA. AC P43754; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdA; OrderedLocusNames=HI_1659; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 to separate CC specificity and activation sites on the alpha subunit. 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 Stimulated by ATP and inhibited by dATP binding to the activity CC site (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 -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|PROSITE- CC ProRule:PRU00492}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23305.1; 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; L42023; AAC23305.1; ALT_INIT; Genomic_DNA. DR PIR; B64135; B64135. DR RefSeq; NP_439801.2; NC_000907.1. DR RefSeq; WP_005694386.1; NC_000907.1. DR ProteinModelPortal; P43754; -. DR SMR; P43754; 5-737. DR STRING; 71421.HI1659; -. DR PRIDE; P43754; -. DR EnsemblBacteria; AAC23305; AAC23305; HI_1659. DR GeneID; 950495; -. DR KEGG; hin:HI1659; -. DR PATRIC; 20192067; VBIHaeInf48452_1737. DR eggNOG; ENOG4105BZH; Bacteria. DR eggNOG; COG0209; LUCA. DR KO; K00525; -. DR OMA; YELLWQM; -. DR OrthoDB; EOG6J48HC; -. DR PhylomeDB; P43754; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF48168; SSF48168; 1. DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1. DR PROSITE; PS51161; ATP_CONE; 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 1 756 Ribonucleoside-diphosphate reductase FT subunit alpha. FT /FTId=PRO_0000187214. FT DOMAIN 5 95 ATP-cone. {ECO:0000255|PROSITE- FT ProRule:PRU00492}. FT REGION 15 21 Allosteric activator binding. FT {ECO:0000250}. FT REGION 224 225 Substrate binding. {ECO:0000250}. FT REGION 437 441 Substrate binding. {ECO:0000250}. FT REGION 621 625 Substrate binding. {ECO:0000250}. FT ACT_SITE 437 437 Proton acceptor. {ECO:0000250}. FT ACT_SITE 439 439 Cysteine radical intermediate. FT {ECO:0000250}. FT ACT_SITE 441 441 Proton acceptor. {ECO:0000250}. FT BINDING 9 9 Allosteric activator. {ECO:0000250}. FT BINDING 55 55 Allosteric activator. {ECO:0000250}. FT BINDING 91 91 Allosteric activator. {ECO:0000250}. FT BINDING 209 209 Substrate. {ECO:0000250}. FT BINDING 253 253 Substrate; via amide nitrogen. FT {ECO:0000250}. FT SITE 225 225 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 232 232 Allosteric effector binding. FT {ECO:0000250}. FT SITE 262 262 Allosteric effector binding. FT {ECO:0000250}. FT SITE 462 462 Important for hydrogen atom transfer. FT {ECO:0000250}. FT SITE 730 730 Important for electron transfer. FT {ECO:0000250}. FT SITE 731 731 Important for electron transfer. FT {ECO:0000250}. FT SITE 749 749 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT SITE 754 754 Interacts with thioredoxin/glutaredoxin. FT {ECO:0000250}. FT DISULFID 225 462 Redox-active. {ECO:0000250}. SQ SEQUENCE 756 AA; 85696 MW; 839D02FA61E185D3 CRC64; MNKSLMVTKR DGTQEQINLD KIHRVITWAA EGLDNVSVSQ VELRSHIQFY EGIRTSDIHE TIIKAAADLI SKDSPDYQYL AARLAIFHLR KKAYGHFDPP RLYDHVKKLV RMEKYDQALL DDYTREEWDT MDGFIDHWRD MTFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYLLVSASL FSKYPKETRL DYVKRFYDAT STFKISLPTP IMAGVRTPTR QFSSCVLIEC DDSLDSINAT ASAIVKYVSQ RAGIGINAGA IRALGSEIRG GEAFHTGCIP FYKYFQTAVK SCSQGGVRGG AATLYYPIWH LEAENLLVLK NNRGVEDNRV RHMDYGVQLN KLMYQRLIKG SEITLFSPSD VPGLYEAFFA DQDKFEELYV KYEQDPTIRK RTVKAVEIFS LLMQERASTG RIYIQNVDHC NTHSPFDPQV APVRQSNLCL EIALPTKPLQ HINDENGEIA LCTLSAFNLG KIENLDELEE LADLAVRSLD ALLDYQDYPV VAAKRSSLAR RSLGIGVINY AYYLAKNGVR YSDGSANDLT HRTFEAIQYY LLKASMNLAK EQGACEYFNE TTYAKGILPI DTYKKDLDSL TQEPLHYDWE SLRKDIQEFG LRNSTLTALM PSETSSQISN ATNGIEPPRG HVSIKASKDG ILKQVVPEYE NLMDNYELLW DIPSNDGYLH LVGIMQKFVD QAISANTNYD PKRFEDGKVP MKVLLKDLLT AYKYGLKTLY YQNTRDGAED VQEDLDDGCA GGACKI // ID RISB_HAEIN Reviewed; 157 AA. AC P45149; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00178}; DE Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178}; DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178}; GN Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178}; GN OrderedLocusNames=HI_1303; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8- CC ribityllumazine by condensation of 5-amino-6-(D- CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. CC This is the penultimate step in the biosynthesis of riboflavin. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5- CC amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D- CC ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00178}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, CC arranged as a dodecamer of pentamers. {ECO:0000255|HAMAP- CC Rule:MF_00178}. CC -!- SIMILARITY: Belongs to the DMRL synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00178}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22950.1; 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; L42023; AAC22950.1; ALT_INIT; Genomic_DNA. DR PIR; C64115; C64115. DR RefSeq; NP_439454.2; NC_000907.1. DR RefSeq; WP_005694466.1; NC_000907.1. DR ProteinModelPortal; P45149; -. DR SMR; P45149; 1-155. DR STRING; 71421.HI1303; -. DR EnsemblBacteria; AAC22950; AAC22950; HI_1303. DR GeneID; 949500; -. DR KEGG; hin:HI1303; -. DR PATRIC; 20191289; VBIHaeInf48452_1355. DR eggNOG; ENOG4108UTT; Bacteria. DR eggNOG; COG0054; LUCA. DR KO; K00794; -. DR OMA; WNYALQA; -. DR OrthoDB; EOG6RC3WC; -. DR PhylomeDB; P45149; -. DR BRENDA; 2.5.1.78; 2529. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.960; -; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR002180; DMRL_synthase. DR PANTHER; PTHR21058; PTHR21058; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; SSF52121; 1. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Riboflavin biosynthesis; KW Transferase. FT CHAIN 1 157 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_0000134761. FT REGION 57 59 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 81 83 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT REGION 86 87 1-deoxy-L-glycero-tetrulose 4-phosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT ACT_SITE 89 89 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00178}. FT BINDING 22 22 5-amino-6-(D-ribitylamino)uracil. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 114 114 5-amino-6-(D-ribitylamino)uracil; via FT amide nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00178}. FT BINDING 128 128 1-deoxy-L-glycero-tetrulose 4-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00178}. SQ SEQUENCE 157 AA; 16419 MW; C811F2BEC4BB1AB2 CRC64; MKVLEGSVAA PNAKVAVVIA RFNSFINESL LEGAIDALKR IGQVKDENIT IVRTPGAYEL PLVARRLAES KKFDAIVALG TVIRGGTAHF EYVAGEASSG LGKVAMDAEI PVAFGVLTTE NIEQAIERAG TKAGNKGAEA ALTALEMVNL IQQIDAA // ID RL13_HAEIN Reviewed; 142 AA. AC P44387; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-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=HI_1443; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23093.1; -; Genomic_DNA. DR PIR; G64123; G64123. DR RefSeq; NP_439595.1; NC_000907.1. DR RefSeq; WP_005650450.1; NC_000907.1. DR ProteinModelPortal; P44387; -. DR SMR; P44387; 1-142. DR STRING; 71421.HI1443; -. DR EnsemblBacteria; AAC23093; AAC23093; HI_1443. DR GeneID; 950831; -. DR KEGG; hin:HI1443; -. DR PATRIC; 20191591; VBIHaeInf48452_1505. DR eggNOG; ENOG4108UM5; Bacteria. DR eggNOG; COG0102; LUCA. DR KO; K02871; -. DR OMA; YTPHMDC; -. DR OrthoDB; EOG628FBD; -. DR PhylomeDB; P44387; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.90.1180.10; -; 1. DR HAMAP; MF_01366; Ribosomal_L13; 1. DR InterPro; IPR005822; Ribosomal_L13. DR InterPro; IPR005823; Ribosomal_L13_bac-type. DR InterPro; IPR023563; Ribosomal_L13_CS. DR InterPro; IPR023564; Ribosomal_L13_dom. DR PANTHER; PTHR11545; PTHR11545; 1. DR Pfam; PF00572; Ribosomal_L13; 1. DR PIRSF; PIRSF002181; Ribosomal_L13; 1. DR SUPFAM; SSF52161; SSF52161; 1. DR TIGRFAMs; TIGR01066; rplM_bact; 1. DR PROSITE; PS00783; RIBOSOMAL_L13; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 142 50S ribosomal protein L13. FT /FTId=PRO_0000133737. SQ SEQUENCE 142 AA; 15978 MW; CF2424E2DAA0C0B8 CRC64; MKTFVAKPET VKRDWYVVDA TGKTLGRLAT ELARRLRGKH KAEYTPHVDT GDYIIVINAD KVAVTGRKET DKLYYWHTGY VGGIKQATFK EMIARRPEAV IEIAVKGMLP KGPLGRAMFR KLKVYAGGEH QHAAQQPQVL DI // ID RL10_HAEIN Reviewed; 163 AA. AC P44350; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 94. DE RecName: Full=50S ribosomal protein L10; GN Name=rplJ; Synonyms=rpl10; OrderedLocusNames=HI_0640; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 2-8. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22300.1; -; Genomic_DNA. DR PIR; E64083; E64083. DR RefSeq; NP_438800.1; NC_000907.1. DR RefSeq; WP_010869025.1; NC_000907.1. DR ProteinModelPortal; P44350; -. DR STRING; 71421.HI0640; -. DR EnsemblBacteria; AAC22300; AAC22300; HI_0640. DR GeneID; 950716; -. DR KEGG; hin:HI0640; -. DR PATRIC; 20189887; VBIHaeInf48452_0668. DR eggNOG; ENOG4108VZM; Bacteria. DR eggNOG; COG0244; LUCA. DR KO; K02864; -. DR OMA; GVYIRVV; -. DR OrthoDB; EOG6DNTDR; -. DR PhylomeDB; P44350; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00362; Ribosomal_L10; 1. DR InterPro; IPR022973; Ribosomal_L10. DR InterPro; IPR002363; Ribosomal_L10_eubac_CS. DR InterPro; IPR001790; Ribosomal_L10P. DR Pfam; PF00466; Ribosomal_L10; 1. DR PROSITE; PS01109; RIBOSOMAL_L10; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10675023}. FT CHAIN 2 163 50S ribosomal protein L10. FT /FTId=PRO_0000154639. SQ SEQUENCE 163 AA; 17763 MW; 01CEEC8F9E314209 CRC64; MALNLQDKQA IVAEVNEAAK GALSAVIADS RGVTVEKMTE LRKSAREAGV TMRVVRNTLL RRAVEGTDYE CLKDTFVGPT LIAFSNEHPG ARARLFKEFA KANDKFEIKG AAFEGKIQDV EFLATLPTYE EAIARLMGTM KEAAAGKLAR TFAALRDKLQ EAA // ID RL16_HAEIN Reviewed; 136 AA. AC P44354; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. 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=HI_0784; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22443.1; -; Genomic_DNA. DR PIR; C64093; C64093. DR RefSeq; NP_438943.1; NC_000907.1. DR RefSeq; WP_005648425.1; NC_000907.1. DR ProteinModelPortal; P44354; -. DR SMR; P44354; 1-136. DR STRING; 71421.HI0784; -. DR PRIDE; P44354; -. DR EnsemblBacteria; AAC22443; AAC22443; HI_0784. DR GeneID; 950752; -. DR KEGG; hin:HI0784; -. DR PATRIC; 20190219; VBIHaeInf48452_0823. DR eggNOG; ENOG4108R70; Bacteria. DR eggNOG; COG0197; LUCA. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR PhylomeDB; P44354; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1170.10; -; 1. DR HAMAP; MF_01342; Ribosomal_L16; 1. DR InterPro; IPR016180; Ribosomal_L10e/L16. DR InterPro; IPR000114; Ribosomal_L16. DR InterPro; IPR020798; Ribosomal_L16_CS. DR PANTHER; PTHR12220; PTHR12220; 1. DR Pfam; PF00252; Ribosomal_L16; 1. DR PRINTS; PR00060; RIBOSOMALL16. DR SUPFAM; SSF54686; SSF54686; 1. DR TIGRFAMs; TIGR01164; rplP_bact; 1. DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1. DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 136 50S ribosomal protein L16. FT /FTId=PRO_0000062112. SQ SEQUENCE 136 AA; 15232 MW; 7D785E27C8349AA0 CRC64; MLQPKRTKFR KVHKGRNRGI ASGTEVSFGT YGLKAVGRCR LTARQIEAAR RAMSRAVKRQ GKIWIRVFPD KPITEKPLEV RMGKGKGNVE YWVALIQPGK VLYEMDGVSE EVARNAFALA AAKLPVKTTF VTKTVM // ID RL18_HAEIN Reviewed; 117 AA. AC P44356; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 94. 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=HI_0794; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22452.1; -; Genomic_DNA. DR PIR; C64094; C64094. DR RefSeq; NP_438953.1; NC_000907.1. DR RefSeq; WP_005625873.1; NC_000907.1. DR ProteinModelPortal; P44356; -. DR SMR; P44356; 1-117. DR STRING; 71421.HI0794; -. DR PRIDE; P44356; -. DR EnsemblBacteria; AAC22452; AAC22452; HI_0794. DR GeneID; 950639; -. DR KEGG; hin:HI0794; -. DR PATRIC; 20190239; VBIHaeInf48452_0833. DR eggNOG; ENOG4105K4C; Bacteria. DR eggNOG; COG0256; LUCA. DR KO; K02881; -. DR OMA; RAAKTRH; -. DR OrthoDB; EOG64NB48; -. DR PhylomeDB; P44356; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01337_B; Ribosomal_L18_B; 1. DR InterPro; IPR005484; Ribosomal_L18. DR InterPro; IPR004389; Ribosomal_L18_bac-type. DR Pfam; PF00861; Ribosomal_L18p; 1. DR TIGRFAMs; TIGR00060; L18_bact; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 117 50S ribosomal protein L18. FT /FTId=PRO_0000131272. SQ SEQUENCE 117 AA; 12768 MW; 1049FCF217D3037D CRC64; MDKKSARIRR AARARHMMRE QGVTRLVIHR TPRHIYAQVI APNGSEVLAA ASTVEKAIRE QVKYTGNKDA AAAVGKAVAE RALAKGVQAV AFDRSGFKYH GRVQTLADAA REAGLQF // ID RL20_HAEIN Reviewed; 117 AA. AC P44358; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 96. DE RecName: Full=50S ribosomal protein L20; GN Name=rplT; Synonyms=rpl20; OrderedLocusNames=HI_1320; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22965.1; -; Genomic_DNA. DR PIR; C64116; C64116. DR RefSeq; NP_439471.1; NC_000907.1. DR RefSeq; WP_005596075.1; NC_000907.1. DR ProteinModelPortal; P44358; -. DR SMR; P44358; 3-117. DR STRING; 71421.HI1320; -. DR PRIDE; P44358; -. DR EnsemblBacteria; AAC22965; AAC22965; HI_1320. DR GeneID; 4849480; -. DR GeneID; 950247; -. DR KEGG; hin:HI1320; -. DR PATRIC; 20191323; VBIHaeInf48452_1372. DR eggNOG; ENOG4108YZX; Bacteria. DR eggNOG; COG0292; LUCA. DR KO; K02887; -. DR OMA; WIRNRGP; -. DR OrthoDB; EOG6CGCMB; -. DR PhylomeDB; P44358; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:InterPro. DR HAMAP; MF_00382; Ribosomal_L20; 1. DR InterPro; IPR005813; Ribosomal_L20. DR PANTHER; PTHR10986; PTHR10986; 1. DR Pfam; PF00453; Ribosomal_L20; 1. DR PRINTS; PR00062; RIBOSOMALL20. DR TIGRFAMs; TIGR01032; rplT_bact; 1. DR PROSITE; PS00937; RIBOSOMAL_L20; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 117 50S ribosomal protein L20. FT /FTId=PRO_0000177165. SQ SEQUENCE 117 AA; 13341 MW; 086D2983B38E6BFC CRC64; MARVKRGVIA RARHKKVLKA AKGYYGARSR VYRVAFQAVI KAGQYAYRDR RQRKRQFRQL WIARINAAAR QNGLSYSKFI NGLKKASVEI DRKILADIAV FDKVAFAALV EKAKSAL // ID RL27_HAEIN Reviewed; 85 AA. AC P44363; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 94. 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=HI_0879; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22535.1; -; Genomic_DNA. DR PIR; F64099; F64099. DR RefSeq; NP_439040.1; NC_000907.1. DR RefSeq; WP_010869080.1; NC_000907.1. DR ProteinModelPortal; P44363; -. DR SMR; P44363; 2-85. DR STRING; 71421.HI0879; -. DR EnsemblBacteria; AAC22535; AAC22535; HI_0879. DR GeneID; 950621; -. DR KEGG; hin:HI0879; -. DR PATRIC; 20190415; VBIHaeInf48452_0921. DR eggNOG; ENOG4105K46; Bacteria. DR eggNOG; COG0211; LUCA. DR KO; K02899; -. DR OMA; NGRNNKK; -. DR OrthoDB; EOG6N94H6; -. DR PhylomeDB; P44363; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00539; Ribosomal_L27; 1. DR InterPro; IPR001684; Ribosomal_L27. DR InterPro; IPR018261; Ribosomal_L27_CS. DR PANTHER; PTHR15893; PTHR15893; 1. DR Pfam; PF01016; Ribosomal_L27; 1. DR PRINTS; PR00063; RIBOSOMALL27. DR ProDom; PD003114; Ribosomal_L27; 1. DR TIGRFAMs; TIGR00062; L27; 1. DR PROSITE; PS00831; RIBOSOMAL_L27; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 85 50S ribosomal protein L27. FT /FTId=PRO_0000181097. SQ SEQUENCE 85 AA; 9151 MW; 817170ED448324BD CRC64; MATKKAGGST RNGRDSEAKR LGVKRFGGES VLAGSIIVRQ RGTKFHAGNN VGMGRDHTLF ATADGKVKFE VKGEKSRKYV VIVTE // ID RL21_HAEIN Reviewed; 103 AA. AC P44359; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 91. 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=HI_0880; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22536.1; -; Genomic_DNA. DR PIR; G64099; G64099. DR RefSeq; NP_439041.1; NC_000907.1. DR RefSeq; WP_010869081.1; NC_000907.1. DR STRING; 71421.HI0880; -. DR PRIDE; P44359; -. DR EnsemblBacteria; AAC22536; AAC22536; HI_0880. DR GeneID; 950467; -. DR KEGG; hin:HI0880; -. DR PATRIC; 20190417; VBIHaeInf48452_0922. DR eggNOG; ENOG4105KK9; Bacteria. DR eggNOG; COG0261; LUCA. DR KO; K02888; -. DR OMA; QGHRQPF; -. DR OrthoDB; EOG6TJ84X; -. DR PhylomeDB; P44359; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01363; Ribosomal_L21; 1. DR InterPro; IPR028909; L21p-like. DR InterPro; IPR001787; Ribosomal_L21. DR InterPro; IPR018258; Ribosomal_L21_CS. DR Pfam; PF00829; Ribosomal_L21p; 1. DR SUPFAM; SSF141091; SSF141091; 1. DR TIGRFAMs; TIGR00061; L21; 1. DR PROSITE; PS01169; RIBOSOMAL_L21; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 103 50S ribosomal protein L21. FT /FTId=PRO_0000181002. SQ SEQUENCE 103 AA; 11382 MW; 253893D3A5A35C4B CRC64; MYAVFQSGGK QHRVSEGQVV RLEKLELATG ATVEFDSXLM VVNGEDVKIG APVVAGAKVV AEVVAQGRGE KVKIVKFRRR KHSRKQQGHR QWFTEVKITG IQA // ID RL25_HAEIN Reviewed; 95 AA. AC P45281; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01336}; GN Name=rplY {ECO:0000255|HAMAP-Rule:MF_01336}; Synonyms=rpl25; GN OrderedLocusNames=HI_1630; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in CC the ribosome where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01336}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S CC rRNA independently of L5 and L18. {ECO:0000255|HAMAP- CC Rule:MF_01336}. CC -!- SIMILARITY: Belongs to the ribosomal protein L25P family. CC {ECO:0000255|HAMAP-Rule:MF_01336}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23277.1; -; Genomic_DNA. DR PIR; E64133; E64133. DR RefSeq; NP_439772.1; NC_000907.1. DR RefSeq; WP_005691222.1; NC_000907.1. DR ProteinModelPortal; P45281; -. DR SMR; P45281; 3-95. DR STRING; 71421.HI1630; -. DR EnsemblBacteria; AAC23277; AAC23277; HI_1630. DR GeneID; 950473; -. DR KEGG; hin:HI1630; -. DR PATRIC; 20191995; VBIHaeInf48452_1705. DR eggNOG; ENOG4105KW6; Bacteria. DR eggNOG; COG1825; LUCA. DR KO; K02897; -. DR OMA; HAGKFPA; -. DR OrthoDB; EOG6SZ1PC; -. DR PhylomeDB; P45281; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.240.10; -; 1. DR HAMAP; MF_01336; Ribosomal_L25; 1. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR029751; Ribosomal_L25. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR020055; Ribosomal_L25_short. DR Pfam; PF01386; Ribosomal_L25p; 1. DR ProDom; PD012503; Ribosomal_L25; 1. DR SUPFAM; SSF50715; SSF50715; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 95 50S ribosomal protein L25. FT /FTId=PRO_0000181484. SQ SEQUENCE 95 AA; 10652 MW; A6711F78691B2A57 CRC64; MAFKFNAEVR TAQGKGASRR LRHNGQIPAI VYGGSEEPVS IILNHDELNN AQAHESFYSE VITLVVEGKE VAVKVQAMQR HPFKPKLVHI DFKRA // ID RL17_HAEIN Reviewed; 128 AA. AC P44355; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 87. 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=HI_0803; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22462.1; -; Genomic_DNA. DR PIR; C64095; C64095. DR RefSeq; NP_438963.1; NC_000907.1. DR RefSeq; WP_005648400.1; NC_000907.1. DR ProteinModelPortal; P44355; -. DR SMR; P44355; 1-127. DR STRING; 71421.HI0803; -. DR EnsemblBacteria; AAC22462; AAC22462; HI_0803. DR GeneID; 949819; -. DR KEGG; hin:HI0803; -. DR PATRIC; 20190259; VBIHaeInf48452_0843. DR eggNOG; ENOG4108ZT0; Bacteria. DR eggNOG; COG0203; LUCA. DR KO; K02879; -. DR OMA; TVHAQRE; -. DR OrthoDB; EOG6GR3GR; -. DR PhylomeDB; P44355; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1030.10; -; 1. DR HAMAP; MF_01368; Ribosomal_L17; 1. DR InterPro; IPR000456; Ribosomal_L17. DR PANTHER; PTHR14413; PTHR14413; 1. DR Pfam; PF01196; Ribosomal_L17; 1. DR SUPFAM; SSF64263; SSF64263; 1. DR TIGRFAMs; TIGR00059; L17; 1. DR PROSITE; PS01167; RIBOSOMAL_L17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 128 50S ribosomal protein L17. FT /FTId=PRO_0000175527. SQ SEQUENCE 128 AA; 14473 MW; 3EC2B34943B12F3E CRC64; MRHRKSGRQL NRNSSHRQAM FRNLASALVS HEIIKTTLPK AKELRRVVEP LITLAKVDSV ANRRLAFART RNVETVAKLF NELGPRFAQR AGGYTRILKC GFRAGDNAPM AYIELVDRPE VAEATTEE // ID RL14_HAEIN Reviewed; 123 AA. AC P66067; P44352; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 73. 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=HI_0788; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22446.1; -; Genomic_DNA. DR PIR; F64093; F64093. DR RefSeq; NP_438947.1; NC_000907.1. DR RefSeq; WP_005548786.1; NC_000907.1. DR ProteinModelPortal; P66067; -. DR SMR; P66067; 2-123. DR STRING; 71421.HI0788; -. DR EnsemblBacteria; AAC22446; AAC22446; HI_0788. DR GeneID; 1244752; -. DR GeneID; 949802; -. DR KEGG; hin:HI0788; -. DR PATRIC; 20190227; VBIHaeInf48452_0827. DR eggNOG; ENOG4108UNN; Bacteria. DR eggNOG; COG0093; LUCA. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR PhylomeDB; P66067; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.150.20; -; 1. DR HAMAP; MF_01367; Ribosomal_L14; 1. DR InterPro; IPR000218; Ribosomal_L14P. DR InterPro; IPR005745; Ribosomal_L14P_bac-type. DR InterPro; IPR019972; Ribosomal_L14P_CS. DR PANTHER; PTHR11761; PTHR11761; 1. DR Pfam; PF00238; Ribosomal_L14; 1. DR SMART; SM01374; Ribosomal_L14; 1. DR SUPFAM; SSF50193; SSF50193; 1. DR TIGRFAMs; TIGR01067; rplN_bact; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 123 50S ribosomal protein L14. FT /FTId=PRO_0000128543. SQ SEQUENCE 123 AA; 13501 MW; E2991D9551CAD2E0 CRC64; MIQEQTMLDV ADNSGARSVM CIKVLGGSHR RYAAIGDIIK ITVKEAIPRG KVKKGDVLKA VVVRTKKGVR RPDGSVIRFD GNACVILNNN TEQPIGTRIF GPVTRELRSE KFMKIISLAP EVL // ID RL1_HAEIN Reviewed; 229 AA. AC P44342; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 96. 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=HI_0516; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22174.1; -; Genomic_DNA. DR PIR; I64073; I64073. DR RefSeq; NP_438674.1; NC_000907.1. DR RefSeq; WP_005649467.1; NC_000907.1. DR ProteinModelPortal; P44342; -. DR SMR; P44342; 6-227. DR STRING; 71421.HI0516; -. DR PRIDE; P44342; -. DR EnsemblBacteria; AAC22174; AAC22174; HI_0516. DR GeneID; 949582; -. DR KEGG; hin:HI0516; -. DR PATRIC; 20189585; VBIHaeInf48452_0535. DR eggNOG; ENOG4105C64; Bacteria. DR eggNOG; COG0081; LUCA. DR KO; K02863; -. DR OMA; HGTIGRR; -. DR OrthoDB; EOG6FBX2G; -. DR PhylomeDB; P44342; -. DR Proteomes; UP000000579; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 229 50S ribosomal protein L1. FT /FTId=PRO_0000125665. SQ SEQUENCE 229 AA; 24107 MW; 7EB37FB44828DCA4 CRC64; MAKLTKKMKA IKAGVDSTKA YEINEAIAVL KQFATAKFVE SVDVAVNLGI DPRKSDQNVR GATVLPHGTG REVRVAVFTQ GANADAAKEA GADLVGMEDL AEQIKKGEMN FDVVIASPDA MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA EAVKNAKSGQ IRYRNDKNGI IHTTIGKANF SEVQLKENLQ ALLAALNKAK PTTAKGIFIK KVSISTTMGA GVAVDQASL // ID RL22_HAEIN Reviewed; 110 AA. AC P44360; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=50S ribosomal protein L22; GN Name=rplV; Synonyms=rpl22; OrderedLocusNames=HI_0782; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP MACROLIDE RESISTANT VARIANTS. RC STRAIN=S1, S2, S26, S3, S49, S58, and S60; RX PubMed=12604536; DOI=10.1128/AAC.47.3.1017-1022.2003; RA Peric M., Bozdogan B., Jacobs M.R., Appelbaum P.C.; RT "Effects of an efflux mechanism and ribosomal mutations on macrolide RT susceptibility of Haemophilus influenzae clinical isolates."; RL Antimicrob. Agents Chemother. 47:1017-1022(2003). 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). {ECO:0000250}. 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:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein L22P 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; L42023; AAC22441.1; -; Genomic_DNA. DR PIR; A64093; A64093. DR RefSeq; NP_438941.1; NC_000907.1. DR RefSeq; WP_005625897.1; NC_000907.1. DR ProteinModelPortal; P44360; -. DR SMR; P44360; 1-110. DR STRING; 71421.HI0782; -. DR EnsemblBacteria; AAC22441; AAC22441; HI_0782. DR GeneID; 25057705; -. DR GeneID; 949798; -. DR KEGG; hin:HI0782; -. DR PATRIC; 20190215; VBIHaeInf48452_0821. DR eggNOG; ENOG4105KAP; Bacteria. DR eggNOG; COG0091; LUCA. DR KO; K02890; -. DR OMA; MKRIQPR; -. DR OrthoDB; EOG6V4GKB; -. DR PhylomeDB; P44360; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 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 Antibiotic resistance; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 110 50S ribosomal protein L22. FT /FTId=PRO_0000125161. FT VARIANT 77 77 D -> DDEGPSM (in strain: S1; confers FT macrolide resistance). FT VARIANT 81 81 Missing (in strain: S42; confers FT macrolide resistance). FT VARIANT 82 82 Missing (in strain: S53; confers FT macrolide resistance). FT VARIANT 88 88 R -> RRAKG (in strain: S26; confers FT macrolide resistance). FT VARIANT 91 91 G -> D (in strain: S2 and S3; confers FT macrolide resistance). FT VARIANT 91 91 G -> GKG (in strain: S49; confers FT macrolide resistance). FT VARIANT 91 91 G -> GRADR (in strain: S60; confers FT macrolide resistance). FT VARIANT 91 91 G -> GRAG (in strain: S58; confers FT macrolide resistance). FT VARIANT 95 96 Missing (in strain: S40; confers FT macrolide resistance). FT VARIANT 96 98 Missing (in strain: S23; confers FT macrolide resistance). SQ SEQUENCE 110 AA; 12148 MW; 196E517BDC27AC62 CRC64; METIAKHRYA RTSAQKARLV ADLIRGKKVA QALEILTFTN KKAAALVKKV LESAIANAEH NDGADIDDLK VAKIFVDEGP SMKRVMPRAK GRADRILKRT SHITVVVSDR // ID RL19_HAEIN Reviewed; 116 AA. AC P44357; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 91. DE RecName: Full=50S ribosomal protein L19; GN Name=rplS; Synonyms=rpl19; OrderedLocusNames=HI_0201; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21870.1; -; Genomic_DNA. DR PIR; B64054; B64054. DR RefSeq; NP_438370.2; NC_000907.1. DR RefSeq; WP_005648735.1; NC_000907.1. DR ProteinModelPortal; P44357; -. DR SMR; P44357; 2-114. DR STRING; 71421.HI0201; -. DR EnsemblBacteria; AAC21870; AAC21870; HI_0201. DR GeneID; 951102; -. DR KEGG; hin:HI0201; -. DR PATRIC; 20188899; VBIHaeInf48452_0206. DR eggNOG; ENOG4108YY1; Bacteria. DR eggNOG; COG0335; LUCA. DR KO; K02884; -. DR OMA; EAEQCAK; -. DR OrthoDB; EOG6DZF5W; -. DR PhylomeDB; P44357; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00402; Ribosomal_L19; 1. DR InterPro; IPR001857; Ribosomal_L19. DR InterPro; IPR018257; Ribosomal_L19_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR15680; PTHR15680; 1. DR Pfam; PF01245; Ribosomal_L19; 1. DR PIRSF; PIRSF002191; Ribosomal_L19; 1. DR PRINTS; PR00061; RIBOSOMALL19. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01024; rplS_bact; 1. DR PROSITE; PS01015; RIBOSOMAL_L19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 116 50S ribosomal protein L19. FT /FTId=PRO_0000163463. SQ SEQUENCE 116 AA; 13070 MW; AAA55DB910F10035 CRC64; MSNIIKQLEQ EQLKQNVPSF RPGDTLEVKV WVVEGSKRRL QAFEGVVIAI RNRGLHSAFT LRKVSNGVGV ERVFQTHSPA VDSIAVKRKG AVRKAKLYYL RERSGKSARI KERLGA // ID RL3_HAEIN Reviewed; 208 AA. AC P44344; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. 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=HI_0777; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-208. RA Zengel J.M., Vorozheikina D., Li X., Lindahl L.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. 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 -!- PTM: Methylated by PrmB. {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; L42023; AAC22436.1; -; Genomic_DNA. DR EMBL; U37797; AAB41510.1; -; Genomic_DNA. DR PIR; E64092; E64092. DR RefSeq; NP_438936.1; NC_000907.1. DR RefSeq; WP_005632753.1; NC_000907.1. DR ProteinModelPortal; P44344; -. DR SMR; P44344; 1-208. DR STRING; 71421.HI0777; -. DR EnsemblBacteria; AAC22436; AAC22436; HI_0777. DR GeneID; 25057874; -. DR GeneID; 950820; -. DR KEGG; hin:HI0777; -. DR PATRIC; 20190205; VBIHaeInf48452_0816. DR eggNOG; ENOG4105EEE; Bacteria. DR eggNOG; COG0087; LUCA. DR KO; K02906; -. DR OMA; VMEFRLE; -. DR OrthoDB; EOG6WDSMH; -. DR PhylomeDB; P44344; -. DR Proteomes; UP000000579; 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; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 208 50S ribosomal protein L3. FT /FTId=PRO_0000077106. FT MOD_RES 149 149 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_01325}. SQ SEQUENCE 208 AA; 22364 MW; BC73B3C0DC925228 CRC64; MIGLVGRKVG MTRIFNEDGV SVPVTVIEIE ANRVTQVKTL ENDGYTAVQV TTGSKKANRV TKPEAGHFVK AGVEAGRGLW EFRTEGEEFT LGQEINVDIF ADVKKVDVTG TSKGKGFQGG VKRWNFRTQD ATHGNSLSHR VLGSIGQNQT PGRVFKGKKM AGHLGAERVT VQSLEVVRVD AERKLLLVKG SVPGAINGDV IVKPAVKA // ID RL23_HAEIN Reviewed; 99 AA. AC P44361; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 91. 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=HI_0779; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22438.1; -; Genomic_DNA. DR PIR; G64092; G64092. DR RefSeq; NP_438938.1; NC_000907.1. DR RefSeq; WP_005632756.1; NC_000907.1. DR ProteinModelPortal; P44361; -. DR SMR; P44361; 1-98. DR STRING; 71421.HI0779; -. DR EnsemblBacteria; AAC22438; AAC22438; HI_0779. DR GeneID; 25058572; -. DR GeneID; 949793; -. DR KEGG; hin:HI0779; -. DR PATRIC; 20190209; VBIHaeInf48452_0818. DR eggNOG; ENOG41080KG; Bacteria. DR eggNOG; COG0089; LUCA. DR KO; K02892; -. DR OMA; QISEKAT; -. DR OrthoDB; EOG6HTP4P; -. DR PhylomeDB; P44361; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 99 50S ribosomal protein L23. FT /FTId=PRO_0000129410. SQ SEQUENCE 99 AA; 10898 MW; 9619D21D36EC67EC CRC64; MSQERLLSVL RAPHISEKAT NNAEKSNTVV LKVALDANKA EIAAAVAQLF EVKVDSVRTV VVKGKTKRRG NKMGRRSDWK KAYVTLAEGQ NLDFVDSAE // ID RL30_HAEIN Reviewed; 59 AA. AC P44366; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 98. DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371}; GN Name=rpmD {ECO:0000255|HAMAP-Rule:MF_01371}; Synonyms=rpl30; GN OrderedLocusNames=HI_0796; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01371}. CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family. CC {ECO:0000255|HAMAP-Rule:MF_01371}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22454.1; -; Genomic_DNA. DR PIR; E64094; E64094. DR RefSeq; NP_438955.1; NC_000907.1. DR RefSeq; WP_005693169.1; NC_000907.1. DR ProteinModelPortal; P44366; -. DR SMR; P44366; 2-59. DR STRING; 71421.HI0796; -. DR EnsemblBacteria; AAC22454; AAC22454; HI_0796. DR GeneID; 949787; -. DR KEGG; hin:HI0796; -. DR PATRIC; 20190243; VBIHaeInf48452_0835. DR eggNOG; ENOG4105VPB; Bacteria. DR eggNOG; COG1841; LUCA. DR KO; K02907; -. DR OMA; LEDTACV; -. DR OrthoDB; EOG6BGP7P; -. DR PhylomeDB; P44366; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1390.20; -; 1. DR HAMAP; MF_01371_B; Ribosomal_L30_B; 1. DR InterPro; IPR005996; Ribosomal_L30_bac-type. DR InterPro; IPR018038; Ribosomal_L30_CS. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR Pfam; PF00327; Ribosomal_L30; 1. DR PIRSF; PIRSF002211; Ribosomal_L30_bac-type; 1. DR SUPFAM; SSF55129; SSF55129; 1. DR TIGRFAMs; TIGR01308; rpmD_bact; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 59 50S ribosomal protein L30. FT /FTId=PRO_0000104594. SQ SEQUENCE 59 AA; 6660 MW; EB2C07EEB2D49BE5 CRC64; MAKTIKVTQV RSSIARLPKH KATLRGLGLR HIHHTVELID TPAVRGMINQ VSYMVKVEE // ID RL24_HAEIN Reviewed; 103 AA. AC P44362; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 99. 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=HI_0789; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22447.1; -; Genomic_DNA. DR PIR; G64093; G64093. DR RefSeq; NP_438948.1; NC_000907.1. DR RefSeq; WP_010869054.1; NC_000907.1. DR ProteinModelPortal; P44362; -. DR SMR; P44362; 3-103. DR STRING; 71421.HI0789; -. DR EnsemblBacteria; AAC22447; AAC22447; HI_0789. DR GeneID; 949805; -. DR KEGG; hin:HI0789; -. DR PATRIC; 20190229; VBIHaeInf48452_0828. DR eggNOG; ENOG4105KAR; Bacteria. DR eggNOG; COG0198; LUCA. DR KO; K02895; -. DR OMA; QISNIAL; -. DR OrthoDB; EOG6FFSDM; -. DR PhylomeDB; P44362; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR003256; Ribosomal_L24. DR InterPro; IPR005825; Ribosomal_L24/26_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF17136; ribosomal_L24; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01079; rplX_bact; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 103 50S ribosomal protein L24. FT /FTId=PRO_0000130662. SQ SEQUENCE 103 AA; 11285 MW; 3AD4903377702F19 CRC64; MPAKIRQNDE VIVLTGKDKG KRGKVTKVLP NGKVFVEGIN IITKHEKPVP ALGKAGGLVK KEAAIDASNV AIFNPKTNKA DRVGFRFEDG KKVRFFKSNN EII // ID RL28_HAEIN Reviewed; 78 AA. AC P44364; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 89. 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=HI_0951; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22612.1; -; Genomic_DNA. DR PIR; E64104; E64104. DR RefSeq; NP_439112.1; NC_000907.1. DR RefSeq; WP_005542826.1; NC_000907.1. DR ProteinModelPortal; P44364; -. DR SMR; P44364; 2-77. DR STRING; 71421.HI0951; -. DR EnsemblBacteria; AAC22612; AAC22612; HI_0951. DR GeneID; 949955; -. DR KEGG; hin:HI0951; -. DR PATRIC; 20190561; VBIHaeInf48452_0993. DR eggNOG; ENOG4105KDC; Bacteria. DR eggNOG; COG0227; LUCA. DR KO; K02902; -. DR OMA; WLPSERR; -. DR OrthoDB; EOG6W727M; -. DR PhylomeDB; P44364; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00373; Ribosomal_L28; 1. DR InterPro; IPR026569; Ribo_L28/L24. DR InterPro; IPR001383; Ribosomal_L28. DR PANTHER; PTHR13528; PTHR13528; 1. 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 78 50S ribosomal protein L28. FT /FTId=PRO_0000178480. SQ SEQUENCE 78 AA; 8985 MW; E76BC2C97FFCB8B3 CRC64; MSRVCQVTGK RPAVGNNRSH AMNATRRRFL PNLHTHRFWV ESENRFVTLR LTAKGMRIID KKGIDAVLAE IRARGEKI // ID RL29_HAEIN Reviewed; 63 AA. AC P44365; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=50S ribosomal protein L29; GN Name=rpmC; Synonyms=rpl29; OrderedLocusNames=HI_0785; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22444.1; -; Genomic_DNA. DR PIR; D64093; D64093. DR RefSeq; NP_438944.1; NC_000907.1. DR RefSeq; WP_005625888.1; NC_000907.1. DR ProteinModelPortal; P44365; -. DR SMR; P44365; 1-62. DR STRING; 71421.HI0785; -. DR EnsemblBacteria; AAC22444; AAC22444; HI_0785. DR GeneID; 950743; -. DR KEGG; hin:HI0785; -. DR PATRIC; 20190221; VBIHaeInf48452_0824. DR eggNOG; ENOG41083MP; Bacteria. DR eggNOG; COG0255; LUCA. DR KO; K02904; -. DR OMA; MRMQAST; -. DR OrthoDB; EOG6VTK8Z; -. DR PhylomeDB; P44365; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.310; -; 1. DR HAMAP; MF_00374; Ribosomal_L29; 1. DR InterPro; IPR001854; Ribosomal_L29. DR InterPro; IPR018254; Ribosomal_L29_CS. DR Pfam; PF00831; Ribosomal_L29; 1. DR SUPFAM; SSF46561; SSF46561; 1. DR TIGRFAMs; TIGR00012; L29; 1. DR PROSITE; PS00579; RIBOSOMAL_L29; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 63 50S ribosomal protein L29. FT /FTId=PRO_0000130398. SQ SEQUENCE 63 AA; 7178 MW; D883F5B96342E180 CRC64; MKAQDLRTKS VEELNAELVN LLGEQFKLRM QTATGQLQQT HQAKQVRRDI ARVKTVLTEK AGE // ID RL4_HAEIN Reviewed; 200 AA. AC P44345; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=50S ribosomal protein L4; GN Name=rplD; Synonyms=rpl4; OrderedLocusNames=HI_0778; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ABILITY TO REPRESS THE E.COLI RP S10 OPERON. RX PubMed=8722027; DOI=10.1139/o95-119; RA Zengel J.M., Vorozheikina D., Li X., Lindahl L.; RT "Regulation of the Escherichia coli S10 ribosomal protein operon by RT heterologous L4 ribosomal proteins."; RL Biochem. Cell Biol. 73:1105-1112(1995). RN [3] RP EVIDENCE FOR REGULATION OF THE S10 OPERON. RX PubMed=10498727; RA Allen T., Shen P., Samsel L., Liu R., Lindahl L., Zengel J.M.; RT "Phylogenetic analysis of L4-mediated autogenous control of the S10 RT ribosomal protein operon."; RL J. Bacteriol. 181:6124-6132(1999). RN [4] RP MACROLIDE RESISTANT VARIANTS. RX PubMed=12604536; DOI=10.1128/AAC.47.3.1017-1022.2003; RA Peric M., Bozdogan B., Jacobs M.R., Appelbaum P.C.; RT "Effects of an efflux mechanism and ribosomal mutations on macrolide RT susceptibility of Haemophilus influenzae clinical isolates."; RL Antimicrob. Agents Chemother. 47:1017-1022(2003). CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein CC initially binds near the 5'-end of the 23S rRNA. It is important CC during the early stages of 50S assembly. It makes multiple CC contacts with different domains of the 23S rRNA in the assembled CC 50S subunit and ribosome (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protein L4 is a both a transcriptional repressor and a CC translational repressor protein. It regulates transcription of the CC S10 operon (to which L4 belongs) by causing premature termination CC of transcription within the S10 leader. L4 controls the CC translation of the S10 operon by binding to its mRNA (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: This protein when expressed in E.coli represses both CC transcription and translation of the endogenous S10 operon. As the CC H.influenzae S10 leader can be regulated in vitro by the E.coli L4 CC protein this strongly suggests the endogenous protein controls its CC own S10 operon in a similar fashion. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000250}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- SIMILARITY: Belongs to the ribosomal protein L4P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22437.1; -; Genomic_DNA. DR EMBL; U37797; AAB41511.1; -; Genomic_DNA. DR PIR; F64092; F64092. DR RefSeq; NP_438937.1; NC_000907.1. DR RefSeq; WP_005652369.1; NC_000907.1. DR ProteinModelPortal; P44345; -. DR SMR; P44345; 1-200. DR STRING; 71421.HI0778; -. DR DrugBank; DB01321; Josamycin. DR PRIDE; P44345; -. DR EnsemblBacteria; AAC22437; AAC22437; HI_0778. DR GeneID; 950806; -. DR KEGG; hin:HI0778; -. DR PATRIC; 20190207; VBIHaeInf48452_0817. DR eggNOG; ENOG4106U5A; Bacteria. DR eggNOG; COG0088; LUCA. DR KO; K02926; -. DR OMA; TKSFVSW; -. DR OrthoDB; EOG6M0T9G; -. DR PhylomeDB; P44345; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 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 Antibiotic resistance; Complete proteome; Reference proteome; KW Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding; Transcription; Transcription regulation; KW Transcription termination; Translation regulation. FT CHAIN 1 200 50S ribosomal protein L4. FT /FTId=PRO_0000129223. FT VARIANT 63 63 G -> GGT (in strain: S4; confers FT macrolide resistance). FT VARIANT 64 64 T -> K (in strain: S39; confers macrolide FT resistance). FT VARIANT 65 65 G -> D (in strain: S27 and S47; confers FT macrolide resistance). FT VARIANT 69 69 A -> S (in strain: S50; confers macrolide FT resistance). FT VARIANT 82 82 T -> I (in strain: S54; confers macrolide FT resistance). FT CONFLICT 65 65 G -> A (in Ref. 2; AAB41511). FT {ECO:0000305}. SQ SEQUENCE 200 AA; 21954 MW; A135A4762FE50927 CRC64; MELQVVGANA LTVSETTFGR EFNEALIHQV VVAYAAGARQ GTRAQKTRAE VSGSGKKPWR QKGTGRARAG DIKSPIWRSG GTTFAAKPQD HSQKVNKKMY RGAIKSILSE LVRQDRLVVV EKFELDAPKT KVLVQKLKDL AVEDALIITA SLDENLFLAA RNLYKVDVRD VQGIDPVSLI AFDKVIVTVD AVKQIEEILA // ID RL2_HAEIN Reviewed; 273 AA. AC P44343; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 104. 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=HI_0780; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22439.1; -; Genomic_DNA. DR PIR; H64092; H64092. DR RefSeq; NP_438939.1; NC_000907.1. DR RefSeq; WP_005652371.1; NC_000907.1. DR ProteinModelPortal; P44343; -. DR SMR; P44343; 2-271. DR STRING; 71421.HI0780; -. DR EnsemblBacteria; AAC22439; AAC22439; HI_0780. DR GeneID; 949796; -. DR KEGG; hin:HI0780; -. DR PATRIC; 20190211; VBIHaeInf48452_0819. DR eggNOG; ENOG4105CFD; Bacteria. DR eggNOG; COG0090; LUCA. DR KO; K02886; -. DR OMA; NKRTTSM; -. DR OrthoDB; EOG6TR0J1; -. DR PhylomeDB; P44343; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 4.10.950.10; -; 1. DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR005880; Ribosomal_L2_bac/org-type. DR InterPro; IPR022669; Ribosomal_L2_C. DR InterPro; IPR022671; Ribosomal_L2_CS. DR InterPro; IPR014726; Ribosomal_L2_dom3. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR13691; PTHR13691; 1. DR 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 273 50S ribosomal protein L2. FT /FTId=PRO_0000129567. SQ SEQUENCE 273 AA; 30138 MW; 69611CB038238302 CRC64; MAIVKCKPTS AGRRHVVKIV NPELHKGKPY APLLDTKSKT GGRNNYGRIT TRHIGGGHKQ HYRLIDFKRN KLDIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL SVGDQIQAGI NSPIKVGNSL PMRNIPVGST VHNVELKPGK GGQIARSAGA YVQIIAREGN YVTLRLRSGE MRKVLAECVA TIGEVGNSEH MLRVLGKAGA NRWRGIRPTV RGTAMNPVDH PHGGGEGRNF GKHPVTPWGV QTKGKKTRHN KRTDKYIVRR RGK // ID RL35_HAEIN Reviewed; 65 AA. AC P67917; P45519; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 62. 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=HI_1319; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L35P family. CC {ECO:0000255|HAMAP-Rule:MF_00514}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22964.1; 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; L42023; AAC22964.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_439470.1; NC_000907.1. DR RefSeq; WP_005596065.1; NC_000907.1. DR ProteinModelPortal; P67917; -. DR SMR; P67917; 2-65. DR STRING; 71421.HI1319m; -. DR EnsemblBacteria; AAC22964; AAC22964; HI_1319. DR GeneID; 7278779; -. DR GeneID; 950241; -. DR KEGG; hin:HI1319m; -. DR PATRIC; 20191321; VBIHaeInf48452_1371. DR eggNOG; ENOG41082NX; Bacteria. DR eggNOG; COG0291; LUCA. DR KO; K02916; -. DR OMA; AYKRHIL; -. DR OrthoDB; EOG651T3B; -. DR PhylomeDB; P67917; -. DR Proteomes; UP000000579; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 65 50S ribosomal protein L35. FT /FTId=PRO_0000177366. SQ SEQUENCE 65 AA; 7438 MW; 19881A037B84B77A CRC64; MPKIKTVRGA AKRFKKTASG GFKRKQSHLR HILTKKTTKR KRHLRHKSMV AKADQVLVVA CLPYA // ID RL36_HAEIN Reviewed; 37 AA. AC P46361; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 83. 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=HI_0798.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22457.1; -; Genomic_DNA. DR RefSeq; NP_438958.1; NC_000907.1. DR RefSeq; WP_005625868.1; NC_000907.1. DR ProteinModelPortal; P46361; -. DR SMR; P46361; 1-37. DR STRING; 71421.HI0798.1; -. DR EnsemblBacteria; AAC22457; AAC22457; HI_0798.1. DR GeneID; 25059329; -. DR GeneID; 949814; -. DR KEGG; hin:HI0798.1; -. DR PATRIC; 20190249; VBIHaeInf48452_0838. DR eggNOG; ENOG41067V7; Bacteria. DR eggNOG; COG0257; LUCA. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR Proteomes; UP000000579; 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_0000126193. SQ SEQUENCE 37 AA; 4297 MW; 53AEE5B5DB28F83D CRC64; MKVRASVKKM CRNCKIVKRE GVVRVLCSDP KHKQRQG // ID RL5_HAEIN Reviewed; 179 AA. AC P44346; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 96. 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=HI_0790; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22448.1; -; Genomic_DNA. DR PIR; H64093; H64093. DR RefSeq; NP_438949.3; NC_000907.1. DR RefSeq; WP_005625881.1; NC_000907.1. DR ProteinModelPortal; P44346; -. DR SMR; P44346; 2-179. DR STRING; 71421.HI0790; -. DR EnsemblBacteria; AAC22448; AAC22448; HI_0790. DR GeneID; 949806; -. DR KEGG; hin:HI0790; -. DR PATRIC; 20190231; VBIHaeInf48452_0829. DR eggNOG; COG0094; LUCA. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01333_B; Ribosomal_L5_B; 1. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR020930; Ribosomal_L5_bac-type. DR InterPro; IPR031309; Ribosomal_L5_C. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR031310; Ribosomal_L5_N. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; SSF55282; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 179 50S ribosomal protein L5. FT /FTId=PRO_0000124933. SQ SEQUENCE 179 AA; 20311 MW; C3BC98E91C42A042 CRC64; MAKLHDYYRD QVVSELKNKF GYKSVMQVPR IEKITLNMGV GEALTDKKLL DNAVADLAAI SGQKPLVTKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR GLDITITTTA KNDEEGQALL AAFNFPFRK // ID RLMC_HAEIN Reviewed; 392 AA. AC P44083; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase RlmC {ECO:0000255|HAMAP-Rule:MF_01012}; DE EC=2.1.1.189 {ECO:0000255|HAMAP-Rule:MF_01012}; DE AltName: Full=23S rRNA(m5U747)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01012}; GN Name=rlmC {ECO:0000255|HAMAP-Rule:MF_01012}; Synonyms=rumB; GN OrderedLocusNames=HI_0958; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position CC 747 (m5U747) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(747) in 23S CC rRNA = S-adenosyl-L-homocysteine + 5-methyluracil(747) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01012}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC RlmC subfamily. {ECO:0000255|HAMAP-Rule:MF_01012}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22619.1; -; Genomic_DNA. DR PIR; B64017; B64017. DR RefSeq; NP_439119.1; NC_000907.1. DR RefSeq; WP_005693305.1; NC_000907.1. DR ProteinModelPortal; P44083; -. DR STRING; 71421.HI0958; -. DR EnsemblBacteria; AAC22619; AAC22619; HI_0958. DR GeneID; 949964; -. DR KEGG; hin:HI0958; -. DR PATRIC; 20190575; VBIHaeInf48452_1000. DR eggNOG; ENOG4107SFS; Bacteria. DR eggNOG; COG2265; LUCA. DR KO; K03212; -. DR OMA; NIQPIHM; -. DR OrthoDB; EOG6V4GKM; -. DR PhylomeDB; P44083; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01012; 23SrRNA_methyltr_RlmC; 1. DR InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR030391; MeTrfase_TrmA_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR010280; U5_MeTrfase_fam. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02085; meth_trns_rumB; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS01230; TRMA_1; 1. DR PROSITE; PS01231; TRMA_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 392 23S rRNA (uracil(747)-C(5))- FT methyltransferase RlmC. FT /FTId=PRO_0000161930. FT ACT_SITE 348 348 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT METAL 4 4 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT METAL 12 12 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT METAL 15 15 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT METAL 93 93 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT BINDING 218 218 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01012}. FT BINDING 247 247 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01012}. FT BINDING 275 275 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01012}. FT BINDING 321 321 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01012}. SQ SEQUENCE 392 AA; 44724 MW; 52375FA7A744AE6D CRC64; MIDCRYYQQN ECRSCQWLEI PCSQQLTEKQ YHLKQQLISI NYDEAQWVAP FQSNQQGFRN KAKMVVSGSV ERPILGILKN PNDPQSAIDL CDCPLYPTHF SAIFSILKDF IGRAGLVPYN IAKQKGELKY ILLTESIATE KLMLRFVLRT ENKLPLIRRE LPKLLEKLPH LEVISINLQP QHAAILEGEQ EIFLTEQQFL PENFNGIPLF IRPRGFFQTN PKVAAGLYAT AQQWVAEFPI YNLWDLFCGV GGFGLHCAKA LQEKWGKPIK LTGIEISSSA ILAASHSAKI LGLEHVNFQS LDAASVIENK NENKPDLVIV NPPRRGIGKE LSEFLNQIQP HFILYSSCNA MTMGKDLQHL TCYKPLKIQL FDMFPQTSHY EVLVLLERKK IN // ID RL31_HAEIN Reviewed; 70 AA. AC P44367; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. 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=HI_0758; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00501}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00501}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00501}. CC -!- SIMILARITY: Belongs to the ribosomal protein L31P family. Type A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00501}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22417.1; -; Genomic_DNA. DR PIR; B64091; B64091. DR RefSeq; NP_438917.1; NC_000907.1. DR RefSeq; WP_005625828.1; NC_000907.1. DR ProteinModelPortal; P44367; -. DR SMR; P44367; 1-70. DR STRING; 71421.HI0758; -. DR EnsemblBacteria; AAC22417; AAC22417; HI_0758. DR GeneID; 950704; -. DR KEGG; hin:HI0758; -. DR PATRIC; 20190161; VBIHaeInf48452_0796. DR eggNOG; ENOG4105VFB; Bacteria. DR eggNOG; COG0254; LUCA. DR KO; K02909; -. DR OMA; YTGQQKA; -. DR OrthoDB; EOG6DVJZM; -. DR PhylomeDB; P44367; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00501; Ribosomal_L31_1; 1. DR InterPro; IPR002150; Ribosomal_L31. DR InterPro; IPR027491; Ribosomal_L31_A. DR Pfam; PF01197; Ribosomal_L31; 1. DR PRINTS; PR01249; RIBOSOMALL31. DR TIGRFAMs; TIGR00105; L31; 1. DR PROSITE; PS01143; RIBOSOMAL_L31; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc. FT CHAIN 1 70 50S ribosomal protein L31. FT /FTId=PRO_0000173113. FT METAL 16 16 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 18 18 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 37 37 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. FT METAL 40 40 Zinc. {ECO:0000255|HAMAP-Rule:MF_00501}. SQ SEQUENCE 70 AA; 7833 MW; 20BEA094F8C51D67 CRC64; MKQGIHPEYK EITATCSCGN VIKTRSTLGK DINLDVCGNC HPFYTGKQRV VDTGGRVERF NSRFKIPSTK // ID RL6_HAEIN Reviewed; 177 AA. AC P44347; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 96. 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=HI_0793; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22451.1; -; Genomic_DNA. DR PIR; B64094; B64094. DR RefSeq; NP_438952.1; NC_000907.1. DR RefSeq; WP_005655593.1; NC_000907.1. DR ProteinModelPortal; P44347; -. DR SMR; P44347; 2-177. DR STRING; 71421.HI0793; -. DR PRIDE; P44347; -. DR EnsemblBacteria; AAC22451; AAC22451; HI_0793. DR GeneID; 950560; -. DR KEGG; hin:HI0793; -. DR PATRIC; 20190237; VBIHaeInf48452_0832. DR eggNOG; ENOG4108R5J; Bacteria. DR eggNOG; COG0097; LUCA. DR KO; K02933; -. DR OMA; TIGYSHP; -. DR OrthoDB; EOG67DPRD; -. DR PhylomeDB; P44347; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 3.90.930.12; -; 2. DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR020040; Ribosomal_L6_a/b-dom. DR InterPro; IPR019906; Ribosomal_L6_bac-type. DR 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 177 50S ribosomal protein L6. FT /FTId=PRO_0000131051. SQ SEQUENCE 177 AA; 19078 MW; 42E3D9206648F0FB CRC64; MSRVAKAPVN IPAGVEVKLD GQLLTVKGKN GELSRKIHES VEVKQDNGQF TFTPREGFVE ANAQSGTARA LVNAMVIGVT EGFTKKLVLV GVGYRAQLKG NAIALSLGYS HPVEHTLPVG ITAECPSQTE IVLKGADKQL IGQVAADIRA YRRPEPYKGK GVRYADEVVR IKEAKKK // ID RLME_HAEIN Reviewed; 209 AA. AC P45162; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547}; DE EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; GN Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547}; GN Synonyms=ftsJ {ECO:0000255|HAMAP-Rule:MF_01547}, GN rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=HI_1334; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the uridine in position 2552 of CC 23S rRNA at the 2'-O position of the ribose in the fully assembled CC 50S ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uridine(2552) in 23S CC rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase RlmE family. CC {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01547}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22978.1; -; Genomic_DNA. DR PIR; C64117; C64117. DR RefSeq; NP_439485.1; NC_000907.1. DR RefSeq; WP_005694443.1; NC_000907.1. DR ProteinModelPortal; P45162; -. DR SMR; P45162; 31-208. DR STRING; 71421.HI1334; -. DR EnsemblBacteria; AAC22978; AAC22978; HI_1334. DR GeneID; 950794; -. DR KEGG; hin:HI1334; -. DR PATRIC; 20191351; VBIHaeInf48452_1386. DR eggNOG; ENOG4105F7M; Bacteria. DR eggNOG; COG0293; LUCA. DR KO; K02427; -. DR OMA; DKRWVLQ; -. DR OrthoDB; EOG657JC0; -. DR PhylomeDB; P45162; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01547; RNA_methyltr_E; 1. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR004512; rRNA_MeTrfase_gammaproteobac. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR10920; PTHR10920; 1. DR Pfam; PF01728; FtsJ; 1. DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00438; rrmJ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 209 Ribosomal RNA large subunit FT methyltransferase E. FT /FTId=PRO_0000155503. FT DOMAIN 191 209 TRAM. {ECO:0000255|HAMAP-Rule:MF_01547}. FT ACT_SITE 164 164 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 63 63 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 65 65 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 83 83 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 99 99 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 124 124 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. SQ SEQUENCE 209 AA; 23408 MW; C1B166BCB142CC8C CRC64; MGKKKRSASS SRWLNEHFSD QFVQKAHKQK LRSRAYFKID EIQQTDKLFK QGMTVVDLGA APGGWSQYVV SQIGGKGRVI ACDILEMDPI VGVDFLQGDF RDENVLNALL ARVGEDKVDV VMSDMAPNFS GMPSVDIPRA MYLVELALDM CKQVLASKGS FVVKVFQGEG FDEYLREIRS LFDVVKVRKP EASRGRSREV YIVATGYKG // ID RL32_HAEIN Reviewed; 56 AA. AC P44368; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 87. DE RecName: Full=50S ribosomal protein L32; GN Name=rpmF; Synonyms=rpl32; OrderedLocusNames=HI_0158; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21827.1; -; Genomic_DNA. DR PIR; G64051; G64051. DR RefSeq; NP_438328.1; NC_000907.1. DR RefSeq; WP_005544470.1; NC_000907.1. DR ProteinModelPortal; P44368; -. DR SMR; P44368; 2-56. DR STRING; 71421.HI0158; -. DR EnsemblBacteria; AAC21827; AAC21827; HI_0158. DR GeneID; 25059508; -. DR GeneID; 951068; -. DR KEGG; hin:HI0158; -. DR PATRIC; 20188815; VBIHaeInf48452_0164. DR eggNOG; ENOG4105VGS; Bacteria. DR eggNOG; COG0333; LUCA. DR KO; K02911; -. DR OMA; HRAHDFL; -. DR OrthoDB; EOG6VMTT4; -. DR PhylomeDB; P44368; -. DR Proteomes; UP000000579; 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 56 50S ribosomal protein L32. FT /FTId=PRO_0000172346. SQ SEQUENCE 56 AA; 6392 MW; 5645EE3724D783AF CRC64; MAVQQNKKSR SRRDMRRSHD ALTTAAVSVD KASGETHLRH HVTADGYYRG RKVINK // ID RL33_HAEIN Reviewed; 56 AA. AC P44369; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=50S ribosomal protein L33; GN Name=rpmG; Synonyms=rpl33; OrderedLocusNames=HI_0950; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22611.1; -; Genomic_DNA. DR PIR; D64104; D64104. DR RefSeq; NP_439111.1; NC_000907.1. DR RefSeq; WP_005613503.1; NC_000907.1. DR ProteinModelPortal; P44369; -. DR SMR; P44369; 3-56. DR STRING; 71421.HI0950; -. DR PRIDE; P44369; -. DR EnsemblBacteria; AAC22611; AAC22611; HI_0950. DR GeneID; 25057700; -. DR GeneID; 949952; -. DR KEGG; hin:HI0950; -. DR PATRIC; 20190559; VBIHaeInf48452_0992. DR eggNOG; ENOG4105W0E; Bacteria. DR eggNOG; COG0267; LUCA. DR KO; K02913; -. DR OMA; ARKHVLY; -. DR OrthoDB; EOG60KNBM; -. DR PhylomeDB; P44369; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_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 56 50S ribosomal protein L33. FT /FTId=PRO_0000170167. SQ SEQUENCE 56 AA; 6563 MW; 47B5A850660C58DC CRC64; MAAKGAREKI RLVSTAETGH FYTTDKNKRN MPEKMEIKKF DPVVRKHVIY KEAKIK // ID RL9_HAEIN Reviewed; 149 AA. AC P44349; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN Synonyms=rpl9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=HI_0544; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22202.1; -; Genomic_DNA. DR PIR; D64076; D64076. DR RefSeq; NP_438702.1; NC_000907.1. DR RefSeq; WP_005649511.1; NC_000907.1. DR ProteinModelPortal; P44349; -. DR SMR; P44349; 1-149. DR STRING; 71421.HI0544; -. DR EnsemblBacteria; AAC22202; AAC22202; HI_0544. DR GeneID; 950774; -. DR KEGG; hin:HI0544; -. DR PATRIC; 20189641; VBIHaeInf48452_0563. DR eggNOG; ENOG4105K9Q; Bacteria. DR eggNOG; COG0359; LUCA. DR KO; K02939; -. DR OMA; AIRWTKG; -. DR OrthoDB; EOG6D8BH0; -. DR PhylomeDB; P44349; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.10.430.100; -; 1. DR Gene3D; 3.40.5.10; -; 1. DR HAMAP; MF_00503; Ribosomal_L9; 1. DR InterPro; IPR000244; Ribosomal_L9. DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N. DR InterPro; IPR020594; Ribosomal_L9_bac/chp. DR InterPro; IPR020069; Ribosomal_L9_C. DR InterPro; IPR020070; Ribosomal_L9_N. DR PANTHER; PTHR21368; PTHR21368; 1. DR Pfam; PF03948; Ribosomal_L9_C; 1. DR Pfam; PF01281; Ribosomal_L9_N; 1. DR SUPFAM; SSF55653; SSF55653; 1. DR SUPFAM; SSF55658; SSF55658; 1. DR TIGRFAMs; TIGR00158; L9; 1. DR PROSITE; PS00651; RIBOSOMAL_L9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 149 50S ribosomal protein L9. FT /FTId=PRO_0000176641. SQ SEQUENCE 149 AA; 15636 MW; D0DA6F7E64FEFF9A CRC64; MQVILLDKIV HLGQVGDQVN VKSGFARNFL IPQGKAVMAT KANIEHFEAR RAELEATAAA NLAAAQARAA EVTALGSVTI ASKAGDEGRL FGAITTRDVA EAVTAAGVKI AKSEVRLPNG PIRTLGDHDV RFQLHGEVFA ALDVIVVAE // ID RLMB_HAEIN Reviewed; 246 AA. AC P44906; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000255|HAMAP-Rule:MF_01887}; DE EC=2.1.1.185 {ECO:0000255|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887}; GN Name=rlmB {ECO:0000255|HAMAP-Rule:MF_01887}; GN OrderedLocusNames=HI_0860; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in CC 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(2251) in CC 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(2251) CC in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01887}. CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC RlmB subfamily. {ECO:0000255|HAMAP-Rule:MF_01887}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22519.1; -; Genomic_DNA. DR PIR; E64160; E64160. DR RefSeq; NP_439020.1; NC_000907.1. DR RefSeq; WP_005655733.1; NC_000907.1. DR ProteinModelPortal; P44906; -. DR SMR; P44906; 1-243. DR STRING; 71421.HI0860; -. DR EnsemblBacteria; AAC22519; AAC22519; HI_0860. DR GeneID; 949872; -. DR KEGG; hin:HI0860; -. DR PATRIC; 20190375; VBIHaeInf48452_0901. DR eggNOG; ENOG4105C2N; Bacteria. DR eggNOG; COG0566; LUCA. DR KO; K03218; -. DR OMA; HAGIDFL; -. DR OrthoDB; EOG6GBMDM; -. DR PhylomeDB; P44906; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_01887; 23SrRNA_methyltr_B; 1. DR InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR004441; rRNA_MeTrfase_TrmH. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR013123; SpoU_subst-bd. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR Pfam; PF08032; SpoU_sub_bind; 1. DR SMART; SM00967; SpoU_sub_bind; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 246 23S rRNA (guanosine-2'-O-)- FT methyltransferase RlmB. FT /FTId=PRO_0000159790. FT BINDING 197 197 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01887}. FT BINDING 217 217 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01887}. FT BINDING 226 226 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01887}. SQ SEQUENCE 246 AA; 26602 MW; 4DE308D46F6E1D45 CRC64; MSEQIYGIHA VNSILTHSPE RLIEVFVLKG REDKRLQPLL NELYSLGIGV QFVNRQTLDK KADGEVHQGV IARVQAAKEL NENDLDEILA NKQNPLLLVL DGVTDPHNLG ACLRTADAAG AVAVIVPKDK SAQLTSIARK VACGAAETVP LIRVTNLSRT LRDLQQNHNI WVVGTAGEAT ETIYQSKLTG PLALVMGAEG EGMRRLTREH CDQLISIPMA GSVSSLNVSV ATGVCLFEIV RQRLGS // ID RLUA_HAEIN Reviewed; 219 AA. AC P44782; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Ribosomal large subunit pseudouridine synthase A; DE EC=5.4.99.28; DE EC=5.4.99.29; DE AltName: Full=23S rRNA pseudouridine(746) synthase; DE AltName: Full=rRNA pseudouridylate synthase A; DE AltName: Full=rRNA-uridine isomerase A; DE AltName: Full=tRNA pseudouridine(32) synthase; GN Name=rluA; OrderedLocusNames=HI_0617; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem CC and loop of transfer RNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(32) = tRNA pseudouridine(32). CC -!- CATALYTIC ACTIVITY: 23S rRNA uridine(746) = 23S rRNA CC pseudouridine(746). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA 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; L42023; AAC22276.1; -; Genomic_DNA. DR PIR; E64155; E64155. DR RefSeq; NP_438775.1; NC_000907.1. DR RefSeq; WP_005654471.1; NC_000907.1. DR ProteinModelPortal; P44782; -. DR SMR; P44782; 6-219. DR STRING; 71421.HI0617; -. DR EnsemblBacteria; AAC22276; AAC22276; HI_0617. DR GeneID; 950684; -. DR KEGG; hin:HI0617; -. DR PATRIC; 20189817; VBIHaeInf48452_0641. DR eggNOG; ENOG4105D3G; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06177; -. DR OMA; EKYGFCE; -. DR OrthoDB; EOG6P070X; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR PROSITE; PS01129; PSI_RLU; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; rRNA processing; KW tRNA processing. FT CHAIN 1 219 Ribosomal large subunit pseudouridine FT synthase A. FT /FTId=PRO_0000162655. FT ACT_SITE 64 64 {ECO:0000250}. SQ SEQUENCE 219 AA; 25138 MW; F9A0FA264D882CAF CRC64; MALIEYNPPL EPYLDIIYQD NHLCVVNKPS GLLSVPGNQP QYYDSAMSRV KEKFGFCEPA HRLDMATSGI IVFALSKAAD RELKRQFRER EPKKHYQAIV WGHLENDYGE VNLPMICDWE NRPRQRLDFV LGKRAVTKFE VLARLPNNST RVKLTPVTGR SHQLRLHMLA LGHPILGDKF YSHPQAKVMS PRLCLHAEEL TITHPITGET MTFNAKSDF // ID RMLB_HAEIN Reviewed; 338 AA. AC P44914; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=dTDP-glucose 4,6-dehydratase; DE EC=4.2.1.46; GN Name=rffG; OrderedLocusNames=HI_0873; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form CC dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving CC oxidation, dehydration and reduction. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy- CC alpha-D-glucose + H(2)O. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. dTDP-glucose dehydratase 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; L42023; AAC22531.1; -; Genomic_DNA. DR PIR; C64099; C64099. DR RefSeq; NP_439034.2; NC_000907.1. DR ProteinModelPortal; P44914; -. DR SMR; P44914; 1-336. DR STRING; 71421.HI0873; -. DR EnsemblBacteria; AAC22531; AAC22531; HI_0873. DR GeneID; 949510; -. DR KEGG; hin:HI0873; -. DR PATRIC; 20190401; VBIHaeInf48452_0914. DR eggNOG; ENOG4105C1B; Bacteria. DR eggNOG; COG1088; LUCA. DR KO; K01710; -. DR OMA; PDEQEGQ; -. DR OrthoDB; EOG6PZXCX; -. DR UniPathway; UPA00124; -. DR UniPathway; UPA00281; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB. DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005888; dTDP_Gluc_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR10366:SF41; PTHR10366:SF41; 1. DR Pfam; PF16363; GDP_Man_Dehyd; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1. PE 3: Inferred from homology; KW Complete proteome; Lipopolysaccharide biosynthesis; Lyase; NAD; KW Reference proteome. FT CHAIN 1 338 dTDP-glucose 4,6-dehydratase. FT /FTId=PRO_0000183237. FT NP_BIND 8 14 NAD. {ECO:0000255}. FT NP_BIND 33 36 NAD. {ECO:0000250}. FT NP_BIND 59 60 NAD. {ECO:0000250}. FT NP_BIND 160 164 NAD. {ECO:0000250}. FT REGION 134 136 Substrate binding. {ECO:0000250}. FT REGION 199 200 Substrate binding. {ECO:0000250}. FT REGION 215 217 Substrate binding. {ECO:0000250}. FT REGION 294 297 Substrate binding. {ECO:0000250}. FT ACT_SITE 135 135 Proton donor. {ECO:0000250}. FT ACT_SITE 136 136 Proton acceptor. {ECO:0000250}. FT ACT_SITE 160 160 Proton acceptor. {ECO:0000250}. FT BINDING 81 81 NAD; via carbonyl oxygen. {ECO:0000250}. FT BINDING 85 85 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 100 100 NAD. {ECO:0000250}. FT BINDING 189 189 Substrate. {ECO:0000250}. FT BINDING 190 190 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 224 224 Substrate. {ECO:0000250}. FT BINDING 259 259 Substrate. {ECO:0000250}. SQ SEQUENCE 338 AA; 38329 MW; B44BCC29D6C7D04B CRC64; MMNILVTGGS GFIGSALIRY IINHTQDFVI NIDKLTYAAN QSALREVENN PRYVFEKVDI CDLNVIENIF EKYQPDAVMH LAAESHVDRS ISGAADFVQT NIVGTYTLLE VAKNYWHTLD EAKKTTFRFH HISTDEVYGD LSLSEPAFTE QSPYHPSSPY SASKAASNHL VQAWHRTYGL PVIITNSSNN YGAYQHAEKL IPLMISNAVM GKPLPIYGDG QQIRDWLFVE DHVQASYLVL TKGRVGENYN IGGNCEKTNL EVVKRICQLL EELAPSKPNH IKYYEDLMTF VKDRPGHDVR YSLDCSKIHA ELGWQPQITF EQGLRQTVKW YLFNSSSS // ID RMUC_HAEIN Reviewed; 450 AA. AC P44733; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 2. DT 11-NOV-2015, entry version 75. DE RecName: Full=DNA recombination protein RmuC homolog; GN Name=rmuC; OrderedLocusNames=HI_0500; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in DNA recombination. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RmuC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22158.1; 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; L42023; AAC22158.1; ALT_INIT; Genomic_DNA. DR PIR; F64153; F64153. DR RefSeq; NP_438658.2; NC_000907.1. DR ProteinModelPortal; P44733; -. DR STRING; 71421.HI0500; -. DR EnsemblBacteria; AAC22158; AAC22158; HI_0500. DR GeneID; 949635; -. DR KEGG; hin:HI0500; -. DR PATRIC; 20189553; VBIHaeInf48452_0519. DR eggNOG; ENOG4105CGY; Bacteria. DR eggNOG; COG1322; LUCA. DR KO; K09760; -. DR OMA; VANLWRI; -. DR OrthoDB; EOG6T4S02; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR InterPro; IPR003798; DNA_recombination_RmuC. DR Pfam; PF02646; RmuC; 1. PE 3: Inferred from homology; KW Coiled coil; Complete proteome; DNA recombination; Reference proteome. FT CHAIN 1 450 DNA recombination protein RmuC homolog. FT /FTId=PRO_0000202044. FT COILED 3 89 {ECO:0000255}. SQ SEQUENCE 450 AA; 51257 MW; 287FCED1515BCDE7 CRC64; MHQELSKTTQ DYNQLASKFD ELSSIKNQFE QQTIKVQTEN QGLQYRLTER DEQIHHLTQE RQNLTEKLTA LSQELTGLQT TLTEKEKYFS AQQQNFEQSK QQLGVEFQNL ANRILDEKSR SFSQSNQTAL ETLLKPFREQ IEGFQKRVNE IHSESVKGNA GLEAEIKKVL EIGLNMSQEA SNLTSALKGE KKTLGNWGEV QLERALQLAG LEENVHYRAQ AHFKDEQGGR NYPDFVLNLP DEKHLIIDSK MSLVAYESAV NSEDDFERER LLKEHISALK THINDLHKKD YSNLIGMCSP NFVLMFIAVE PAYIEALKAD PALFNYGYER NVIMVSHTTL MPILRTVANL WRIERGNAEA KEIAEKAGEI YNQICLVAER LNKLGNTLST VSNQYNSTVT ALVGQQGLVG KVERFKTLSA KANKTMPDVD LLNNQLDLAR LNVLNQENLQ // ID RL34_HAEIN Reviewed; 44 AA. AC P66244; P44370; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 13-APR-2016, entry version 61. DE RecName: Full=50S ribosomal protein L34; GN Name=rpmH; Synonyms=rpl34; OrderedLocusNames=HI_0998; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22660.1; -; Genomic_DNA. DR PIR; E64107; E64107. DR RefSeq; NP_439160.1; NC_000907.1. DR RefSeq; WP_005539760.1; NC_000907.1. DR ProteinModelPortal; P66244; -. DR SMR; P66244; 1-44. DR STRING; 71421.HI0998; -. DR EnsemblBacteria; AAC22660; AAC22660; HI_0998. DR GeneID; 25057576; -. DR GeneID; 949994; -. DR KEGG; hin:HI0998; -. DR PATRIC; 20190657; VBIHaeInf48452_1041. DR eggNOG; ENOG4105VG0; Bacteria. DR eggNOG; COG0230; LUCA. DR KO; K02914; -. DR OrthoDB; EOG6DZF71; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00391; Ribosomal_L34; 1. DR InterPro; IPR000271; Ribosomal_L34. DR InterPro; IPR020939; Ribosomal_L34_CS. DR PANTHER; PTHR14503; PTHR14503; 1. DR Pfam; PF00468; Ribosomal_L34; 1. DR ProDom; PD003101; Ribosomal_L34; 1. DR TIGRFAMs; TIGR01030; rpmH_bact; 1. DR PROSITE; PS00784; RIBOSOMAL_L34; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 44 50S ribosomal protein L34. FT /FTId=PRO_0000187390. SQ SEQUENCE 44 AA; 5098 MW; F7F978922AF57213 CRC64; MKRTFQPSVL KRSRTHGFRA RMATKNGRQV LARRRAKGRK SLSA // ID RLMD_HAEIN Reviewed; 438 AA. AC P44643; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000255|HAMAP-Rule:MF_01010}; DE EC=2.1.1.190 {ECO:0000255|HAMAP-Rule:MF_01010}; DE AltName: Full=23S rRNA(m5U1939)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01010}; GN Name=rlmD {ECO:0000255|HAMAP-Rule:MF_01010}; Synonyms=rumA; GN OrderedLocusNames=HI_0333; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position CC 1939 (m5U1939) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01010}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(1939) in 23S CC rRNA = S-adenosyl-L-homocysteine + 5-methyluracil(1939) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01010}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC RlmD subfamily. {ECO:0000255|HAMAP-Rule:MF_01010}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP- CC Rule:MF_01010}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21995.1; -; Genomic_DNA. DR PIR; C64148; C64148. DR RefSeq; NP_438497.1; NC_000907.1. DR RefSeq; WP_005694340.1; NC_000907.1. DR ProteinModelPortal; P44643; -. DR STRING; 71421.HI0333; -. DR EnsemblBacteria; AAC21995; AAC21995; HI_0333. DR GeneID; 949426; -. DR KEGG; hin:HI0333; -. DR PATRIC; 20189209; VBIHaeInf48452_0350. DR eggNOG; ENOG4105BZT; Bacteria. DR eggNOG; COG2265; LUCA. DR KO; K03215; -. DR OMA; DLDPFGQ; -. DR OrthoDB; EOG6V4GKM; -. DR PhylomeDB; P44643; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01010; 23SrRNA_methyltr_RlmD; 1. DR InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR030391; MeTrfase_TrmA_CS. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR002792; TRAM_dom. DR InterPro; IPR010280; U5_MeTrfase_fam. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00479; rumA; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS50926; TRAM; 1. DR PROSITE; PS01230; TRMA_1; 1. DR PROSITE; PS01231; TRMA_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 438 23S rRNA (uracil(1939)-C(5))- FT methyltransferase RlmD. FT /FTId=PRO_0000161898. FT DOMAIN 10 68 TRAM. {ECO:0000255|HAMAP-Rule:MF_01010}. FT ACT_SITE 395 395 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT METAL 81 81 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT METAL 87 87 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT METAL 90 90 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT METAL 168 168 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT BINDING 271 271 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01010}. FT BINDING 300 300 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01010}. FT BINDING 305 305 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01010}. FT BINDING 321 321 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01010}. FT BINDING 348 348 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01010}. FT BINDING 369 369 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01010}. SQ SEQUENCE 438 AA; 49870 MW; A8E5657266786046 CRC64; MVLLYTPKQK TKNVQTITAD ILDLDYQGLG VAKINGKTWF IENALPHEKV ECRILEDKRQ YGHAIVKKWR VKSPERLEPK CAHFMRCGGC QGQHIPIEMQ RKAKESALFK RLSKLQSEPI SFQPMICGDA WAYRRRVRLS LWFNPSTKQI EMGFRQKNTN DLIPVQSCEV AEPAINYLLP KLTALLEKFS APKQLGHIEL VAADNGVAML LRYTKNLAEI DRTLLLKFAE QEKLMLFLQS DKGIEQIYGD APYYQFSDGI KLHFDIRDFI QVNSALNEPM VNTALDWLEL SQQDCVLDLF CGMGNFTLPL AKRVKSAVGI EGVFEMVQKA AQNAERNQIK NIEFFQADLD QSFVEQPWAN QSFNKILLDP PRSGAAFALN ALCELKAEKI LYVSCNPATL VRDAEILCNF GYKIEKSAVI DMFPHTGHLE SITLFTTK // ID RLMH_HAEIN Reviewed; 155 AA. AC P44470; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_00658}; DE EC=2.1.1.177 {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00658}; DE AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN Name=rlmH {ECO:0000255|HAMAP-Rule:MF_00658}; GN OrderedLocusNames=HI_0033; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the pseudouridine at position CC 1915 (m3Psi1915) in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + pseudouridine(1915) CC in 23S rRNA = S-adenosyl-L-homocysteine + N(3)- CC methylpseudouridine(1915) in 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00658}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family. CC {ECO:0000255|HAMAP-Rule:MF_00658}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21711.1; -; Genomic_DNA. DR PIR; G64140; G64140. DR RefSeq; NP_438206.1; NC_000907.1. DR RefSeq; WP_005649848.1; NC_000907.1. DR ProteinModelPortal; P44470; -. DR SMR; P44470; 1-155. DR STRING; 71421.HI0033; -. DR EnsemblBacteria; AAC21711; AAC21711; HI_0033. DR GeneID; 950930; -. DR KEGG; hin:HI0033; -. DR PATRIC; 20188517; VBIHaeInf48452_0033. DR eggNOG; ENOG4108UXA; Bacteria. DR eggNOG; COG1576; LUCA. DR KO; K00783; -. DR OMA; NGEPYHK; -. DR OrthoDB; EOG6S26HR; -. DR PhylomeDB; P44470; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00658; 23SrRNA_methyltr_H; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR016051; RlmH. DR InterPro; IPR003742; SPOUT_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF02590; SPOUT_MTase; 1. DR PIRSF; PIRSF004505; MT_bac; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00246; tRNA_RlmH_YbeA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 155 Ribosomal RNA large subunit FT methyltransferase H. FT /FTId=PRO_0000198126. SQ SEQUENCE 155 AA; 17250 MW; D147B9FA24389A1E CRC64; MKITLIAVGT KMPSWVTTGF EEYQRRFPKD MPFELIEIPA GKRGKNADIK RILEQEGKAM LAACGKGKVV TLDIPGKPWT TPQLAEQLEA WKNDGRDVCL LIGGPEGLSP ECKAAAEQSW SLSPLTLPHP LVRVVVAESL YRAWSLTTNH PYHRE // ID RLMKL_HAEIN Reviewed; 711 AA. AC P44524; P43945; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000255|HAMAP-Rule:MF_01858}; DE Includes: DE RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858}; DE EC=2.1.1.173 {ECO:0000255|HAMAP-Rule:MF_01858}; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000255|HAMAP-Rule:MF_01858}; DE Includes: DE RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858}; DE EC=2.1.1.264 {ECO:0000255|HAMAP-Rule:MF_01858}; DE AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000255|HAMAP-Rule:MF_01858}; GN Name=rlmL {ECO:0000255|HAMAP-Rule:MF_01858}; GN OrderedLocusNames=HI_0116; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the guanine in position 2445 CC (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. CC {ECO:0000255|HAMAP-Rule:MF_01858}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(2445) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(2445) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01858}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(2069) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(2069) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01858}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01858}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL CC family. {ECO:0000255|HAMAP-Rule:MF_01858}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|HAMAP- CC Rule:MF_01858}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=182; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P44524; -. DR OMA; MSNTYLN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 3. DR HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1. DR InterPro; IPR017244; 23SrRNA_methyltr_KL. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR000241; RNA_methylase_dom. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF10672; Methyltrans_SAM; 1. DR Pfam; PF02926; THUMP; 1. DR Pfam; PF01170; UPF0020; 1. DR PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF53335; SSF53335; 3. DR PROSITE; PS51165; THUMP; 1. DR PROSITE; PS01261; UPF0020; 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 1 711 Ribosomal RNA large subunit FT methyltransferase K/L. FT /FTId=PRO_0000140474. FT DOMAIN 43 154 THUMP. {ECO:0000255|HAMAP-Rule:MF_01858}. SQ SEQUENCE 711 AA; 81502 MW; BC5ABB77B60BDD03 CRC64; MKQLFATTSR GFEELLKVEL TELGAQEAKV VQGGVHYQAD DETLYRTLLW SRLASRILFP LIETKIYSDL DLYAAVSGFN WLAQFDERVT FFVDFNGTNQ EIRHTQFGAM RVKDGIVDYF ERQGKTRPDV DKIQPDVRIH AYLNRENLVI SLDLSGEALH LRGYREDAGQ APLRETLAAA IVMRSGWQVG SPLVDPMCGS GTLLIEAAQM EAKIAPQLYR LHWGFDFWKA HNQSAWEKVK NEAIELAEEK QREIQPHFYG FDLDHRVLKK AQKNAQNAGV SHLIKWQQAD VAALKNPRLN EVGTVICNPP YGERLGTTPA LIALYSVFGQ RLKKEFCGWN VSVFSSESTL LDCLRMRASR QFKAKNGPLD CVQKNYQVSE RKSDAITDEK ELEFNRTSEV APDFANRLQK NIKKISKWAK QQELDAYRLY DADLPEYNLA VDRYADYIVV QEYAAPKNID ENKARQRLLD AVTATLQVTG VETNKLILKV RQKQKGTNQY EKLANKGEYF YVNEYGTQLW VNLTDYLDTG LFLDHRLTRK MIGELAKGKD FLNLFAYTGS ATVHAALGGA KSTTTVDMSN TYLNWAEQNL ILNDIEGKQH KLIQADCLQW LEKCDRQFDL IFADPPTFSN SKRMEESWDV QRDHVKLMRN LKRVLSNNGT IVFSNNKRGF KMNLVALEEL GLSAIEISHK TLPLDFERNK QIHNCWMIQH I // ID RLPA_HAEIN Reviewed; 287 AA. AC Q57092; O05005; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 91. DE RecName: Full=RlpA-like protein; DE Flags: Precursor; GN OrderedLocusNames=HI_0030; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the RlpA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SPOR 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; L42023; AAC21708.1; -; Genomic_DNA. DR PIR; A64044; A64044. DR RefSeq; NP_438203.1; NC_000907.1. DR RefSeq; WP_005668014.1; NC_000907.1. DR STRING; 71421.HI0030; -. DR EnsemblBacteria; AAC21708; AAC21708; HI_0030. DR GeneID; 950926; -. DR KEGG; hin:HI0030; -. DR PATRIC; 20188511; VBIHaeInf48452_0030. DR eggNOG; ENOG4105K6T; Bacteria. DR eggNOG; COG0797; LUCA. DR KO; K03642; -. DR OMA; LYTAAHK; -. DR OrthoDB; EOG6X3W9K; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR Gene3D; 3.30.70.1070; -; 1. DR InterPro; IPR009009; RlpA-like_DPBB. DR InterPro; IPR012997; RplA. DR InterPro; IPR007730; SPOR_dom. DR Pfam; PF03330; DPBB_1; 1. DR Pfam; PF05036; SPOR; 1. DR SUPFAM; SSF110997; SSF110997; 1. DR SUPFAM; SSF50685; SSF50685; 1. DR TIGRFAMs; TIGR00413; rlpA; 1. DR PROSITE; PS51724; SPOR; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 287 RlpA-like protein. FT /FTId=PRO_0000030803. FT DOMAIN 209 284 SPOR. SQ SEQUENCE 287 AA; 31803 MW; C786B574600CA29D CRC64; MKLKTGLNLT ALLLFMISVA FPAQADTQKM YGIRGDNLSI ATQMPAPRTY SVKGQTYTTK SGNEAKSYIK EGLASYYHLK FDGRKTASGD VYNSKQFTAA HKTLPINSYA LVTNLHNNRK VIVRINDRGP FSDKRLIDLS HAAAKEIGLI SRGIGQVRIE ALHVAKNGNL SGAATKTLAK QAKTQEAADR LVLKSNTLFD NTSKSINALK GTEFYCLKML ELTSRSQANK LITQLALANI QTEVNRSGNK YEIYIGPFDD KTKMAQVRTK LQKMANNKPL IVYTYKN // ID RLUB_HAEIN Reviewed; 357 AA. AC P45104; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Ribosomal large subunit pseudouridine synthase B; DE EC=5.4.99.22; DE AltName: Full=23S rRNA pseudouridine(2605) synthase; DE AltName: Full=rRNA pseudouridylate synthase B; DE AltName: Full=rRNA-uridine isomerase B; GN Name=rluB; OrderedLocusNames=HI_1199; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 2605 in 23S ribosomal RNA. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 23S rRNA uridine(2605) = 23S rRNA CC pseudouridine(2605). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA 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; L42023; AAC22853.1; -; Genomic_DNA. DR PIR; A64169; A64169. DR RefSeq; NP_439355.1; NC_000907.1. DR RefSeq; WP_005694244.1; NC_000907.1. DR ProteinModelPortal; P45104; -. DR STRING; 71421.HI1199; -. DR EnsemblBacteria; AAC22853; AAC22853; HI_1199. DR GeneID; 950150; -. DR KEGG; hin:HI1199; -. DR PATRIC; 20191077; VBIHaeInf48452_1251. DR eggNOG; ENOG4105FE9; Bacteria. DR eggNOG; COG1187; LUCA. DR KO; K06178; -. DR OMA; QKEICRV; -. DR OrthoDB; EOG6130DV; -. DR PhylomeDB; P45104; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. DR PROSITE; PS50889; S4; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Reference proteome; RNA-binding; KW rRNA processing. FT CHAIN 1 357 Ribosomal large subunit pseudouridine FT synthase B. FT /FTId=PRO_0000099986. FT DOMAIN 76 148 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 183 183 Nucleophile. {ECO:0000250}. SQ SEQUENCE 357 AA; 40637 MW; 0A31F0D384CBBE82 CRC64; MKPSQKQTQR QPHFSKDSAK KRDFSAKNDR RSVSRTARIE TANTKKSAVN SDNKFLSKPK AKPVVRASNQ PKAEGEKLQK VLARAGQGSR REIETMIAAG RVSVEGKIAT LGDRIDVHSG VKVRIDGQII NLSHTQKEIC RVLMYYKPEG ELCTRSDPEG RATVFDRLPR LTGSRWIAVG RLDINTSGLL LFTTDGELAN RLMHPSREVE REYSVRVFGQ VDDAMLARLR KGVQLEDGLA NFKEIKFTGG VGINQWYDVT LMEGRNREVR RLWESQGIQV SRLIRIRYGN IKLMKGLPRG GWEEMDLENV NYLRELVGLP AETETKLDVK QASRRPKSGQ IRKAVKRYSE MNKRYKK // ID RN26_HAEIN Reviewed; 272 AA. AC P44012; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Probable ribonuclease HI_0526; DE Flags: Precursor; GN OrderedLocusNames=HI_0526; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the RNase T2 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; L42023; AAC22192.1; -; Genomic_DNA. DR PIR; C64009; C64009. DR RefSeq; NP_438684.1; NC_000907.1. DR RefSeq; WP_005694129.1; NC_000907.1. DR ProteinModelPortal; P44012; -. DR STRING; 71421.HI0526; -. DR EnsemblBacteria; AAC22192; AAC22192; HI_0526. DR GeneID; 949589; -. DR KEGG; hin:HI0526; -. DR PATRIC; 20189605; VBIHaeInf48452_0545. DR eggNOG; ENOG41083KI; Bacteria. DR eggNOG; COG3719; LUCA. DR KO; K01166; -. DR OMA; MLALSWS; -. DR OrthoDB; EOG6MWN93; -. DR PhylomeDB; P44012; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.90.730.10; -; 1. DR InterPro; IPR001568; RNase_T2-like. DR InterPro; IPR018188; RNase_T2_His_AS_1. DR InterPro; IPR033130; RNase_T2_His_AS_2. DR PANTHER; PTHR11240; PTHR11240; 1. DR Pfam; PF00445; Ribonuclease_T2; 1. DR SUPFAM; SSF55895; SSF55895; 1. DR PROSITE; PS00530; RNASE_T2_1; 1. DR PROSITE; PS00531; RNASE_T2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 272 Probable ribonuclease HI_0526. FT /FTId=PRO_0000030963. FT ACT_SITE 148 148 {ECO:0000250}. FT ACT_SITE 195 195 {ECO:0000250}. FT ACT_SITE 199 199 {ECO:0000250}. SQ SEQUENCE 272 AA; 31482 MW; 9D580FF9C2CEB392 CRC64; MKKLTSILSL IVLVILAIWQ YFTDTTKTKH QSSSPVIEQT KQTKVSEPKF EPKFEPKFEP KFEPQFETKR TDIEKSAVKN PDVFANYDVI MRNDHIGQNA KAPVDYYMLA LSWSPGFCDI QREKYGDQLP YSSQYQCGNN RTFGWVVHGL WPQNANARAV SDHPRFCKGD LPALPKGLLA QYLAISPGEK LLQGEWEKHG SCAFDSAQQY FAKEQELFNA LKLPNQKLSR DELFGWMKQH NPQLKNAYLR ASRNELFICY DKKWQVMNCQ SK // ID RNC_HAEIN Reviewed; 227 AA. AC P44441; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. 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=HI_0014; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 DRBM (double-stranded RNA-binding) domain. CC {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; L42023; AAC21692.1; -; Genomic_DNA. DR PIR; G64042; G64042. DR RefSeq; NP_438187.1; NC_000907.1. DR RefSeq; WP_005693887.1; NC_000907.1. DR ProteinModelPortal; P44441; -. DR STRING; 71421.HI0014; -. DR EnsemblBacteria; AAC21692; AAC21692; HI_0014. DR GeneID; 950910; -. DR KEGG; hin:HI0014; -. DR PATRIC; 20188479; VBIHaeInf48452_0014. DR eggNOG; ENOG4108ZBM; Bacteria. DR eggNOG; COG0571; LUCA. DR KO; K03685; -. DR OMA; LTHKSCK; -. DR OrthoDB; EOG6T1WVS; -. DR PhylomeDB; P44441; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IBA:GO_Central. DR GO; GO:0016075; P:rRNA catabolic process; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 1.10.1520.10; -; 1. DR Gene3D; 3.30.160.20; -; 1. DR HAMAP; MF_00104; RNase_III; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR011907; RNase_III. DR InterPro; IPR000999; RNase_III_dom. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF14622; Ribonucleas_3_3; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00535; RIBOc; 1. DR SUPFAM; SSF69065; SSF69065; 1. DR TIGRFAMs; TIGR02191; RNaseIII; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; mRNA processing; Nuclease; Reference proteome; KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing. FT CHAIN 1 227 Ribonuclease 3. FT /FTId=PRO_0000180400. FT DOMAIN 4 126 RNase III. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT DOMAIN 153 226 DRBM. {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 43 43 {ECO:0000255|HAMAP-Rule:MF_00104}. FT ACT_SITE 115 115 {ECO:0000255|HAMAP-Rule:MF_00104}. FT METAL 39 39 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 112 112 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. FT METAL 115 115 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00104}. SQ SEQUENCE 227 AA; 25728 MW; 69F5DD1DAA71EB50 CRC64; MNHLDRLERK IGYRFNDIAL LKQALTHRSA ATQHNERLEF LGDSILNFTI AEALYHQFPR CNEGELSRMR ATLVREPTLA ILARQFELGD YMSLGSGELK NGGFRRESIL ADCVEAIIGA MSLDQGLAVT TQVIRNWYQQ LLAEIKPGDN QKDAKTRLQE YLQGKHLPLP TYEVVNIQGE AHCQIFTVKC KVKSAEKIDR TFVAKGSSRR KAEQAAAEQI LKELDIK // ID RND_HAEIN Reviewed; 399 AA. AC P44442; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Ribonuclease D {ECO:0000255|HAMAP-Rule:MF_01899}; DE Short=RNase D {ECO:0000255|HAMAP-Rule:MF_01899}; DE EC=3.1.13.5 {ECO:0000255|HAMAP-Rule:MF_01899}; GN Name=rnd {ECO:0000255|HAMAP-Rule:MF_01899}; OrderedLocusNames=HI_0390; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Exonuclease involved in the 3' processing of various CC precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA CC molecule and releases 5'-mononucleotides. {ECO:0000255|HAMAP- CC Rule:MF_01899}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage that removes extra CC residues from the 3'-terminus of tRNA to produce 5'- CC mononucleotides. {ECO:0000255|HAMAP-Rule:MF_01899}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01899}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01899}. CC -!- SIMILARITY: Belongs to the RNase D family. {ECO:0000255|HAMAP- CC Rule:MF_01899}. CC -!- SIMILARITY: Contains 1 3'-5' exonuclease domain. CC {ECO:0000255|HAMAP-Rule:MF_01899}. CC -!- SIMILARITY: Contains 1 HRDC domain. {ECO:0000255|HAMAP- CC Rule:MF_01899}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22048.1; -; Genomic_DNA. DR PIR; B64065; B64065. DR RefSeq; NP_438552.1; NC_000907.1. DR RefSeq; WP_010868981.1; NC_000907.1. DR ProteinModelPortal; P44442; -. DR STRING; 71421.HI0390; -. DR EnsemblBacteria; AAC22048; AAC22048; HI_0390. DR GeneID; 950674; -. DR KEGG; hin:HI0390; -. DR PATRIC; 20189331; VBIHaeInf48452_0409. DR eggNOG; ENOG4105ZIE; Bacteria. DR eggNOG; COG0349; LUCA. DR KO; K03684; -. DR OMA; HKLQERD; -. DR OrthoDB; EOG6MM1MT; -. DR PhylomeDB; P44442; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0033890; F:ribonuclease D activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042780; P:tRNA 3'-end processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_01899; RNase_D; 1. DR InterPro; IPR002562; 3'-5'_exonuclease_dom. DR InterPro; IPR010997; HRDC-like. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR006292; RNase_D. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF01612; DNA_pol_A_exo1; 1. DR Pfam; PF00570; HRDC; 1. DR SMART; SM00474; 35EXOc; 1. DR SMART; SM00341; HRDC; 1. DR SUPFAM; SSF47819; SSF47819; 2. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR01388; rnd; 1. DR PROSITE; PS50967; HRDC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome; tRNA processing. FT CHAIN 1 399 Ribonuclease D. FT /FTId=PRO_0000097369. FT DOMAIN 31 197 3'-5' exonuclease. {ECO:0000255|HAMAP- FT Rule:MF_01899}. FT DOMAIN 239 318 HRDC. {ECO:0000255|HAMAP-Rule:MF_01899}. SQ SEQUENCE 399 AA; 46065 MW; DC0C40933F234DA8 CRC64; MSKWDSNIPF LFFSNKKITM IKECQNPPHF RVVTDNTALL EVCNLAQQKS AVALDTEFMR VSTYFPKLGL IQLYDGEHVS LIDPLAITDF SPFVALLANP KVLKILHSCS EDLLVFLQEF DQLPRPMIDT QIMARFLGLG TSAGLAKLAQ QYLNVEIDKG ATRTNWIKRP LSDIQLQYAA GDVWYLLPLY HILEKELAKT PWEQAVRDDC ELVLAKTHKL QERDSEKAYL DIPNAWKLNP LELSRLRVLA QWRQNVAIER DLALSYIVKS EHLWKVAKNN PRNTSEMLEM GLTENEVRVR GKEILQLLSQ ARRISSNDYP KSIERISEDP RYKKTIRLLQ EKVNSLTPEG LTPEIVASKR TLEELIKWVW KYDCSQDKRP ELLIGWRKPI GEKLVDALK // ID RNH_HAEIN Reviewed; 154 AA. AC P43807; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Ribonuclease HI; DE Short=RNase HI; DE EC=3.1.26.4; GN Name=rnhA; Synonyms=rnh; OrderedLocusNames=HI_0138; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-123. RA Mizrahi V., Dudding L.R.; RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion CC at a regulatory site, or after substrate binding. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 RNase H 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; L42023; AAC21809.1; -; Genomic_DNA. DR EMBL; L11915; AAA25000.1; -; Genomic_DNA. DR PIR; C64050; C64050. DR RefSeq; NP_438307.1; NC_000907.1. DR RefSeq; WP_010868943.1; NC_000907.1. DR ProteinModelPortal; P43807; -. DR SMR; P43807; 1-151. DR STRING; 71421.HI0138; -. DR EnsemblBacteria; AAC21809; AAC21809; HI_0138. DR GeneID; 951050; -. DR KEGG; hin:HI0138; -. DR PATRIC; 20188767; VBIHaeInf48452_0140. DR eggNOG; ENOG4108UMW; Bacteria. DR eggNOG; COG0328; LUCA. DR KO; K03469; -. DR OMA; LVTDSQY; -. DR OrthoDB; EOG696BTR; -. DR PhylomeDB; P43807; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00042; RNase_H; 1. DR InterPro; IPR022892; RNaseH. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR002156; RNaseH_domain. DR Pfam; PF00075; RNase_H; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50879; RNASE_H; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 154 Ribonuclease HI. FT /FTId=PRO_0000195377. FT DOMAIN 1 142 RNase H. FT METAL 10 10 Magnesium 1. {ECO:0000250}. FT METAL 10 10 Magnesium 2. {ECO:0000250}. FT METAL 48 48 Magnesium 1. {ECO:0000250}. FT METAL 70 70 Magnesium 1. {ECO:0000250}. FT METAL 134 134 Magnesium 2. {ECO:0000250}. SQ SEQUENCE 154 AA; 17640 MW; 79A413E23DD2BD5A CRC64; MPKQIEIFTD GSCLGNPGAG GIGAVLRYKQ HEKTLSKGYF QTTNNRMELR AVIEALNTLK EPCLITLYSD SQYMKNGITK WIFNWKKNNW KASSGKPVKN QDLWIALDES IQRHKINWQW VKGHAGHREN EICDELAKKG AENPTLEDMG YIEE // ID RLMJ_HAEIN Reviewed; 281 AA. AC P31777; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Ribosomal RNA large subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_00934}; DE EC=2.1.1.266 {ECO:0000255|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA (adenine(2030)-N6)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00934}; DE AltName: Full=23S rRNA m6A2030 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00934}; DE AltName: Full=ORFJ; GN Name=rlmJ {ECO:0000255|HAMAP-Rule:MF_00934}; GN OrderedLocusNames=HI_0441; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M; RA Tomb J.-F., El-Hajj H., Smith H.O.; RT "Nucleotide sequence of a cluster of genes involved in the RT transformation of Haemophilus influenzae Rd."; RL Gene 104:1-10(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Specifically methylates the adenine in position 2030 of CC 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00934}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(2030) in 23S CC rRNA = S-adenosyl-L-homocysteine + N(6)-methyladenine(2030) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_00934}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00934}. CC -!- SIMILARITY: Belongs to the RlmJ family. {ECO:0000255|HAMAP- CC Rule:MF_00934}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62809; AAA25006.1; -; Genomic_DNA. DR EMBL; L42023; AAC22100.1; -; Genomic_DNA. DR PIR; E64068; E64068. DR RefSeq; NP_438602.1; NC_000907.1. DR RefSeq; WP_005693720.1; NC_000907.1. DR ProteinModelPortal; P31777; -. DR STRING; 71421.HI0441; -. DR EnsemblBacteria; AAC22100; AAC22100; HI_0441. DR GeneID; 949523; -. DR KEGG; hin:HI0441; -. DR PATRIC; 20189435; VBIHaeInf48452_0461. DR eggNOG; ENOG4105D6S; Bacteria. DR eggNOG; COG2961; LUCA. DR KO; K07115; -. DR OMA; TYAIWYP; -. DR OrthoDB; EOG6Q8J0P; -. DR PhylomeDB; P31777; -. DR BioCyc; RETL1328306-WGS:GSTH-1496-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0036307; F:23S rRNA (adenine(2030)-N(6))-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00934; 23SrRNA_methyltr_J; 1. DR InterPro; IPR007473; RlmJ. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04378; RsmJ; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 2. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Reference proteome; RNA-binding; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 281 Ribosomal RNA large subunit FT methyltransferase J. FT /FTId=PRO_0000169568. FT REGION 144 145 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00934}. FT ACT_SITE 165 165 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00934}. FT BINDING 19 19 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00934}. FT BINDING 42 42 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00934}. FT BINDING 101 101 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00934}. FT BINDING 119 119 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00934}. FT BINDING 165 165 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00934}. FT SITE 4 4 Interaction with substrate rRNA. FT {ECO:0000255|HAMAP-Rule:MF_00934}. SQ SEQUENCE 281 AA; 32217 MW; 5A66A59357A80F34 CRC64; MLSYHHSFHA GNHADVLKHI VLMLILENLK LKEKGFFYLD THSGVGRYRL SSNESEKTGE YKEGIGRLWD QTDLPEDIAR YVKMIKKLNY GGKELRYYAG SPLIAAELLR SQDRALLTEL HPSDYPILRN NFSDDKNVTV KCDNGFQQVK ATLPPKERRG LVLIDPPYEL KDDYDLVVKA IEEGYKRFAT GTYAIWYPVV LRQQTKRIFK GLEATGIRKI LKIELAVRPD SDQRGMTASG MVVINPPWTL ETQMKEILPY LTKTLVPEGT GSWTVEWITP E // ID RLUD_HAEIN Reviewed; 324 AA. AC P44445; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Ribosomal large subunit pseudouridine synthase D; DE EC=5.4.99.23; DE AltName: Full=23S rRNA pseudouridine(1911/1915/1917) synthase; DE AltName: Full=rRNA pseudouridylate synthase D; DE AltName: Full=rRNA-uridine isomerase D; GN Name=rluD; Synonyms=sfhB; OrderedLocusNames=HI_0176; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil CC at positions 1911, 1915 and 1917 in 23S ribosomal RNA. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 23S rRNA CC uridine(1911)/uridine(1915)/uridine(1917) = 23S rRNA CC pseudouridine(1911)/pseudouridine(1915)/pseudouridine(1917). 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; L42023; AAC21845.1; -; Genomic_DNA. DR PIR; F64144; F64144. DR RefSeq; NP_438344.1; NC_000907.1. DR RefSeq; WP_005694111.1; NC_000907.1. DR ProteinModelPortal; P44445; -. DR SMR; P44445; 3-324. DR STRING; 71421.HI0176; -. DR EnsemblBacteria; AAC21845; AAC21845; HI_0176. DR GeneID; 951084; -. DR KEGG; hin:HI0176; -. DR PATRIC; 20188847; VBIHaeInf48452_0180. DR eggNOG; ENOG4105C34; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06180; -. DR OMA; TYGGRPR; -. DR OrthoDB; EOG6P070X; -. DR PhylomeDB; P44445; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; 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; KW rRNA processing. FT CHAIN 1 324 Ribosomal large subunit pseudouridine FT synthase D. FT /FTId=PRO_0000162692. FT DOMAIN 17 90 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 138 138 {ECO:0000250}. SQ SEQUENCE 324 AA; 37110 MW; 35F452DF65FB9145 CRC64; MPQITLSAEV QPEQMGQRLD QTLAELFPEY SRSRLKTWIE ADLVKLNDRI TNIPREKVLG GERIEIIVEV EDETRFEAEN IPLNIVYEDD DIIVINKPKD LVVHPGAGNP NGTVLNALLY HYPPIVEVPR AGIVHRLDKD TTGLMVVAKT IPAQTKLVRD LQKRKITREY EAVASGIMTK GGTVDQPMAR HATKRTLMAV HPMGKPAVTH YRIMENYRNY TRLRLRLETG RTHQIRVHMA HIAHPLLGDQ TYGGRPRPPK NASEDFMEVL RNFKRQALHA VMLRLAHPIT GEMMEWYAPL PDDFVELLNA LKADYLEHQD ELDY // ID RLUE_HAEIN Reviewed; 240 AA. AC P44827; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Ribosomal large subunit pseudouridine synthase E; DE EC=5.4.99.20; DE AltName: Full=rRNA pseudouridylate synthase E; DE AltName: Full=rRNA-uridine isomerase E; GN Name=rluE; OrderedLocusNames=HI_0694; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 2457 in 23S ribosomal RNA. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 23S rRNA uridine(2457) = 23S rRNA CC pseudouridine(2457). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA 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; L42023; AAC22354.1; -; Genomic_DNA. DR PIR; I64156; I64156. DR RefSeq; NP_438854.1; NC_000907.1. DR RefSeq; WP_010869034.1; NC_000907.1. DR ProteinModelPortal; P44827; -. DR SMR; P44827; 51-224. DR STRING; 71421.HI0694; -. DR EnsemblBacteria; AAC22354; AAC22354; HI_0694. DR GeneID; 950211; -. DR KEGG; hin:HI0694; -. DR PATRIC; 20190009; VBIHaeInf48452_0726. DR eggNOG; ENOG4108R99; Bacteria. DR eggNOG; COG1187; LUCA. DR KO; K06181; -. DR OMA; TWIELSI; -. DR OrthoDB; EOG6130DV; -. DR PhylomeDB; P44827; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; rRNA processing. FT CHAIN 1 240 Ribosomal large subunit pseudouridine FT synthase E. FT /FTId=PRO_0000100004. FT ACT_SITE 91 91 Nucleophile. {ECO:0000250}. SQ SEQUENCE 240 AA; 27464 MW; 0AD99EC61F52C01C CRC64; MMLQAFQNRN HKLMKKNFSA GKLPSKGKSA VNFHRTFKPK LKPKTLSLDE TKVVLFNKPF DVLTQFTDEQ GRATLKDFIS IPNVYAAGRL DRDSEGLLIL TNNGELQHRL ADPKFKTEKT YWVQVEGIPE ETDLAQLRKG VELKDGVTKS AKVRLISEPN LWERNPPIRE RKNIPTSWLE IKISEGRNRQ VRRMTAHIGF PTLRLVRVSM GLLSINGLEN GSFRLLSLDE IKALFQTVKL // ID RL7_HAEIN Reviewed; 123 AA. AC P44348; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 101. DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368}; GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; GN OrderedLocusNames=HI_0641; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22301.1; -; Genomic_DNA. DR PIR; F64083; F64083. DR RefSeq; NP_438801.1; NC_000907.1. DR RefSeq; WP_005650892.1; NC_000907.1. DR ProteinModelPortal; P44348; -. DR SMR; P44348; 2-123. DR STRING; 71421.HI0641; -. DR PRIDE; P44348; -. DR EnsemblBacteria; AAC22301; AAC22301; HI_0641. DR GeneID; 949690; -. DR KEGG; hin:HI0641; -. DR PATRIC; 20189889; VBIHaeInf48452_0669. DR eggNOG; ENOG4105KBC; Bacteria. DR eggNOG; COG0222; LUCA. DR KO; K02935; -. DR OMA; AGDQKIK; -. DR PhylomeDB; P44348; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1390.10; -; 1. DR HAMAP; MF_00368; Ribosomal_L7_L12; 1. DR InterPro; IPR000206; Ribosomal_L7/12. DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like. DR InterPro; IPR013823; Ribosomal_L7/L12_C. DR InterPro; IPR008932; Ribosomal_L7/L12_oligo. DR Pfam; PF00542; Ribosomal_L12; 1. DR Pfam; PF16320; Ribosomal_L12_N; 1. DR ProDom; PD001326; Ribosomal_L7/L12_C; 1. DR SUPFAM; SSF48300; SSF48300; 1. DR SUPFAM; SSF54736; SSF54736; 1. DR TIGRFAMs; TIGR00855; L12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 123 50S ribosomal protein L7/L12. FT /FTId=PRO_0000157533. SQ SEQUENCE 123 AA; 12463 MW; 588274B80E594AD7 CRC64; MSLTNEQIIE AIASKTVTEI VELIAAMEEK FGVSAAAAVA AAPAAGGAAA AEEKTEFDVV LKSAGANKVA VIKAVRGATG LGLKEAKDLV ESAPANLKEG VSKEEAEALK KELEEAGAEV EVK // ID RNE_HAEIN Reviewed; 935 AA. AC P44443; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Ribonuclease E {ECO:0000255|HAMAP-Rule:MF_00970}; DE Short=RNase E {ECO:0000255|HAMAP-Rule:MF_00970}; DE EC=3.1.26.12 {ECO:0000255|HAMAP-Rule:MF_00970}; GN Name=rne {ECO:0000255|HAMAP-Rule:MF_00970}; OrderedLocusNames=HI_0413; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA CC processing and decay. Required for the maturation of 5S and 16S CC rRNAs and the majority of tRNAs. Also involved in the degradation CC of most mRNAs. {ECO:0000255|HAMAP-Rule:MF_00970}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of single-stranded CC RNA in A- and U-rich regions. {ECO:0000255|HAMAP-Rule:MF_00970}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970}; CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000255|HAMAP- CC Rule:MF_00970}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00970}; CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein CC complex involved in RNA processing and mRNA degradation. Within CC the RNA degradosome, Rnase E assembles into a homotetramer formed CC by a dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00970}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00970}. CC Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00970}; Peripheral CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00970}; Cytoplasmic CC side {ECO:0000255|HAMAP-Rule:MF_00970}. CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00970}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|HAMAP- CC Rule:MF_00970}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22072.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22072.1; ALT_INIT; Genomic_DNA. DR PIR; E64066; E64066. DR RefSeq; NP_438575.2; NC_000907.1. DR RefSeq; WP_010868984.1; NC_000907.1. DR ProteinModelPortal; P44443; -. DR SMR; P44443; 1-504. DR STRING; 71421.HI0413; -. DR PRIDE; P44443; -. DR EnsemblBacteria; AAC22072; AAC22072; HI_0413. DR GeneID; 949934; -. DR KEGG; hin:HI0413; -. DR PATRIC; 20189379; VBIHaeInf48452_0433. DR eggNOG; ENOG4105C03; Bacteria. DR eggNOG; COG1530; LUCA. DR KO; K08300; -. DR OMA; LHHWEAI; -. DR OrthoDB; EOG6PCPTH; -. DR PhylomeDB; P44443; -. DR BRENDA; 3.1.26.12; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central. DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00970; RNase_E; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR021968; PNPase_C. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR028878; RNase_E. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF12111; PNPase_C; 1. DR Pfam; PF10150; RNase_E_G; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00757; RNaseEG; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; KW Endonuclease; Hydrolase; Magnesium; Membrane; Metal-binding; Nuclease; KW Reference proteome; RNA-binding; rRNA processing; tRNA processing; KW Zinc. FT CHAIN 1 935 Ribonuclease E. FT /FTId=PRO_0000097375. FT DOMAIN 39 119 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_00970}. FT REGION 403 406 Required for zinc-mediated FT homotetramerization and catalytic FT activity. {ECO:0000255|HAMAP- FT Rule:MF_00970}. FT METAL 302 302 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00970}. FT METAL 345 345 Magnesium; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00970}. FT METAL 403 403 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00970}. FT METAL 406 406 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00970}. SQ SEQUENCE 935 AA; 106584 MW; 1493239989920023 CRC64; MKRMLINATQ KEELRVALVD GQRLFDLDIE SPGHEQKKAN IYKGKITRVE PSLEAAFVDY GAERHGFLPL KEIAREYFPD DYVFQGRPNI RDILVEGQEV IVQVNKEERG NKGAALTTFV SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKEALSSLDV PDGVGLIVRT AGVGKSPEEL QWDLKVLLHH WEAIKQASQS RPAPFLIHQE SDVIVRAIRD YLRRDIGEIL IDSPKIFEKA KEHIKLVRPD FINRVKLYQG EVPLFSHYQI ESQIESAFQR EVRLPSGGSI VIDVTEALTA IDINSARSTR GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PIRHQREVEN RIRDAVRPDR ARIQISRISR FGLLEMSRQR LSPSLGESSH HICPRCQGTG KVRDNESLSL SILRLLEEEA LKENTKQVHT IVPVQIASYL LNEKRKAISN IEKRHNVDII VAPNEAMETP HFSVFRLRDG EEVNELSYNL AKIHCAQDEN TEESLLSRNV ETTAVIEQPA VESAVVALSI SEAAPTPVER KSNEPSLLAK IIAKIKGLFA TKSEENKPKN NRTSRNPNRN QRRSQDRRSS RRPRSENNET ERTEEQVRNV RERNQRRPRR NLVEESIAES AVNSTPVFEA KEERTEPVTQ RRQRRDLRKR VRVEDNETVV ENNFSTTEKM PEVDVITVQN NDEKPVHQNQ RSERQERQRR TPRHLRAANN QRRRRDQEPK SPMPLFAAVV SPELASGKAW IDYSTVNLPK ENHFLSVDEL LEQEKTKKGF ITPAMGIVVE EKSPDVKPAL DFITQPANES VQKKVQESLD RLSSYKPQEV VESIDPAINV DEPETLEKVS KFVRTYEFNG RLGTISSVPH TKAEMTLAKA NDEMPEDFPI RAWQDSRYYF YGKGAAGHHC AISHVYSEPT RTKSE // ID RNT_HAEIN Reviewed; 229 AA. AC P44639; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Ribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157}; DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_00157}; DE AltName: Full=Exoribonuclease T {ECO:0000255|HAMAP-Rule:MF_00157}; DE Short=RNase T {ECO:0000255|HAMAP-Rule:MF_00157}; GN Name=rnt {ECO:0000255|HAMAP-Rule:MF_00157}; OrderedLocusNames=HI_0324; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Trims short 3' overhangs of a variety of RNA species, CC leaving a one or two nucleotide 3' overhang. Responsible for the CC end-turnover of tRNA: specifically removes the terminal AMP CC residue from uncharged tRNA (tRNA-C-C-A). Also appears to be CC involved in tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00157}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00157}; CC Note=Binds two Mg(2+) per subunit. The active form of the enzyme CC binds two Mg(2+) ions in its active site. The first Mg(2+) forms CC only one salt bridge with the protein. {ECO:0000255|HAMAP- CC Rule:MF_00157}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00157}. CC -!- SIMILARITY: Belongs to the RNase T family. {ECO:0000255|HAMAP- CC Rule:MF_00157}. CC -!- SIMILARITY: Contains 1 exonuclease domain. {ECO:0000255|HAMAP- CC Rule:MF_00157}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21987.1; -; Genomic_DNA. DR PIR; H64061; H64061. DR RefSeq; NP_438489.1; NC_000907.1. DR RefSeq; WP_005694345.1; NC_000907.1. DR ProteinModelPortal; P44639; -. DR SMR; P44639; 13-211. DR STRING; 71421.HI0324; -. DR EnsemblBacteria; AAC21987; AAC21987; HI_0324. DR GeneID; 949924; -. DR KEGG; hin:HI0324; -. DR PATRIC; 20189189; VBIHaeInf48452_0341. DR eggNOG; ENOG4105DH5; Bacteria. DR eggNOG; COG0847; LUCA. DR KO; K03683; -. DR OMA; CYMVNHL; -. DR OrthoDB; EOG6QG8H4; -. DR PhylomeDB; P44639; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; 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:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00157; RNase_T; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR005987; RNase_T. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00929; RNase_T; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR01298; RNaseT; 1. PE 3: Inferred from homology; KW Complete proteome; Exonuclease; Hydrolase; Magnesium; Metal-binding; KW Nuclease; Reference proteome; tRNA processing. FT CHAIN 1 229 Ribonuclease T. FT /FTId=PRO_0000208964. FT DOMAIN 23 197 Exonuclease. {ECO:0000255|HAMAP- FT Rule:MF_00157}. FT ACT_SITE 184 184 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT METAL 26 26 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT METAL 26 26 Magnesium 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT METAL 28 28 Magnesium 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT METAL 184 184 Magnesium 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT METAL 189 189 Magnesium 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00157}. FT SITE 32 32 Important for substrate binding and FT specificity. {ECO:0000255|HAMAP- FT Rule:MF_00157}. FT SITE 80 80 Important for substrate binding and FT specificity. {ECO:0000255|HAMAP- FT Rule:MF_00157}. FT SITE 127 127 Important for substrate binding and FT specificity. {ECO:0000255|HAMAP- FT Rule:MF_00157}. FT SITE 149 149 Important for substrate binding and FT specificity. {ECO:0000255|HAMAP- FT Rule:MF_00157}. SQ SEQUENCE 229 AA; 25544 MW; 44A1C54EE1C0A3E2 CRC64; MSDSQEIPYH NQLKNRFRGY FPVIIDVETA GFDAKKDALL ELAAITLKMD ENGYLHPDQK CHFHIKPFEG ANINPESLKF NGIDIHNPLR GAVSELDAIT GLFQMVRRGQ KDADCQRSII VAHNAAFDQS FVMAAAERTG VKRNPFHPFG MFDTASLAGL MFGQTVLVKA CQAAKIPFDG KQAHSALYDT ERTAKLFCYM VNHLKDLGGF PHIASELEQE KTTEKETAL // ID RLMM_HAEIN Reviewed; 363 AA. AC P45100; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000255|HAMAP-Rule:MF_01551}; DE EC=2.1.1.186 {ECO:0000255|HAMAP-Rule:MF_01551}; DE AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01551}; DE AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000255|HAMAP-Rule:MF_01551}; GN Name=rlmM {ECO:0000255|HAMAP-Rule:MF_01551}; GN OrderedLocusNames=HI_1195; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in CC 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01551}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(2498) in CC 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(2498) CC in 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01551}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01551}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01551}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase RlmE family. CC RlmM subfamily. {ECO:0000255|HAMAP-Rule:MF_01551}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22849.1; 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; L42023; AAC22849.1; ALT_INIT; Genomic_DNA. DR PIR; H64168; H64168. DR RefSeq; NP_439351.1; NC_000907.1. DR RefSeq; WP_010869151.1; NC_000907.1. DR ProteinModelPortal; P45100; -. DR STRING; 71421.HI1195m; -. DR EnsemblBacteria; AAC22849; AAC22849; HI_1195. DR GeneID; 950147; -. DR KEGG; hin:HI1195m; -. DR PATRIC; 20191069; VBIHaeInf48452_1247. DR eggNOG; ENOG4105EZ6; Bacteria. DR eggNOG; COG2933; LUCA. DR KO; K06968; -. DR OMA; VIFECYQ; -. DR OrthoDB; EOG651SSR; -. DR PhylomeDB; P45100; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01551; 23SrRNA_methyltr_M; 1. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR011224; rRNA_MeTrfase_M. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01728; FtsJ; 1. DR PIRSF; PIRSF028774; UCP028774; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 363 Ribosomal RNA large subunit FT methyltransferase M. FT /FTId=PRO_0000070406. FT REGION 227 230 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01551}. FT ACT_SITE 313 313 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01551}. FT BINDING 194 194 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01551}. FT BINDING 246 246 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01551}. FT BINDING 266 266 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01551}. FT BINDING 284 284 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01551}. SQ SEQUENCE 363 AA; 41563 MW; DC7B76D1B192D524 CRC64; MNKLALYCRP GFEKEVAAEI TDQASHLGVF GFARVQDNSG YVIFECYQPD EADRLARDIP FNRLIFARQM MVISDLLEDL DPADRISPIV VAFEELSQQV NFAQSSELFV ETADTNEAKE LSTFCRKFTV PLRQALKKQG WLSAKASQKC GQFLHCFFVK PNCCYVGYSY VDNHSSHFMG IPRLKFPADA PSRSTLKLEE AILTFIPRKE ENKRLNENMI GVDLGACPGG WTYQLVKRGL FVYAVDHGKM AASLHDTGRI EHCAEDGFKF QPPKRKKVDW LVCDMVEQPS RISLLIGKWL LNGWCRETIF NLKLPMKKRY QEVILCLENL AVMLAEQNLN FDIQAKHLYH DREEITVHIA LKP // ID RLUC_HAEIN Reviewed; 322 AA. AC P44433; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Ribosomal large subunit pseudouridine synthase C; DE EC=5.4.99.24; DE AltName: Full=23S rRNA pseudouridine(955/2504/2580) synthase; DE AltName: Full=rRNA pseudouridylate synthase C; DE AltName: Full=rRNA-uridine isomerase C; GN Name=rluC; OrderedLocusNames=HI_0412; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil CC at positions 955, 2504 and 2580 in 23S ribosomal RNA. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 23S rRNA CC uridine(955)/uridine(2504)/uridine(2580) = 23S rRNA CC pseudouridine(955)/pseudouridine(2504)/pseudouridine(2580). 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; L42023; AAC22071.1; -; Genomic_DNA. DR PIR; G64151; G64151. DR RefSeq; NP_438574.1; NC_000907.1. DR RefSeq; WP_005693754.1; NC_000907.1. DR ProteinModelPortal; P44433; -. DR SMR; P44433; 94-319. DR STRING; 71421.HI0412; -. DR EnsemblBacteria; AAC22071; AAC22071; HI_0412. DR GeneID; 949514; -. DR KEGG; hin:HI0412; -. DR PATRIC; 20189375; VBIHaeInf48452_0431. DR eggNOG; ENOG4105EI2; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06179; -. DR OMA; IVRVPPV; -. DR OrthoDB; EOG6P070X; -. DR PhylomeDB; P44433; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; 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; KW rRNA processing. FT CHAIN 1 322 Ribosomal large subunit pseudouridine FT synthase C. FT /FTId=PRO_0000162671. FT DOMAIN 25 82 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 149 149 {ECO:0000250}. SQ SEQUENCE 322 AA; 36588 MW; 3640CBBD83106463 CRC64; MTKQNEKIIN SSVKMLTISE DESGQRIDNY LLAKLKGVPK SLIYRIVRKG EVRVNKGRIK PEYKLQTGDV VRIPPVRVAE KNDAPISKNL NKVAALENQI LFEDDCLIIL NKPSGIAVHG GSGLNFGVIE ALRALRPEAR FLELVHRLDR DTSGILLIAK KRSALRNLHE QLRVKTVQKD YLALVRGQWQ SHIKVIQASL LKNELSSGER IVRVSEQGKP SETRFSIEER YINATLVKAS PVTGRTHQIR VHTQYAGHPI ALDDKYGDKD FDKQMNELGL NRLFLHAFSI RFEHPKNGET LRFNASLDHQ MKAILQKLRE SK // ID RNB_HAEIN Reviewed; 659 AA. AC P44440; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Exoribonuclease 2; DE EC=3.1.13.1; DE AltName: Full=Exoribonuclease II; DE Short=RNase II; DE Short=Ribonuclease II; GN Name=rnb; OrderedLocusNames=HI_1733; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded CC polyribonucleotides processively in the 3' to 5' direction (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'- CC direction to yield nucleoside 5'-phosphates. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S1 motif 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; L42023; AAC23378.1; -; Genomic_DNA. DR PIR; A64139; A64139. DR RefSeq; NP_439875.1; NC_000907.1. DR RefSeq; WP_005694220.1; NC_000907.1. DR ProteinModelPortal; P44440; -. DR STRING; 71421.HI1733; -. DR EnsemblBacteria; AAC23378; AAC23378; HI_1733. DR GeneID; 950879; -. DR KEGG; hin:HI1733; -. DR PATRIC; 20192223; VBIHaeInf48452_1814. DR eggNOG; ENOG4108IEC; Bacteria. DR eggNOG; COG4776; LUCA. DR KO; K01147; -. DR OMA; RLETRSI; -. DR OrthoDB; EOG6Q5NRD; -. DR PhylomeDB; P44440; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central. DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01036; RNase_II; 1. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013223; RNase_B_OB_dom. DR InterPro; IPR011804; RNase_II. DR InterPro; IPR022966; RNase_II/R_CS. DR InterPro; IPR004476; RNase_II/RNase_R. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF08206; OB_RNB; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 4. DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1. DR TIGRFAMs; TIGR02062; RNase_B; 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 1 659 Exoribonuclease 2. FT /FTId=PRO_0000166384. FT DOMAIN 576 658 S1 motif. SQ SEQUENCE 659 AA; 75782 MW; FDADA9097A7D3B66 CRC64; MFQDNPLLAQ LKQQIHDSKE QVEGVVKSTD KAYGFLECDK KTYFIAPPSM KKVMHGDKIK ATIEKQGDKE QAEPEALIEP MLTRFIAKVR FNKDKKLQVL VDHPSINQPI GAQQAKSVKE ELQEGDWVVA NLKTHPLRDD RFFYATINQL ICRADDELAP WWVTLARHEQ SRYPVRGAEP YEMLDQKTRE NLTALHFVTI DSESTMDMDD ALYIEPIAQN STQTGWKLVV AIADPTAYIA LDSQIEQEAK QRCFTNYLPG FNIPMLPREL SDELCSLIAN ETRPALVCYI ETDLTGNITA KPHFVSAYVQ SKAKLAYNKV SDYLEQADNA WQPEMPETAQ QIHWLHQFTK ARIQWRKTHS LFFKEKPDYA FVLAENGKVQ EIKAEYRRIA NQIVEEAMII ANICAAQFLH EQAKTGIFNT HSGFDKKFLE NAHNFLMANL ANEQNQTELA ERYSVENLAT LNGYCQMRHD IEPIESDYLE LRLRRYLTFA EFKSELAPHF GLGLEGYATW TSPIRKYSDM VNHRLIKAVL AKQPYEKPQN DVLARLQEAR RQNRLVERDI ADWLYCRYLA DKVASNAEFE AEVQDVMRAG LRVQLLENGA SLFIPAATLH NNKEEIQLNP DELALYIKGE RTYKIGDMVK VKLTEVKEAT RSIVGEILQ // ID RNPA_HAEIN Reviewed; 119 AA. AC P44306; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=Ribonuclease P protein component {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNase P protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE Short=RNaseP protein {ECO:0000255|HAMAP-Rule:MF_00227}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00227}; DE AltName: Full=Protein C5 {ECO:0000255|HAMAP-Rule:MF_00227}; GN Name=rnpA {ECO:0000255|HAMAP-Rule:MF_00227}; GN OrderedLocusNames=HI_0999; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC22661.1; -; Genomic_DNA. DR RefSeq; NP_439161.1; NC_000907.1. DR RefSeq; WP_005647913.1; NC_000907.1. DR ProteinModelPortal; P44306; -. DR STRING; 71421.HI0999; -. DR EnsemblBacteria; AAC22661; AAC22661; HI_0999. DR GeneID; 950612; -. DR KEGG; hin:HI0999; -. DR PATRIC; 20190659; VBIHaeInf48452_1042. DR eggNOG; ENOG4105NVJ; Bacteria. DR eggNOG; COG0594; LUCA. DR KO; K03536; -. DR OMA; PPMDFVV; -. DR OrthoDB; EOG6C01C6; -. DR PhylomeDB; P44306; -. DR Proteomes; UP000000579; 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 1 119 Ribonuclease P protein component. FT /FTId=PRO_0000198467. SQ SEQUENCE 119 AA; 14138 MW; 1DF3C520FAA8724A CRC64; MVKLNFSREL RLLTPIQFKN VFEQPFRAST PEITILARKN NLEHPRLGLT VAKKHLKRAH ERNRIKRLVR ESFRLSQHRL PAYDFVFVAK NGIGKLDNNT FAQILEKLWQ RHIRLAQKS // ID RNPH_HAEIN Reviewed; 238 AA. AC P44444; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Ribonuclease PH; DE Short=RNase PH; DE EC=2.7.7.56; DE AltName: Full=tRNA nucleotidyltransferase; GN Name=rph; OrderedLocusNames=HI_0273; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide CC residues following the -CCA terminus of tRNA and adds nucleotides CC to the ends of RNA molecules by using nucleoside diphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside CC diphosphate. CC -!- SIMILARITY: Belongs to the RNase PH 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; L42023; AAC21939.1; -; Genomic_DNA. DR PIR; A64059; A64059. DR RefSeq; NP_438442.1; NC_000907.1. DR RefSeq; WP_005632808.1; NC_000907.1. DR ProteinModelPortal; P44444; -. DR SMR; P44444; 2-237. DR STRING; 71421.HI0273; -. DR EnsemblBacteria; AAC21939; AAC21939; HI_0273. DR GeneID; 949396; -. DR KEGG; hin:HI0273; -. DR PATRIC; 20189073; VBIHaeInf48452_0288. DR eggNOG; ENOG4105ED0; Bacteria. DR eggNOG; COG0689; LUCA. DR KO; K00989; -. DR OMA; KGKGQGW; -. DR OrthoDB; EOG6CZQQP; -. DR PhylomeDB; P44444; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro. DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.70; -; 1. DR HAMAP; MF_00564; RNase_PH; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR027408; PNPase/RNase_PH_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR002381; RNase_PH_bac-type. DR InterPro; IPR018336; RNase_PH_CS. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55666; SSF55666; 1. DR TIGRFAMs; TIGR01966; RNasePH; 1. DR PROSITE; PS01277; RIBONUCLEASE_PH; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Reference proteome; KW Transferase; tRNA processing. FT CHAIN 1 238 Ribonuclease PH. FT /FTId=PRO_0000139897. SQ SEQUENCE 238 AA; 25789 MW; B67015EBF8FBA23F CRC64; MRPNNRENNQ PRQIKITRNY TKHAEGSVLV EFGDTKVLCT ATVEDAVPRF LKGQGQGWVT AEYGMLPRST HSRMQREAAK GKQGGRTMEI QRLIARSLRA MVDLKALGER AITLDCDVIQ ADGGTRTASI TGAAVALCDA INGLIENGTL KTNPIKGLVS AISVGIVDGQ AVCDLEYVED SAAETDMNVV MMEDGRMIEV QGTAEGEPFS HEELLTLLDL AKQGCNQIFI AQREALGL // ID RLMN_HAEIN Reviewed; 390 AA. AC P44665; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=Dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849}; GN OrderedLocusNames=HI_0365; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in CC 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 CC modification seems to play a crucial role in the proofreading step CC occurring at the peptidyl transferase center and thus would serve CC to optimize ribosomal fidelity. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in CC 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L- CC homocysteine + L-methionine + 5'-deoxyadenosine + 2- CC methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in CC tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + CC L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01849}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism CC involving intermediate methylation of a conserved cysteine CC residue. {ECO:0000255|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000255|HAMAP-Rule:MF_01849}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22023.1; -; Genomic_DNA. DR PIR; I64149; I64149. DR RefSeq; NP_438526.1; NC_000907.1. DR RefSeq; WP_005693801.1; NC_000907.1. DR ProteinModelPortal; P44665; -. DR STRING; 71421.HI0365; -. DR EnsemblBacteria; AAC22023; AAC22023; HI_0365. DR GeneID; 949466; -. DR KEGG; hin:HI0365; -. DR PATRIC; 20189275; VBIHaeInf48452_0383. DR eggNOG; ENOG4105C55; Bacteria. DR eggNOG; COG0820; LUCA. DR KO; K06941; -. DR OMA; EGSKFER; -. DR OrthoDB; EOG6DJZ2N; -. DR PhylomeDB; P44665; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR30544; PTHR30544; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron; KW Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 390 Dual-specificity RNA methyltransferase FT RlmN. FT /FTId=PRO_0000171920. FT REGION 184 185 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT REGION 238 240 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT ACT_SITE 110 110 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01849}. FT ACT_SITE 360 360 S-methylcysteine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 130 130 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 134 134 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT METAL 137 137 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 216 216 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT BINDING 317 317 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01849}. FT DISULFID 123 360 (transient). {ECO:0000255|HAMAP- FT Rule:MF_01849}. SQ SEQUENCE 390 AA; 43597 MW; 34EA75DE8DEA356E CRC64; MCNNEAKMSE LLSVQSDAPA KKINLMDLTR QQMREFFKEL GEKPFRADQL VKWIYHFGED NFDNMTNINK KLREKLKAVA EIKAPEVAVE QRSADGTIKW AMQVGEQQVE TVYIPEADRA TLCVSSQVGC ALACTFCSTA QQGFNRNLTV SEIIGQVWRA SKIIGNFGVT GVRPITNVVM MGMGEPLLNV ANVVPAMEIM LDDFAYGLSK RRVTLSTSGV VPALDNLSKM IDVALAISLH APNDELRDEI VPINKKYNIK TLIDSVNRYL NVSNANHGKV TIEYVMLDHV NDGVEHAHQL AEVLKNTPCK INLIPWNPFP EAPYAKSSNT RIDRFQKTLM EYDFTVIIRK TRGDDIDAAC GQLAGDVIDR TKRTAMKRQF GQNIGVTEVN // ID RNAAM_HAEIN Reviewed; 274 AA. AC P44176; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=5'-3' exoribonuclease {ECO:0000250|UniProtKB:P77766}; DE EC=3.1.13.- {ECO:0000250|UniProtKB:P77766}; DE AltName: Full=3',5'-nucleotide bisphosphate phosphatase {ECO:0000250|UniProtKB:P77766}; DE EC=3.1.3.97 {ECO:0000250|UniProtKB:P77766}; DE AltName: Full=RNase AM {ECO:0000250|UniProtKB:P77766}; GN OrderedLocusNames=HI_1400 {ECO:0000312|EMBL:AAC23046.1}; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Efficiently catalyzes the hydrolysis of the 3'-phosphate CC from 3',5'-bis-phosphonucleotides as well as the successive CC hydrolysis of 5'-phosphomononucleotides from the 5'-end of short CC pieces of RNA and DNA, with no specificity toward the identity of CC the nucleotide base. Is more efficient at hydrolyzing RNA CC oligonucleotides than DNA oligonucleotides. This enzyme can also CC hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency CC lower than that of the corresponding single-stranded CC oligonucleotides. {ECO:0000250|UniProtKB:P77766}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 5'- to 3'- CC direction to yield nucleoside 5'-phosphates. CC {ECO:0000250|UniProtKB:P77766}. CC -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-bisphosphate + H(2)O = CC nucleoside 5'-phosphate + phosphate. CC {ECO:0000250|UniProtKB:P77766}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P77766}; CC -!- SIMILARITY: Belongs to the PHP family. TrpH/YciV 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; L42023; AAC23046.1; -; Genomic_DNA. DR PIR; F64027; F64027. DR RefSeq; NP_439553.1; NC_000907.1. DR RefSeq; WP_005693963.1; NC_000907.1. DR ProteinModelPortal; P44176; -. DR STRING; 71421.HI1400; -. DR EnsemblBacteria; AAC23046; AAC23046; HI_1400. DR GeneID; 950717; -. DR KEGG; hin:HI1400; -. DR PATRIC; 20191499; VBIHaeInf48452_1460. DR eggNOG; ENOG4105DB7; Bacteria. DR eggNOG; COG0613; LUCA. DR KO; K07053; -. DR OMA; TRAHYAR; -. DR OrthoDB; EOG6KMB5P; -. DR PhylomeDB; P44176; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 2. PE 3: Inferred from homology; KW Complete proteome; Exonuclease; Hydrolase; Manganese; Metal-binding; KW Nuclease; Nucleotide-binding; Reference proteome. FT CHAIN 1 274 5'-3' exoribonuclease. FT /FTId=PRO_0000065639. FT METAL 8 8 Manganese 1; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 10 10 Manganese 1; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 15 15 Manganese 2. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 40 40 Manganese 2; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 65 65 Manganese 1. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 65 65 Manganese 3. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 76 76 Manganese 3; via pros nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 190 190 Manganese 3; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 247 247 Manganese 1. FT {ECO:0000250|UniProtKB:Q7NXD4}. FT METAL 249 249 Manganese 2; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q7NXD4}. SQ SEQUENCE 274 AA; 30116 MW; F7ED7B0BDFB850D3 CRC64; MTKKYDLHCH STASDGVLSP TELVHRAYAQ GVNVLALCDH DTIAGIDEAE IAAKEVGIEL ITGVEISTNW EGRGIHIVGL NFDKTHPKMT ALLQSQKALR EKRAVEIGDK LEKAGIPNAY DGAKALADGE VTRAHYARYL VQIGKVSNDG QAFKRYLGQG KSAFVKAEWA DIPTAIETIH AAGGIAIIAH PLRYNMTGKW VRKLIVDFKA WGGDGMEMAD CGQTKDQRQM LARWAKEFDL QGSVGSDFHF PCGWIELGKN LDLVDSVIPV WEKF // ID RNG_HAEIN Reviewed; 491 AA. AC P45175; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Ribonuclease G; DE Short=RNase G; DE EC=3.1.26.-; DE AltName: Full=Cytoplasmic axial filament protein; GN Name=rng; OrderedLocusNames=HI_1353; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the processing of the 5'-end of 16S rRNA. CC Could be involved in chromosome segregation and cell division. It CC may be one of the components of the cytoplasmic axial filaments CC bundles or merely regulate the formation of this structure (By CC 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, cytoskeleton. CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23000.1; -; Genomic_DNA. DR PIR; F64118; F64118. DR RefSeq; NP_439504.1; NC_000907.1. DR RefSeq; WP_010869189.1; NC_000907.1. DR ProteinModelPortal; P45175; -. DR STRING; 71421.HI1353; -. DR EnsemblBacteria; AAC23000; AAC23000; HI_1353. DR GeneID; 950270; -. DR KEGG; hin:HI1353; -. DR PATRIC; 20191391; VBIHaeInf48452_1406. DR eggNOG; ENOG4105C03; Bacteria. DR eggNOG; COG1530; LUCA. DR KO; K08301; -. DR OMA; FGVIIRT; -. DR OrthoDB; EOG6PCPTH; -. DR PhylomeDB; P45175; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; 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:0004540; F:ribonuclease activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G. DR InterPro; IPR004659; RNase_E/G. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF10150; RNase_E_G; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00757; RNaseEG; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 491 Ribonuclease G. FT /FTId=PRO_0000097384. FT DOMAIN 40 129 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT METAL 305 305 Magnesium; catalytic. {ECO:0000250}. FT METAL 348 348 Magnesium; catalytic. {ECO:0000250}. SQ SEQUENCE 491 AA; 55928 MW; 3CFD0E9ACB39FA37 CRC64; MDAVELLMNV TPNETRIALV ETGMLREVHI ERQAKRGIVG NIYKGRVTRV LPGMQSAFVD IGLEKAAFLH AADIVSHTEC VDENEQKQFK VKSISELVRE GQDIVVQVVK EPLGTKGARL TTDITLPSRH LVFMPENSHV GVSQRIESEE ERARLKALVE PFCDELGGFI IRTATEGASE EELRQDAEFL KRLWRKVLER KSKYPTKSKI YGEPALPQRI LRDFIGTNLE KIRIDSKLCF GEVKEFTDEF MPELSDKLVL YSGNQPIFDV YGVENAIQTA LDKRVNLKSG GYLIIEQTEA MTTIDINTGA FVGHRNLEET IFNTNIEATK AIAHELQLRN LGGIIIIDFI DMQTDEHRNR VLQSLCDALS KDRMKTNVNG FTQLGLVEMT RKRTRESLEH VLCDECPTCH GRGRVKTVET VCYEIMREII RVYHLFSSEQ FVVYASPAVS EYLINEESHG LLPEVEMFIG KRVKVKTEQF YNQEQFDVVV M // ID RPOB_HAEIN Reviewed; 1343 AA. AC P43738; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321}; GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; GN OrderedLocusNames=HI_0515; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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_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; L42023; AAC22173.1; -; Genomic_DNA. DR PIR; H64073; H64073. DR RefSeq; NP_438673.1; NC_000907.1. DR RefSeq; WP_005666423.1; NC_000907.1. DR ProteinModelPortal; P43738; -. DR STRING; 71421.HI0515; -. DR PRIDE; P43738; -. DR EnsemblBacteria; AAC22173; AAC22173; HI_0515. DR GeneID; 949581; -. DR KEGG; hin:HI0515; -. DR PATRIC; 20189583; VBIHaeInf48452_0534. DR eggNOG; ENOG4107QIH; Bacteria. DR eggNOG; COG0085; LUCA. DR KO; K03043; -. DR OMA; YFNPKRY; -. DR OrthoDB; EOG6M9DS6; -. DR PhylomeDB; P43738; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.150.10; -; 1. DR Gene3D; 2.40.270.10; -; 2. DR Gene3D; 2.40.50.150; -; 2. DR Gene3D; 3.90.1110.10; -; 2. DR HAMAP; MF_01321; RNApol_bact_RpoB; 1. DR InterPro; IPR010243; DNA-dir_RNA_pol_bsu. DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR PANTHER; PTHR20856; PTHR20856; 5. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 2. 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 1343 DNA-directed RNA polymerase subunit beta. FT /FTId=PRO_0000047906. SQ SEQUENCE 1343 AA; 149784 MW; 4EF99CD648686A44 CRC64; MGYSYSEKKR IRKDFGKRPQ VLNVPYLLTI QLDSFDKFIQ KDPEGQQGLE AAFRSVFPIV SNNGYTELQY VDYRLEEPEF DVRECQIRGS TYAAGLRVKL RLVSYDKESS SRAVKDIKEN EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR GSWLDFEFDP KDNLFARIDR RRKLPATIIL RALGYTTEEI LNLFFDKITF EIAGDKLLMT LVPERLRGET ASFDIEANGK VYVERGRRIT ARHIKALEKD NISQVVVPSE YILGKVASKD YVDLESGEII CPANGEISLE TLAKLAQAGY TTIETLFTND LDYGPYISET LRVDPTYDKT SALYEIYRMM RPGEPPTPES SEALFNNLFF SAERYDLSTV GRMKFNRSLA FPEGEGAGIL SNEDIIAVMR KLIDIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVKERLS LGDLDAITPQ DLINPKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR ERAGFEVRDV HNTHYGRLCP IETPEGPNIG LINSLSAFAR TNDYGFLETP YRKVVDGQVT EEIEYLSVID EANYIIAQAN SNLDENNRFT DAFVTARGER GESGLYKPED IHYMDVSTQQ VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGMEKPIA LDSGVAVVAK RGGTVQYVDA SRIVIKVNED ETIAGEAGID IYNLIKYTRS NQNTCINQIP CVNLGDPINR GEVLADGPST DLGELALGQN IRVAFMPWNG YNFEDSMLVS ERVVQQDRFT TIHIQELSCV ARDTKLGAEE ITADIPNVGE SALSKLDESG IVYVGAEVKG GDILVGKVTP KGETQLTPEE KLLRAIFGEK ASDVKDSSLR VPNGTSGTVI DVQVFTRDGV EKDKRALEIE EMQLREAKKD LTEELEILEA GLFARVRNLL ISSGADAAQL DKLDRTKWLE QTIADEEKQN QLEQLAEQYE ELRKEFEHKL EVKRKKIIKG DDLAPGVLKV VKVYLAVKRQ IQPGDKMAGR HGNKGVISKI NPVEDMPYDE NGQPVEIVLN PLGVPSRMNI GQILETHLGL AAKGIGDQIN AMLKQKQEVE KLRSYIQKAY DLLGNGSQKV DLSTFTDEEV LRLAGNLRKG LPVATPVFDG ADEAEIKELL KLGGLPTSGQ ITLYDGRTGE KFERPVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTKMYKNIV SGNQHMEPGT PESFNVIMKE IRSLGLNIEL DEE // ID RPOC_HAEIN Reviewed; 1415 AA. AC P43739; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322}; GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; GN OrderedLocusNames=HI_0514; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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_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; L42023; AAC22172.1; -; Genomic_DNA. DR PIR; G64073; G64073. DR RefSeq; NP_438672.1; NC_000907.1. DR RefSeq; WP_005693659.1; NC_000907.1. DR ProteinModelPortal; P43739; -. DR SMR; P43739; 909-943, 945-1129. DR STRING; 71421.HI0514; -. DR PRIDE; P43739; -. DR EnsemblBacteria; AAC22172; AAC22172; HI_0514. DR GeneID; 949579; -. DR KEGG; hin:HI0514; -. DR PATRIC; 20189581; VBIHaeInf48452_0533. DR eggNOG; ENOG4105D27; Bacteria. DR eggNOG; COG0086; LUCA. DR KO; K03046; -. DR OMA; YFAAYMI; -. DR OrthoDB; EOG6M9DS6; -. DR PhylomeDB; P43739; -. DR Proteomes; UP000000579; 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 HAMAP; MF_01323; RNApol_bact_RpoC1; 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; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SMART; SM00663; RPOLA_N; 1. 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 1415 DNA-directed RNA polymerase subunit FT beta'. FT /FTId=PRO_0000067747. SQ SEQUENCE 1415 AA; 157210 MW; 09FA68FACB49A40B CRC64; MKDLVKFLKA QSKTSEDFDV IKIGLASPDM IRSWSFGEVK KPETINYRTF KPERDGLFCA RIFGPVKDYE CLCGKYKRLK HRGVICEKCG VEVTQTKVRR ERMGHIELAS PVAHIWFLKS LPSRIGLLLD MPLRDIERVL YFEMYIVTEP GMTDLERGQL LTEEQYLDAE DRWQDEFEAK MGAEAIQDLL KGMDLEAECE KLREELQETN SETKRKKITK RLKLLEAFVQ SGNKPEWMVM TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLIAPD IIVRNEKRML QESVDALLDN GRRGRAITGS NRRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP YLHLHQCGLP KKMALELFRP FIYAKLESRG YATTIKAAKK MVEREDAIVW DILAEVIREH PILLNRAPTL HRLGIQAFEP ILIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLTLEAQLE ARALMMSTNN VLSPANGDPI IVPSQDVVLG LYYMTREKVN GKGEGMLLQD PREAEKAYRT GEAELHSRVK VRITEYVKNE AGEFDAKTTL TDTTIGRAIL WMIAPKGMPY SLFNQTLGKK AISKLINEAY RRLGLKEAVM FADQIMYTGF AYAARSGSSV GIDDMEIPAK KYEIISAAEE EVAEIQEQFQ SGLVTAGERY NKVIDIWAAA NERVAKAMME NLSQEEVINR EGNPEKQASF NSIFMMADSG ARGSAAQIRQ LAGMRGLMAR PDGSIIETPI TANFREGLNV LQYFISTHGA RKGLADTALK TANSGYLTRR LVDVAQDLVI VEDDCGTHEG LVMTPLIEGG DEKVPLRELV LGRVAAEDIL KPGTEEVLIP RNTLLDEKLC DVLDANSVDS VKVRSVVTCD TDFGVCAKCY GRDLARGHLI NQGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASAAAKESS VQVKNTGTVH LMNAKFVTND ESKLVLTSRN TELTITDAFG RTKEHYKVPY GAVLSKGDGQ EVTAGETIAN WDPHTMPVVS EVSGFVKFVD IIDGLTVTRQ TDELTGLSSI VVQDVGERAT AGKDLRPTIK LVDANGNDIF LPETDVLAQY FLPGKAIVSL DDGTAVKVGE PLARIPQESV GTKDITGGLP RVADLFEARK PKEPAILAEI SGIVSFGKET KGKRRLLITP AEGETYEEMI PKWRQLNVFE GEMVQRGDVI SDGAETPHDI LRLRGVRAVT EYIVNEVQDV YRLQGVKIND KHIEVIVRQM LRKAVITKAY DSEFLEGEQV EVARVKIVNR QREAEGKPPV EFERELLGIT KASLATESFI SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGFAYHQNRH KHRLVDDVVA KLSEEDEAAI ADEFVITADD ATQNLATLLN SEIED // ID RPOH_HAEIN Reviewed; 281 AA. AC P44404; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=RNA polymerase sigma factor RpoH {ECO:0000255|HAMAP-Rule:MF_00961}; DE AltName: Full=RNA polymerase sigma-32 factor {ECO:0000255|HAMAP-Rule:MF_00961}; GN Name=rpoH {ECO:0000255|HAMAP-Rule:MF_00961}; GN OrderedLocusNames=HI_0269; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 involved in regulation of CC expression of heat shock genes. {ECO:0000255|HAMAP-Rule:MF_00961}. CC -!- SUBUNIT: Interacts with the RNA polymerase core enzyme. CC {ECO:0000255|HAMAP-Rule:MF_00961}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00961}. CC -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00961}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21935.1; -; Genomic_DNA. DR PIR; H64058; H64058. DR RefSeq; NP_438438.1; NC_000907.1. DR RefSeq; WP_005694033.1; NC_000907.1. DR ProteinModelPortal; P44404; -. DR STRING; 71421.HI0269; -. DR EnsemblBacteria; AAC21935; AAC21935; HI_0269. DR GeneID; 949393; -. DR KEGG; hin:HI0269; -. DR PATRIC; 20189065; VBIHaeInf48452_0284. DR eggNOG; ENOG4105DEK; Bacteria. DR eggNOG; COG0568; LUCA. DR KO; K03089; -. DR OMA; EIHEYIV; -. DR OrthoDB; EOG6D5G0W; -. DR PhylomeDB; P44404; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0016987; F:sigma factor activity; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR GO; GO:0001123; P:transcription initiation from bacterial-type RNA polymerase promoter; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00961; Sigma70_RpoH; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR009042; RNA_pol_sigma70_r1_2. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR012759; RNA_pol_sigma_RpoH_proteobac. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00140; Sigma70_r1_2; 1. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02392; rpoH_proteo; 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; Stress response; Transcription; KW Transcription regulation. FT CHAIN 1 281 RNA polymerase sigma factor RpoH. FT /FTId=PRO_0000093960. FT DNA_BIND 250 269 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00961}. FT REGION 52 121 Sigma-70 factor domain-2. FT {ECO:0000255|HAMAP-Rule:MF_00961}. FT REGION 226 277 Sigma-70 factor domain-4. FT {ECO:0000255|HAMAP-Rule:MF_00961}. FT MOTIF 76 79 Interaction with polymerase core subunit FT RpoC. SQ SEQUENCE 281 AA; 32033 MW; 7EC9C03543DA7FD2 CRC64; MDKETQMMLV PQGSIEGYIR AANEYPMLTA EEEKELAERL YYHEDLDAAK KLILSHLRFV IHVARGYSGY GLPQADLIQE GNIGLMKAVK RFNPEVGVRL VSFAVHWIKA EIHEYVLRNW RIVKVATTKA QRKLFFNLRK TKQRLGWFNE NEVDMVANEL GVSKEDVIEM ESRMSGADVG FDLPTDDAET ETYSPALYLE DKSSNFAAEL ENENFESQAT EQLGAALQSL DARSQDIIKA RWLDDNKATL HDLAAKYNVS AERIRQLETN ALKKLKSAVN F // ID RNH2_HAEIN Reviewed; 197 AA. AC P43808; P94808; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Ribonuclease HII; DE Short=RNase HII; DE EC=3.1.26.4; GN Name=rnhB; OrderedLocusNames=HI_1059; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97. RC STRAIN=RM 7004 / Serotype B; RX PubMed=8917090; DOI=10.1016/0378-1119(96)00139-4; RA Servos S., Khan S., Maskell D.; RT "Cloning and expression of genes encoding lipid A biosynthesis from RT Haemophilus influenzae type b."; RL Gene 175:137-141(1996). CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per CC monomer in the absence of substrate. May bind a second metal ion CC after substrate binding. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22714.1; -; Genomic_DNA. DR EMBL; X87416; CAA60867.1; -; Genomic_DNA. DR PIR; D64180; D64180. DR RefSeq; NP_439217.1; NC_000907.1. DR RefSeq; WP_005693388.1; NC_000907.1. DR ProteinModelPortal; P43808; -. DR STRING; 71421.HI1059; -. DR EnsemblBacteria; AAC22714; AAC22714; HI_1059. DR GeneID; 950033; -. DR KEGG; hin:HI1059; -. DR PATRIC; 20190781; VBIHaeInf48452_1103. DR eggNOG; ENOG4108UH2; Bacteria. DR eggNOG; COG0164; LUCA. DR KO; K03470; -. DR OMA; GFASHKG; -. DR OrthoDB; EOG6BKJC8; -. DR PhylomeDB; P43808; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00052_B; RNase_HII_B; 1. DR InterPro; IPR022898; RNase_HII. DR InterPro; IPR001352; RNase_HII/HIII. DR InterPro; IPR024567; RNase_HII/HIII_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR PANTHER; PTHR10954; PTHR10954; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Manganese; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 197 Ribonuclease HII. FT /FTId=PRO_0000111578. FT METAL 15 15 Divalent metal cation. {ECO:0000250}. FT METAL 16 16 Divalent metal cation. {ECO:0000250}. FT METAL 107 107 Divalent metal cation. {ECO:0000250}. FT CONFLICT 65 65 R -> L (in Ref. 2; CAA60867). FT {ECO:0000305}. SQ SEQUENCE 197 AA; 21610 MW; 94C00762C1053F7D CRC64; MFEYPQGYKL IAGVDEVGRG PLVGAVVTAA VILDPHNPIE GLADSKKLSE KKRLALAEEI KEKARAWALG RAEADEIDEI NILQASLLAM TRAVKSLKIQ PHFVLIDGNK IPKDLAIPAQ AVVKGDSLVA EISAASILAK VARDQEMEEL DKQYPEYAFA QHKGYPTKLH LEKLAELGAL PQHRRSFAPV KKALEQF // ID RNR_HAEIN Reviewed; 782 AA. AC P44907; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. 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=HI_0861; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22520.1; -; Genomic_DNA. DR PIR; G64098; G64098. DR RefSeq; NP_439021.1; NC_000907.1. DR RefSeq; WP_010869073.1; NC_000907.1. DR ProteinModelPortal; P44907; -. DR STRING; 71421.HI0861; -. DR EnsemblBacteria; AAC22520; AAC22520; HI_0861. DR GeneID; 949873; -. DR KEGG; hin:HI0861; -. DR PATRIC; 20190377; VBIHaeInf48452_0902. DR eggNOG; ENOG4105C40; Bacteria. DR eggNOG; COG0557; LUCA. DR KO; K12573; -. DR OMA; YRVHEGP; -. DR OrthoDB; EOG6Q5NRD; -. DR PhylomeDB; P44907; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central. DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central. DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01895; RNase_R; 1. DR InterPro; IPR011129; Cold_shock_prot. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013223; RNase_B_OB_dom. DR InterPro; IPR022966; RNase_II/R_CS. DR InterPro; IPR004476; RNase_II/RNase_R. DR InterPro; IPR011805; RNase_R. DR InterPro; IPR013668; RNase_R_HTH_12. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF08461; HTH_12; 1. DR Pfam; PF08206; OB_RNB; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00357; CSP; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 4. DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1. DR TIGRFAMs; TIGR02063; RNase_R; 1. DR PROSITE; PS01175; RIBONUCLEASE_II; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Nuclease; KW Reference proteome; RNA-binding. FT CHAIN 1 782 Ribonuclease R. FT /FTId=PRO_0000166403. FT DOMAIN 651 732 S1 motif. {ECO:0000255|HAMAP- FT Rule:MF_01895}. SQ SEQUENCE 782 AA; 89848 MW; 131E6AF65AF2537E CRC64; MTKKRKNLIN QDPHYKRELE KYGNPIPSRE FILTVIRDNN APMNRDEILT ALSIRNEDQI EAMRRRLRAM ENDGQLVFTK RKRYALPEKL DLFKGTVIGH REGFGFLQVD GKKDDLFIPN HQMQRVMHGD FVLAQPAGLD RRGRREVRIV RVLESRKKQI VGRFFLENGF GYVVPDDSRI GRDILVPNEH RNGARMGQVV VVELQERSAS FNQPIGVITE ILGDNMAKGM EVEIALRNHD ILHKFPSAVE KYVKKFTEEV SEEAKKGRVD LRNLPLVTID GEDARDFDDA VYCEKHGKGW KLWVAIADVS YYVRLRSTLD VEAHNRGNSV YFPNRVVPML PEILSNGLCS LNPQVDRLCM VCEMQISAKG KLTDYRFYEA VMNSHARLTY TKVAKMLEGD EELRTRYSTL VPHLEELYKL YQALLSARHQ RGAIDFETIE TKFIFNAMGR IERIEPVVRN DAXKIIEECM XLANIAAANF MEKHKEPALY RIHATPSEEK LTSFRTFLSE FGLTLEGGLK PTTKDYAALL EKVKERPDHE LIQTMLLRSL SQAVYHADNI GHFGLALEEY AHFTSPIRRY PDLTLHRGIK YLLAKEQGAK RKTTDTGGYH YSFDEMDLLG NHCSMTERRA DDATREVADW LKCEYMQDHV GGEFSGVISS VTGFGLFVRL DDLFIDGLVH ISTLENDYYQ FDAAKQRLIG ENSGMQYRLG DKVRIKVEAV HLENKMVDFS LIGSERKPRR AGKTAKEKAK KVFKELPSKA SKKRKSAVKK KDVSKKTSRK RK // ID RODA_HAEIN Reviewed; 371 AA. AC P44468; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Rod shape-determining protein RodA; GN Name=mrdB; Synonyms=rodA; OrderedLocusNames=HI_0031; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for the maintenance of the rod cell shape. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SEDS family. RodA 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; L42023; AAC21709.1; -; Genomic_DNA. DR PIR; B64044; B64044. DR RefSeq; NP_438204.1; NC_000907.1. DR RefSeq; WP_005649852.1; NC_000907.1. DR STRING; 71421.HI0031; -. DR EnsemblBacteria; AAC21709; AAC21709; HI_0031. DR GeneID; 950927; -. DR KEGG; hin:HI0031; -. DR PATRIC; 20188513; VBIHaeInf48452_0031. DR eggNOG; ENOG4105CNI; Bacteria. DR eggNOG; COG0772; LUCA. DR KO; K05837; -. DR OMA; FMSYGRT; -. DR OrthoDB; EOG68M4JQ; -. DR PhylomeDB; P44468; -. DR Proteomes; UP000000579; 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:0007049; P:cell cycle; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:InterPro. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS. DR InterPro; IPR001182; Cell_cycle_FtsW/RodA. DR InterPro; IPR011923; RodA_shape. DR PANTHER; PTHR30474; PTHR30474; 1. DR PANTHER; PTHR30474:SF1; PTHR30474:SF1; 1. DR Pfam; PF01098; FTSW_RODA_SPOVE; 1. DR TIGRFAMs; TIGR02210; rodA_shape; 1. DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Cell shape; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 371 Rod shape-determining protein RodA. FT /FTId=PRO_0000062717. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 313 333 Helical. {ECO:0000255}. FT TRANSMEM 337 357 Helical. {ECO:0000255}. SQ SEQUENCE 371 AA; 41164 MW; 85D5DDDE60B87E30 CRC64; MEDKIPFWLR VWQRLHIDFW LFIGLLAITA YGMLVLYSAS GASETMFNSR IIQVLLGFIV MLLMAQFPPR FYQRIAPYLY LIGFVLLILV DVIGTTSKGA QRWLDLGFIR FQPSEIVKLA VPLMVAVYLG NRPLPPKLSE TFIAIAMILL PTLLVAIQPD LGTSILVSAS GLFVVFLAGM SWWLILAAVI GLAGFIPIMW LYLMHDYQRT RVLTLLDPEK DPLGAGYHIL QSKIAIGSGG LSGKGWMQGT QSQLEFLPEP HTDFIFAVMG EEHGMIGFLI LMAIYLFIIV RGLMIAVNAQ TSFGRILAGA TTLIFFVYVF VNIGMVSGIL PVVGVPLPLF SYGGTSYVAI MASFGLLMSI HTHKSQFMKR S // ID RPE_HAEIN Reviewed; 224 AA. AC P44756; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=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; Synonyms=dod; OrderedLocusNames=HI_0566; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC22224.1; 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; L42023; AAC22224.1; ALT_INIT; Genomic_DNA. DR PIR; I64077; I64077. DR RefSeq; NP_438723.2; NC_000907.1. DR RefSeq; WP_010869007.1; NC_000907.1. DR ProteinModelPortal; P44756; -. DR STRING; 71421.HI0566; -. DR EnsemblBacteria; AAC22224; AAC22224; HI_0566. DR GeneID; 949612; -. DR KEGG; hin:HI0566; -. DR PATRIC; 20189687; VBIHaeInf48452_0586. DR eggNOG; ENOG4105DJV; Bacteria. DR eggNOG; COG0036; LUCA. DR KO; K01783; -. DR OMA; GANYITF; -. DR OrthoDB; EOG67HK17; -. DR PhylomeDB; P44756; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IBA:GO_Central. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR026019; Ribul_P_3_epim. DR InterPro; IPR000056; Ribul_P_3_epim-like. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR11749; PTHR11749; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01163; rpe; 1. DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1. DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cobalt; Complete proteome; Iron; Isomerase; KW Manganese; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 224 Ribulose-phosphate 3-epimerase. FT /FTId=PRO_0000171571. FT REGION 144 147 Substrate binding. {ECO:0000250}. FT REGION 199 200 Substrate binding. {ECO:0000250}. FT ACT_SITE 36 36 Proton acceptor. {ECO:0000250}. FT ACT_SITE 177 177 Proton donor. {ECO:0000250}. FT METAL 34 34 Divalent metal cation. {ECO:0000250}. FT METAL 36 36 Divalent metal cation. {ECO:0000250}. FT METAL 68 68 Divalent metal cation. {ECO:0000250}. FT METAL 177 177 Divalent metal cation. {ECO:0000250}. FT BINDING 9 9 Substrate. {ECO:0000250}. FT BINDING 68 68 Substrate. {ECO:0000250}. FT BINDING 179 179 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 224 AA; 24276 MW; FC62AD17398341F3 CRC64; MKPYLIAPSI LSADLARLGD DVQNVLNAGA DVIHFDVMDN HYVPNLTFGP AVCQALRDYG ITAPIDVHLM VKPVDRIIPD FAKAGANYIT FHPESSEHID RSLQLIRDCG CKSGLVFNPA MPLSYLDYVL DKVDVVLLMS VNPGFGGQSF IPATLKKLQQ ARKIIDESGY DIRLEVDGGV KVDNIAEIAA AGADMFVAGS AIFGKPDYKQ VIDQIRTQLA SVSA // ID RPOZ_HAEIN Reviewed; 88 AA. AC P43740; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=DNA-directed RNA polymerase subunit omega; DE Short=RNAP omega subunit; DE EC=2.7.7.6; DE AltName: Full=RNA polymerase omega subunit; DE AltName: Full=Transcriptase subunit omega; GN Name=rpoZ; OrderedLocusNames=HI_1742; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- CC terminal regions of the beta' subunit thereby facilitating its CC interaction with the beta and alpha subunits (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 CC beta' and 1 omega subunit. When a sigma factor is associated with CC the core the holoenzyme is formed, which can initiate CC transcription (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23389.1; -; Genomic_DNA. DR PIR; G64139; G64139. DR RefSeq; NP_439886.1; NC_000907.1. DR RefSeq; WP_005693900.1; NC_000907.1. DR STRING; 71421.HI1742; -. DR EnsemblBacteria; AAC23389; AAC23389; HI_1742. DR GeneID; 950552; -. DR KEGG; hin:HI1742; -. DR PATRIC; 20192255; VBIHaeInf48452_1825. DR eggNOG; ENOG4105VFG; Bacteria. DR eggNOG; COG1758; LUCA. DR KO; K03060; -. DR OMA; LINGQIM; -. DR OrthoDB; EOG6Q5NV5; -. DR PhylomeDB; P43740; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.940.10; -; 1. DR HAMAP; MF_00366; RNApol_bact_RpoZ; 1. DR InterPro; IPR003716; DNA-dir_RNA_pol_omega. DR InterPro; IPR006110; Pol_omega/K/RPB6. DR InterPro; IPR012293; RNAP_RPB6_omega. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR SMART; SM01409; RNA_pol_Rpb6; 1. DR SUPFAM; SSF63562; SSF63562; 1. DR TIGRFAMs; TIGR00690; rpoZ; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 88 DNA-directed RNA polymerase subunit FT omega. FT /FTId=PRO_0000128941. SQ SEQUENCE 88 AA; 9860 MW; 46E5B7377A2F7C77 CRC64; MARVTVQDAV EKIGNRFDLI LTAARRARQL QLNQSAPLVP EDNDKPTVIA LREIEKGLIN QDIMDAQEFQ KMAKVQETEE AAVALITE // ID RRAB_HAEIN Reviewed; 153 AA. AC P44831; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Regulator of ribonuclease activity B {ECO:0000255|HAMAP-Rule:MF_01888}; GN Name=rraB {ECO:0000255|HAMAP-Rule:MF_01888}; GN OrderedLocusNames=HI_0700; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Globally modulates RNA abundance by binding to RNase E CC (Rne) and regulating its endonucleolytic activity. Can modulate CC Rne action in a substrate-dependent manner by altering the CC composition of the degradosome. {ECO:0000255|HAMAP-Rule:MF_01888}. CC -!- SUBUNIT: Interacts with the C-terminal region of Rne. CC {ECO:0000255|HAMAP-Rule:MF_01888}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01888}. CC -!- SIMILARITY: Belongs to the RraB family. {ECO:0000255|HAMAP- CC Rule:MF_01888}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22359.1; -; Genomic_DNA. DR PIR; T09405; T09405. DR RefSeq; NP_438859.1; NC_000907.1. DR RefSeq; WP_010869036.1; NC_000907.1. DR ProteinModelPortal; P44831; -. DR SMR; P44831; 3-116. DR STRING; 71421.HI0700; -. DR EnsemblBacteria; AAC22359; AAC22359; HI_0700. DR GeneID; 949725; -. DR KEGG; hin:HI0700; -. DR PATRIC; 20190019; VBIHaeInf48452_0731. DR eggNOG; ENOG4105KQT; Bacteria. DR eggNOG; COG3076; LUCA. DR KO; K09893; -. DR OMA; FCFDAIA; -. DR OrthoDB; EOG66TG7Q; -. DR PhylomeDB; P44831; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.970; -; 1. DR HAMAP; MF_01888; RraB; 1. DR InterPro; IPR016716; RraB. DR InterPro; IPR009671; RraB_dom. DR Pfam; PF06877; RraB; 1. DR PIRSF; PIRSF018193; UCP018193; 1. DR SUPFAM; SSF89946; SSF89946; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 153 Regulator of ribonuclease activity B. FT /FTId=PRO_0000169764. FT COMPBIAS 124 149 Asp/Glu-rich (acidic). SQ SEQUENCE 153 AA; 17592 MW; E327B2EFCA148354 CRC64; MSKLAELQAE TREIIEDLLN DGSEPNALYI IEHHIAHHDF DLLEKIAVDA FKAGYEVSEA EEFKDDDGKP IFCFDIISEV ELKAEIIDAQ QKEILPLLEK HNGIYDGWGT YFEDPNADDD EYGDDGEFLD DEDEYGDDGE FFDDEDEEEP RVH // ID RRAA_HAEIN Reviewed; 162 AA. AC P44738; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 100. DE RecName: Full=Regulator of ribonuclease activity A {ECO:0000255|HAMAP-Rule:MF_00471}; GN Name=rraA {ECO:0000255|HAMAP-Rule:MF_00471}; GN OrderedLocusNames=HI_0508; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Globally modulates RNA abundance by binding to RNase E CC (Rne) and regulating its endonucleolytic activity. Can modulate CC Rne action in a substrate-dependent manner by altering the CC composition of the degradosome. Modulates RNA-binding and helicase CC activities of the degradosome. {ECO:0000255|HAMAP-Rule:MF_00471}. CC -!- SUBUNIT: Homotrimer. Binds to both RNA-binding sites in the C- CC terminal region of Rne and to RhlB. {ECO:0000255|HAMAP- CC Rule:MF_00471}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00471}. CC -!- SIMILARITY: Belongs to the RraA family. {ECO:0000255|HAMAP- CC Rule:MF_00471}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22166.1; -; Genomic_DNA. DR PIR; G64153; G64153. DR RefSeq; NP_438666.1; NC_000907.1. DR RefSeq; WP_005669389.1; NC_000907.1. DR ProteinModelPortal; P44738; -. DR SMR; P44738; 4-161. DR STRING; 71421.HI0508; -. DR PRIDE; P44738; -. DR EnsemblBacteria; AAC22166; AAC22166; HI_0508. DR GeneID; 949667; -. DR KEGG; hin:HI0508; -. DR PATRIC; 20189569; VBIHaeInf48452_0527. DR eggNOG; ENOG4108YYX; Bacteria. DR eggNOG; COG0684; LUCA. DR KO; K02553; -. DR OMA; LQICRQS; -. DR OrthoDB; EOG6Z3KKK; -. DR PhylomeDB; P44738; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.30.40; -; 1. DR HAMAP; MF_00471; RraA; 1. DR InterPro; IPR010203; RraA. DR InterPro; IPR005493; RraA/RraA-like. DR InterPro; IPR014339; RraA_gpbac. DR Pfam; PF03737; Methyltransf_6; 1. DR SUPFAM; SSF89562; SSF89562; 1. DR TIGRFAMs; TIGR01935; NOT-MenG; 1. DR TIGRFAMs; TIGR02998; RraA_entero; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 162 Regulator of ribonuclease activity A. FT /FTId=PRO_0000209616. SQ SEQUENCE 162 AA; 17388 MW; B86E0E9BD2D8796A CRC64; MFIDTSELCD LYAEQVDVVE PIFSSFGGVS NFYGKVTTVK CFESNGLIAE VLEENGEGRV LVIDGGGAVR RGLIDAELAQ LAVDNGWEGI IVYGAVRQIQ QLENLDIGIH ALAPIPVSAD ESSAGESDIP VNFGGVTFFP EDYIYADLTG IILSQEPLDL ED // ID RPIA_HAEIN Reviewed; 219 AA. AC P44725; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170}; DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170}; GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; GN OrderedLocusNames=HI_0464; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND RP SUBUNIT. RA Das K., Xiao R., Acton T., Montelione G., Arnold E.; RT "D-ribose-5-phosphate isomerase, IR21."; RL Submitted (JUN-2002) to the PDB data bank. CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5- CC phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00170}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative CC stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170, CC ECO:0000269|Ref.3}. CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22123.1; -; Genomic_DNA. DR PIR; B64153; B64153. DR RefSeq; NP_438625.1; NC_000907.1. DR RefSeq; WP_005693699.1; NC_000907.1. DR PDB; 1M0S; X-ray; 1.90 A; A/B=1-219. DR PDBsum; 1M0S; -. DR ProteinModelPortal; P44725; -. DR SMR; P44725; 1-219. DR STRING; 71421.HI0464; -. DR PRIDE; P44725; -. DR EnsemblBacteria; AAC22123; AAC22123; HI_0464. DR GeneID; 949550; -. DR KEGG; hin:HI0464; -. DR PATRIC; 20189483; VBIHaeInf48452_0484. DR eggNOG; ENOG4105E66; Bacteria. DR eggNOG; COG0120; LUCA. DR KO; K01807; -. DR OMA; GACHVQE; -. DR OrthoDB; EOG67MF61; -. DR PhylomeDB; P44725; -. DR UniPathway; UPA00115; UER00412. DR EvolutionaryTrace; P44725; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00170; Rib_5P_isom_A; 1. DR InterPro; IPR004788; Ribose5P_isomerase_typA. DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr. DR PANTHER; PTHR11934; PTHR11934; 1. DR Pfam; PF06026; Rib_5-P_isom_A; 1. DR TIGRFAMs; TIGR00021; rpiA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 219 Ribose-5-phosphate isomerase A. FT /FTId=PRO_0000158423. FT REGION 28 31 Substrate binding. FT REGION 81 84 Substrate binding. {ECO:0000305}. FT REGION 94 97 Substrate binding. FT ACT_SITE 103 103 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT BINDING 121 121 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT HELIX 3 14 {ECO:0000244|PDB:1M0S}. FT HELIX 15 17 {ECO:0000244|PDB:1M0S}. FT STRAND 22 26 {ECO:0000244|PDB:1M0S}. FT HELIX 30 40 {ECO:0000244|PDB:1M0S}. FT HELIX 41 45 {ECO:0000244|PDB:1M0S}. FT STRAND 48 53 {ECO:0000244|PDB:1M0S}. FT HELIX 54 62 {ECO:0000244|PDB:1M0S}. FT HELIX 70 72 {ECO:0000244|PDB:1M0S}. FT STRAND 76 81 {ECO:0000244|PDB:1M0S}. FT STRAND 84 86 {ECO:0000244|PDB:1M0S}. FT HELIX 100 109 {ECO:0000244|PDB:1M0S}. FT STRAND 110 118 {ECO:0000244|PDB:1M0S}. FT HELIX 119 121 {ECO:0000244|PDB:1M0S}. FT STRAND 128 130 {ECO:0000244|PDB:1M0S}. FT STRAND 132 136 {ECO:0000244|PDB:1M0S}. FT HELIX 138 140 {ECO:0000244|PDB:1M0S}. FT HELIX 141 150 {ECO:0000244|PDB:1M0S}. FT STRAND 154 157 {ECO:0000244|PDB:1M0S}. FT STRAND 168 174 {ECO:0000244|PDB:1M0S}. FT HELIX 180 188 {ECO:0000244|PDB:1M0S}. FT STRAND 193 199 {ECO:0000244|PDB:1M0S}. FT STRAND 205 211 {ECO:0000244|PDB:1M0S}. FT STRAND 214 218 {ECO:0000244|PDB:1M0S}. SQ SEQUENCE 219 AA; 23094 MW; BB8ABD085BADA3C1 CRC64; MNQLEMKKLA AQAALQYVKA DTIVGVGSGS TVNCFIEALG TIKDKIQGAV AASKESEELL RKQGIEVFNA NDVSSLDIYV DGADEINPQK MMIKGGGAAL TREKIVAALA KKFICIVDSS KQVDVLGSTF PLPVEVIPMA RSQVGRKLAA LGGSPEYREG VVTDNGNVIL DVHNFSILNP VEIEKELNNV AGVVTNGIFA LRGADVVIVG TPEGAKVID // ID RPOA_HAEIN Reviewed; 328 AA. AC P43737; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 112. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; GN OrderedLocusNames=HI_0802; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22461.1; -; Genomic_DNA. DR PIR; B64095; B64095. DR RefSeq; NP_438962.1; NC_000907.1. DR RefSeq; WP_010869058.1; NC_000907.1. DR ProteinModelPortal; P43737; -. DR SMR; P43737; 1-234. DR STRING; 71421.HI0802; -. DR PRIDE; P43737; -. DR EnsemblBacteria; AAC22461; AAC22461; HI_0802. DR GeneID; 949818; -. DR KEGG; hin:HI0802; -. DR PATRIC; 20190257; VBIHaeInf48452_0842. DR eggNOG; ENOG4105CTF; Bacteria. DR eggNOG; COG0202; LUCA. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR PhylomeDB; P43737; -. DR Proteomes; UP000000579; 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_0000175314. FT REGION 1 234 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. FT REGION 248 328 Alpha C-terminal domain (alpha-CTD). FT {ECO:0000255|HAMAP-Rule:MF_00059}. SQ SEQUENCE 328 AA; 36414 MW; 2D2721A4248E999B CRC64; MQGSVTEFLK PRLVDIEQIS STHAKVILEP LERGFGHTLG NALRRILLSS MPGCAVTEVE IDGVLHEYSS KEGVQEDILE VLLNLKGLAV KVQNKDDVIL TLNKSGIGPV VAADITYDGD VEIVNPDHVI CHLTDENASI SMRIRVQRGR GYVPASSRTH TQEERPIGRL LVDACYSPVE RIAYNVEAAR VEQRTDLDKL VIELETNGAL EPEEAIRRAA TILAEQLDAF VDLRDVRQPE IKEEKPEFXP ILLRPVDDLE LTVRSANCLK AETIHYIGDL VQRTEVELLK TPNLGKKSLT EIKDVLASRG LSLGMRLENW PPASIAED // ID RPOD_HAEIN Reviewed; 629 AA. AC P43766; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=RNA polymerase sigma factor RpoD {ECO:0000255|HAMAP-Rule:MF_00963}; DE AltName: Full=Sigma-70 {ECO:0000255|HAMAP-Rule:MF_00963}; GN Name=rpoD {ECO:0000255|HAMAP-Rule:MF_00963}; GN OrderedLocusNames=HI_0533; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22190.1; -; Genomic_DNA. DR PIR; B64075; B64075. DR RefSeq; NP_438691.1; NC_000907.1. DR RefSeq; WP_005694135.1; NC_000907.1. DR ProteinModelPortal; P43766; -. DR SMR; P43766; 122-628. DR STRING; 71421.HI0533; -. DR PRIDE; P43766; -. DR EnsemblBacteria; AAC22190; AAC22190; HI_0533. DR GeneID; 949596; -. DR KEGG; hin:HI0533; -. DR PATRIC; 20189619; VBIHaeInf48452_0552. DR eggNOG; ENOG4105DG1; Bacteria. DR eggNOG; COG0568; LUCA. DR KO; K03086; -. DR OMA; RDAKKEM; -. DR OrthoDB; EOG6XHC70; -. DR PhylomeDB; P43766; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0001123; P:transcription initiation from bacterial-type RNA polymerase promoter; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 2. DR HAMAP; MF_00963; Sigma70_RpoD_SigA; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000943; RNA_pol_sigma70. DR InterPro; IPR009042; RNA_pol_sigma70_r1_2. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR007624; RNA_pol_sigma70_r3. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR007631; RNA_pol_sigma_70_non-ess. DR InterPro; IPR007127; RNA_pol_sigma_70_r1_1. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR012760; RNA_pol_sigma_RpoD_C. DR InterPro; IPR028630; Sigma70_RpoD. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04546; Sigma70_ner; 1. DR Pfam; PF03979; Sigma70_r1_1; 1. DR Pfam; PF00140; Sigma70_r1_2; 1. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF04539; Sigma70_r3; 1. DR Pfam; PF04545; Sigma70_r4; 1. DR PRINTS; PR00046; SIGMA70FCT. DR SUPFAM; SSF88659; SSF88659; 2. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02393; RpoD_Cterm; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS00715; SIGMA70_1; 1. DR PROSITE; PS00716; SIGMA70_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Sigma factor; Transcription; Transcription regulation. FT CHAIN 1 629 RNA polymerase sigma factor RpoD. FT /FTId=PRO_0000093889. FT DNA_BIND 589 608 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00963}. FT REGION 395 465 Sigma-70 factor domain-2. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 474 550 Sigma-70 factor domain-3. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT REGION 563 616 Sigma-70 factor domain-4. FT {ECO:0000255|HAMAP-Rule:MF_00963}. FT MOTIF 419 422 Interaction with polymerase core subunit FT RpoC. SQ SEQUENCE 629 AA; 72085 MW; BCC84EB8CBFB9CF5 CRC64; MEKNQQSTAE QYSEQIEQLM ELGRTQGYLT FAEINDLLPE DAIDPEYYDK LLQTLQNDAG IPVLDEAPES DDMMLSDTIP DEDAVEEATQ ILSNVESEIG RTTDPVRMYM REMGTVDLLT REDEISIAKR IEGGIDEVQT SISAYPEALN GLLKNYDDVE KGNFRLTDLI TGFVDPNAEI EEHNGLDEDF SDEDDEEESS NADVEDNEDE EDNESESTSD SSDSDNSIDP EVAREKFQQL REQHSKTLAV IEKHGRSGKR AQDQIALLGE IFKQFRLVPK QFDLLVLSMK EMMKRVRYQE RQLQKILVDI AGMPKDDFEK IITTNGSNSE WVAKALKSSK PWAKRLIKYE DRIYEALNNL AITEENTKLT ITQMRDICDA VARGEQKARR AKKEMVEANL RLVISIAKKY TNRGLQFLDL IQEGNIGLMK AVDKFEYRRG YKFSTYATWW IRQAITRSIA DQARTIRIPV HMIETINKLN RISRQLLQEM GREATPEELA ERMGMPEDKI RKVLKIAKEP ISMETPIGDD DDSHLGDFIE DSTLELPLDS ATAQSLKVAT HEVLEGLTPR EAKVLRMRFG IDMNTDHTLE EVGKQFDVTR ERIRQIEAKA LRKLRHPSRS ETLRSFLDE // ID RPPH_HAEIN Reviewed; 196 AA. AC Q57045; O05036; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 17-FEB-2016, entry version 94. DE RecName: Full=RNA pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00298}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00298}; DE AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000255|HAMAP-Rule:MF_00298}; GN Name=rppH {ECO:0000255|HAMAP-Rule:MF_00298}; GN Synonyms=nudH {ECO:0000255|HAMAP-Rule:MF_00298}; GN OrderedLocusNames=HI_0901; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Accelerates the degradation of transcripts by removing CC pyrophosphate from the 5'-end of triphosphorylated RNA, leading to CC a more labile monophosphorylated state that can stimulate CC subsequent ribonuclease cleavage. {ECO:0000255|HAMAP- CC Rule:MF_00298}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00298}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00298}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. {ECO:0000255|HAMAP- CC Rule:MF_00298}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22561.1; -; Genomic_DNA. DR PIR; E64101; E64101. DR RefSeq; NP_439062.1; NC_000907.1. DR RefSeq; WP_005693252.1; NC_000907.1. DR ProteinModelPortal; Q57045; -. DR STRING; 71421.HI0901; -. DR EnsemblBacteria; AAC22561; AAC22561; HI_0901. DR GeneID; 950618; -. DR KEGG; hin:HI0901; -. DR PATRIC; 20190459; VBIHaeInf48452_0943. DR eggNOG; ENOG4105EJF; Bacteria. DR eggNOG; COG0494; LUCA. DR KO; K08311; -. DR OMA; ERNEVFW; -. DR OrthoDB; EOG6Q2SKR; -. DR PhylomeDB; Q57045; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034353; F:RNA pyrophosphohydrolase activity; IBA:GO_Central. DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central. DR Gene3D; 3.90.79.10; -; 1. DR HAMAP; MF_00298; Nudix_RppH; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR022927; RppH. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 196 RNA pyrophosphohydrolase. FT /FTId=PRO_0000057009. FT DOMAIN 6 149 Nudix hydrolase. {ECO:0000255|HAMAP- FT Rule:MF_00298}. FT MOTIF 38 59 Nudix box. SQ SEQUENCE 196 AA; 23461 MW; B1E7E375AC0701F2 CRC64; MIDFDGYRPN VGIVICNRKG QVLWAKRCGQ NSWQFPQGGI NDNESAEQAM YRELHEEVGL QPKDVRLLYV SKHWLRYKLP KRLLRYDSKP MCIGQKQRWF LLQLVSDEKN INMQTTKSPE FDGWRWVSFW YPVRQVVSFK RDVYRKVMKE FASILFTDNP LIFSASREAN SLHYSANKKY SQTKYTKRHF YKSRGQ // ID RS11_HAEIN Reviewed; 129 AA. AC P44379; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 93. 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=HI_0800; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22459.1; -; Genomic_DNA. DR PIR; I64094; I64094. DR RefSeq; NP_438960.1; NC_000907.1. DR RefSeq; WP_010869057.1; NC_000907.1. DR ProteinModelPortal; P44379; -. DR SMR; P44379; 13-129. DR STRING; 71421.HI0800; -. DR PRIDE; P44379; -. DR EnsemblBacteria; AAC22459; AAC22459; HI_0800. DR GeneID; 949749; -. DR KEGG; hin:HI0800; -. DR PATRIC; 20190253; VBIHaeInf48452_0840. DR eggNOG; ENOG4108UHH; Bacteria. DR eggNOG; COG0100; LUCA. DR KO; K02948; -. DR OMA; NTPYASQ; -. DR OrthoDB; EOG6ZSPF3; -. DR PhylomeDB; P44379; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.420.80; -; 1. DR HAMAP; MF_01310; Ribosomal_S11; 1. DR InterPro; IPR001971; Ribosomal_S11. DR InterPro; IPR019981; Ribosomal_S11_bac-type. DR InterPro; IPR018102; Ribosomal_S11_CS. DR PANTHER; PTHR11759; PTHR11759; 1. DR Pfam; PF00411; Ribosomal_S11; 1. DR PIRSF; PIRSF002131; Ribosomal_S11; 1. DR TIGRFAMs; TIGR03632; uS11_bact; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 129 30S ribosomal protein S11. FT /FTId=PRO_0000123155. SQ SEQUENCE 129 AA; 13984 MW; F5B8B696748D0C80 CRC64; MAKTPVRARK RVKKQVVDGV RHIHASFNNT IVTITDRQGN ALAWATAGGS GFRGSRKSTP FAAQVAAERC AEIVKEFGLK NLEVMVKGPG PGRESTIRAL NAAGFRITNI TDVTPIPHNG CRPPKKRRV // ID RPOE_HAEIN Reviewed; 189 AA. AC P44790; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=ECF RNA polymerase sigma-E factor; DE AltName: Full=RNA polymerase sigma-E factor; DE AltName: Full=Sigma-24; GN Name=rpoE; OrderedLocusNames=HI_0628; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Sigma factors are initiation factors that promote the CC attachment of RNA polymerase (RNAP) to specific initiation sites CC and are then released. Extracytoplasmic function (ECF) sigma-E CC controls the envelope stress response, responding to periplasmic CC protein stress, increased levels of periplasmic lipopolysaccharide CC (LPS) as well as heat shock and oxidative stress; it controls CC protein processing in the extracytoplasmic compartment (By CC similarity). {ECO:0000250}. CC -!- ENZYME REGULATION: ECF sigma-E is held in an inactive form by its CC cognate anti-sigma factor (RseA) until released by regulated CC intramembrane proteolysis (RIP). RIP occurs when an CC extracytoplasmic signal (periplasmic stress and excess LPS) CC triggers a concerted proteolytic cascade to transmit information CC and elicit cellular responses. The anti-sigma factor RseA is an CC inner membrane protein, binding sigma-E in the cytoplasm and RseB CC in the periplasm. RseA is first cut extracytoplasmically (site-1 CC protease, S1P, by DegS), then within the membrane itself (site-2 CC protease, S2P, by RseP), while cytoplasmic proteases CC (predominantly ClpX-ClpP) finish degrading the regulatory protein, CC liberating sigma-E. Degradation of RseA requires 2 signals to CC activate DegS; an outer membrane protein (OMP) signal activates CC DegS, while an LPS signal causes release of RseB from RseA, CC freeing RseA to be cleaved (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts transiently with the RNAP catalytic core formed CC by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega CC subunit) to form the RNAP holoenzyme that can initiate CC transcription. Interacts 1:1 with anti-sigma-E factor RseA which CC prevents binding to RNAP catalytic core (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates CC with the inner membrane via RseA. {ECO:0000250}. CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific CC interaction with the -10 element in promoter DNA, and plays an CC important role in melting the double-stranded DNA and the CC formation of the transcription bubble. The sigma-70 factor domain- CC 2 mediates interaction with the RNA polymerase subunits RpoB and CC RpoC (By similarity). {ECO:0000250}. CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix CC (H-T-H) motif that mediates interaction with the -35 element in CC promoter DNA. The domain also mediates interaction with the RNA CC polymerase subunit RpoA. Interactions between sigma-70 factor CC domain-4 and anti-sigma factors prevents interaction of sigma CC factors with the RNA polymerase catalytic core (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF 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; L42023; AAC22288.1; -; Genomic_DNA. DR PIR; F64082; F64082. DR RefSeq; NP_438788.1; NC_000907.1. DR RefSeq; WP_005658683.1; NC_000907.1. DR ProteinModelPortal; P44790; -. DR SMR; P44790; 1-187. DR STRING; 71421.HI0628; -. DR EnsemblBacteria; AAC22288; AAC22288; HI_0628. DR GeneID; 950801; -. DR KEGG; hin:HI0628; -. DR PATRIC; 20189851; VBIHaeInf48452_0654. DR eggNOG; ENOG4105EMN; Bacteria. DR eggNOG; COG1595; LUCA. DR KO; K03088; -. DR OMA; DAENYES; -. DR OrthoDB; EOG6ZD6DW; -. DR PhylomeDB; P44790; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2. DR InterPro; IPR014286; RNA_pol_sigma70_RpoE. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF08281; Sigma70_r4_2; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02939; RpoE_Sigma70; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS01063; SIGMA70_ECF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Sigma factor; Stress response; Transcription; KW Transcription regulation. FT CHAIN 1 189 ECF RNA polymerase sigma-E factor. FT /FTId=PRO_0000094003. FT DNA_BIND 156 175 H-T-H motif. {ECO:0000250}. FT REGION 1 153 Binds RNAP core. {ECO:0000250}. FT REGION 25 92 Sigma-70 factor domain-2. {ECO:0000250}. FT REGION 129 180 Sigma-70 factor domain-4. {ECO:0000250}. FT MOTIF 48 61 Polymerase core binding. {ECO:0000250}. SQ SEQUENCE 189 AA; 21792 MW; C47C224D73C52B43 CRC64; MAEQLTDQAL VERVQQGDKK AFNLLVSRYQ NKVAGLLTRY VSRNDIPDVV QESFIKAYRS IESFRGESAF YTWLYRIAVN TAKNYLTAQG RRPPNEDILA EDAENYDVGT HLRDVDTPEN EMLSSELERI VFDTIHNLPE DLKTAITLRE LEGLSYEDIA EIMDCPVGTV RSRIFRAREM IENKIQPLM // ID RS10_HAEIN Reviewed; 103 AA. AC P67901; O68928; P44378; Q9CL31; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-MAY-2016, entry version 67. 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=HI_0776; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC22435.1; 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; L42023; AAC22435.1; ALT_INIT; Genomic_DNA. DR PIR; D64092; D64092. DR RefSeq; NP_438935.2; NC_000907.1. DR RefSeq; WP_001181005.1; NC_000907.1. DR ProteinModelPortal; P67901; -. DR SMR; P67901; 5-102. DR STRING; 71421.HI0776; -. DR PRIDE; P67901; -. DR EnsemblBacteria; AAC22435; AAC22435; HI_0776. DR GeneID; 950681; -. DR GeneID; 9735586; -. DR KEGG; hin:HI0776; -. DR PATRIC; 20190203; VBIHaeInf48452_0815. DR eggNOG; ENOG4108Z10; Bacteria. DR eggNOG; COG0051; LUCA. DR KO; K02946; -. DR OMA; KIRRYTV; -. DR OrthoDB; EOG6VXFHB; -. DR PhylomeDB; P67901; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.600; -; 1. DR HAMAP; MF_00508; Ribosomal_S10; 1. DR InterPro; IPR001848; Ribosomal_S10. DR InterPro; IPR018268; Ribosomal_S10_CS. DR InterPro; IPR027486; Ribosomal_S10_dom. DR PANTHER; PTHR11700; PTHR11700; 1. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR SMART; SM01403; Ribosomal_S10; 1. DR SUPFAM; SSF54999; SSF54999; 1. DR TIGRFAMs; TIGR01049; rpsJ_bact; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 103 30S ribosomal protein S10. FT /FTId=PRO_0000146537. SQ SEQUENCE 103 AA; 11767 MW; 5CBA6EADB48102B8 CRC64; MQNQRIRIRL KAFDHRLIDQ STAEIVETAK RTGAQVRGPI PLPTRKERFT VLISPHVNKD ARDQYEIRTH KRLVDIVEPT EKTVDALMRL DLAAGVDVQI SLG // ID RS2_HAEIN Reviewed; 240 AA. AC P44371; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 17-FEB-2016, entry version 96. DE RecName: Full=30S ribosomal protein S2; GN Name=rpsB; Synonyms=rps2; OrderedLocusNames=HI_0913; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 2-8. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the ribosomal protein S2P family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22571.1; 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; L42023; AAC22571.1; ALT_INIT; Genomic_DNA. DR PIR; B64102; B64102. DR RefSeq; NP_439073.2; NC_000907.1. DR RefSeq; WP_005645552.1; NC_000907.1. DR ProteinModelPortal; P44371; -. DR SMR; P44371; 6-240. DR STRING; 71421.HI0913; -. DR PRIDE; P44371; -. DR EnsemblBacteria; AAC22571; AAC22571; HI_0913. DR GeneID; 949913; -. DR KEGG; hin:HI0913; -. DR PATRIC; 20190481; VBIHaeInf48452_0954. DR eggNOG; ENOG4105CE9; Bacteria. DR eggNOG; COG0052; LUCA. DR KO; K02967; -. DR OMA; RYIYCAR; -. DR OrthoDB; EOG6XWV6P; -. DR PhylomeDB; P44371; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid. DR InterPro; IPR018130; Ribosomal_S2_CS. DR InterPro; IPR023591; Ribosomal_S2_flav_dom. DR PANTHER; PTHR12534; PTHR12534; 1. DR Pfam; PF00318; Ribosomal_S2; 1. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; SSF52313; 1. DR TIGRFAMs; TIGR01011; rpsB_bact; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10675023}. FT CHAIN 2 240 30S ribosomal protein S2. FT /FTId=PRO_0000134176. SQ SEQUENCE 240 AA; 26264 MW; 5F20206A4A3FDE74 CRC64; MAQVSMRDMI NAGVHFGHQT RYWNPQMKPF IFGARNGVHI INLEKTLPLF NEALAELTRI ASNNGKVLFV GTKRAASEAV QAAALDCQQY YVNHRWLGGM LTNWKTVRQS IKRLKDLETQ SQDGTFDKLT KKEALMRSRE MEKLELSLGG IKDMGGLPDA LFVIGADHEH IAVKEANNLG IPVFAIVDTN STPAGVDFVI PGNDDATRAI QLYVSAAAAA VKEGRGNEAQ VAEELAADAE // ID RS16_HAEIN Reviewed; 82 AA. AC P44382; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 91. 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=HI_0204; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21873.1; -; Genomic_DNA. DR PIR; D64054; D64054. DR RefSeq; NP_438373.1; NC_000907.1. DR RefSeq; WP_005653865.1; NC_000907.1. DR ProteinModelPortal; P44382; -. DR SMR; P44382; 1-82. DR STRING; 71421.HI0204; -. DR EnsemblBacteria; AAC21873; AAC21873; HI_0204. DR GeneID; 951113; -. DR KEGG; hin:HI0204; -. DR PATRIC; 20188905; VBIHaeInf48452_0209. DR eggNOG; ENOG4105K5M; Bacteria. DR eggNOG; COG0228; LUCA. DR KO; K02959; -. DR OMA; TRMGRNK; -. DR OrthoDB; EOG6CVVKH; -. DR PhylomeDB; P44382; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1320.10; -; 1. DR HAMAP; MF_00385; Ribosomal_S16; 1. DR InterPro; IPR000307; Ribosomal_S16. DR InterPro; IPR020592; Ribosomal_S16_CS. DR InterPro; IPR023803; Ribosomal_S16_dom. DR PANTHER; PTHR12919; PTHR12919; 1. DR Pfam; PF00886; Ribosomal_S16; 1. DR SUPFAM; SSF54565; SSF54565; 1. DR TIGRFAMs; TIGR00002; S16; 1. DR PROSITE; PS00732; RIBOSOMAL_S16; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 82 30S ribosomal protein S16. FT /FTId=PRO_0000167192. SQ SEQUENCE 82 AA; 9179 MW; E4C0B7CE97FB76C1 CRC64; MVTIRLSRGG AKKRPFYQIV VADSRSPRDG RFIERVGFFN PIAQGNAERL RINLERVNHW VAQGASLSDR VASLVKEAQK AA // ID RS19_HAEIN Reviewed; 91 AA. AC P67899; P44385; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 67. DE RecName: Full=30S ribosomal protein S19; GN Name=rpsS; Synonyms=rps19; OrderedLocusNames=HI_0781; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22440.1; -; Genomic_DNA. DR PIR; I64092; I64092. DR RefSeq; NP_438940.1; NC_000907.1. DR RefSeq; WP_005539416.1; NC_000907.1. DR ProteinModelPortal; P67899; -. DR SMR; P67899; 2-88. DR STRING; 71421.HI0781; -. DR PRIDE; P67899; -. DR EnsemblBacteria; AAC22440; AAC22440; HI_0781. DR GeneID; 7278421; -. DR GeneID; 949797; -. DR KEGG; hin:HI0781; -. DR PATRIC; 20190213; VBIHaeInf48452_0820. DR eggNOG; ENOG4105K7S; Bacteria. DR eggNOG; COG0185; LUCA. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR PhylomeDB; P67899; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.860.10; -; 1. DR HAMAP; MF_00531; Ribosomal_S19; 1. DR InterPro; IPR002222; Ribosomal_S19. DR InterPro; IPR005732; Ribosomal_S19_bac-type. DR InterPro; IPR020934; Ribosomal_S19_CS. DR InterPro; IPR023575; Ribosomal_S19_SF. DR PANTHER; PTHR11880; PTHR11880; 1. DR Pfam; PF00203; Ribosomal_S19; 1. DR PIRSF; PIRSF002144; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR SUPFAM; SSF54570; SSF54570; 1. DR TIGRFAMs; TIGR01050; rpsS_bact; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 91 30S ribosomal protein S19. FT /FTId=PRO_0000129831. SQ SEQUENCE 91 AA; 10259 MW; 56B221F8BAD41E1D CRC64; MPRSLKKGPF LDLHLLKKVE KAVESGDKKP IKTWSRRSMI IPSMIGLTIA VHNGRQHVPV YVSDEMIGHK LGEFAPTRTY RGHAADKKAK K // ID RRF_HAEIN Reviewed; 185 AA. AC P44307; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. 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=HI_0808; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 1-7. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22467.1; -; Genomic_DNA. DR PIR; D64095; D64095. DR RefSeq; NP_438968.1; NC_000907.1. DR RefSeq; WP_005632773.1; NC_000907.1. DR ProteinModelPortal; P44307; -. DR SMR; P44307; 1-184. DR STRING; 71421.HI0808; -. DR EnsemblBacteria; AAC22467; AAC22467; HI_0808. DR GeneID; 949822; -. DR KEGG; hin:HI0808; -. DR PATRIC; 20190271; VBIHaeInf48452_0849. DR eggNOG; ENOG4108VCV; Bacteria. DR eggNOG; COG0233; LUCA. DR KO; K02838; -. DR OMA; VQPWEKK; -. DR OrthoDB; EOG6SV5F9; -. DR PhylomeDB; P44307; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GOC. DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central. DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central. DR Gene3D; 1.10.132.20; -; 1. DR HAMAP; MF_00040; RRF; 1. DR InterPro; IPR002661; Ribosome_recyc_fac. DR InterPro; IPR023584; Ribosome_recyc_fac_dom. DR PANTHER; PTHR20982; PTHR20982; 1. DR Pfam; PF01765; RRF; 1. DR SUPFAM; SSF55194; SSF55194; 1. DR TIGRFAMs; TIGR00496; frr; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 185 Ribosome-recycling factor. FT /FTId=PRO_0000167468. SQ SEQUENCE 185 AA; 20729 MW; 14977357A3288A04 CRC64; MLNQIKKDAQ DRMEKSLEAL KGHISKIRTG RAQPSLLDAI QVEYYGAATP LRQLANVVAE DARTLAVTVF DRSLISAVEK AILTSDLGLN PSSAGTTIRV PLPPLTEERR RDLIKIVKGE GEQGKVAVRN VRRDANDKIK ALLKDKEISE NEQHKAEEEI QKITDIYIKK VDEVLADKEK ELMDF // ID RS12_HAEIN Reviewed; 124 AA. AC P63196; P44412; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 78. DE RecName: Full=30S ribosomal protein S12; DE AltName: Full=Streptomycin resistance protein; GN Name=rpsL; Synonyms=rps12, strA; OrderedLocusNames=HI_0581; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS STREPTOMYCIN RESISTANT RP ARG-43 AND VAL-81. RC STRAIN=Rd / BC200; RX PubMed=1512195; RA Stuy J.H., Walter R.B.; RT "Cloning, characterization, and DNA base sequence of the high-level RT streptomycin resistance gene strA1 of Haemophilus influenzae Rd."; RL J. Bacteriol. 174:5604-5608(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. {ECO:0000250}. 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 (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8 CC and S17. May interact with IF1 in the 30S initiation complex (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S12P 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; M86701; AAA25003.1; -; Genomic_DNA. DR EMBL; M86702; AAA25004.1; -; Genomic_DNA. DR EMBL; L42023; AAC22239.1; -; Genomic_DNA. DR PIR; B42939; A42939. DR RefSeq; NP_438739.1; NC_000907.1. DR RefSeq; WP_005543325.1; NC_000907.1. DR ProteinModelPortal; P63196; -. DR SMR; P63196; 2-124. DR STRING; 71421.HI0581; -. DR PRIDE; P63196; -. DR EnsemblBacteria; AAC22239; AAC22239; HI_0581. DR GeneID; 4849900; -. DR GeneID; 949625; -. DR KEGG; hin:HI0581; -. DR PATRIC; 20189719; VBIHaeInf48452_0602. DR eggNOG; ENOG4108UKE; Bacteria. DR eggNOG; COG0048; LUCA. DR KO; K02950; -. DR OMA; KSKVPAM; -. DR OrthoDB; EOG61ZTNF; -. DR PhylomeDB; P63196; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00403_B; Ribosomal_S12_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006032; Ribosomal_S12/S23. DR InterPro; IPR005679; Ribosomal_S12_bac. DR PANTHER; PTHR11652; PTHR11652; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Complete proteome; Methylation; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding; tRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 124 30S ribosomal protein S12. FT /FTId=PRO_0000146232. FT MOD_RES 89 89 3-methylthioaspartic acid. {ECO:0000250}. FT VARIANT 43 43 K -> R (in streptomycin resistant strA1). FT {ECO:0000269|PubMed:1512195}. FT VARIANT 81 81 L -> V (in streptomycin resistant stra1). FT {ECO:0000269|PubMed:1512195}. SQ SEQUENCE 124 AA; 13749 MW; D51C8A7BDD4E1D45 CRC64; MATINQLVRK PRVKKVVKSN VPALEACPQK RGVCTRVYTT TPKKPNSALR KVCRIRLTNG FEVTSYIGGE GHNLQEHSVV LIRGGRVKDL PGVRYHTVRG ALDCAGVKDR KQGRSKYGVK RPKA // ID RS14_HAEIN Reviewed; 101 AA. AC P44381; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 88. DE RecName: Full=30S ribosomal protein S14 {ECO:0000255|HAMAP-Rule:MF_00537}; GN Name=rpsN {ECO:0000255|HAMAP-Rule:MF_00537}; GN Synonyms=rps14 {ECO:0000255|HAMAP-Rule:MF_00537}; GN OrderedLocusNames=HI_0791; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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_00537}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S3 CC and S10. {ECO:0000255|HAMAP-Rule:MF_00537}. CC -!- SIMILARITY: Belongs to the ribosomal protein S14P family. CC {ECO:0000255|HAMAP-Rule:MF_00537}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22449.1; -; Genomic_DNA. DR PIR; I64093; I64093. DR RefSeq; NP_438950.1; NC_000907.1. DR RefSeq; WP_005625879.1; NC_000907.1. DR ProteinModelPortal; P44381; -. DR SMR; P44381; 2-101. DR STRING; 71421.HI0791; -. DR EnsemblBacteria; AAC22449; AAC22449; HI_0791. DR GeneID; 949808; -. DR KEGG; hin:HI0791; -. DR PATRIC; 20190233; VBIHaeInf48452_0830. DR eggNOG; ENOG4105VBI; Bacteria. DR eggNOG; COG0199; LUCA. DR KO; K02954; -. DR OMA; GVYSKFG; -. DR OrthoDB; EOG6BCT0K; -. DR PhylomeDB; P44381; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00537; Ribosomal_S14_1; 1. DR InterPro; IPR001209; Ribosomal_S14. DR InterPro; IPR023036; Ribosomal_S14_bac/plaastid. DR InterPro; IPR018271; Ribosomal_S14_CS. 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 101 30S ribosomal protein S14. FT /FTId=PRO_0000130893. SQ SEQUENCE 101 AA; 11676 MW; D98839EF430EA445 CRC64; MAKQSMKARD VKRVKLAEKF YAKRVELKKI ISDVNASDED RWDAVLKLQT LPRDSSPSRQ RNRCRQTGRP HGVLRKFGLS RIKVREAAMR GEIPGLKKAS W // ID RS13_HAEIN Reviewed; 122 AA. AC P44380; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2003, sequence version 2. DT 17-FEB-2016, entry version 102. 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=HI_0799; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22458.1; -; Genomic_DNA. DR PIR; H64094; H64094. DR RefSeq; NP_438959.3; NC_000907.1. DR RefSeq; WP_021018385.1; NC_000907.1. DR ProteinModelPortal; P44380; -. DR SMR; P44380; 2-110. DR STRING; 71421.HI0799; -. DR EnsemblBacteria; AAC22458; AAC22458; HI_0799. DR GeneID; 949817; -. DR KEGG; hin:HI0799; -. DR PATRIC; 20190251; VBIHaeInf48452_0839. DR eggNOG; ENOG4108Z04; Bacteria. DR eggNOG; COG0099; LUCA. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR PhylomeDB; P44380; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.910.10; -; 1. DR HAMAP; MF_01315; Ribosomal_S13_S18; 1. DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C. DR InterPro; IPR001892; Ribosomal_S13. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR019980; Ribosomal_S13_bac-type. DR InterPro; IPR018269; Ribosomal_S13_CS. DR Pfam; PF00416; Ribosomal_S13; 1. DR PIRSF; PIRSF002134; Ribosomal_S13; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR TIGRFAMs; TIGR03631; uS13_bact; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 122 30S ribosomal protein S13. FT /FTId=PRO_0000132095. SQ SEQUENCE 122 AA; 13696 MW; 486DCC4ABF70E9E5 CRC64; MARIAGINIP DHKHAVIALT AIYGIGKTRS QAICAAAGIA EDVKIRELSE EQIDKLRDEV GKFTVEGDLR REVTLNIKRL LDLGCYRGLR HRRSLPVRGQ RTKTNARTRK VHVSRSKNSR GK // ID RS15_HAEIN Reviewed; 89 AA. AC P44389; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 102. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO1 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Synonyms=rps15-A {ECO:0000255|HAMAP-Rule:MF_01343}, rpsO-A; GN OrderedLocusNames=HI_1328; GN and GN Name=rpsO2 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Synonyms=rps15-B {ECO:0000255|HAMAP-Rule:MF_01343}, rpsO-B; GN OrderedLocusNames=HI_1468; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22973.1; -; Genomic_DNA. DR EMBL; L42023; AAC23117.1; -; Genomic_DNA. DR PIR; H64116; H64116. DR RefSeq; NP_439479.1; NC_000907.1. DR RefSeq; NP_439619.1; NC_000907.1. DR RefSeq; WP_005652821.1; NC_000907.1. DR ProteinModelPortal; P44389; -. DR SMR; P44389; 2-89. DR STRING; 71421.HI1468; -. DR EnsemblBacteria; AAC22973; AAC22973; HI_1328. DR EnsemblBacteria; AAC23117; AAC23117; HI_1468. DR GeneID; 950244; -. DR GeneID; 950650; -. DR KEGG; hin:HI1328; -. DR KEGG; hin:HI1468; -. DR PATRIC; 20191339; VBIHaeInf48452_1380. DR eggNOG; ENOG4105K77; Bacteria. DR eggNOG; COG0184; LUCA. DR KO; K02956; -. DR OMA; TEHFKSH; -. DR OrthoDB; EOG6B368J; -. DR PhylomeDB; P44389; -. DR Proteomes; UP000000579; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 89 30S ribosomal protein S15. FT /FTId=PRO_0000115447. SQ SEQUENCE 89 AA; 10196 MW; 1FA6E4FF16C3ED43 CRC64; MSLSTEKKAA IVAEFGRDAK DTGSSEVQIA LLTAQINHLQ THFAEHKKDH HGRRGLLRMV SRRRKLLDYL KRTDLALYQS TIARLGLRR // ID RS18_HAEIN Reviewed; 75 AA. AC P66457; P44384; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 62. DE RecName: Full=30S ribosomal protein S18; GN Name=rpsR; Synonyms=rps18; OrderedLocusNames=HI_0545; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight CC heterodimer with protein S6 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S18P 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; L42023; AAC22203.1; -; Genomic_DNA. DR PIR; E64076; E64076. DR RefSeq; NP_438703.1; NC_000907.1. DR RefSeq; WP_005598105.1; NC_000907.1. DR ProteinModelPortal; P66457; -. DR SMR; P66457; 7-75. DR STRING; 71421.HI0545; -. DR EnsemblBacteria; AAC22203; AAC22203; HI_0545. DR GeneID; 7277137; -. DR GeneID; 950770; -. DR KEGG; hin:HI0545; -. DR PATRIC; 20189643; VBIHaeInf48452_0564. DR eggNOG; ENOG4105VH8; Bacteria. DR eggNOG; COG0238; LUCA. DR KO; K02963; -. DR OMA; GDIRYLT; -. DR OrthoDB; EOG6PCQ4R; -. DR PhylomeDB; P66457; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.640.10; -; 1. DR HAMAP; MF_00270; Ribosomal_S18; 1. DR InterPro; IPR001648; Ribosomal_S18. DR InterPro; IPR018275; Ribosomal_S18_CS. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR SUPFAM; SSF46911; SSF46911; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. PE 3: Inferred from homology; KW Acetylation; Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 75 30S ribosomal protein S18. FT /FTId=PRO_0000111162. FT MOD_RES 2 2 N-acetylalanine. {ECO:0000250}. SQ SEQUENCE 75 AA; 8942 MW; AC39F71DFC127AB8 CRC64; MARYFRRRKF CRFTAENVVE IDYKDIATLK NYISESGKIV PSRITGTRAK YQRQLARAIK RARYLALLPY TDNHQ // ID RS20_HAEIN Reviewed; 87 AA. AC P44959; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 87. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=HI_0965; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22624.1; ALT_SEQ; Genomic_DNA. DR PIR; A64163; A64163. DR RefSeq; NP_439126.2; NC_000907.1. DR RefSeq; WP_005651580.1; NC_000907.1. DR ProteinModelPortal; P44959; -. DR SMR; P44959; 3-87. DR STRING; 71421.HI0965; -. DR EnsemblBacteria; AAC22624; AAC22624; HI_0965. DR GeneID; 950750; -. DR KEGG; hin:HI0965; -. DR PATRIC; 20190589; VBIHaeInf48452_1007. DR eggNOG; ENOG4105KQV; Bacteria. DR eggNOG; COG0268; LUCA. DR KO; K02968; -. DR OMA; HACKGLI; -. DR OrthoDB; EOG6HMXNQ; -. DR PhylomeDB; P44959; -. DR Proteomes; UP000000579; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 87 30S ribosomal protein S20. FT /FTId=PRO_0000167969. SQ SEQUENCE 87 AA; 9638 MW; F28249F3A4067A48 CRC64; MANIKSAKKR AVQSEKRRQH NASQRSMMRT YIKKVYAQVA AGEKSAAEAA FVEMQKVVDR MASKGLIHAN KAANHKSKLA AQIKKLA // ID RS3_HAEIN Reviewed; 235 AA. AC P44372; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 110. 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=HI_0783; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22442.1; -; Genomic_DNA. DR PIR; B64093; B64093. DR RefSeq; NP_438942.1; NC_000907.1. DR RefSeq; WP_005693167.1; NC_000907.1. DR ProteinModelPortal; P44372; -. DR SMR; P44372; 2-207. DR STRING; 71421.HI0783; -. DR EnsemblBacteria; AAC22442; AAC22442; HI_0783. DR GeneID; 949799; -. DR KEGG; hin:HI0783; -. DR PATRIC; 20190217; VBIHaeInf48452_0822. DR eggNOG; ENOG4105CKE; Bacteria. DR eggNOG; COG0092; LUCA. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR PhylomeDB; P44372; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1140.32; -; 1. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_01309_B; Ribosomal_S3_B; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004088; KH_dom_type_1. 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 2 235 30S ribosomal protein S3. FT /FTId=PRO_0000130128. FT DOMAIN 39 107 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 235 AA; 25852 MW; 853D0A7E1A7793A6 CRC64; MGQKVHPHGI RLGIVKPWSS TWFANTQDFA DNLEGDFKVR KFLNKELASA SVSRITIERP AKSIRVTIHT ARPGIVIGKK GEDVEKLRNA VSKIAGVPAQ INIAEVKKPE LDAKLVADSI ASQLERRVMF RRAMKRAVQS AMRLGAKGIK VEVSGRLGGA EIARSEWYRE GRVPLHTLRA DIDYNTAEAH TTYGVIGVKV WIFKGEILGG MAAVAQSEQQ PADKPKKAPR GKGRK // ID RS4_HAEIN Reviewed; 206 AA. AC P44373; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-MAY-2016, entry version 99. 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=HI_0801; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22460.1; -; Genomic_DNA. DR PIR; A64095; A64095. DR RefSeq; NP_438961.1; NC_000907.1. DR RefSeq; WP_005693170.1; NC_000907.1. DR ProteinModelPortal; P44373; -. DR SMR; P44373; 2-206. DR STRING; 71421.HI0801; -. DR EnsemblBacteria; AAC22460; AAC22460; HI_0801. DR GeneID; 950601; -. DR KEGG; hin:HI0801; -. DR PATRIC; 20190255; VBIHaeInf48452_0841. DR eggNOG; ENOG4105G6W; Bacteria. DR eggNOG; COG0522; LUCA. DR KO; K02986; -. DR OMA; VYEWITW; -. DR OrthoDB; EOG6N3CXM; -. DR PhylomeDB; P44373; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1050.10; -; 1. DR Gene3D; 3.10.290.10; -; 1. DR HAMAP; MF_01306_B; Ribosomal_S4_B; 1. DR InterPro; IPR022801; Ribosomal_S4/S9. DR InterPro; IPR001912; Ribosomal_S4/S9_N. DR InterPro; IPR005709; Ribosomal_S4_bac-type. DR InterPro; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 206 30S ribosomal protein S4. FT /FTId=PRO_0000132391. FT DOMAIN 96 156 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_01306}. SQ SEQUENCE 206 AA; 23524 MW; FB0C2EB98212B0F8 CRC64; MARYLGPKLK LSRREGTDLF LKSGVRAIDS KCKIDTAPGQ HGARKPRLSD YGSQLREKQK VRRIYGILER QFRNYYKEAN RLKGNTGENL LVLLEGRLDN VVYRMGFATT RAEARQLVSH KAIVVNGRVV NIPSFQVSVN DVVAIREKSK KQARIKASLE LAEQREKPTW LEVDSAKMEG VFKRVPERSD LSADINEHLI VELYSK // ID RS17_HAEIN Reviewed; 85 AA. AC P44383; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 96. 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=HI_0786; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22445.1; -; Genomic_DNA. DR PIR; E64093; E64093. DR RefSeq; NP_438945.1; NC_000907.1. DR RefSeq; WP_005625886.1; NC_000907.1. DR ProteinModelPortal; P44383; -. DR SMR; P44383; 4-84. DR STRING; 71421.HI0786; -. DR EnsemblBacteria; AAC22445; AAC22445; HI_0786. DR GeneID; 949800; -. DR KEGG; hin:HI0786; -. DR PATRIC; 20190223; VBIHaeInf48452_0825. DR eggNOG; ENOG4105K87; Bacteria. DR eggNOG; COG0186; LUCA. DR KO; K02961; -. DR OMA; LKAHDEQ; -. DR OrthoDB; EOG63JRH2; -. DR PhylomeDB; P44383; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000266; Ribosomal_S17/S11. DR InterPro; IPR019984; Ribosomal_S17_bac-type. DR InterPro; IPR019979; Ribosomal_S17_CS. DR PANTHER; PTHR10744; PTHR10744; 1. DR Pfam; PF00366; Ribosomal_S17; 1. DR PRINTS; PR00973; RIBOSOMALS17. DR ProDom; PD001295; Ribosomal_S17; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR03635; uS17_bact; 1. DR PROSITE; PS00056; RIBOSOMAL_S17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 85 30S ribosomal protein S17. FT /FTId=PRO_0000128459. SQ SEQUENCE 85 AA; 9789 MW; A751ACD6DBE564BF CRC64; MTDKIRSVQG KVVSDKMEKS FVVAIERKVK HPLYGKFIRR TTKLHVHDEN NEAKVGDTVE IRECRPLSKT KSWTLVRVVE KAVIA // ID RS1_HAEIN Reviewed; 549 AA. AC Q48082; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=30S ribosomal protein S1; GN Name=rpsA; OrderedLocusNames=HI_1220; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds mRNA; thus facilitating recognition of the CC initiation point. It is needed to translate mRNA with a short CC Shine-Dalgarno (SD) purine-rich sequence (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S1P family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 6 S1 motif domains. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22873.1; -; Genomic_DNA. DR RefSeq; NP_439376.1; NC_000907.1. DR RefSeq; WP_010869157.1; NC_000907.1. DR ProteinModelPortal; Q48082; -. DR SMR; Q48082; 363-399. DR STRING; 71421.HI1220; -. DR EnsemblBacteria; AAC22873; AAC22873; HI_1220. DR GeneID; 950163; -. DR KEGG; hin:HI1220; -. DR PATRIC; 20191119; VBIHaeInf48452_1272. DR eggNOG; ENOG4105CAV; Bacteria. DR eggNOG; COG0539; LUCA. DR KO; K02945; -. DR OMA; ISWDKNV; -. DR OrthoDB; EOG6WT8CC; -. DR PhylomeDB; Q48082; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 6. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000110; Ribosomal_S1. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF00575; S1; 6. DR PIRSF; PIRSF002111; RpsA; 1. DR PRINTS; PR00681; RIBOSOMALS1. DR SMART; SM00316; S1; 6. DR SUPFAM; SSF50249; SSF50249; 6. DR TIGRFAMs; TIGR00717; rpsA; 1. DR PROSITE; PS50126; S1; 6. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; Ribonucleoprotein; KW Ribosomal protein; RNA-binding. FT CHAIN 1 549 30S ribosomal protein S1. FT /FTId=PRO_0000196037. FT DOMAIN 21 87 S1 motif 1. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 105 171 S1 motif 2. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 192 260 S1 motif 3. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 277 347 S1 motif 4. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 364 434 S1 motif 5. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT DOMAIN 451 512 S1 motif 6. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. SQ SEQUENCE 549 AA; 59558 MW; 122264FDD1EE10F8 CRC64; MSESFAQLFE ESLKVLETRQ GSIVSGTVVA IQKGFVLVDA GLKSESAIPV AEFLNAQGEL EIQVGDTVNV ALDAVEDGFG ETKLSREKAV RHESWIELEK AYEEKATVIG LIXGKVKGGF TVELNGVRAF LPGSLVDTRP AREADHLLGK ELEFKVIKLD QKRNNVVVSR RAVIESENSQ EREQVLENLV EGSEVKGVVK NLTEYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE VTVKVLKFDK DRTRVSLGLK QLGQDPWAAI AENHPVNSKL TGKVTNLTDY GCFVEILDGV EGLVHVSEMD WTNKNIHPSK VVSLGDTVEV MVLEIDEERR RISLGLKQCK ANPWTQFADT HNKGDKVTGK IKSITDFGIF IGLEGGIDGL VHLSDISWSI SGEEAVRQYK KGDEVSAVVL AVDAVKERIS LGIKQLEEDP FNNFVAINKK GAVVSATVVE ADAKGAKVEL AGGVEGYIRS ADLTSEVAVG DVVEAKYTGV DRKSRIVHLS VKAKDQAEEA AAVASVNNKQ EDIVIPNAMA EAFKAAKGE // ID RS21_HAEIN Reviewed; 71 AA. AC P44386; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 87. DE RecName: Full=30S ribosomal protein S21; GN Name=rpsU; Synonyms=rps21; OrderedLocusNames=HI_0531; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-71. RC STRAIN=Isolate 1775; RX PubMed=8316085; DOI=10.1111/j.1365-2958.1993.tb01578.x; RA Versalovic J., Lupski J.R.; RT "Conservation and evolution of the rpsU-dnaG-rpoD macromolecular RT synthesis operon in bacteria."; RL Mol. Microbiol. 8:343-355(1993). 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; L42023; AAC22188.1; -; Genomic_DNA. DR EMBL; L01756; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I64074; I64074. DR RefSeq; NP_438689.1; NC_000907.1. DR RefSeq; WP_005627632.1; NC_000907.1. DR ProteinModelPortal; P44386; -. DR SMR; P44386; 4-54. DR STRING; 71421.HI0531; -. DR EnsemblBacteria; AAC22188; AAC22188; HI_0531. DR GeneID; 950699; -. DR KEGG; hin:HI0531; -. DR PATRIC; 20189615; VBIHaeInf48452_0550. DR eggNOG; ENOG4105VCC; Bacteria. DR eggNOG; COG0828; LUCA. DR KO; K02970; -. DR OMA; KRHFKRL; -. DR OrthoDB; EOG6FBX3Z; -. DR PhylomeDB; P44386; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0044391; C:ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00358; Ribosomal_S21; 1. DR InterPro; IPR001911; Ribosomal_S21. DR InterPro; IPR018278; Ribosomal_S21_CS. DR Pfam; PF01165; Ribosomal_S21; 1. DR PRINTS; PR00976; RIBOSOMALS21. DR ProDom; PD005521; Ribosomal_S21; 1. DR TIGRFAMs; TIGR00030; S21p; 1. DR PROSITE; PS01181; RIBOSOMAL_S21; 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 71 30S ribosomal protein S21. FT /FTId=PRO_0000178339. FT CONFLICT 32 32 V -> I (in Ref. 2). {ECO:0000305}. SQ SEQUENCE 71 AA; 8462 MW; BA7CB923AD8A7FB3 CRC64; MPVIKVRENE SFDVALRRFK RSCEKAGILA EVRAREFYEK PTTIRKRENA TLAKRHAKRN ARENARNTRL Y // ID RSMC_HAEIN Reviewed; 330 AA. AC P44453; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000255|HAMAP-Rule:MF_01862}; DE EC=2.1.1.172 {ECO:0000255|HAMAP-Rule:MF_01862}; DE AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01862}; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000255|HAMAP-Rule:MF_01862}; GN Name=rsmC {ECO:0000255|HAMAP-Rule:MF_01862}; GN OrderedLocusNames=HI_0012; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the guanine in position 1207 of CC 16S rRNA in the 30S particle. {ECO:0000255|HAMAP-Rule:MF_01862}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(1207) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1207) in 16S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01862}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01862}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01862}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC CC family. {ECO:0000255|HAMAP-Rule:MF_01862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21690.1; -; Genomic_DNA. DR PIR; B64140; B64140. DR RefSeq; NP_438185.1; NC_000907.1. DR RefSeq; WP_005693888.1; NC_000907.1. DR ProteinModelPortal; P44453; -. DR STRING; 71421.HI0012; -. DR EnsemblBacteria; AAC21690; AAC21690; HI_0012. DR GeneID; 950903; -. DR KEGG; hin:HI0012; -. DR PATRIC; 20188475; VBIHaeInf48452_0012. DR eggNOG; ENOG4105D8J; Bacteria. DR eggNOG; COG2813; LUCA. DR KO; K00564; -. DR OMA; RHCQLWQ; -. DR OrthoDB; EOG67X1ZC; -. DR PhylomeDB; P44453; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01862; 16SrRNA_methyltr_C; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR013675; Mtase_sm_N. DR InterPro; IPR023543; rRNA_ssu_MeTfrase_C. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR Pfam; PF08468; MTS_N; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 330 Ribosomal RNA small subunit FT methyltransferase C. FT /FTId=PRO_0000097491. SQ SEQUENCE 330 AA; 37061 MW; 7FF723E3993D9B69 CRC64; MISLESQVLE RHISFFDGKS VLFAGGISDS FPQTLASKCS SIQIWSCYFD YARTQSAVNF SVEFQGQADL IVYYWTKNKQ EVNFQLIQLL AQASIGQEIL IIGENRCGVR SVEKTLSPYG EIAKIDSARR CGLYHFSLQN KPHFELKNFW RTYQHSTLEN LTIYSLPGVF SAAELDTGTE LLLSTIDNKI KGKVLDLGCG AGVIGSMIKK RTPNAQITMT DIHAMALESA RKTLSENQLQ GEVYASDVFS DIEGKFDLII SNPPFHDGID TAYRAVTELI TQAKWHLNQG GELRIVANSF LPYPELLRQH FNDYQVLAQT GKFKVYSVKN // ID RSMH_HAEIN Reviewed; 321 AA. AC P45057; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. 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=HI_1130; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22785.1; -; Genomic_DNA. DR PIR; F64167; F64167. DR RefSeq; NP_439288.1; NC_000907.1. DR RefSeq; WP_005651812.1; NC_000907.1. DR ProteinModelPortal; P45057; -. DR STRING; 71421.HI1130; -. DR EnsemblBacteria; AAC22785; AAC22785; HI_1130. DR GeneID; 950097; -. DR KEGG; hin:HI1130; -. DR PATRIC; 20190935; VBIHaeInf48452_1180. DR eggNOG; ENOG4105CGJ; Bacteria. DR eggNOG; COG0275; LUCA. DR KO; K03438; -. DR OMA; HVPVMLQ; -. DR OrthoDB; EOG6X9MQ1; -. DR PhylomeDB; P45057; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR Gene3D; 1.10.150.170; -; 1. DR Gene3D; 3.40.50.150; -; 2. DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1. DR InterPro; IPR002903; RsmH. DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11265; PTHR11265; 1. DR Pfam; PF01795; Methyltransf_5; 1. DR PIRSF; PIRSF004486; MraW; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR SUPFAM; SSF81799; SSF81799; 1. DR TIGRFAMs; TIGR00006; TIGR00006; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 321 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108635. FT REGION 40 42 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 60 60 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 84 84 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01007}. FT BINDING 106 106 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. FT BINDING 113 113 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01007}. SQ SEQUENCE 321 AA; 36052 MW; F3265EFE29687491 CRC64; MNSENSFSSS EHITVLLHEA VNGLALKENG IYIDGTFGRG GHSRFILSQL SSNGRLIAVD RDPRAIAEAH KIQDLRFQIE HNSFSHIPEI CDKLNLVGKI DGILLDLGVS SPQLDEAERG FSFMKDGPLD MRMDTTQGLS AEEWLKQVSI EDLTWVLKTF GEERFAKRIA TAIVDFNKSA VKNGTEFLSR TSQLAELISQ AVPFKDKHKH PATRSFQAIR IFINSELDEL ESLLNSALDM LAPEGRLSII SFHSLEDRMV KHFMKKQSKG EDIPKGLPLR EDQIQRNQKL RIIGKAIQPS DAEIQANPRS RSAILRVAER I // ID RS5_HAEIN Reviewed; 166 AA. AC P44374; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. 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=HI_0795; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22453.1; -; Genomic_DNA. DR PIR; D64094; D64094. DR RefSeq; NP_438954.1; NC_000907.1. DR RefSeq; WP_005625871.1; NC_000907.1. DR ProteinModelPortal; P44374; -. DR SMR; P44374; 10-159. DR STRING; 71421.HI0795; -. DR PRIDE; P44374; -. DR EnsemblBacteria; AAC22453; AAC22453; HI_0795. DR GeneID; 949813; -. DR KEGG; hin:HI0795; -. DR PATRIC; 20190241; VBIHaeInf48452_0834. DR eggNOG; ENOG4108RA9; Bacteria. DR eggNOG; COG0098; LUCA. DR KO; K02988; -. DR OMA; NERDSEW; -. DR OrthoDB; EOG6FJNM5; -. DR PhylomeDB; P44374; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01307_B; Ribosomal_S5_B; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000851; Ribosomal_S5. DR InterPro; IPR005712; Ribosomal_S5_bac-type. DR InterPro; IPR005324; Ribosomal_S5_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR013810; Ribosomal_S5_N. DR InterPro; IPR018192; Ribosomal_S5_N_CS. DR PANTHER; PTHR13718; PTHR13718; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR01021; rpsE_bact; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 166 30S ribosomal protein S5. FT /FTId=PRO_0000131523. FT DOMAIN 11 74 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 166 AA; 17500 MW; 27A789D3D92B3C45 CRC64; MSNIEKQVGE LQEKLIAVNR VSKTVKGGRI MSFTALTVVG DGNGRVGFGY GKAREVPAAI QKAMEKARRN MINVALNEGT LQHPVKGVHT GSRVFMQPAS EGTGIIAGGA MRAVLEVAGV RNVLSKAYGS TNPINVVRAT IDALANMKSP EMVAAKRGKT VDEILG // ID RS6_HAEIN Reviewed; 125 AA. AC P44375; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=30S ribosomal protein S6; GN Name=rpsF; Synonyms=rps6; OrderedLocusNames=HI_0547; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA. CC {ECO:0000250}. CC -!- PTM: Modified post-translationally by the addition of C-terminal CC Glu residues by the RIMK enzyme. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S6P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22205.1; -; Genomic_DNA. DR PIR; G64076; G64076. DR RefSeq; NP_438705.1; NC_000907.1. DR RefSeq; WP_005627620.1; NC_000907.1. DR ProteinModelPortal; P44375; -. DR SMR; P44375; 1-100. DR STRING; 71421.HI0547; -. DR PRIDE; P44375; -. DR EnsemblBacteria; AAC22205; AAC22205; HI_0547. DR GeneID; 25058039; -. DR GeneID; 949602; -. DR KEGG; hin:HI0547; -. DR PATRIC; 20189647; VBIHaeInf48452_0566. DR eggNOG; ENOG4108ZDX; Bacteria. DR eggNOG; COG0360; LUCA. DR KO; K02990; -. DR OMA; ITEASPM; -. DR OrthoDB; EOG6P33DH; -. DR PhylomeDB; P44375; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.60; -; 1. DR HAMAP; MF_00360; Ribosomal_S6; 1. DR InterPro; IPR000529; Ribosomal_S6. DR InterPro; 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 1 125 30S ribosomal protein S6. FT /FTId=PRO_0000176774. SQ SEQUENCE 125 AA; 14484 MW; A3804A2FEFBE8EAC CRC64; MRHYEIVFMV HPDQSEQVPG MIERYTGSVK EAGGQVHRLE DWGRRQLAYP INKLHKAHYV LMNVEAPQQV IDELETTFRY NDAVLRSLVI HTKHAVTEAS PMKAAKEERK PLAEVENNDF EDAEE // ID RSEA_HAEIN Reviewed; 195 AA. AC P44791; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Anti-sigma-E factor RseA; DE AltName: Full=Regulator of SigE; DE AltName: Full=Sigma-E anti-sigma factor RseA; DE AltName: Full=Sigma-E factor negative regulatory protein; GN Name=rseA; Synonyms=mclA; OrderedLocusNames=HI_0629; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF) CC sigma factor sigma-E (RpoE). ECF sigma factors are held in an CC inactive form by an anti-sigma factor until released by regulated CC intramembrane proteolysis (RIP). RIP occurs when an CC extracytoplasmic signal triggers a concerted proteolytic cascade CC to transmit information and elicit cellular responses. The CC membrane-spanning regulatory substrate protein is first cut CC periplasmically (site-1 protease, S1P, DegS), then within the CC membrane itself (site-2 protease, S2P, RseP), while cytoplasmic CC proteases finish degrading the anti-sigma factor, liberating CC sigma-E (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); CC this inhibits the interaction of sigma-E with the RNA polymerase CC catalytic core and leads to a decreased expression of sigma-E- CC regulated genes. Interacts with RseB with 1:1 stoichiometry. The CC liberated N-terminus forms a complex with SspB and RpoE (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. Note=Following CC cleavage by DegS the large fragment of the protein is still in the CC inner membrane and retains its anti-sigma-E activity. CC {ECO:0000250}. CC -!- DOMAIN: The N-terminal cytosolic domain interacts with sigma-E. CC After degradation by RseP binds to SspB, targeting RseA for CC degradation by the ClpX-ClpP protease (By similarity). CC {ECO:0000250}. CC -!- DOMAIN: The C-terminal periplasmic domain interacts with RseB and CC is also the target for DegS. {ECO:0000250}. CC -!- PTM: Sequentially cleaved by DegS (a site-1 protease) in its CC periplasmic domain between Val-147 and Ser-148, then by RseP (a CC site-2 protease). The N-terminal fragment is then degraded by CC primarily ClpX-ClpP in an ATP-dependent fashion. Sequential CC cleavage by DegS, RseP and ClpX-ClpP frees RpoE from RseA (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RseA 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; L42023; AAC22289.1; -; Genomic_DNA. DR PIR; G64082; G64082. DR RefSeq; NP_438789.1; NC_000907.1. DR RefSeq; WP_005651258.1; NC_000907.1. DR ProteinModelPortal; P44791; -. DR STRING; 71421.HI0629; -. DR EnsemblBacteria; AAC22289; AAC22289; HI_0629. DR GeneID; 949684; -. DR KEGG; hin:HI0629; -. DR PATRIC; 20189853; VBIHaeInf48452_0655. DR eggNOG; ENOG41069PW; Bacteria. DR eggNOG; COG3073; LUCA. DR KO; K03597; -. DR OMA; GVQHYNQ; -. DR OrthoDB; EOG6V7BSG; -. DR PhylomeDB; P44791; -. DR Proteomes; UP000000579; 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:0016989; F:sigma factor antagonist activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR005573; Anti-sigma_E_RseA_C. DR InterPro; IPR005572; Anti-sigma_E_RseA_N. DR InterPro; IPR026279; RseA. DR Pfam; PF03873; RseA_C; 1. DR Pfam; PF03872; RseA_N; 1. DR PIRSF; PIRSF016938; RseA; 1. DR SUPFAM; SSF89069; SSF89069; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Coiled coil; Complete proteome; KW Membrane; Reference proteome; Signal-anchor; Transcription; KW Transcription regulation; Transmembrane; Transmembrane helix. FT CHAIN 1 195 Anti-sigma-E factor RseA. FT /FTId=PRO_0000097482. FT TOPO_DOM 1 94 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 95 117 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 118 195 Periplasmic. {ECO:0000255}. FT COILED 160 181 {ECO:0000255}. FT SITE 148 149 Cleavage; by DegS. {ECO:0000250}. SQ SEQUENCE 195 AA; 21733 MW; 9BA4C6AA8F91CA0F CRC64; MQKEQLSAYM DGEQVETDLI DALLRDEELQ ASWHSFHTVR SVMRKESAVF LGADFTAKMA DLIELEDVKK VDVIAVSQPE PEDAHNSVFM QKLKAFFAPM TQVAVAAGVC LVAVLGVQSF NNKNDASNLP ETPVLQTLPF NNAVQEVSYN APSKDTLTSD QLEKKSRRIG AMLQNYELQR RMHSDALDVS SSQVR // ID RSEP_HAEIN Reviewed; 443 AA. AC P44936; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Regulator of sigma E protease; DE EC=3.4.24.-; DE AltName: Full=S2P endopeptidase; DE AltName: Full=Site-2 protease RseP; DE Short=S2P protease RseP; DE AltName: Full=Site-2-type intramembrane protease; GN Name=rsep; OrderedLocusNames=HI_0918; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A site-2 regulated intramembrane protease (S2P) that CC cleaves a peptide bond in the transmembrane region of RseA. Part CC of a regulated intramembrane proteolysis (RIP) cascade. Acts on CC DegS-cleaved RseA to release the cytoplasmic domain of RseA. This CC provides the cell with sigma-E (RpoE) activity through the CC proteolysis of RseA (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with RseA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- DOMAIN: The 2 circularly premutated PDZ domains act to negatively CC regulate protease action on intact RseA. {ECO:0000250}. CC -!- MISCELLANEOUS: Regulated intramembrane proteolysis (RIP) occurs CC when an extracytoplasmic signal triggers a concerted proteolytic CC cascade to transmit information and elicit cellular responses. A CC membrane-spanning regulatory substrate protein is first cut CC extracytoplasmically (site-1 protease, S1P), then within the CC membrane itself (site-2 protease, S2P, this enzyme), while CC cytoplasmic proteases finish degrading the regulatory protein, CC liberating the effector protein (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 PDZ (DHR) domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22576.1; -; Genomic_DNA. DR PIR; D64161; D64161. DR RefSeq; NP_439078.1; NC_000907.1. DR RefSeq; WP_005693265.1; NC_000907.1. DR ProteinModelPortal; P44936; -. DR STRING; 71421.HI0918; -. DR MEROPS; M50.004; -. DR EnsemblBacteria; AAC22576; AAC22576; HI_0918. DR GeneID; 949920; -. DR KEGG; hin:HI0918; -. DR PATRIC; 20190491; VBIHaeInf48452_0959. DR eggNOG; ENOG4105DZP; Bacteria. DR eggNOG; COG0750; LUCA. DR KO; K11749; -. DR OMA; QMIVGKR; -. DR OrthoDB; EOG66F07W; -. DR PhylomeDB; P44936; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 2.30.42.10; -; 2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR004387; Pept_M50_Zn. DR InterPro; IPR008915; Peptidase_M50. DR Pfam; PF02163; Peptidase_M50; 1. DR SMART; SM00228; PDZ; 2. DR SUPFAM; SSF50156; SSF50156; 2. DR TIGRFAMs; TIGR00054; TIGR00054; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 443 Regulator of sigma E protease. FT /FTId=PRO_0000088442. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 369 389 Helical. {ECO:0000255}. FT TRANSMEM 423 443 Helical. {ECO:0000255}. FT DOMAIN 106 185 PDZ 1. FT DOMAIN 198 287 PDZ 2. FT ACT_SITE 22 22 {ECO:0000255|PROSITE-ProRule:PRU10095}. FT METAL 21 21 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. FT METAL 25 25 Zinc; catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU10095}. SQ SEQUENCE 443 AA; 49070 MW; A4C98A2AD2B6BBBE CRC64; MSFLWSLGSF IIAIAVLVSV HEYGHFWAAR KCGIKVHRFS IGFGKVIWKR IDKYGTEFAV SMIPLGGYVK MLDGRNEVVP AEQKSQAFDS KSVLQRSFVI IAGPLANFIF AIFAYWVIYL YGMPTVKPVI ESITPNSIAA QAHIEPNTQI LTIDGEETQD WETINMLLAT KMGEPNVEIS LSPFNSNIEQ QRTLNLTNWT FDPEKESAFE ALGIMPMRPK IEMVLSKVVQ NSPAEKAGLQ IGDKILKENL TALPWQDFIK QVEQGESFSI KVERNGETFD KVLTPVRNQN GKWFVGVSPA LTKLADEYRT ELKYGILESL QKGIEKTGQL SLLTLKILGK LLTGDLSLNN LSGPISIAKG AGASANIGLV YFLSFMALIS VNLGIMNLFP LPVLDGGHLV FLTMEAVKGK PVSERVQSIC YRIGAALLLS LTVFALFNDF LRL // ID RSMD_HAEIN Reviewed; 193 AA. AC P44869; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Ribosomal RNA small subunit methyltransferase D; DE EC=2.1.1.171; DE AltName: Full=16S rRNA m2G966 methyltransferase; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase; GN Name=rsmD; OrderedLocusNames=HI_0767; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RG Northeast structural genomics consortium (NESG); RT "Crystal structure of the putative methylase HI0767 from Haemophilus RT influenzae."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Specifically methylates the guanine in position 966 of CC 16S rRNA in the assembled 30S particle. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(966) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(966) in 16S CC rRNA. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD 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; L42023; AAC22425.1; -; Genomic_DNA. DR PIR; F64158; F64158. DR RefSeq; NP_438926.1; NC_000907.1. DR RefSeq; WP_005693161.1; NC_000907.1. DR PDB; 2IFT; X-ray; 2.30 A; A/B=1-193. DR PDBsum; 2IFT; -. DR ProteinModelPortal; P44869; -. DR SMR; P44869; 35-193. DR STRING; 71421.HI0767; -. DR DNASU; 949786; -. DR EnsemblBacteria; AAC22425; AAC22425; HI_0767. DR GeneID; 949786; -. DR KEGG; hin:HI0767; -. DR PATRIC; 20190185; VBIHaeInf48452_0806. DR eggNOG; ENOG4106H78; Bacteria. DR eggNOG; COG0742; LUCA. DR KO; K08316; -. DR OMA; PHFDVVF; -. DR OrthoDB; EOG64XXSX; -. DR PhylomeDB; P44869; -. DR EvolutionaryTrace; P44869; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0052913; F:16S rRNA (guanine(966)-N(2))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004398; RNA_MeTrfase_RsmD. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF004553; CHP00095; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00095; TIGR00095; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 193 Ribosomal RNA small subunit FT methyltransferase D. FT /FTId=PRO_0000169550. FT STRAND 12 14 {ECO:0000244|PDB:2IFT}. FT TURN 19 22 {ECO:0000244|PDB:2IFT}. FT STRAND 24 26 {ECO:0000244|PDB:2IFT}. FT HELIX 39 52 {ECO:0000244|PDB:2IFT}. FT STRAND 56 59 {ECO:0000244|PDB:2IFT}. FT HELIX 66 73 {ECO:0000244|PDB:2IFT}. FT STRAND 77 82 {ECO:0000244|PDB:2IFT}. FT HELIX 86 98 {ECO:0000244|PDB:2IFT}. FT TURN 103 105 {ECO:0000244|PDB:2IFT}. FT STRAND 106 109 {ECO:0000244|PDB:2IFT}. FT HELIX 113 116 {ECO:0000244|PDB:2IFT}. FT STRAND 126 131 {ECO:0000244|PDB:2IFT}. FT STRAND 135 137 {ECO:0000244|PDB:2IFT}. FT HELIX 139 149 {ECO:0000244|PDB:2IFT}. FT STRAND 153 167 {ECO:0000244|PDB:2IFT}. FT STRAND 175 183 {ECO:0000244|PDB:2IFT}. FT STRAND 186 193 {ECO:0000244|PDB:2IFT}. SQ SEQUENCE 193 AA; 22001 MW; C0D6FC3CF0A831B7 CRC64; MKKIQTPNAK GEVRIIAGLW RGRKLPVLNS EGLRPTGDRV KETLFNWLMP YIHQSECLDG FAGSGSLGFE ALSRQAKKVT FLELDKTVAN QLKKNLQTLK CSSEQAEVIN QSSLDFLKQP QNQPHFDVVF LDPPFHFNLA EQAISLLCEN NWLKPNALIY VETEKDKPLI TPENWTLLKE KTTGIVSYRL YQN // ID RSMG_HAEIN Reviewed; 203 AA. AC P44728; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074}; DE EC=2.1.1.170 {ECO:0000255|HAMAP-Rule:MF_00074}; DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074}; GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; GN OrderedLocusNames=HI_0486; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the N7 position of guanine in CC position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(527) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(527) in 16S CC 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; L42023; AAC22146.1; -; Genomic_DNA. DR PIR; B64072; B64072. DR RefSeq; NP_438647.1; NC_000907.1. DR RefSeq; WP_005652031.1; NC_000907.1. DR ProteinModelPortal; P44728; -. DR STRING; 71421.HI0486; -. DR EnsemblBacteria; AAC22146; AAC22146; HI_0486. DR GeneID; 950623; -. DR KEGG; hin:HI0486; -. DR PATRIC; 20189527; VBIHaeInf48452_0506. DR eggNOG; ENOG4105D28; Bacteria. DR eggNOG; COG0357; LUCA. DR KO; K03501; -. DR OMA; MVKHILD; -. DR OrthoDB; EOG6HF639; -. DR PhylomeDB; P44728; -. DR Proteomes; UP000000579; 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 1 203 Ribosomal RNA small subunit FT methyltransferase G. FT /FTId=PRO_0000184259. FT REGION 124 125 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00074}. FT BINDING 73 73 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 78 78 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00074}. FT BINDING 139 139 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00074}. SQ SEQUENCE 203 AA; 23178 MW; 9D702411258A0604 CRC64; MKAKLVSLLA QANIKISDQQ IQQLINLVNL LNKWNKAYNL TSVRDPQEML VKHILDSLVV SPYLQGDRFI DVGTGPGLPG LPLAIINPSK QFVLLDSLGK RISFIRNAIR ELRLTNVTPV LSRVEEYQPE DKFDGVLSRA FASLKDMTDW CHHLPKENGY FYALKGIYQE DEINELNKKY TIQKVIELSV PELIGERHLI VLR // ID RS7_HAEIN Reviewed; 156 AA. AC P44376; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 95. 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=HI_0580; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22238.1; -; Genomic_DNA. DR PIR; G64078; G64078. DR RefSeq; NP_438738.1; NC_000907.1. DR RefSeq; WP_005626581.1; NC_000907.1. DR ProteinModelPortal; P44376; -. DR SMR; P44376; 3-154. DR STRING; 71421.HI0580; -. DR PRIDE; P44376; -. DR EnsemblBacteria; AAC22238; AAC22238; HI_0580. DR GeneID; 949475; -. DR KEGG; hin:HI0580; -. DR PATRIC; 20189717; VBIHaeInf48452_0601. DR eggNOG; ENOG4108UHY; Bacteria. DR eggNOG; COG0049; LUCA. DR KO; K02992; -. DR OMA; EVHRMAD; -. DR OrthoDB; EOG6P5ZKW; -. DR PhylomeDB; P44376; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.455.10; -; 1. DR HAMAP; MF_00480_B; Ribosomal_S7_B; 1. DR InterPro; IPR000235; Ribosomal_S5/S7. DR InterPro; IPR005717; Ribosomal_S7_bac/org-type. DR InterPro; IPR020606; Ribosomal_S7_CS. DR InterPro; IPR023798; Ribosomal_S7_dom. DR PANTHER; PTHR11205; PTHR11205; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; SSF47973; 1. DR TIGRFAMs; TIGR01029; rpsG_bact; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 156 30S ribosomal protein S7. FT /FTId=PRO_0000124271. SQ SEQUENCE 156 AA; 17543 MW; CB386422AFDFFBEE CRC64; MPRRRSVEAR KILPDPKFGS ELLAKFINVI MVDGKKSVAE SIVYGALETL AQRTGKEPLE AFEVALENVR PTVEVKSRRV GGSTYQVPVE VRPVRRNALG MRWIVEAARK RGDKSMALRL ANELSDASDN KGAAVKKRED VHRMAEANKA FAHYRW // ID RSMA_HAEIN Reviewed; 287 AA. AC P44749; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. 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=HI_0549; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22207.1; -; Genomic_DNA. DR PIR; I64076; I64076. DR RefSeq; NP_438707.1; NC_000907.1. DR RefSeq; WP_005649513.1; NC_000907.1. DR ProteinModelPortal; P44749; -. DR SMR; P44749; 17-272. DR STRING; 71421.HI0549; -. DR EnsemblBacteria; AAC22207; AAC22207; HI_0549. DR GeneID; 949586; -. DR KEGG; hin:HI0549; -. DR PATRIC; 20189653; VBIHaeInf48452_0569. DR eggNOG; ENOG4105D1X; Bacteria. DR eggNOG; COG0030; LUCA. DR KO; K02528; -. DR OMA; HYPGRLE; -. DR OrthoDB; EOG66F08Z; -. DR PhylomeDB; P44749; -. DR Proteomes; UP000000579; 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 1 287 Ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101538. FT BINDING 18 18 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 20 20 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 45 45 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 66 66 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 91 91 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. FT BINDING 118 118 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00607}. SQ SEQUENCE 287 AA; 32526 MW; EAB50E96E824E016 CRC64; MNSKKHLGHT ARKRFGQNFL HDTSVIQGIV AAIYPQPNQF LVEIGPGLGA LTEPVGELVD HLTVVELDRD LAERLRHHPF LHQKLTVIET DAMQFDFGAL YTKENLAEKG QKLRVFGNLP YNISTPLMFH LFKYHDVIQD MHFMLQKEVV KRLCAAPNSK AYGRLTIMAQ YFCQVMPVLE VPPSAFKPAP KVDSAVVRLI PHKELPHPVK DLYWLNRVCS QAFNQRRKTL RNALSTLFSP ENLTALGIDL NARAENLAIA DYARLANWLA DNPPADVNKD EILDSEE // ID RUVA_HAEIN Reviewed; 204 AA. AC P44632; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031}; GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; GN OrderedLocusNames=HI_0313; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21976.1; -; Genomic_DNA. DR PIR; C64061; C64061. DR RefSeq; NP_438479.1; NC_000907.1. DR RefSeq; WP_005694351.1; NC_000907.1. DR ProteinModelPortal; P44632; -. DR SMR; P44632; 1-141. DR STRING; 71421.HI0313; -. DR EnsemblBacteria; AAC21976; AAC21976; HI_0313. DR GeneID; 949429; -. DR KEGG; hin:HI0313; -. DR PATRIC; 20189167; VBIHaeInf48452_0330. DR eggNOG; ENOG4105KA4; Bacteria. DR eggNOG; COG0632; LUCA. DR KO; K03550; -. DR OMA; RNQETIF; -. DR OrthoDB; EOG679THG; -. DR PhylomeDB; P44632; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00031; DNA_helic_RuvA; 1. DR InterPro; IPR011114; DNA_helicas_Holl-junc_RuvA_C. DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000085; RuvA. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF07499; RuvA_C; 1. DR Pfam; PF01330; RuvA_N; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF46929; SSF46929; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00084; ruvA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome; SOS response. FT CHAIN 1 204 Holliday junction ATP-dependent DNA FT helicase RuvA. FT /FTId=PRO_0000094636. SQ SEQUENCE 204 AA; 22603 MW; 6BB6502656D65C07 CRC64; MIGRLQGILL EKQPPEILLN VQGVGYELLL PMTSFYDLPE IGQETTLFTH LVVREDAHLL FGFAQKTDRT LFRELIKTNG VGPKLALAIL SAMSVEQFAY AIEREELSKL TKIPGVGKKT AERLLVELKG KFKGVKQSDF FVESTHIPLS PSIESHSESS SDEAISALIA LGYKPVEAEK MVKRVAKPEL TSEQVIREAL KVAL // ID RSMB_HAEIN Reviewed; 451 AA. AC P44788; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=Ribosomal RNA small subunit methyltransferase B; DE EC=2.1.1.176; DE AltName: Full=16S rRNA m5C967 methyltransferase; DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB; GN Name=rsmB; Synonyms=rrmB, sun; OrderedLocusNames=HI_0624; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the cytosine at position 967 CC (m5C967) of 16S rRNA. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S CC rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S CC rRNA. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RsmB/NOP family. CC {ECO:0000255|PROSITE-ProRule:PRU01023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22284.1; -; Genomic_DNA. DR PIR; F64155; F64155. DR RefSeq; NP_438784.1; NC_000907.1. DR RefSeq; WP_005694643.1; NC_000907.1. DR ProteinModelPortal; P44788; -. DR SMR; P44788; 21-448. DR STRING; 71421.HI0624; -. DR EnsemblBacteria; AAC22284; AAC22284; HI_0624. DR GeneID; 949681; -. DR KEGG; hin:HI0624; -. DR PATRIC; 20189843; VBIHaeInf48452_0650. DR eggNOG; ENOG4105CYJ; Bacteria. DR eggNOG; COG0144; LUCA. DR KO; K03500; -. DR OMA; LRVNRQH; -. DR OrthoDB; EOG6091D0; -. DR PhylomeDB; P44788; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.940.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR006027; NusB_RsmB_TIM44. DR InterPro; IPR023267; RCMT. DR InterPro; IPR004573; rRNA_ssu_MeTfrase_B. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR Pfam; PF01029; NusB; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF48013; SSF48013; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00563; rsmB; 1. DR PROSITE; PS01153; NOL1_NOP2_SUN; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW Ribosome biogenesis; RNA-binding; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 451 Ribosomal RNA small subunit FT methyltransferase B. FT /FTId=PRO_0000211795. FT REGION 266 272 S-adenosyl-L-methionine binding. FT {ECO:0000255|PROSITE-ProRule:PRU01023}. FT ACT_SITE 392 392 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU01023}. FT BINDING 289 289 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01023}. FT BINDING 315 315 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01023}. FT BINDING 339 339 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01023}. SQ SEQUENCE 451 AA; 50598 MW; D91FAB88FFDE34B0 CRC64; MKKFSSKTIK AKNSVKMTAL STRAIAANLI LQVLDEGKSL SALIPEVQLS VKAQDLPLLQ EICFGVCRVL PRLEQIIKRL VDKPLKGKTR IVHCLLLVGL YQLLYMRVPA HAAVDEVVNA TKSLKSDSFR GLVNAVLRRF LREQDEILAI IDKNWQTLHP EWFVNKLKKA YPNWREIIEA NNQKPPMWLR VNSQKNALET YRTLLEEQGV SSKTSHHPNA LCLDIPIAVQ KLPHFEEGAV TVQDLSAQWA ATLLEPKNEE WILDACAAPG GKTTHILELA PQANVIALDV ESHRLKRVEE NLERLNQQAI VVCGDASKPD EWLAEIGKSA AKFDRILLDA PCSATGVIRR HPDIKWLRKE TDIAQLVELQ KKILSALWEK LKPNGVLLYA TCSVLPEENC EQIQAFLNAH ADAELLSLPF SDDKSAVGFQ FIPQPNSGDG FYYAKLLKRA S // ID RS8_HAEIN Reviewed; 130 AA. AC P44377; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 92. 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=HI_0792; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22450.1; -; Genomic_DNA. DR PIR; A64094; A64094. DR RefSeq; NP_438951.1; NC_000907.1. DR RefSeq; WP_005625877.1; NC_000907.1. DR ProteinModelPortal; P44377; -. DR SMR; P44377; 2-130. DR STRING; 71421.HI0792; -. DR PRIDE; P44377; -. DR EnsemblBacteria; AAC22450; AAC22450; HI_0792. DR GeneID; 25059372; -. DR GeneID; 949811; -. DR KEGG; hin:HI0792; -. DR PATRIC; 20190235; VBIHaeInf48452_0831. DR eggNOG; ENOG4108UJY; Bacteria. DR eggNOG; COG0096; LUCA. DR KO; K02994; -. DR OMA; RIYKNTR; -. DR OrthoDB; EOG6Z0QH1; -. DR PhylomeDB; P44377; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01302_B; Ribosomal_S8_B; 1. DR InterPro; IPR000630; Ribosomal_S8. DR PANTHER; PTHR11758; PTHR11758; 1. DR Pfam; PF00410; Ribosomal_S8; 1. DR SUPFAM; SSF56047; SSF56047; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 130 30S ribosomal protein S8. FT /FTId=PRO_0000126417. SQ SEQUENCE 130 AA; 13986 MW; A2A30923CAC559B9 CRC64; MSMQDPIADM LTRIRNGQAA NKVAINMPSS KLKVAIANVL AAEGYIESVK VLEGAKPELE ITLKYFQGKP VVESIQRVSR PGLRIYKRKD ELPKVMGGLG VAVISTSKGV MTDRAARQAG LGGEIICYVA // ID RSEB_HAEIN Reviewed; 315 AA. AC P44792; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Sigma-E factor regulatory protein RseB; DE Flags: Precursor; GN Name=rseB; OrderedLocusNames=HI_0630; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Negatively modulates the activity of sigma-E (RpoE) by CC stabilizing RseA under non-stress conditions. Although not CC essential for association of sigma-E with Rsea it increases their CC affinity 2- to 3-fold. When bound to RseA it prevents proteolysis CC by DegS, which is probably relieved by lipopolysaccharide binding CC (LPS) (By similarity). {ECO:0000250}. CC -!- ENZYME REGULATION: Binding to RseA is inhibited by LPS fragments; CC phosphorylated N-acetylglucosamine (GlcNAc) with N-linked acyl CC chains are minimally necessary to disrupt binding to RseA. Once CC RseB is no longer bound to RseA the latter is susceptible to DegS CC degradation. Thus if periplasmic LPS levels increase the sigma-E CC regulon is induced (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with RseA (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Partially CC associates with the inner membrane via RseA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RseB 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; L42023; AAC22290.1; -; Genomic_DNA. DR PIR; H64082; H64082. DR RefSeq; NP_438790.1; NC_000907.1. DR RefSeq; WP_005694646.1; NC_000907.1. DR ProteinModelPortal; P44792; -. DR STRING; 71421.HI0630; -. DR DNASU; 949706; -. DR EnsemblBacteria; AAC22290; AAC22290; HI_0630. DR GeneID; 949706; -. DR KEGG; hin:HI0630; -. DR PATRIC; 20189855; VBIHaeInf48452_0656. DR eggNOG; ENOG4105VQK; Bacteria. DR eggNOG; COG3026; LUCA. DR KO; K03598; -. DR OMA; DDFRYQY; -. DR OrthoDB; EOG6N0HP4; -. DR PhylomeDB; P44792; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR033436; MucB/RseB_C. DR InterPro; IPR033434; MucB/RseB_N. DR InterPro; IPR005588; MucB_RseB. DR Pfam; PF03888; MucB_RseB; 1. DR Pfam; PF17188; MucB_RseB_C; 1. DR PIRSF; PIRSF005427; RseB; 1. PE 3: Inferred from homology; KW Complete proteome; Lipid-binding; Periplasm; Reference proteome; KW Signal; Transcription; Transcription regulation. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 315 Sigma-E factor regulatory protein RseB. FT /FTId=PRO_0000022250. SQ SEQUENCE 315 AA; 35907 MW; 4FA6BC3FA76EB5CA CRC64; MKKIPLKFTA LSLSLLLSSI ASAEELSAKQ SLDKMTQALD NLNYEIAFVQ TTPANMDSFR YRHIKQDNKT YAQLVTLDGR QQEIIQRDNL VSYFQPNAQA FTLNSGNIVD AMPAVVRANF DKLSSDYDFV KLGKDRVAGR FADTIRIVPK DDFRYQYLVF IDEENGLLLR SDMLDREGKL LDQFRVVTLY IDDRLRGLTD YINKVSLPPL LKESKNEQSS DITWSAGWLP QGFSLIRYTQ EILENEIIDS ALYSDGLFTF TLFVSNVGSN DLPENTWKQG AYTIYSEVIG GKEITFIGQL PISTAKRIVQ EVKFR // ID RSME_HAEIN Reviewed; 245 AA. AC P44627; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Ribosomal RNA small subunit methyltransferase E; DE EC=2.1.1.193; DE AltName: Full=16S rRNA m3U1498 methyltransferase; GN Name=rsmE; OrderedLocusNames=HI_0303; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-245, AND IDENTIFICATION AS RP PUTATIVE RNA METHYLTRANSFERASE. RX PubMed=14517985; DOI=10.1002/prot.10510; RA Forouhar F., Shen J., Xiao R., Acton T.B., Montelione G.T., Tong L.; RT "Functional assignment based on structural analysis: crystal structure RT of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA RT methyltransferase with a deep trefoil knot."; RL Proteins 53:329-332(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-245. RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- FUNCTION: Specifically methylates the N3 position of the uracil CC ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully CC assembled 30S ribosomal subunit (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(1498) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(3)-methyluracil(1498) in 16S CC rRNA. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE 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; L42023; AAC21968.1; -; Genomic_DNA. DR PIR; D64147; D64147. DR RefSeq; NP_438470.1; NC_000907.1. DR RefSeq; WP_005694361.1; NC_000907.1. DR PDB; 1NXZ; X-ray; 2.00 A; A/B=2-245. DR PDB; 1VHY; X-ray; 1.90 A; A/B=2-245. DR PDBsum; 1NXZ; -. DR PDBsum; 1VHY; -. DR ProteinModelPortal; P44627; -. DR SMR; P44627; 2-245. DR STRING; 71421.HI0303; -. DR EnsemblBacteria; AAC21968; AAC21968; HI_0303. DR GeneID; 950245; -. DR KEGG; hin:HI0303; -. DR PATRIC; 20189147; VBIHaeInf48452_0320. DR eggNOG; ENOG4105QF0; Bacteria. DR eggNOG; COG1385; LUCA. DR KO; K09761; -. DR OMA; ERMEFTI; -. DR OrthoDB; EOG6FJNHQ; -. DR PhylomeDB; P44627; -. DR EvolutionaryTrace; P44627; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR006700; rRNA_ssu_MeTrfase-E. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF04452; Methyltrans_RNA; 1. DR PIRSF; PIRSF015601; MTase_slr0722; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00046; TIGR00046; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; rRNA processing; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 245 Ribosomal RNA small subunit FT methyltransferase E. FT /FTId=PRO_0000176202. FT STRAND 5 7 {ECO:0000244|PDB:1VHY}. FT STRAND 16 19 {ECO:0000244|PDB:1VHY}. FT HELIX 22 29 {ECO:0000244|PDB:1VHY}. FT STRAND 39 43 {ECO:0000244|PDB:1VHY}. FT STRAND 45 57 {ECO:0000244|PDB:1VHY}. FT STRAND 62 66 {ECO:0000244|PDB:1VHY}. FT STRAND 80 85 {ECO:0000244|PDB:1VHY}. FT STRAND 88 90 {ECO:0000244|PDB:1NXZ}. FT HELIX 93 101 {ECO:0000244|PDB:1VHY}. FT STRAND 106 111 {ECO:0000244|PDB:1VHY}. FT STRAND 115 117 {ECO:0000244|PDB:1VHY}. FT HELIX 121 142 {ECO:0000244|PDB:1VHY}. FT HELIX 156 160 {ECO:0000244|PDB:1VHY}. FT STRAND 167 171 {ECO:0000244|PDB:1VHY}. FT HELIX 179 181 {ECO:0000244|PDB:1VHY}. FT STRAND 190 194 {ECO:0000244|PDB:1VHY}. FT HELIX 202 210 {ECO:0000244|PDB:1VHY}. FT STRAND 214 217 {ECO:0000244|PDB:1VHY}. FT HELIX 225 239 {ECO:0000244|PDB:1VHY}. FT HELIX 242 244 {ECO:0000244|PDB:1VHY}. SQ SEQUENCE 245 AA; 27373 MW; 1F6BEA83A791328C CRC64; MRIPRIYHPI SLENQTQCYL SEDAANHVAR VLRMTEGEQL ELFDGSNHIY PAKIIESNKK SVKVEILGRE LADKESHLKI HLGQVISRGE RMEFTIQKSV ELGVNVITPL WSERCGVKLD AERMDKKIQQ WQKIAIAACE QCGRNIVPEI RPLMKLQDWC AENDGALKLN LHPRAHYSIK TLPTIPAGGV RLLIGSEGGL SAQEIAQTEQ QGFTEILLGK RVLRTETASL AAISALQICF GDLGE // ID RSMI_HAEIN Reviewed; 283 AA. AC P45298; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877}; DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877}; DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; GN OrderedLocusNames=HI_1654; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23298.1; -; Genomic_DNA. DR PIR; A64174; A64174. DR RefSeq; NP_439796.1; NC_000907.1. DR RefSeq; WP_005694380.1; NC_000907.1. DR ProteinModelPortal; P45298; -. DR STRING; 71421.HI1654; -. DR EnsemblBacteria; AAC23298; AAC23298; HI_1654. DR GeneID; 950491; -. DR KEGG; hin:HI1654; -. DR PATRIC; 20192057; VBIHaeInf48452_1732. DR eggNOG; ENOG4105CU0; Bacteria. DR eggNOG; COG0313; LUCA. DR KO; K07056; -. DR OMA; IALHDHN; -. DR OrthoDB; EOG6677TH; -. DR PhylomeDB; P45298; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I. DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR00096; TIGR00096; 1. DR PROSITE; PS01296; RSMI; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 283 Ribosomal RNA small subunit FT methyltransferase I. FT /FTId=PRO_0000211940. SQ SEQUENCE 283 AA; 31463 MW; 5348B41BE197F83C CRC64; MTDLTGILYI VATPIGNLQD ITQRALETFA QVDLIAAEDT RHSGLLLSHY GIKKPFFALH DHNEQEKAHI LVEKLKQGSN IALISDAGTP LISDPGFHLV RQCREAGIRV VPLPGACAAI TALCASGIAS DRFCFEGFLP AKSKARKDKL ENIAEEDRTL IFYESTHRIL DTLEDMQAVL GEERYIVLAR EMTKTWETIT GNTIKNLREW LLEDPNRTKG EMVLIVEGKP KSDNNDEISP QAVKALELIA EELPLKKAAA IVAELYGYKK NALYQFGLAH LEK // ID RSUA_HAEIN Reviewed; 232 AA. AC P45124; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Ribosomal small subunit pseudouridine synthase A; DE EC=5.4.99.19; DE AltName: Full=16S pseudouridylate 516 synthase; DE AltName: Full=16S rRNA pseudouridine(516) synthase; DE AltName: Full=rRNA pseudouridylate synthase A; DE AltName: Full=rRNA-uridine isomerase A; GN Name=rsuA; OrderedLocusNames=HI_1243; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS). RX PubMed=16511038; DOI=10.1107/S1744309105005920; RA Matte A., Louie G.V., Sivaraman J., Cygler M., Burley S.K.; RT "Structure of the pseudouridine synthase RsuA from Haemophilus RT influenzae."; RL Acta Crystallogr. F 61:350-354(2005). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 516 in 16S ribosomal RNA. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 16S rRNA uridine(516) = 16S rRNA CC pseudouridine(516). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA 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; L42023; AAC22895.1; -; Genomic_DNA. DR PIR; F64169; F64169. DR RefSeq; NP_439399.1; NC_000907.1. DR RefSeq; WP_005694303.1; NC_000907.1. DR PDB; 1VIO; X-ray; 1.59 A; A/B=2-232. DR PDBsum; 1VIO; -. DR ProteinModelPortal; P45124; -. DR SMR; P45124; 1-231. DR STRING; 71421.HI1243; -. DR EnsemblBacteria; AAC22895; AAC22895; HI_1243. DR GeneID; 950576; -. DR KEGG; hin:HI1243; -. DR PATRIC; 20191165; VBIHaeInf48452_1295. DR eggNOG; ENOG4105I08; Bacteria. DR eggNOG; COG1187; LUCA. DR KO; K06183; -. DR OMA; CTVTLHE; -. DR OrthoDB; EOG6130DV; -. DR PhylomeDB; P45124; -. DR EvolutionaryTrace; P45124; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central. DR Gene3D; 3.10.290.10; -; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F. DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR InterPro; IPR002942; S4_RNA-bd. DR Pfam; PF00849; PseudoU_synth_2; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00093; TIGR00093; 1. DR PROSITE; PS01149; PSI_RSU; 1. DR PROSITE; PS50889; S4; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome; KW RNA-binding; rRNA processing. FT CHAIN 1 232 Ribosomal small subunit pseudouridine FT synthase A. FT /FTId=PRO_0000099969. FT DOMAIN 1 68 S4 RNA-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00182}. FT ACT_SITE 102 102 Nucleophile. {ECO:0000250}. FT HELIX 3 11 {ECO:0000244|PDB:1VIO}. FT HELIX 15 23 {ECO:0000244|PDB:1VIO}. FT STRAND 27 29 {ECO:0000244|PDB:1VIO}. FT STRAND 47 49 {ECO:0000244|PDB:1VIO}. FT STRAND 62 67 {ECO:0000244|PDB:1VIO}. FT STRAND 72 74 {ECO:0000244|PDB:1VIO}. FT HELIX 83 86 {ECO:0000244|PDB:1VIO}. FT HELIX 91 94 {ECO:0000244|PDB:1VIO}. FT STRAND 96 99 {ECO:0000244|PDB:1VIO}. FT STRAND 106 113 {ECO:0000244|PDB:1VIO}. FT HELIX 115 122 {ECO:0000244|PDB:1VIO}. FT STRAND 130 138 {ECO:0000244|PDB:1VIO}. FT HELIX 144 150 {ECO:0000244|PDB:1VIO}. FT STRAND 165 168 {ECO:0000244|PDB:1VIO}. FT STRAND 170 179 {ECO:0000244|PDB:1VIO}. FT HELIX 185 192 {ECO:0000244|PDB:1VIO}. FT STRAND 197 205 {ECO:0000244|PDB:1VIO}. FT STRAND 219 221 {ECO:0000244|PDB:1VIO}. FT HELIX 224 229 {ECO:0000244|PDB:1VIO}. SQ SEQUENCE 232 AA; 26213 MW; E7590EE1A6BE8416 CRC64; MRLDKFIAEN VGLTRSQATK AIRQSAVKIN GEIVKSGSVQ ISQEDEIYFE DELLTWIEEG QYFMLNKPQG CVCSNDDGDY PTIYQFFDYP LAGKLHSAGR LDVDTTGLVL LTDDGQWSHR ITSPKHHCEK TYLVTLADPV EENYSAACAE GILLRGEKEP TKPAKLEILD DYNVNLTISE GRYHQVKRMF AALGNKVVGL HRWKIGDVVL DESLEEGEYR PLTQSEIEKL VK // ID RUVC_HAEIN Reviewed; 190 AA. AC P44633; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Crossover junction endodeoxyribonuclease RuvC; DE EC=3.1.22.4; DE AltName: Full=Holliday junction nuclease RuvC; DE AltName: Full=Holliday junction resolvase RuvC; GN Name=ruvC; OrderedLocusNames=HI_0314; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Nuclease that resolves Holliday junction intermediates CC in genetic recombination. Cleaves the cruciform structure in CC supercoiled DNA by nicking to strands with the same polarity at CC sites symmetrically opposed at the junction in the homologous arms CC and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl CC group (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at a junction such as CC a reciprocal single-stranded crossover between two homologous DNA CC duplexes (Holliday junction). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the RuvC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21978.1; -; Genomic_DNA. DR PIR; D64061; D64061. DR RefSeq; NP_438480.1; NC_000907.1. DR RefSeq; WP_005694350.1; NC_000907.1. DR ProteinModelPortal; P44633; -. DR SMR; P44633; 2-159. DR STRING; 71421.HI0314; -. DR EnsemblBacteria; AAC21978; AAC21978; HI_0314. DR GeneID; 949435; -. DR KEGG; hin:HI0314; -. DR PATRIC; 20189169; VBIHaeInf48452_0331. DR eggNOG; ENOG4105NHU; Bacteria. DR eggNOG; COG0817; LUCA. DR KO; K01159; -. DR OMA; ILHMIKL; -. DR OrthoDB; EOG6RG044; -. DR PhylomeDB; P44633; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central. DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central. DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00034; RuvC; 1. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR020563; X-over_junc_endoDNase_Mg_BS. DR InterPro; IPR002176; X-over_junc_endoDNase_RuvC. DR Pfam; PF02075; RuvC; 1. DR PRINTS; PR00696; RSOLVASERUVC. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00228; ruvC; 1. DR PROSITE; PS01321; RUVC; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 190 Crossover junction endodeoxyribonuclease FT RuvC. FT /FTId=PRO_0000183102. FT METAL 8 8 Magnesium. {ECO:0000250}. FT METAL 67 67 Magnesium. {ECO:0000250}. FT METAL 139 139 Magnesium. {ECO:0000250}. FT METAL 142 142 Magnesium. {ECO:0000250}. SQ SEQUENCE 190 AA; 20815 MW; 523AA38682784DFB CRC64; MSIILGIDPG SRVTGYGVIR QTGKHLEYLG SGAIRTQVED LPTRLKRIYA GVTEIITQFQ PNMFAIEQVF MAKNADSALK LGQARGTAIV AAVNNDLPVF EYAARLVKQT VVGIGSADKV QVQEMVTRIL KLSDKPQADA ADALAIAITH AHSIQHSLHI ANSVKMTETQ EKMTALLKTR YSRGRFRLKI // ID RS9_HAEIN Reviewed; 130 AA. AC P44388; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 93. DE RecName: Full=30S ribosomal protein S9; GN Name=rpsI; Synonyms=rps9; OrderedLocusNames=HI_1442; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23092.1; -; Genomic_DNA. DR PIR; F64123; F64123. DR RefSeq; NP_439594.1; NC_000907.1. DR RefSeq; WP_010869215.1; NC_000907.1. DR STRING; 71421.HI1442; -. DR EnsemblBacteria; AAC23092; AAC23092; HI_1442. DR GeneID; 950342; -. DR KEGG; hin:HI1442; -. DR PATRIC; 20191589; VBIHaeInf48452_1504. DR eggNOG; ENOG4108UJD; Bacteria. DR eggNOG; COG0103; LUCA. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR PhylomeDB; P44388; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000754; Ribosomal_S9. DR InterPro; IPR023035; Ribosomal_S9_bac/plastid. DR InterPro; IPR020574; Ribosomal_S9_CS. DR PANTHER; PTHR21569; PTHR21569; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 130 30S ribosomal protein S9. FT /FTId=PRO_0000111361. SQ SEQUENCE 130 AA; 14697 MW; BE4C393E41DE13CA CRC64; MAENQNYGTG RRKSSSARVF IKPGSGKITI NQRELDVYFG RETARMVVRQ PLELVXLTDK LDLYITVKGG GISGQAGAIR HGITRALMEY DETLRPALRA AGFVTRDARR VERKKVGLHK ARRRPQYSKR // ID RSGA_HAEIN Reviewed; 346 AA. AC P45339; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. 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=HI_1714; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23359.1; -; Genomic_DNA. DR PIR; B64176; B64176. DR RefSeq; NP_439856.1; NC_000907.1. DR RefSeq; WP_005694198.1; NC_000907.1. DR ProteinModelPortal; P45339; -. DR SMR; P45339; 36-335. DR STRING; 71421.HI1714; -. DR EnsemblBacteria; AAC23359; AAC23359; HI_1714. DR GeneID; 950871; -. DR KEGG; hin:HI1714; -. DR PATRIC; 20192179; VBIHaeInf48452_1793. DR eggNOG; ENOG4105E06; Bacteria. DR eggNOG; COG1162; LUCA. DR KO; K06949; -. DR OMA; TARLFHF; -. DR OrthoDB; EOG69SKDD; -. DR PhylomeDB; P45339; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA. DR InterPro; IPR010914; RsgA_GTPase_dom. DR 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 1 346 Putative ribosome biogenesis GTPase RsgA. FT /FTId=PRO_0000171480. FT DOMAIN 103 271 CP-type G. FT NP_BIND 159 162 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT NP_BIND 213 221 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}. FT MOTIF 295 308 Knuckle-like cysteine cluster. FT METAL 295 295 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 300 300 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 302 302 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. FT METAL 308 308 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}. SQ SEQUENCE 346 AA; 38886 MW; A0D1F57D4EEC58A1 CRC64; MAKRKLTQNQ TRRIQSNNAK TLHRHKKKEI EWSDEMLGES QEGVVVTRYS IHADVENEQG EIYRCNLRRT LSSLVVGDKV VWRKGNEQLQ GVSGVIEAIH PRENEISRPD YYDGLKPIAA NIDRIIIVSA VLPTLSLNII DRYLVVCEIA GITPLIVLNK VDLLAQEQRQ EIEDQLKIYQ DIGYEILMIS AKSGENMEKL TALLAQGTAI FVGQSGVGKS SLINHILPSV NAQVGDVSET SGLGQHTTTS SRLYHLPQGG NLIDSPGIRE FGLWHLDAEQ ITKGYREFQY VLGTCKFRDC KHLSDPGCAL REAVEQGKIS PVRYDNYHRL IESLSETKSQ RHFSLV // ID RSMJ_HAEIN Reviewed; 257 AA. AC P44901; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 11-NOV-2015, entry version 81. DE RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523}; DE EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523}; DE AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523}; DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523}; GN Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; GN OrderedLocusNames=HI_0849; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates the guanosine in position 1516 CC of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(1516) in 16S CC rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1516) in 16S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ CC family. {ECO:0000255|HAMAP-Rule:MF_01523}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22506.1; 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; L42023; AAC22506.1; ALT_INIT; Genomic_DNA. DR PIR; I64159; I64159. DR RefSeq; NP_439009.1; NC_000907.1. DR RefSeq; WP_005693198.1; NC_000907.1. DR ProteinModelPortal; P44901; -. DR SMR; P44901; 11-253. DR STRING; 71421.HI0849m; -. DR DNASU; 949861; -. DR EnsemblBacteria; AAC22506; AAC22506; HI_0849. DR GeneID; 949861; -. DR KEGG; hin:HI0849m; -. DR PATRIC; 20190353; VBIHaeInf48452_0890. DR eggNOG; ENOG4105FFN; Bacteria. DR eggNOG; ENOG410XPRJ; LUCA. DR KO; K15984; -. DR OMA; SSRYDIY; -. DR OrthoDB; EOG657J92; -. DR PhylomeDB; P44901; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01523; 16SrRNA_methyltr_J; 1. DR InterPro; IPR007536; 16SrRNA_methylTrfase_J. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF04445; SAM_MT; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 257 Ribosomal RNA small subunit FT methyltransferase J. FT /FTId=PRO_0000212069. FT REGION 107 108 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01523}. FT REGION 123 124 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01523}. FT BINDING 177 177 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01523}. SQ SEQUENCE 257 AA; 28549 MW; 7B63FEF72989D941 CRC64; MAHSQVGIQL ISESTEKTLA ELIALCAEHN IIHNEKSPLA LVQTDDRLEL RKLDEPKLGA VYVDFVGGTM AHRRKFGGGR GEAVAKAVGI KGSALPTVID ATAGLGRDAF VLAAIGCQVR LVERHPVVFL LLQDGLNRAY QDEEIGEMLQ QNLHLLNVQH INELDPNSDY ADVVYLDPMY PHKQKSALVK KEMRVFQHLV GADLDADELL LPALQLAKKR VVVKRPDYAE FLCGKQPHFS HETKNHRFDI YMGASQC // ID RUVB_HAEIN Reviewed; 335 AA. AC P44631; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016}; GN Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; GN OrderedLocusNames=HI_0312; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21975.1; -; Genomic_DNA. DR PIR; B64061; B64061. DR RefSeq; NP_438478.1; NC_000907.1. DR RefSeq; WP_005694352.1; NC_000907.1. DR ProteinModelPortal; P44631; -. DR SMR; P44631; 22-332. DR STRING; 71421.HI0312; -. DR EnsemblBacteria; AAC21975; AAC21975; HI_0312. DR GeneID; 950827; -. DR KEGG; hin:HI0312; -. DR PATRIC; 20189165; VBIHaeInf48452_0329. DR eggNOG; ENOG4105CKJ; Bacteria. DR eggNOG; COG2255; LUCA. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR PhylomeDB; P44631; -. DR Proteomes; UP000000579; 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 1 335 Holliday junction ATP-dependent DNA FT helicase RuvB. FT /FTId=PRO_0000165537. FT NP_BIND 62 69 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. SQ SEQUENCE 335 AA; 37018 MW; B7D7F71A03E9CDA6 CRC64; MIEADRIISG QAKVDEDVID RAIRPKLLAD YVGQPQVREQ MDIFIKAAKL RQDALDHLLI FGPPGLGKTT LANIVANEMG VNIRTTSGPV LEKAGDLAAM LTNLEPHDVL FIDEIHRLSP AIEEVLYPAM EDYQLDIMIG EGPAARSIKL DLPPFTLVGA TTRAGSLTSP LRDRFGIVQR LEFYSVEDLT SIVARSAGCL NLELEQQAAF EVARRSRGTP RIANRLLRRV RDYADVRNGG IISINVAKQA LSMLDVDDAG FDYLDRKLLS AVIERFDGGP VGLDNLAAAI GEERDTIEDV LEPYLIQQGF LQRTPRGRIA TSQTYRHFGL QKLSD // ID SAPA_HAEIN Reviewed; 565 AA. AC P45285; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Peptide transport periplasmic protein SapA; DE Flags: Precursor; GN Name=sapA; OrderedLocusNames=HI_1638; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a peptide intake transport system that plays CC a role in the resistance to antimicrobial peptides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 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; L42023; AAC23285.1; -; Genomic_DNA. DR PIR; A64134; A64134. DR RefSeq; NP_439780.1; NC_000907.1. DR RefSeq; WP_005693646.1; NC_000907.1. DR ProteinModelPortal; P45285; -. DR STRING; 71421.HI1638; -. DR EnsemblBacteria; AAC23285; AAC23285; HI_1638. DR GeneID; 950479; -. DR KEGG; hin:HI1638; -. DR PATRIC; 20192021; VBIHaeInf48452_1714. DR eggNOG; ENOG4108EVY; Bacteria. DR eggNOG; COG4166; LUCA. DR KO; K19226; -. DR OMA; AQLDTHP; -. DR OrthoDB; EOG63C0PB; -. DR PhylomeDB; P45285; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 3: Inferred from homology; KW Complete proteome; Peptide transport; Periplasm; Protein transport; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 565 Peptide transport periplasmic protein FT SapA. FT /FTId=PRO_0000031803. SQ SEQUENCE 565 AA; 64504 MW; 449E454F1278C2A7 CRC64; MLRLNLRFLS FLLCIIQSVE LQAAPSVPTF LTENGLTYCT HASGFSFNPQ TADAGTSMNV VTEQIYNKLF DIKNHSATLT PMLAQSYSIS ADGKEILLNL RHGVKFHQTP WFTPTRDFNA EDVVFSINRV LGGHNTYLPT LAETNVTYSN PQYRVFHEQA RKVRFPYFDS IKLNEKIKSV TALSPYQVKI ELFAPDSSIL SHLASQYAII FSQEYAYQLS ADDNLAQLDT HPVGTGPYQV KDYVYNQYVR LVRNENYWKK EAKIEHIIVD LSTDRSGRLV KFFNNECQIA SYPEVSQIGL LKNDDKHYYM QSTDGMNLAY LAFNFDKPLM RDHEIRAAIS QSLNRARIIH SIYHNTATVA NNIIPEVSWA SSVNTPEFEF DYNPKIAKNK LADKNLLLNL WVINEEQVYN PAPFKIAEMI KWDLAQAGVK VKVRAVTRPF LTAQLRNQSE NYDLILSGWL AGNLDPDGFM RPILSCGTKN ELTNLSNWCN EEFDQFMDRA ITTSHLSSRA KAYNEAQELV LRELPIIPIA NVKRILVANS RVKGVKMTPF GSLDFSTLYF IQEKY // ID SDAC_HAEIN Reviewed; 412 AA. AC P44615; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Serine transporter; GN Name=sdaC; OrderedLocusNames=HI_0289; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the import of serine into the cell. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 CC family. SdaC/TdcC 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; L42023; AAC21954.1; -; Genomic_DNA. DR PIR; G64059; G64059. DR RefSeq; NP_438456.1; NC_000907.1. DR RefSeq; WP_005666700.1; NC_000907.1. DR STRING; 71421.HI0289; -. DR EnsemblBacteria; AAC21954; AAC21954; HI_0289. DR GeneID; 950177; -. DR KEGG; hin:HI0289; -. DR PATRIC; 20189117; VBIHaeInf48452_0305. DR eggNOG; ENOG4105C44; Bacteria. DR eggNOG; COG0814; LUCA. DR KO; K03837; -. DR OMA; NVHDSGF; -. DR OrthoDB; EOG6X10TH; -. DR PhylomeDB; P44615; -. DR Proteomes; UP000000579; 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:0003333; P:amino acid transmembrane transport; IEA:InterPro. DR InterPro; IPR004694; Hydroxy_aa_transpt. DR InterPro; IPR018227; Tryptophan/tyrosine_permease. DR Pfam; PF03222; Trp_Tyr_perm; 1. DR TIGRFAMs; TIGR00814; stp; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 412 Serine transporter. FT /FTId=PRO_0000093810. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 338 358 Helical. {ECO:0000255}. FT TRANSMEM 361 381 Helical. {ECO:0000255}. FT TRANSMEM 391 411 Helical. {ECO:0000255}. SQ SEQUENCE 412 AA; 45895 MW; 147C1DA2E9099008 CRC64; MKSTEKLKWN KFDATWMLNL FGTAVGAGVL FLPINAGMGG FWPLVLMAII VGPMTYFAHR GLAYFVLSSK NPGSDITEVV EEHFGKTAGK LITLLYFFAI FPILLIYGNG ITNTVDSFIV NQLGMASPNR VILSFVLIAV LISVMLFNEK VMLKITEWLV YPLVLILFVL SIYLIPEWNS AVLYEFPTVG GFLTTLWLTI PVLVFSFNHS PAISSFTCSQ FREYKTFDGA ERHISHTEKG ASTILLFFVM FFVFSCVLTL TPEELVAAKE QNISILSFLA NKFDNPYISY FGPLVAFLAI TSSFFGHYMG AREGLEGLYL KMKGEAVNRK KLNYATALFF LLTLWGVAII NPSILGLIES LGGPIIAMIL FIMPMYAIRK IPAMKRYSGR FSNVFVTIMG LIAISAVVYG LL // ID SANA_HAEIN Reviewed; 244 AA. AC P45130; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Protein SanA homolog; GN Name=sanA; OrderedLocusNames=HI_1262; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Participates in the barrier function of the cell CC envelope. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane CC protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22915.1; -; Genomic_DNA. DR PIR; H64169; H64169. DR RefSeq; NP_439417.2; NC_000907.1. DR STRING; 71421.HI1262; -. DR EnsemblBacteria; AAC22915; AAC22915; HI_1262. DR GeneID; 950206; -. DR KEGG; hin:HI1262; -. DR PATRIC; 20191205; VBIHaeInf48452_1314. DR eggNOG; ENOG4107GZ4; Bacteria. DR eggNOG; COG2949; LUCA. DR KO; K03748; -. DR OMA; DNAQQSY; -. DR OrthoDB; EOG6WMJ3Z; -. DR Proteomes; UP000000579; 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; IPR003848; DUF218. DR Pfam; PF02698; DUF218; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 244 Protein SanA homolog. FT /FTId=PRO_0000097580. FT TOPO_DOM 1 31 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TOPO_DOM 53 244 Periplasmic. {ECO:0000255}. SQ SEQUENCE 244 AA; 28188 MW; 23852BB32FFB9696 CRC64; MRFTKSIKFS LKCGRFFIMF TTMLVKKFSP KFTALFRTLL YAIFALIILC LLVDRGISFY VRDKIFTNID ELPFRPCALV LGTSKYTVSG KPNVYYDSRL MAAKSLIEQQ KVNYLLLSGD NRTLQYNEPR AMFRDLRKMG VPKTLMFRDF AGFRTLDSVI RADKIFQVKT FTIVSQKFHC ERALLIAQAH NIDAICFVAK QPELHFSTQI REVFARIKAV FDLILGVEPY FLGEPQPLPN STTL // ID SAPB_HAEIN Reviewed; 321 AA. AC P45286; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Peptide transport system permease protein SapB; GN Name=sapB; OrderedLocusNames=HI_1639; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a peptide intake transport system that plays CC a role in the resistance to antimicrobial peptides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC23286.1; -; Genomic_DNA. DR PIR; B64134; B64134. DR RefSeq; NP_439781.1; NC_000907.1. DR RefSeq; WP_005693647.1; NC_000907.1. DR STRING; 71421.HI1639; -. DR EnsemblBacteria; AAC23286; AAC23286; HI_1639. DR GeneID; 950849; -. DR KEGG; hin:HI1639; -. DR PATRIC; 20192023; VBIHaeInf48452_1715. DR eggNOG; COG4168; LUCA. DR KO; K19227; -. DR OMA; EMITEVV; -. DR OrthoDB; EOG66F098; -. DR PhylomeDB; P45286; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0042936; F:dipeptide transporter activity; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042938; P:dipeptide transport; IBA:GOC. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 2. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 321 Peptide transport system permease protein FT SapB. FT /FTId=PRO_0000060162. FT TRANSMEM 8 28 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 41 61 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 82 102 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 117 137 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 150 170 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 180 200 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 249 269 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 289 309 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 75 303 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 321 AA; 36529 MW; 369BF447BD34C782 CRC64; MLWSVLRHIL WVALLLLVLS LLGFVILLRD PLNANLVTQN IYIGYFHYLG TLLQGDFGIT YNGGKSLMNL ILTVLPPTLE LCFITLFLAF IFGLPLGIIS AVNSEQVFAK SLQILSYVGL SIPIFWLAPI LLYVAALSHW EIAAIGQYNL LYEIKSITGF PVIDMWFMEV PYRTKIVQNI LQHLALPTLV LCILPTMEII RIIHQRAEYI LNQNFSKVAT TRGWSKWKIL HQYVFRNTFP LLVPQVPRVF TLVLTQCMLV ETALGWPGIG RWLINAVNEQ DYNSIAAGVI VIGVCIILID TFTKIFTFIL DPFKKKGWYA K // ID SAPF_HAEIN Reviewed; 269 AA. AC P45289; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Peptide transport system ATP-binding protein SapF; GN Name=sapF; OrderedLocusNames=HI_1642; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a peptide intake transport system that plays CC a role in the resistance to antimicrobial peptides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC23289.1; -; Genomic_DNA. DR PIR; E64134; E64134. DR RefSeq; NP_439784.1; NC_000907.1. DR RefSeq; WP_005670537.1; NC_000907.1. DR ProteinModelPortal; P45289; -. DR STRING; 71421.HI1642; -. DR EnsemblBacteria; AAC23289; AAC23289; HI_1642. DR GeneID; 950853; -. DR KEGG; hin:HI1642; -. DR PATRIC; 20192029; VBIHaeInf48452_1718. DR eggNOG; COG4167; LUCA. DR KO; K19230; -. DR OMA; SRAKHIR; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45289; -. DR Proteomes; UP000000579; 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; 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; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 269 Peptide transport system ATP-binding FT protein SapF. FT /FTId=PRO_0000092972. FT DOMAIN 4 249 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 45 52 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 269 AA; 30295 MW; E5C044EECBDE801F CRC64; MPLLQVEDLT KTFKGHASLF GRNQFNAVDK VSFTLERKQT LAIIGNNGSG KSTLVKMIAG IIPPTSGRIL FNDRELQYQD AQSRAKHIRM VFQDANSAFN PRLNIGQILD EPLSLATDWT ETQRNEKIFE TLSLVGLYPD YTNLNIKHLS ISQKQRVALA RALILEPEII IIDDAIGNLD ASVRIQLLNL TLDLQQRLGI SYIYVGQDLG VIKHIADTII VMDEGKMIEY GSPQNLFTDP QTDVTRRLVE SYFGKILDET AWVKDKNAH // ID SECA_HAEIN Reviewed; 901 AA. AC P43803; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=HI_0909; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 875-901 IN COMPLEX WITH SECB, RP MUTAGENESIS OF ARG-878; ASN-879; LYS-888; LYS-889 AND LYS-891, AND RP COFACTOR. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=14517549; DOI=10.1038/nsb980; RA Zhou J., Xu Z.; RT "Structural determinants of SecB recognition by SecA in bacterial RT protein translocation."; RL Nat. Struct. Biol. 10:942-947(2003). 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 both as a receptor for the CC preprotein-SecB complex and as an ATP-driven molecular motor CC driving the stepwise translocation of polypeptide chains across CC the membrane. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:14517549}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14517549}; CC -!- SUBUNIT: Monomer and homodimer (By similarity). Part of the CC essential Sec protein translocation apparatus which comprises CC SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC (By CC similarity). Forms a complex with SecB. {ECO:0000255|HAMAP- CC Rule:MF_01382, ECO:0000269|PubMed:14517549}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. CC Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}. CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP- CC Rule:MF_01382}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22566.1; -; Genomic_DNA. DR PIR; H64101; H64101. DR RefSeq; NP_439069.1; NC_000907.1. DR RefSeq; WP_005693259.1; NC_000907.1. DR PDB; 1OZB; X-ray; 2.80 A; I/J=875-901. DR PDBsum; 1OZB; -. DR ProteinModelPortal; P43803; -. DR SMR; P43803; 7-834. DR IntAct; P43803; 1. DR STRING; 71421.HI0909; -. DR EnsemblBacteria; AAC22566; AAC22566; HI_0909. DR GeneID; 949911; -. DR KEGG; hin:HI0909; -. DR PATRIC; 20190473; VBIHaeInf48452_0950. DR eggNOG; ENOG4105CI6; Bacteria. DR eggNOG; COG0653; LUCA. DR KO; K03070; -. DR OMA; IATERHE; -. DR OrthoDB; EOG654P48; -. DR PhylomeDB; P43803; -. DR EvolutionaryTrace; P43803; -. DR Proteomes; UP000000579; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR004027; SEC_C_motif. 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; PF02810; SEC-C; 1. DR Pfam; PF07517; SecA_DEAD; 1. DR Pfam; PF01043; SecA_PP_bind; 1. DR Pfam; PF07516; SecA_SW; 1. DR PRINTS; PR00906; SECA. DR SMART; SM00957; SecA_DEAD; 1. DR SMART; SM00958; SecA_PP_bind; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF81767; SSF81767; 1. DR SUPFAM; SSF81886; SSF81886; 2. DR TIGRFAMs; TIGR00963; secA; 1. DR PROSITE; PS01312; SECA; 1. DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Cytoplasm; Membrane; Metal-binding; KW Nucleotide-binding; Protein transport; Reference proteome; KW Translocation; Transport; Zinc. FT CHAIN 1 901 Protein translocase subunit SecA. FT /FTId=PRO_0000109586. FT NP_BIND 100 107 ATP. {ECO:0000255|HAMAP-Rule:MF_01382}. FT METAL 882 882 Zinc. FT METAL 884 884 Zinc. FT METAL 893 893 Zinc. FT METAL 894 894 Zinc. FT MUTAGEN 878 878 R->A: Binds zinc, unable to bind secB. FT {ECO:0000269|PubMed:14517549}. FT MUTAGEN 879 879 N->A: Binds zinc, unable to bind secB. FT {ECO:0000269|PubMed:14517549}. FT MUTAGEN 888 888 K->A: Binds zinc, still binds secB. FT {ECO:0000269|PubMed:14517549}. FT MUTAGEN 889 889 K->A: Binds zinc, unable to bind secB. FT {ECO:0000269|PubMed:14517549}. FT MUTAGEN 891 891 K->A: Binds zinc, unable to bind secB. FT {ECO:0000269|PubMed:14517549}. FT STRAND 887 889 {ECO:0000244|PDB:1OZB}. FT HELIX 890 892 {ECO:0000244|PDB:1OZB}. FT TURN 893 895 {ECO:0000244|PDB:1OZB}. SQ SEQUENCE 901 AA; 102587 MW; 2BD0190266BD77AE CRC64; MSILTRIFGS RNERVLRKLK KQVVKINKME PAFEALSDDE LKAKTQEFRD RLSGGETLQQ ILPEAFATVR EASKRVLGMR HFDVQLIGGM VLTNRCIAEM RTGEGKTLTA TLPCYLIALE GKGVHVVTVN DYLARRDAET NRPLFEFLGM SVGVNIPGLS PEEKRAAYAA DITYATNSEL GFDYLRDNLA HSKEERFQRT LGYALVDEVD SILIDEARTP LIISGQAENS SELYIAVNKL IPSLIKQEKE DTEEYQGEGD FTLDLKSKQA HLTERGQEKV EDWLIAQGLM PEGDSLYSPS RIVLLHHVMA ALRAHTLFEK DVDYIVKDGE IVIVDEHTGR TMAGRRWSDG LHQAIEAKEG VDVKSENQTV ASISYQNYFR LYERLAGMTG TADTEAFEFQ QIYGLETVVI PTNRPMIRDD RTDVMFENEQ YKFNAIIEDI KDCVERQQPV LVGTISVEKS EELSKALDKA GIKHNVLNAK FHQQEAEIVA EAGFPSAVTI ATNMAGRGTD IILGGNWKAQ AAKLENPTQE QIEALKAEWE KNHEIVMKAG GLHIIGTERH ESRRIDNQLR GRSGRQGDPG SSRFYLSLED GLMRIYLNEG KLNLMRKAFT VAGEAMESKM LAKVIASAQA KVEAFHFDGR KNLLEYDDVA NDQRHAIYEQ RNHLLDNDDI SETINAIRHD VFNGVIDQYI PPQSLEEQWD IKGLEERLSQ EFGMELPISN WLEEDNNLHE ESLRERIVEI AEKEYKEKEA LVGEDAMRHF EKGVMLQTLD ELWKEHLASM DYLRQGIHLR GYAQKDPKQE YKKESFRMFT EMLDSLKHQV ITALTRVRVR TQEEMEEAER ARQEMAARIN QNNLPVDENS QTTQNSETED YSDRRIGRNE PCPCGSGKKY KHCHGSRVAR Q // ID SECY_HAEIN Reviewed; 441 AA. AC P43804; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; GN OrderedLocusNames=HI_0798; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner 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; L42023; AAC22456.1; -; Genomic_DNA. DR PIR; G64094; G64094. DR RefSeq; NP_438957.1; NC_000907.1. DR RefSeq; WP_005652382.1; NC_000907.1. DR ProteinModelPortal; P43804; -. DR STRING; 71421.HI0798; -. DR EnsemblBacteria; AAC22456; AAC22456; HI_0798. DR GeneID; 949574; -. DR KEGG; hin:HI0798; -. DR PATRIC; 20190247; VBIHaeInf48452_0837. DR eggNOG; ENOG4105CGG; Bacteria. DR eggNOG; COG0201; LUCA. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR PhylomeDB; P43804; -. DR Proteomes; UP000000579; 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 inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 441 Protein translocase subunit SecY. FT /FTId=PRO_0000131724. FT TRANSMEM 24 44 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 77 97 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 123 143 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 152 172 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 181 201 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 215 235 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 272 292 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 313 333 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 373 393 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. FT TRANSMEM 397 417 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01465}. SQ SEQUENCE 441 AA; 48290 MW; 246467E7F0062DF3 CRC64; MAKQPGYQAR STNSGKGELK SRLLFVLGAL IVYRIGSFIP VPGIDAAVLA QLVEQQKGTI IDMFNMFSGG ALSRASILAL GIMPYISASI VIQLLATVSP ALAELKKEGA AGQRKISKYT RYATVVFATI QAVAISTGLP NMLSGLVPNV GFSFYFTSVV SLVTGTMFLM WLGEQITERG IGNGISILVF GGIVAGLPSA ILQTIEQARQ GQMHPLVLLL IAAIVFAVTY FVVFVERGQR RIRVEYAKRQ QGRQILGGHS THLPLKVNMA NVMPAIFASS IILFPATLTQ WFGQNDKFEW LNNLSMLLNP GQPLYLLVYA VAIIFFSFFY TAMQYNPRDT ADNLKKSGAF IPGIRPGEQT SRYIDKVMTR LTLIGGLYVT FVCLVPYIMT SAWDVKFYFG GTSLLIVVVV IMDFIVQVQS HLMSSQYESA LKKANLKGFG Q // ID SAPC_HAEIN Reviewed; 295 AA. AC P45287; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Peptide transport system permease protein SapC; GN Name=sapC; OrderedLocusNames=HI_1640; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a peptide intake transport system that plays CC a role in the resistance to antimicrobial peptides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC23287.1; -; Genomic_DNA. DR PIR; C64134; C64134. DR RefSeq; NP_439782.1; NC_000907.1. DR RefSeq; WP_005693648.1; NC_000907.1. DR STRING; 71421.HI1640; -. DR EnsemblBacteria; AAC23287; AAC23287; HI_1640. DR GeneID; 950835; -. DR KEGG; hin:HI1640; -. DR PATRIC; 20192025; VBIHaeInf48452_1716. DR eggNOG; ENOG4108EU3; Bacteria. DR eggNOG; COG4171; LUCA. DR KO; K19228; -. DR OMA; QLTHAML; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45287; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. 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 inner membrane; Cell membrane; Complete proteome; Membrane; KW Peptide transport; Protein transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 295 Peptide transport system permease protein FT SapC. FT /FTId=PRO_0000060168. FT TRANSMEM 27 47 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 102 122 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 129 149 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 157 177 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 219 239 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 262 282 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 98 278 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 295 AA; 33014 MW; FA57161321F4120F CRC64; MQNKEPDEFR ESTSIFQIWL RFRQNTIALF SFYLLIALIF TALFASYLAP YADNRQFIGQ ELMPPSWVDR GKIAFFFGTD DLGRDILSRL IMGTRYTLGS ALLVVFSVAI IGGALGIIAG LLKGIKARFV GHIFDAFLSL PILLIAVVIS TLMEPSLWNA MFATLLAILP YFIHTIYRAI QKELEKDYVV MLKLEGISNQ ALLKSTILPN ITVIYIQEVA RAFVIAVLDI SALSFISLGA QRPTPEWGAM IKDSLELLYL APWTVLLPGF AIIFTILLSI IFSNGLTKAI NQHQE // ID SAPD_HAEIN Reviewed; 349 AA. AC P45288; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Peptide transport system ATP-binding protein SapD; GN Name=sapD; OrderedLocusNames=HI_1641; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in a peptide intake transport system that plays CC a role in the resistance to antimicrobial peptides. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC23288.1; -; Genomic_DNA. DR PIR; D64134; D64134. DR RefSeq; NP_439783.1; NC_000907.1. DR RefSeq; WP_005693649.1; NC_000907.1. DR ProteinModelPortal; P45288; -. DR STRING; 71421.HI1641; -. DR EnsemblBacteria; AAC23288; AAC23288; HI_1641. DR GeneID; 950483; -. DR KEGG; hin:HI1641; -. DR PATRIC; 20192027; VBIHaeInf48452_1717. DR eggNOG; ENOG4108JQ3; Bacteria. DR eggNOG; COG4170; LUCA. DR KO; K19229; -. DR OMA; IASMSHS; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; P45288; -. DR Proteomes; UP000000579; 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; IPR013563; Oligopep_ABC_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF08352; oligo_HPY; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01727; oligo_HPY; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Transport. FT CHAIN 1 349 Peptide transport system ATP-binding FT protein SapD. FT /FTId=PRO_0000092967. FT DOMAIN 1 259 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 349 AA; 39478 MW; 25FD3241F1570D7A CRC64; MALLDICNLN IEIQTSNGRI KIVDGVNLSL NEGEISGLVG ESGSGKSLIA KVICNAIKEN WIITADRFRF HDVELLKLSP NKRRKLVGKE ISMIFQNPLS CLDPSRKIGK QLIQNIPNWT FKNKWWKWFG WKKRRAIELL HRVGIKDHRD IMASYPNELT EGEGQKVMIA MAVANQPRLL IADEPTNALE STTALQVFRL LSSMNQNQGT TILLTSNDIK SISEWCDQIS VLYCGQNTES APTEILIESP HHPYTQALIN AVPDFTQPLG FKTKLGTLEG TAPILEQMPI GCRLGPRCPF AQKKCMEKPR RLKIKQHEFS CHYPINLREK NFKEKTTATP FILNCKGNE // ID SEQA_HAEIN Reviewed; 197 AA. AC P44564; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Negative modulator of initiation of replication {ECO:0000255|HAMAP-Rule:MF_00908}; GN Name=seqA {ECO:0000255|HAMAP-Rule:MF_00908}; GN OrderedLocusNames=HI_0192; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Negative regulator of replication initiation, which CC contributes to regulation of DNA replication and ensures that CC replication initiation occurs exactly once per chromosome per cell CC cycle. Binds to pairs of hemimethylated GATC sequences in the oriC CC region, thus preventing assembly of replication proteins and re- CC initiation at newly replicated origins. Repression is relieved CC when the region becomes fully methylated. {ECO:0000255|HAMAP- CC Rule:MF_00908}. CC -!- SUBUNIT: Homodimer. Polymerizes to form helical filaments. CC {ECO:0000255|HAMAP-Rule:MF_00908}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00908}. CC -!- SIMILARITY: Belongs to the SeqA family. {ECO:0000255|HAMAP- CC Rule:MF_00908}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21861.1; -; Genomic_DNA. DR PIR; D64053; D64053. DR RefSeq; NP_438362.1; NC_000907.1. DR RefSeq; WP_005648714.1; NC_000907.1. DR ProteinModelPortal; P44564; -. DR SMR; P44564; 1-35, 83-192. DR STRING; 71421.HI0192; -. DR PRIDE; P44564; -. DR EnsemblBacteria; AAC21861; AAC21861; HI_0192. DR GeneID; 951105; -. DR KEGG; hin:HI0192; -. DR PATRIC; 20188883; VBIHaeInf48452_0198. DR eggNOG; ENOG4107CDU; Bacteria. DR eggNOG; COG3057; LUCA. DR KO; K03645; -. DR OMA; RTRTYFA; -. DR OrthoDB; EOG6XSZTV; -. DR PhylomeDB; P44564; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.1220.10; -; 1. DR Gene3D; 1.20.1380.10; -; 1. DR HAMAP; MF_00908; SeqA; 1. DR InterPro; IPR013321; Arc_rbn_hlx_hlx. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR005621; SeqA. DR InterPro; IPR026577; SeqA_DNA-bd_C. DR Pfam; PF03925; SeqA; 1. DR PIRSF; PIRSF019401; SeqA; 1. DR SUPFAM; SSF47598; SSF47598; 1. DR SUPFAM; SSF82808; SSF82808; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA replication inhibitor; DNA-binding; KW Reference proteome. FT CHAIN 1 197 Negative modulator of initiation of FT replication. FT /FTId=PRO_0000097687. FT REGION 100 101 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00908}. FT REGION 129 133 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00908}. FT REGION 163 169 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00908}. SQ SEQUENCE 197 AA; 22381 MW; 0251E5AF885F30D8 CRC64; MKIIEVDEEL YQYIASQTRS IGESASDILR RLLSLPVHTS IVNDLIITSA ETDQKPKQAI NVKEVNIKTT KKQSITAINQ IVEKVQTLLN STEFQEESKA VVRFLAILRV LYRTNPESFA QATESLQGRT RVYFARDEAT LLMAGNHTKP KQIPDTPYWV ITNTNSGRKM LMLEGAMQSM ELPETLIDEV RSYFTVN // ID SERB_HAEIN Reviewed; 314 AA. AC P44997; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Phosphoserine phosphatase; DE Short=PSP; DE Short=PSPase; DE EC=3.1.3.3; DE AltName: Full=O-phosphoserine phosphohydrolase; GN Name=serB; OrderedLocusNames=HI_1033; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P- CC Ser). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)- CC serine + 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 -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 3/3. CC -!- SIMILARITY: Belongs to the SerB 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; L42023; AAC22693.1; -; Genomic_DNA. DR PIR; I64108; I64108. DR RefSeq; NP_439193.1; NC_000907.1. DR RefSeq; WP_010869109.1; NC_000907.1. DR ProteinModelPortal; P44997; -. DR STRING; 71421.HI1033; -. DR EnsemblBacteria; AAC22693; AAC22693; HI_1033. DR GeneID; 949401; -. DR KEGG; hin:HI1033; -. DR PATRIC; 20190729; VBIHaeInf48452_1077. DR eggNOG; ENOG4105EAC; Bacteria. DR eggNOG; COG0560; LUCA. DR KO; K01079; -. DR OMA; AQYKANT; -. DR OrthoDB; EOG6ZPT4H; -. DR PhylomeDB; P44997; -. DR UniPathway; UPA00135; UER00198. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central. DR Gene3D; 1.10.150.210; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like. DR InterPro; IPR023190; Pser_Pase_dom_2. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Hydrolase; Magnesium; KW Metal-binding; Reference proteome; Serine biosynthesis. FT CHAIN 1 314 Phosphoserine phosphatase. FT /FTId=PRO_0000156888. FT REGION 197 198 Substrate binding. {ECO:0000250}. FT ACT_SITE 109 109 Nucleophile. {ECO:0000250}. FT ACT_SITE 111 111 Proton donor. {ECO:0000250}. FT METAL 109 109 Magnesium. {ECO:0000250}. FT METAL 111 111 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 265 265 Magnesium. {ECO:0000250}. FT BINDING 118 118 Substrate. {ECO:0000250}. FT BINDING 154 154 Substrate. {ECO:0000250}. FT BINDING 242 242 Substrate. {ECO:0000250}. FT BINDING 268 268 Substrate. {ECO:0000250}. SQ SEQUENCE 314 AA; 34720 MW; ED565F9C78CE0FB1 CRC64; MQIQCFESIT QKYPQFPTAL LANEEPIQNG EPFILYGTKL DITKLEKFQQ KCGQNFQIFD VWMVAKNIIV LLKGQWFSDF IKFTHDVEVD IAKLDFSPKL SQAGLLVMDM DSTAIQIECI DEIAKLAGVG ELVSAITESA MRGELDFEQS LRCRVGTLKG APESILQQVR ENLPLMSGLV ETIQTLQKYG WKTAIASGGF TYFADYLKAL LQLDFAASNQ FDIEDGKLTG LVKGDVVDAQ YKAKTLQHLL EEYGIDSRHS IAIGDGANDL AMMNVAGLGV AFHAKPKVQP QAQIVVNFAD LTALLCLLSA NDRI // ID SERC_HAEIN Reviewed; 362 AA. AC P44336; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160}; DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160}; DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160}; GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; GN OrderedLocusNames=HI_1167; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible conversion of 3- CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- CC phosphonooxybutanoate to phosphohydroxythreonine. CC {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3- CC phosphonooxypyruvate + L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate = CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00160}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 2/3. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4- CC phosphate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00160}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22822.1; -; Genomic_DNA. DR PIR; E64187; E64187. DR RefSeq; NP_439325.1; NC_000907.1. DR RefSeq; WP_005694273.1; NC_000907.1. DR ProteinModelPortal; P44336; -. DR SMR; P44336; 3-359. DR STRING; 71421.HI1167; -. DR EnsemblBacteria; AAC22822; AAC22822; HI_1167. DR GeneID; 949636; -. DR KEGG; hin:HI1167; -. DR PATRIC; 20191013; VBIHaeInf48452_1219. DR eggNOG; ENOG4107QM1; Bacteria. DR eggNOG; COG1932; LUCA. DR KO; K00831; -. DR OMA; GAQKNMG; -. DR OrthoDB; EOG60CWP3; -. DR PhylomeDB; P44336; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00160; SerC_aminotrans_5; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS. DR InterPro; IPR022278; Pser_aminoTfrase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000525; SerC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01364; serC_1; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis; KW Reference proteome; Serine biosynthesis; Transferase. FT CHAIN 1 362 Phosphoserine aminotransferase. FT /FTId=PRO_0000150174. FT REGION 76 77 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00160}. FT REGION 237 238 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00160}. FT BINDING 42 42 L-glutamate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 102 102 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 152 152 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 172 172 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT BINDING 195 195 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00160}. FT MOD_RES 196 196 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00160}. SQ SEQUENCE 362 AA; 40313 MW; 1DBDC9F25B76C3F7 CRC64; MSQVFNFSAG PAMIFPEVLQ KAQNELINWL NQGVSVMEVS HRGKYFMELV TQAEKDLREV YNIPDNYRTL FLQGGARGQF ATIPMNLIGK KGKALYLNSG HWSATAAKEA RNFAEIDEIT IVENGEQTRI TDLDFSHIAD QYDYVHYCPN ETISGVEIFD VPNVGNAVLV ADMSSNILSR QIDISKFGVI YAGAQKNLGP AGITLVIIRD DLIGNARKET PSIWNYATQR DADSMINTPP TFAWYLCSLV FKHLKEIGGL EIIEKRNALK AQTLYDYIDS SKLYRNVVAK ENRSTMNVTF ITGNPELDAK FVAESTAAGL QALKGHKVLG GMRASIYNAM SQNGVEALIS FMKKFETENL PQ // ID SGBU_HAEIN Reviewed; 286 AA. AC P44990; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Putative L-ribulose-5-phosphate 3-epimerase SgbU; DE EC=5.1.3.22; DE AltName: Full=L-xylulose-5-phosphate 3-epimerase; GN Name=sgbU; OrderedLocusNames=HI_1026; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to CC L-ribulose-5-phosphate. {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = L-xylulose 5- CC phosphate. CC -!- MISCELLANEOUS: Probably part of a sugar metabolic pathway along CC with SgbH. CC -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22686.1; -; Genomic_DNA. DR PIR; G64164; G64164. DR RefSeq; NP_439186.1; NC_000907.1. DR RefSeq; WP_005693360.1; NC_000907.1. DR ProteinModelPortal; P44990; -. DR STRING; 71421.HI1026; -. DR DNASU; 950012; -. DR EnsemblBacteria; AAC22686; AAC22686; HI_1026. DR GeneID; 950012; -. DR KEGG; hin:HI1026; -. DR PATRIC; 20190715; VBIHaeInf48452_1070. DR eggNOG; ENOG41064BZ; Bacteria. DR eggNOG; COG3623; LUCA. DR KO; K03082; -. DR OMA; SMCLSGH; -. DR OrthoDB; EOG6FFS58; -. DR PhylomeDB; P44990; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro. DR GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR004560; L-Ru-5P_3-Epase. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR00542; hxl6Piso_put; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 286 Putative L-ribulose-5-phosphate 3- FT epimerase SgbU. FT /FTId=PRO_0000097719. SQ SEQUENCE 286 AA; 33062 MW; 689543EBBD5E89BB CRC64; MKKHKIGIYE KALPKNITWQ ERLSLAKACG FEFIEMSIDE SNDRLSRLNW TKSERIALHQ SIIQSGITIP SMCLSAHRRF PFGSKDKKIR QKSFEIMEKA IDLSVNLGIR TIQLAGYDVY YEKQDEETIK YFQEGIEFAV TLAASAQVTL AVEIMDTPFM SSISRWKKWD TIINSPWFTV YPDIGNLSAW NNNIEEELTL GIDKISAIHL KDTYPVTETS KGQFRDVPFG QGCVDFVHFF SLLKKLNYRG AFLIEMWTEK NEEPLLEIIQ ARKWIVQQME KAGLLC // ID SELB_HAEIN Reviewed; 619 AA. AC P43927; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Selenocysteine-specific elongation factor; DE AltName: Full=SelB translation factor; GN Name=selB; OrderedLocusNames=HI_0709; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Translation factor necessary for the incorporation of CC selenocysteine into proteins. It probably replaces EF-Tu for the CC insertion of selenocysteine directed by the UGA codon. SelB binds CC GTP and GDP (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. SelB CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22366.1; -; Genomic_DNA. DR PIR; I64087; I64087. DR RefSeq; NP_438867.1; NC_000907.1. DR RefSeq; WP_005694594.1; NC_000907.1. DR ProteinModelPortal; P43927; -. DR STRING; 71421.HI0709; -. DR PRIDE; P43927; -. DR EnsemblBacteria; AAC22366; AAC22366; HI_0709. DR GeneID; 950261; -. DR KEGG; hin:HI0709; -. DR PATRIC; 20190037; VBIHaeInf48452_0739. DR eggNOG; ENOG4105EM7; Bacteria. DR eggNOG; COG3276; LUCA. DR KO; K03833; -. DR OMA; YAIDRVF; -. DR OrthoDB; EOG6V1M2Q; -. DR PhylomeDB; P43927; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro. DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 2. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2. DR InterPro; IPR015191; Elong_fac_SelB-wing-hlx_typ-3. 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; IPR004535; Transl_elong_SelB. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF09106; SelB-wing_2; 1. DR Pfam; PF09107; SelB-wing_3; 1. DR SUPFAM; SSF46785; SSF46785; 2. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00475; selB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 619 Selenocysteine-specific elongation FT factor. FT /FTId=PRO_0000091475. FT DOMAIN 1 169 tr-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT NP_BIND 7 14 GTP. {ECO:0000250}. FT NP_BIND 56 60 GTP. {ECO:0000250}. FT NP_BIND 111 114 GTP. {ECO:0000250}. FT REGION 7 14 G1. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 35 39 G2. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 56 59 G3. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 111 114 G4. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 144 146 G5. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. SQ SEQUENCE 619 AA; 69975 MW; 5960BACDE578D404 CRC64; MIIVTSGHVD HGKTALLKAL TGTSTAHLPE EKKRGMTIDL GYAYLPLENK VLGFIDVPGH EKFLSNMLAG LGGVHYAMLI VAADEGVAVQ TKEHLAILRQ LQFHEIIVVI TKADRTNSAQ IESLIQTIKQ DYSFLRNANY FVTSAETGQG ISELRHYLAN LAELADTQKP FRYAIDRVFS VKGAGTVVTG TAFSGTVKVN DEIYLSTGQK IRIKAIHAQN TSSEQGIAGQ RLALNLNADL DRTPMKRGDW LLQNEPLPPT DRISVQILAE VPLNESQPVH IYHGASRTTG KLTLLQGKNA AKNDRTLAEI ILDSPLFLAF GDKLILRSGD TKTLIAGARV LEINSPKRHK RTEVRLNFLA NLALAENASQ RIALTLQHNA TTARQLMWTE QLTSLQLDKA LAERDAVRYQ DWCFNPNYVQ EKTQQILTAL NIYHEQHNDQ LGVSKARLYR MATLNQPENL IHHFIDEMLD DGRLQQTRGW IHLPEHKIQF NTEEKSRWTD VLNEFEKANG QAIWVRDMAN ALAIDESIMR NFMYKAGKLG YLTPIVKDRF FLTETLYAYA RLIKQIAEEK GKVSVNEVRD KLNFGRKLTV QLMEYFDRMG FLRRKGNDHI LRDKNVFDL // ID SELD_HAEIN Reviewed; 346 AA. AC P43911; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 11-NOV-2015, entry version 96. DE RecName: Full=Selenide, water dikinase; DE EC=2.7.9.3; DE AltName: Full=Selenium donor protein; DE AltName: Full=Selenophosphate synthase; GN Name=selD; OrderedLocusNames=HI_0200; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. CC Class I subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21869.1; Type=Erroneous termination; Positions=16; Note=Translated as Sec.; 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; L42023; AAC21869.1; ALT_SEQ; Genomic_DNA. DR PIR; A64054; A64054. DR RefSeq; NP_438369.1; NC_000907.1. DR ProteinModelPortal; P43911; -. DR STRING; 71421.HI0200m; -. DR EnsemblBacteria; AAC21869; AAC21869; HI_0200. DR GeneID; 951109; -. DR KEGG; hin:HI0200m; -. DR PATRIC; 20188897; VBIHaeInf48452_0205. DR eggNOG; ENOG4105D4F; Bacteria. DR eggNOG; COG0709; LUCA. DR KO; K01008; -. DR OMA; PGSRFGK; -. DR OrthoDB; EOG6VF32H; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00625; SelD; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR023061; SelD_I. DR InterPro; IPR004536; SPS/SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036407; Selenphspht_syn; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00476; selD; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding; KW Reference proteome; Selenium; Selenocysteine; Transferase. FT CHAIN 1 346 Selenide, water dikinase. FT /FTId=PRO_0000127627. FT NP_BIND 229 235 ATP. {ECO:0000255}. FT ACT_SITE 16 16 {ECO:0000255}. FT SITE 19 19 Important for catalytic activity. FT {ECO:0000250}. FT NON_STD 16 16 Selenocysteine. {ECO:0000255}. SQ SEQUENCE 346 AA; 36400 MW; AFDD459A74D783F7 CRC64; MEEKIRLTQY SHGAGUGCKI SPKVLGTILH SELEKFYDPN LIVGNETADD AAVYDLGNGT AIISTTDFFM PIVDDPFDFG RIAATNAISD IFAMGGKPIM GIAILGFPTN VLPAEVAQKI VDGGRFACHQ AGIALAGGHS IDSPEPIFGL AVTGVIDTEK VKRNASAKSG CKLYMTKPLG IGILTTAEKK GKLKPEHQGL ATAAMCQMNS IGSQFSQVDG VTAMTDVTGF GLLGHLIEIC EGSNLSAVVF SDKIKTLDGV KDYIAQGCVP GGTGRNFDSY GHKVGILTEE QKAILCDPQT SGGLLVAVEL NSVQTVIDIA KDAGIDLYEV GKLKPKSESD IVVEVK // ID SERA_HAEIN Reviewed; 410 AA. AC P43885; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 121. DE RecName: Full=D-3-phosphoglycerate dehydrogenase; DE Short=PGDH; DE EC=1.1.1.95; GN Name=serA; OrderedLocusNames=HI_0465; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3- CC phosphonooxypyruvate + NADH. CC -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + CC NADH. CC -!- ENZYME REGULATION: In bacteria displays feedback inhibition by L- CC serine. {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 1/3. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22124.1; -; Genomic_DNA. DR PIR; C64070; C64070. DR RefSeq; NP_438626.1; NC_000907.1. DR RefSeq; WP_005693698.1; NC_000907.1. DR ProteinModelPortal; P43885; -. DR SMR; P43885; 6-410. DR STRING; 71421.HI0465; -. DR PRIDE; P43885; -. DR EnsemblBacteria; AAC22124; AAC22124; HI_0465. DR GeneID; 950636; -. DR KEGG; hin:HI0465; -. DR PATRIC; 20189485; VBIHaeInf48452_0485. DR eggNOG; ENOG4108JQ1; Bacteria. DR eggNOG; COG0111; LUCA. DR KO; K00058; -. DR OMA; KFVKYSD; -. DR OrthoDB; EOG6VXFC3; -. DR PhylomeDB; P43885; -. DR UniPathway; UPA00135; UER00196. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009070; P:serine family amino acid biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR010771; IgaA. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029015; PGDH_2. DR PANTHER; PTHR10996:SF18; PTHR10996:SF18; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR ProDom; PD147088; IgaA; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase; KW Reference proteome; Serine biosynthesis. FT CHAIN 1 410 D-3-phosphoglycerate dehydrogenase. FT /FTId=PRO_0000076002. FT DOMAIN 341 410 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT NP_BIND 162 163 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT NP_BIND 239 241 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT NP_BIND 293 296 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT ACT_SITE 241 241 {ECO:0000250}. FT ACT_SITE 270 270 {ECO:0000250}. FT ACT_SITE 293 293 Proton donor. {ECO:0000250}. FT BINDING 182 182 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT BINDING 265 265 NAD. {ECO:0000250|UniProtKB:P0A9T0}. SQ SEQUENCE 410 AA; 44665 MW; C5A75E6D685B7C80 CRC64; MTNKVSLDKS KIKFVLFEGV HQSALDTLHA AGYTNIDYYK KALDGDELKE AIKDVHFIGL RSRTHLTAEM IEAAPKLIAV GCFCIGTNQV DLNAAKARGI PVFNAPFSNT RSVAELVLGE ILLLMRNVPQ ANAEVHRGVW NKSATGSHEV RGKKLGIIGY GHIGSQLSII AESLGMDVYF YDIENKLPLG NAKQVRSLEE LLSSCDVVSL HVPELPSTKN LMNVARIAQL KQGAILINAA RGTVVDIDAL AQALKDGKLQ GAAIDVFPVE PASINEEFIS PLREFDNVIL TPHIGGSTAE AQENIGFEVA GKFVKYSDNG STLSSVNFPE VSLPEHEGTK RLLHIHENRP GILNKLNQIF VEANLNIAAQ YLQTDPKIGY VVVDVETNDA SPLLTKLKEI DGTIRARVLY // ID SIAT1_HAEIN Reviewed; 616 AA. AC P44543; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 16-MAR-2016, entry version 96. DE RecName: Full=Sialic acid TRAP transporter permease protein SiaT; DE AltName: Full=N-acetylneuraminic acid permease; DE AltName: Full=N-acetylneuraminic acid transporter; DE AltName: Full=Neu5Ac permease; GN Name=siaT; Synonyms=siaQM; OrderedLocusNames=HI_0147; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, AND SUBUNIT. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=16262798; DOI=10.1111/j.1365-2958.2005.04901.x; RA Severi E., Randle G., Kivlin P., Whitfield K., Young R., Moxon R., RA Kelly D., Hood D., Thomas G.H.; RT "Sialic acid transport in Haemophilus influenzae is essential for RT lipopolysaccharide sialylation and serum resistance and is dependent RT on a novel tripartite ATP-independent periplasmic transporter."; RL Mol. Microbiol. 58:1173-1185(2005). CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic CC (TRAP) transport system SiaPT involved in the uptake of sialic CC acid. {ECO:0000269|PubMed:16262798}. CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute CC receptor protein SiaP, and the fused transmembrane protein SiaT. CC {ECO:0000269|PubMed:16262798}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Is essential for lipopolysaccharide (LPS) CC sialylation and serum resistance. CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAP CC transporter small permease family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAP CC transporter large permease family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21819.1; 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; L42023; AAC21819.1; ALT_INIT; Genomic_DNA. DR PIR; I64143; I64143. DR RefSeq; NP_438316.1; NC_000907.1. DR RefSeq; WP_010868946.1; NC_000907.1. DR STRING; 71421.HI0147; -. DR TCDB; 2.A.56.1.3; the tripartite atp-independent periplasmic transporter (trap-t) family. DR EnsemblBacteria; AAC21819; AAC21819; HI_0147. DR GeneID; 951057; -. DR KEGG; hin:HI0147; -. DR PATRIC; 20188785; VBIHaeInf48452_0149. DR eggNOG; ENOG4105CG6; Bacteria. DR eggNOG; COG1593; LUCA. DR eggNOG; COG3090; LUCA. DR OMA; MTTLNMM; -. DR OrthoDB; EOG64V29B; -. DR Proteomes; UP000000579; 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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR InterPro; IPR010656; DctM. DR InterPro; IPR007387; DctQ_transporter. DR InterPro; IPR004681; TRAP_transpt_permease. DR Pfam; PF06808; DctM; 1. DR Pfam; PF04290; DctQ; 1. DR TIGRFAMs; TIGR00786; dctM; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 616 Sialic acid TRAP transporter permease FT protein SiaT. FT /FTId=PRO_0000169601. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 244 264 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 332 352 Helical. {ECO:0000255}. FT TRANSMEM 357 377 Helical. {ECO:0000255}. FT TRANSMEM 407 427 Helical. {ECO:0000255}. FT TRANSMEM 431 451 Helical. {ECO:0000255}. FT TRANSMEM 459 479 Helical. {ECO:0000255}. FT TRANSMEM 505 525 Helical. {ECO:0000255}. FT TRANSMEM 527 547 Helical. {ECO:0000255}. FT TRANSMEM 552 572 Helical. {ECO:0000255}. FT TRANSMEM 587 607 Helical. {ECO:0000255}. FT REGION 1 190 TRAP transporter small permease. FT REGION 191 616 TRAP transporter large permease. SQ SEQUENCE 616 AA; 67593 MW; 34E3114D54CED802 CRC64; MKYINKLEEW LGGALFIAIF GILIAQILSR QVFHSPLIWS EELAKLLFVY VGMLGISVAV RKQEHVFIDF LTNLMPEKIR KFTNTFVQLL VFICIFLFIH FGIRTFNGAS FPIDALGGIS EKWIFAALPV VAILMMFRFI QAQTLNFKTG KSYLPATFFI ISAVILFAIL FFAPDWFKVL RISNYIKLGS SSVYVALLVW LIIMFIGVPV GWSLFIATLL YFSMTRWNVV NAATEKLVYS LDSFPLLAVP FYILTGILMN TGGITERIFN FAKALLGHYT GGMGHVNIGA SLLFSGMSGS ALADAGGLGQ LEIKAMRDAG YDDDICGGIT AASCIIGPLV PPSIAMIIYG VIANESIAKL FIAGFIPGVL ITLALMAMNY RIAKKRGYPR TPKATREQLC SSFKQSFWAI LTPLLIIGGI FSGLFSPTES AIVAAAYSVI IGKFVYKELT LKSLFNSCIE AMAITGVVAL MIMTVTFFGD MIAREQVAMR VADVFVAVAD SPLTVLIMIN ALLLFLGMFI DALALQFLVL PMLIPIAMQF NIDLIFFGVM TTLNMMVGIL TPPMGMALFV VARVGNMSVS TVTKGVLPFL IPVFVTLVLI TIFPQIITFV PNLLIP // ID SDHL_HAEIN Reviewed; 455 AA. AC P71349; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=L-serine dehydratase; DE Short=SDH; DE EC=4.3.1.17; DE AltName: Full=L-serine deaminase; DE Short=L-SD; GN Name=sdaA; OrderedLocusNames=HI_0288; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine CC dehydratase 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; L42023; AAC21953.1; -; Genomic_DNA. DR RefSeq; NP_438455.1; NC_000907.1. DR RefSeq; WP_005693026.1; NC_000907.1. DR ProteinModelPortal; P71349; -. DR STRING; 71421.HI0288; -. DR EnsemblBacteria; AAC21953; AAC21953; HI_0288. DR GeneID; 949415; -. DR KEGG; hin:HI0288; -. DR PATRIC; 20189115; VBIHaeInf48452_0304. DR eggNOG; ENOG4105EJQ; Bacteria. DR eggNOG; COG1760; LUCA. DR KO; K01752; -. DR OMA; CQATTQQ; -. DR OrthoDB; EOG64V2GZ; -. DR PhylomeDB; P71349; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.1330.90; -; 1. DR InterPro; IPR029009; ASB_dom. DR InterPro; IPR004644; Fe-S_L-Ser_mono. DR InterPro; IPR005130; Ser_deHydtase-like_asu. DR InterPro; IPR005131; Ser_deHydtase_bsu. DR Pfam; PF03313; SDH_alpha; 1. DR Pfam; PF03315; SDH_beta; 1. DR SUPFAM; SSF143548; SSF143548; 1. DR TIGRFAMs; TIGR00720; sda_mono; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Gluconeogenesis; Iron; Iron-sulfur; Lyase; KW Metal-binding; Reference proteome. FT CHAIN 1 455 L-serine dehydratase. FT /FTId=PRO_0000171906. SQ SEQUENCE 455 AA; 49538 MW; 11002A51736DD386 CRC64; MISVFDMFKV GIGPSSSHTV GPMKAGKQFI DDLIKRNQFE QTTEIHVDVY GSLSMTGRGH STDIAIIMGL AGYLPHNVDI DMISGFIEKV KQTALLPINV GQKIVKFDFE NNLIFHRTFL KLHENGMTIT ALDENRTELY RQTYYSIGGG FIVDEAHFGK EEKNTVQVPY PYKNAEDILK HCSDNGLMLS TVMLENEIAL NGKEAVSAHL ENVWKTMQAC IEHGIHTEGI LPGPLRVPRR AASLYRALQA NTNLSNDPMR VIDWVNMFAL AVNEENAAGG RVVTAPTNGA CGIIPAVLAY YEKFISPLTP EIIERYLLAA GMIGSLYKMN ASISGAEVGC QGEVGVACSM AAAGLAEILG GNPLQVCIAA EIAMEHNLGL TCDPVGGQVQ VPCIERNAIA SVKAINASRM ALRRTTNPRV TLDKVIETMY ETGKDMNAKY RETSQGGLAV KIVCN // ID SECB_HAEIN Reviewed; 169 AA. AC P44853; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 103. DE RecName: Full=Protein-export protein SecB; GN Name=secB; OrderedLocusNames=HI_0743; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=11101901; DOI=10.1038/82040; RA Xu Z., Knafels J.D., Yoshino K.; RT "Crystal structure of the bacterial protein export chaperone secB."; RL Nat. Struct. Biol. 7:1172-1177(2000). CC -!- FUNCTION: One of the proteins required for the normal export of CC preproteins out of the cell cytoplasm. It is a molecular chaperone CC that binds to a subset of precursor proteins, maintaining them in CC a translocation-competent state. It also specifically binds to its CC receptor SecA. CC -!- SUBUNIT: Homotetramer, a dimer of dimers. One homotetramer CC interacts with 1 SecA dimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the SecB 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; L42023; AAC22401.1; -; Genomic_DNA. DR PIR; I64089; I64089. DR RefSeq; NP_438902.1; NC_000907.1. DR RefSeq; WP_005630575.1; NC_000907.1. DR PDB; 1FX3; X-ray; 2.50 A; A/B/C/D=1-169. DR PDB; 1OZB; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-169. DR PDBsum; 1FX3; -. DR PDBsum; 1OZB; -. DR ProteinModelPortal; P44853; -. DR SMR; P44853; 15-163. DR IntAct; P44853; 1. DR STRING; 71421.HI0743; -. DR EnsemblBacteria; AAC22401; AAC22401; HI_0743. DR GeneID; 949770; -. DR KEGG; hin:HI0743; -. DR PATRIC; 20190127; VBIHaeInf48452_0779. DR eggNOG; ENOG4105IX2; Bacteria. DR eggNOG; COG1952; LUCA. DR KO; K03071; -. DR OMA; CPNVLFP; -. DR OrthoDB; EOG6DVJZZ; -. DR PhylomeDB; P44853; -. DR EvolutionaryTrace; P44853; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.420.10; -; 1. DR HAMAP; MF_00821; SecB; 1. DR InterPro; IPR003708; SecB. DR Pfam; PF02556; SecB; 1. DR PRINTS; PR01594; SECBCHAPRONE. DR SUPFAM; SSF54611; SSF54611; 1. DR TIGRFAMs; TIGR00809; secB; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Cytoplasm; KW Protein transport; Reference proteome; Translocation; Transport. FT CHAIN 1 169 Protein-export protein SecB. FT /FTId=PRO_0000055378. FT STRAND 17 31 {ECO:0000244|PDB:1FX3}. FT HELIX 35 38 {ECO:0000244|PDB:1FX3}. FT STRAND 51 59 {ECO:0000244|PDB:1FX3}. FT STRAND 62 71 {ECO:0000244|PDB:1FX3}. FT TURN 76 78 {ECO:0000244|PDB:1FX3}. FT STRAND 84 97 {ECO:0000244|PDB:1FX3}. FT HELIX 100 108 {ECO:0000244|PDB:1FX3}. FT HELIX 110 129 {ECO:0000244|PDB:1FX3}. FT HELIX 142 156 {ECO:0000244|PDB:1FX3}. FT HELIX 158 161 {ECO:0000244|PDB:1FX3}. SQ SEQUENCE 169 AA; 19132 MW; 047DCC722965EC7B CRC64; MSEQKQDVAA TEEQQPVLQI QRIYVKDVSF EAPNLPHIFQ QEWKPKLGFD LSTETTQVGD DLYEVVLNIS VETTLEDSGD VAFICEVKQA GVFTISGLED VQMAHCLTSQ CPNMLFPYAR ELVSNLVNRG TFPALNLSPV NFDALFVEYM NRQQAENAEE KSEEEQTKH // ID SECD_HAEIN Reviewed; 616 AA. AC P44591; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; GN OrderedLocusNames=HI_0240; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000255|HAMAP- CC Rule:MF_01463}. CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP- CC Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01463}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01463}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21908.1; -; Genomic_DNA. DR PIR; I64056; I64056. DR RefSeq; NP_438410.1; NC_000907.1. DR RefSeq; WP_005694058.1; NC_000907.1. DR ProteinModelPortal; P44591; -. DR STRING; 71421.HI0240; -. DR EnsemblBacteria; AAC21908; AAC21908; HI_0240. DR GeneID; 951150; -. DR KEGG; hin:HI0240; -. DR PATRIC; 20189005; VBIHaeInf48452_0255. DR eggNOG; ENOG4107QN8; Bacteria. DR eggNOG; COG0342; LUCA. DR KO; K03072; -. DR OMA; AAPMEII; -. DR OrthoDB; EOG6N0HJT; -. DR PhylomeDB; P44591; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01463_B; SecD_B; 1. DR InterPro; IPR001036; Acrflvin-R. DR InterPro; IPR005791; SecD. DR InterPro; IPR027398; SecD-TM. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF13721; SecD-TM1; 1. DR Pfam; PF02355; SecD_SecF; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR01129; secD; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 616 Protein translocase subunit SecD. FT /FTId=PRO_0000095962. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 453 473 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 475 495 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 497 517 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 547 569 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 585 605 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. SQ SEQUENCE 616 AA; 66986 MW; 7DE1E4B085065F8F CRC64; MLNRYPLWKN LMVIFIVAIG ILYSLPNIYG EDPAVQISGT RGQEANTSVL GQVQDVLKTN NLPTKSIVLE NGSILARFTN TDDQLLAKDK IAERLGNNYT TALNLAPATP AWLSMFGANP MKWGLDLRGG VRFLMEVDMN ATLVKRQEQL QDSLRGELRK EKIQYTAIKN TEHFGTLITL ANVSQRAKAE RIIRQLHPTL DITEPDADSI NLGLSTAALN EARDLAIEQN LTILRKRVAE LGVAEAVIQR QGAERIVIEL PGVQDTARAK EILGATATLE FRIVNQNVTA DAISRNMLPA DSEVKYDRQG HPVALFKRAV LGGEHIINSS SGLDQHSSTP QVSVTLDSEG GEIMSQTTKK YYKKPMATLY VEYKDNGKKD ENGKTILEKH EEVINVATIQ GRFGSNFQIT GVDSIAEAHN LSTLLKSGAL IAPIQIVEER TIGPSLGAQN VEQGINASLW GLVAVIAFML FYYKMFGVIA SFALVINIVL LVGLMSILPG ATLSMPGIAG IVLTLGMSVD ANVLIFERIK EEIRNGRSIQ QAINEGYNGA FTSIFDANLT TILTAIILYA VGTGPIQGFA ITLSLGVAIS MFTAITGTRA LVNALYGGKQ LKKLLI // ID SGBH_HAEIN Reviewed; 225 AA. AC P44988; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Probable 3-keto-L-gulonate-6-phosphate decarboxylase; DE Short=KGPDC; DE EC=4.1.1.85; DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase; GN Name=sgbH; OrderedLocusNames=HI_1024; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9274005; RA Reizer J., Reizer A., Saier M.H. Jr.; RT "Is the ribulose monophosphate pathway widely distributed in RT bacteria?"; RL Microbiology 143:2519-2520(1997). CC -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P CC into L-xylulose-5-P. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 3-dehydro-L-gulonate 6-phosphate = L-xylulose CC 5-phosphate + CO(2). 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC 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; L42023; AAC22684.1; -; Genomic_DNA. DR PIR; F64164; F64164. DR RefSeq; NP_439184.1; NC_000907.1. DR RefSeq; WP_005693359.1; NC_000907.1. DR ProteinModelPortal; P44988; -. DR STRING; 71421.HI1024; -. DR EnsemblBacteria; AAC22684; AAC22684; HI_1024. DR GeneID; 950714; -. DR KEGG; hin:HI1024; -. DR PATRIC; 20190711; VBIHaeInf48452_1068. DR eggNOG; COG0269; LUCA. DR KO; K03081; -. DR OMA; CISAGIQ; -. DR OrthoDB; EOG66B435; -. DR PhylomeDB; P44988; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. 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; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Decarboxylase; Lyase; KW Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 225 Probable 3-keto-L-gulonate-6-phosphate FT decarboxylase. FT /FTId=PRO_0000212106. FT METAL 33 33 Magnesium. {ECO:0000250}. FT METAL 62 62 Magnesium. {ECO:0000250}. FT BINDING 11 11 Substrate. {ECO:0000250}. FT BINDING 202 202 Substrate. {ECO:0000250}. FT SITE 64 64 Transition state stabilizer. FT {ECO:0000250}. FT SITE 67 67 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 225 AA; 24867 MW; 3829D48797FA710C CRC64; MGKPLLQIAL DAQYLETALV DVKQIEHNID IIEVGTILAC SEGMRAVRIL RALYPNQILV CDLKTTDAGA TLAKMAFEAG ADWLTVSAAA HPATKAACQK VAEEFNKIQP NLGVPKEIQI ELYGNWNFDE VKNWLQLGIK QAIYHRSRDA ELSGLSWSNQ DIENIEKLDS LGIELSITGG ITPDDLHLFK NTKNLKAFIA GRALVGKSGR EIAEQLKQKI GQFWI // ID SECE_HAEIN Reviewed; 106 AA. AC P43805; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422}; GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; GN OrderedLocusNames=HI_0716; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential subunit of the Sec protein translocation CC channel SecYEG. Clamps together the 2 halves of SecY. May contact CC the channel plug during translocation. {ECO:0000255|HAMAP- CC Rule:MF_00422}. 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_00422}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00422}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00422}. CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. CC {ECO:0000255|HAMAP-Rule:MF_00422}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22373.1; -; Genomic_DNA. DR PIR; F64088; F64088. DR RefSeq; NP_438874.1; NC_000907.1. DR RefSeq; WP_010869040.1; NC_000907.1. DR STRING; 71421.HI0716; -. DR EnsemblBacteria; AAC22373; AAC22373; HI_0716. DR GeneID; 949943; -. DR KEGG; hin:HI0716; -. DR PATRIC; 20190055; VBIHaeInf48452_0748. DR eggNOG; ENOG4105PM1; Bacteria. DR eggNOG; COG0690; LUCA. DR KO; K03073; -. DR OMA; DSRTEAH; -. DR OrthoDB; EOG6DRPR4; -. DR PhylomeDB; P43805; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0006605; P:protein targeting; IEA:InterPro. DR HAMAP; MF_00422; SecE; 1. DR InterPro; IPR022943; SecE. DR InterPro; IPR005807; SecE_bac. DR InterPro; IPR001901; Translocase_SecE/Sec61-g. DR Pfam; PF00584; SecE; 1. DR PRINTS; PR01650; SECETRNLCASE. DR TIGRFAMs; TIGR00964; secE_bact; 1. DR PROSITE; PS01067; SECE_SEC61G; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 106 Protein translocase subunit SecE. FT /FTId=PRO_0000104166. FT TRANSMEM 20 40 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00422}. FT TRANSMEM 75 95 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00422}. SQ SEQUENCE 106 AA; 11817 MW; 80A2F77912B50FF8 CRC64; MIFFAAAAIG NIYFQQIYSL PIRVIGMAIA LVIAFILAAI TNQGTKARAF FNDSRTEARK VVWPTRAEAR QTTLIVIGVT MIASLFFWAV DSIIVTVINF LTDLRF // ID SECF_HAEIN Reviewed; 325 AA. AC P44590; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Protein translocase subunit SecF; GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; GN OrderedLocusNames=HI_0239; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts CC with the SecYEG preprotein conducting channel. SecDF uses the CC proton motive force (PMF) to complete protein translocation after CC the ATP-dependent function of SecA. {ECO:0000255|HAMAP- CC Rule:MF_01464}. CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec CC protein translocation apparatus which comprises SecA, SecYEG and CC auxiliary proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP- CC Rule:MF_01464}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01464}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21907.1; -; Genomic_DNA. DR PIR; H64056; H64056. DR RefSeq; NP_438409.1; NC_000907.1. DR RefSeq; WP_005694059.1; NC_000907.1. DR ProteinModelPortal; P44590; -. DR STRING; 71421.HI0239; -. DR EnsemblBacteria; AAC21907; AAC21907; HI_0239. DR GeneID; 951151; -. DR KEGG; hin:HI0239; -. DR PATRIC; 20189003; VBIHaeInf48452_0254. DR eggNOG; ENOG4107RAB; Bacteria. DR eggNOG; COG0341; LUCA. DR KO; K03074; -. DR OMA; IDMNLEV; -. DR OrthoDB; EOG676Z5R; -. DR PhylomeDB; P44590; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01464_B; SecF_B; 1. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022645; SecD/SecF_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR InterPro; IPR005665; SecF_bac. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF02355; SecD_SecF; 1. DR PRINTS; PR01755; SECFTRNLCASE. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR00966; 3a0501s07; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 325 Protein translocase subunit SecF. FT /FTId=PRO_0000095979. FT TRANSMEM 36 56 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 148 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 175 197 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 202 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 254 274 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 281 301 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. SQ SEQUENCE 325 AA; 36051 MW; EBC59299ED1CF1F2 CRC64; MMKLFTKDKD GHFIREINGI KLPFPLTEFM KVRKLGYILS ALLMVISLFF IITKGFNWGL DFTGGVVFDT HFSQSANLEQ IRSKLHENGI ESPIVQTTGS VQDVMIRLPA SNNDSTIGEH VKSMLQNVDK DIQIRSIEFV GPNVGEELAQ GAVYATLATL AMVLIYVGSR FEWRLGFGSI ASLAHDVIIT LGVFSALQIE IDLTFVAAIL SVVGYSINDS IVVFDRVREN FRKIRRLDTI DIIDISLTQT LSRTIITSVT TLVVVMALFF FGGPSIHNFS LALLVGIGFG TYSSIFVAIA IAYDVGLRRE HMIPPKVDKE IDELP // ID SELA_HAEIN Reviewed; 461 AA. AC P43910; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423}; DE EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423}; DE AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423}; DE Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423}; DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423}; GN Name=selA {ECO:0000255|HAMAP-Rule:MF_00423}; GN OrderedLocusNames=HI_0708; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) CC required for selenoprotein biosynthesis. {ECO:0000255|HAMAP- CC Rule:MF_00423}. CC -!- CATALYTIC ACTIVITY: L-seryl-tRNA(Sec) + selenophosphate = L- CC selenocysteinyl-tRNA(Sec) + phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00423}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00423}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) CC (bacterial route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00423}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}. CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP- CC Rule:MF_00423}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22365.1; -; Genomic_DNA. DR PIR; H64087; H64087. DR RefSeq; NP_438866.1; NC_000907.1. DR RefSeq; WP_005694593.1; NC_000907.1. DR ProteinModelPortal; P43910; -. DR STRING; 71421.HI0708; -. DR DNASU; 950262; -. DR EnsemblBacteria; AAC22365; AAC22365; HI_0708. DR GeneID; 950262; -. DR KEGG; hin:HI0708; -. DR PATRIC; 20190035; VBIHaeInf48452_0738. DR eggNOG; ENOG4105C1Y; Bacteria. DR eggNOG; COG1921; LUCA. DR KO; K01042; -. DR OMA; NRTHARD; -. DR OrthoDB; EOG69WFGN; -. DR PhylomeDB; P43910; -. DR UniPathway; UPA00906; UER00896. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central. DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-HAMAP. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_00423; SelA; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR018319; SelA-like. DR InterPro; IPR004534; SelA_trans. DR InterPro; IPR025862; SelA_trans_N_dom. DR Pfam; PF12390; Se-cys_synth_N; 1. DR Pfam; PF03841; SelA; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00474; selA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Protein biosynthesis; KW Pyridoxal phosphate; Reference proteome; Selenium; Transferase. FT CHAIN 1 461 L-seryl-tRNA(Sec) selenium transferase. FT /FTId=PRO_0000189605. FT MOD_RES 294 294 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00423}. SQ SEQUENCE 461 AA; 51127 MW; FDC5F721498670F3 CRC64; MTALFQQLPS VDKILKTPQG LQLITEFGHT AVVATCRELL TQARQFIKKN NQLPEYFSNF DRTFLEIHSH LQKQNQVQIK AVHNLTGTVL HTNLGRALWS EAAQQAALSA MQKNVSLEYD LDEGKRSHRD NYISELLCKL TGAEAACIVN NNAAAVLLML ATFAQGKEVI ISRGELIEIG GAFRIPDIME QAGCHLVEVG TTNRTHLKDY RNAITENTAF LMKVHSSNYQ ICGFTSSVSE EELTELGQEM NVPVVTDLGS GALVDLSQYG LPKEPTVQEK IAQGVDLVSF SGDKLLGGVQ AGIIVGKKEW IEQLQAHPLK RVLRCDKVIL AGLEATLRLY LNPEKLTEKL PTLRLLTQPL KQLKINAMRL KERLESRLNS QFELQIEASQ AQIGSGSQPM ERIPSVAVTI AEKTNAKLSA LSARFKQLSQ PIIGRMENGK IWLDLRSLAD IETLLNTLDE L // ID SECG_HAEIN Reviewed; 112 AA. AC P44713; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Protein-export membrane protein SecG; GN Name=secG; OrderedLocusNames=HI_0445; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in protein export. Participates in an early CC event of protein translocation (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC22104.1; -; Genomic_DNA. DR PIR; H64068; H64068. DR RefSeq; NP_438606.1; NC_000907.1. DR RefSeq; WP_005693717.1; NC_000907.1. DR STRING; 71421.HI0445; -. DR EnsemblBacteria; AAC22104; AAC22104; HI_0445. DR GeneID; 949417; -. DR KEGG; hin:HI0445; -. DR PATRIC; 20189443; VBIHaeInf48452_0465. DR eggNOG; COG1314; LUCA. DR KO; K03075; -. DR OMA; WENLQQT; -. DR OrthoDB; EOG6DC6SJ; -. DR PhylomeDB; P44713; -. DR Proteomes; UP000000579; 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 Pfam; PF03840; SecG; 1. DR PRINTS; PR01651; SECGEXPORT. DR TIGRFAMs; TIGR00810; secG; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 112 Protein-export membrane protein SecG. FT /FTId=PRO_0000157228. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. SQ SEQUENCE 112 AA; 11538 MW; 1A51CB4C8079E674 CRC64; MYQVLLFIYV VVAIALIGFI LVQQGKGANA GASFGGGASG TMFGSAGAGN FLTRTSAILA TAFFVIALVL GNMNSHKGNV QKGTFDDLSQ AAEQVQQQAA PAKDNKNSDI PQ // ID SIXA_HAEIN Reviewed; 164 AA. AC P44164; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Phosphohistidine phosphatase SixA homolog; DE EC=3.1.3.-; GN Name=sixA-A; OrderedLocusNames=HI_1338; GN and GN Name=sixA-B; OrderedLocusNames=HI_1462.2; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the SixA phosphatase 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; L42023; AAC22985.1; -; Genomic_DNA. DR EMBL; L42023; AAC23109.1; -; Genomic_DNA. DR PIR; B64026; B64026. DR RefSeq; NP_439489.1; NC_000907.1. DR RefSeq; NP_439613.1; NC_000907.1. DR RefSeq; WP_005652786.1; NC_000907.1. DR ProteinModelPortal; P44164; -. DR STRING; 71421.HI1462.2; -. DR EnsemblBacteria; AAC22985; AAC22985; HI_1338. DR EnsemblBacteria; AAC23109; AAC23109; HI_1462.2. DR GeneID; 950260; -. DR GeneID; 950352; -. DR KEGG; hin:HI1338; -. DR KEGG; hin:HI1462.2; -. DR PATRIC; 20191359; VBIHaeInf48452_1390. DR eggNOG; ENOG4108BY2; Bacteria. DR eggNOG; COG2062; LUCA. DR KO; K08296; -. DR OMA; MQVLIMR; -. DR OrthoDB; EOG6QRW8K; -. DR PhylomeDB; P44164; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008969; F:phosphohistidine phosphatase activity; IEA:InterPro. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1240; -; 1. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR InterPro; IPR004449; SixA. DR Pfam; PF00300; His_Phos_1; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR TIGRFAMs; TIGR00249; sixA; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protein phosphatase; Reference proteome. FT CHAIN 1 164 Phosphohistidine phosphatase SixA FT homolog. FT /FTId=PRO_0000214569. SQ SEQUENCE 164 AA; 18701 MW; 5A820F9E41BA744C CRC64; MNIFIMRHGE AEVMANSDKA RHLTVYGSKQ AFLQGQWLKQ HLSTLVINSL DRILVSPYVR AQETFHQVNQ AFDLELENKF EIWEGITPYG HAHSVIDYLE VLKDEGVKSV LIVSHLPLVG EIVAELYGKR NPISFYPATI AQLLWDGNKS EILMHQASPV IYLK // ID SLYX_HAEIN Reviewed; 73 AA. AC P44759; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Protein SlyX homolog; GN Name=slyX; OrderedLocusNames=HI_0573; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the SlyX 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; L42023; AAC22231.1; -; Genomic_DNA. DR PIR; D64078; D64078. DR RefSeq; NP_438730.1; NC_000907.1. DR RefSeq; WP_005694169.1; NC_000907.1. DR STRING; 71421.HI0573; -. DR EnsemblBacteria; AAC22231; AAC22231; HI_0573. DR GeneID; 949619; -. DR KEGG; hin:HI0573; -. DR PATRIC; 20189701; VBIHaeInf48452_0593. DR eggNOG; ENOG41069P5; Bacteria. DR eggNOG; COG2900; LUCA. DR KO; K03745; -. DR OMA; DMQPSNI; -. DR OrthoDB; EOG6H4KCT; -. DR PhylomeDB; P44759; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00715; SlyX; 1. DR InterPro; IPR007236; SlyX. DR Pfam; PF04102; SlyX; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 73 Protein SlyX homolog. FT /FTId=PRO_0000209203. SQ SEQUENCE 73 AA; 8723 MW; A8E683216BF10395 CRC64; MQIQQMLENR IEELEMKIAF QEQLLDELNH ALVQQQFDID KMQVQLRYMA NKLKDFQSSN IASQSEETPP PHY // ID SFGH_HAEIN Reviewed; 275 AA. AC P44556; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=S-formylglutathione hydrolase; DE Short=FGH; DE EC=3.1.2.12; GN OrderedLocusNames=HI_0184; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Serine hydrolase involved in the detoxification of CC formaldehyde. Hydrolyzes S-formylglutathione to glutathione and CC formate (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-formylglutathione + H(2)O = glutathione + CC formate. CC -!- SIMILARITY: Belongs to the esterase D 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; L42023; AAC21853.1; -; Genomic_DNA. DR PIR; A64145; A64145. DR RefSeq; NP_438352.1; NC_000907.1. DR RefSeq; WP_005694102.1; NC_000907.1. DR ProteinModelPortal; P44556; -. DR STRING; 71421.HI0184; -. DR ESTHER; haein-sfgh; A85-EsteraseD-FGH. DR EnsemblBacteria; AAC21853; AAC21853; HI_0184. DR GeneID; 951093; -. DR KEGG; hin:HI0184; -. DR PATRIC; 20188863; VBIHaeInf48452_0188. DR eggNOG; ENOG4105C4W; Bacteria. DR eggNOG; COG0627; LUCA. DR KO; K01070; -. DR OMA; TEQPWAT; -. DR OrthoDB; EOG63587Z; -. DR PhylomeDB; P44556; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000801; Esterase_put. DR InterPro; IPR014186; S-formylglutathione_hydrol. DR PANTHER; PTHR10061; PTHR10061; 1. DR Pfam; PF00756; Esterase; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR TIGRFAMs; TIGR02821; fghA_ester_D; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome; Serine esterase. FT CHAIN 1 275 S-formylglutathione hydrolase. FT /FTId=PRO_0000210344. FT ACT_SITE 145 145 Charge relay system. {ECO:0000250}. FT ACT_SITE 221 221 Charge relay system. {ECO:0000250}. FT ACT_SITE 254 254 Charge relay system. {ECO:0000250}. SQ SEQUENCE 275 AA; 31317 MW; 781F5C0411546D3D CRC64; MKLIEQHQIF GGSQQVWAHN AQTLQCEMKF AVYLPNNPEN RPLGVIYWLS GLTCTEQNFI TKSGFQRYAA EHQVIVVAPD TSPRGEQVPN DAAYDLGQGA GFYLNATEQP WATNYQMYDY ILNELPDLIE ANFPTNGKRS IMGHSMGGHG ALVLALRNRE RYQSVSAFSP ILSPSLVPWG EKAFSAYLGE DREKWQQYDA SSLIQQGYKV QGMRIDQGLE DEFLPTQLRT EDFIETCRVA NQPVDVRFHK GYDHSYYFIA SFIGEHIAYH AEFLK // ID SFSA_HAEIN Reviewed; 238 AA. AC P46457; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Sugar fermentation stimulation protein homolog {ECO:0000255|HAMAP-Rule:MF_00095}; GN Name=sfsA {ECO:0000255|HAMAP-Rule:MF_00095}; GN OrderedLocusNames=HI_1611; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the SfsA family. {ECO:0000255|HAMAP- CC Rule:MF_00095}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23255.1; -; Genomic_DNA. DR RefSeq; NP_439753.1; NC_000907.1. DR RefSeq; WP_010869259.1; NC_000907.1. DR STRING; 71421.HI1611; -. DR DNASU; 950840; -. DR EnsemblBacteria; AAC23255; AAC23255; HI_1611. DR GeneID; 950840; -. DR KEGG; hin:HI1611; -. DR PATRIC; 20191953; VBIHaeInf48452_1684. DR eggNOG; ENOG4105PW4; Bacteria. DR eggNOG; COG1489; LUCA. DR KO; K06206; -. DR OMA; MLYFINR; -. DR OrthoDB; EOG6QZMTM; -. DR PhylomeDB; P46457; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00095; SfsA; 1. DR InterPro; IPR005224; SfsA. DR Pfam; PF03749; SfsA; 1. DR TIGRFAMs; TIGR00230; sfsA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 238 Sugar fermentation stimulation protein FT homolog. FT /FTId=PRO_0000152289. SQ SEQUENCE 238 AA; 26933 MW; E0FC11AC8E93DC30 CRC64; MQLPALQSAT LIRRYKRFLA DIELPTGDVM TIHCANTGAM TGCGEKGDKI WYSHSDSQTR KYPHSWELTQ LANGQLCCIN THRSNQLVFE ALQNKQIKEL AMYDEIYPEV KYGEENSRID FLLKGEGLLD CYVEVKSITL VKGNLGMSPD AVTTRGQKHV RELLAMKKQG HRAVVLFAGL HNGFDRFKIA EYIDPEYDRL LKEAMEQGVE AYAYAGQFEI SNEIPTALSL TESVSYIK // ID SGBE_HAEIN Reviewed; 231 AA. AC P44989; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Probable sugar isomerase SgbE; DE EC=5.1.-.-; GN Name=sgbE; OrderedLocusNames=HI_1025; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable pentulose-5-phosphate-4-epimerase. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA 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; L42023; AAC22685.1; -; Genomic_DNA. DR RefSeq; NP_439185.1; NC_000907.1. DR RefSeq; WP_005669745.1; NC_000907.1. DR ProteinModelPortal; P44989; -. DR SMR; P44989; 1-223. DR STRING; 71421.HI1025; -. DR EnsemblBacteria; AAC22685; AAC22685; HI_1025. DR GeneID; 950011; -. DR KEGG; hin:HI1025; -. DR PATRIC; 20190713; VBIHaeInf48452_1069. DR eggNOG; ENOG4107R0P; Bacteria. DR eggNOG; COG0235; LUCA. DR KO; K03080; -. DR OMA; PNIGTTH; -. DR OrthoDB; EOG6358F1; -. DR PhylomeDB; P44989; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR004661; AraD. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. DR TIGRFAMs; TIGR00760; araD; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 231 Probable sugar isomerase SgbE. FT /FTId=PRO_0000162924. FT METAL 76 76 Zinc. {ECO:0000250}. FT METAL 95 95 Zinc. {ECO:0000250}. FT METAL 97 97 Zinc. {ECO:0000250}. FT METAL 171 171 Zinc. {ECO:0000250}. SQ SEQUENCE 231 AA; 25981 MW; 9DE3485E54B10DC7 CRC64; MLAQLKKEVF EANLALPKHH LVTFTWGNVS AIDREKNLVV IKPSGVDYDV MTENDMVVVD LFTGNIVEGN KKPSSDTPTH LELYRQFPHI GGIVHTHSRH ATIWAQAGLD IIEVGTTHGD YFYGTIPCTR QMTTKEIKGN YELETGKVIV ETFLSRGIEP DNIPAVLVHS HGPFAWGKDA NNAVHNAVVL EEVAYMNLFS QQLNPYLSPM QKDLLDKHYL RKHGQNAYYG Q // ID SLYD_HAEIN Reviewed; 190 AA. AC P44830; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase SlyD; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Metallochaperone SlyD; GN Name=slyD; OrderedLocusNames=HI_0699; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Folding helper with both chaperone and peptidyl-prolyl CC cis-trans isomerase (PPIase) activities. Chaperone activity CC prevents aggregation of unfolded or partially folded proteins and CC promotes their correct folding. PPIases catalyze the cis-trans CC isomerization of Xaa-Pro bonds of peptides, which accelerates slow CC steps of protein folding and thus shortens the lifetime of CC intermediates. Both strategies lower the concentration of CC intermediates and increase the productivity and yield of the CC folding reaction (By similarity). {ECO:0000250}. CC -!- FUNCTION: Also involved in hydrogenase metallocenter assembly, CC probably by participating in the nickel insertion step. This CC function in hydrogenase biosynthesis requires chaperone activity CC and the presence of the metal-binding domain, but not PPIase CC activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: The N-terminal region consists of two globular folded CC domains that contain prolyl isomerase and chaperone activities. CC {ECO:0000250}. CC -!- DOMAIN: The C-terminal region binds nickel ions. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22358.1; -; Genomic_DNA. DR PIR; D64087; D64087. DR RefSeq; NP_438858.1; NC_000907.1. DR RefSeq; WP_005694583.1; NC_000907.1. DR ProteinModelPortal; P44830; -. DR STRING; 71421.HI0699; -. DR EnsemblBacteria; AAC22358; AAC22358; HI_0699. DR GeneID; 949724; -. DR KEGG; hin:HI0699; -. DR PATRIC; 20190017; VBIHaeInf48452_0730. DR eggNOG; ENOG4108YZY; Bacteria. DR eggNOG; COG1047; LUCA. DR KO; K03775; -. DR OMA; PKDVFVG; -. DR OrthoDB; EOG6Q8J79; -. DR PhylomeDB; P44830; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005528; F:FK506 binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central. DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GOC. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PTHR10516; 2. DR Pfam; PF00254; FKBP_C; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Isomerase; Metal-binding; KW Nickel; Reference proteome; Rotamase. FT CHAIN 1 190 FKBP-type peptidyl-prolyl cis-trans FT isomerase SlyD. FT /FTId=PRO_0000075358. FT DOMAIN 1 95 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. FT REGION 1 69 PPIase first part. {ECO:0000250}. FT REGION 76 120 IF-chaperone. {ECO:0000250}. FT REGION 129 151 PPIase second part. {ECO:0000250}. FT REGION 152 190 Metal-binding. {ECO:0000250}. FT COMPBIAS 141 146 Glu-rich (acidic). FT COMPBIAS 148 190 His-rich (basic). FT COMPBIAS 164 190 Gly-rich. SQ SEQUENCE 190 AA; 20658 MW; BB7991BA1F1C980D CRC64; MKVEKNVVVS ISYQVRTQDG VLVDEAPANQ PLEYLQGHNN LVIGLEKALE GKEVGDKFEV RVQPEEGYGA YSENMVQRVP KDVFQGVDEL EVGMRFLADT DIGPVPVVIT EIDGDEVVVD GNHMLAGQEL HFTVEVVAAR EATLEEIAHG HVHGAHSHDD DEEGHGCGCG GHHHEHNHEH NHGSCGCGGH // ID SIAP_HAEIN Reviewed; 329 AA. AC P44542; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Sialic acid-binding periplasmic protein SiaP; DE AltName: Full=Extracytoplasmic solute receptor protein SiaP; DE AltName: Full=N-acetylneuraminic-binding protein; DE AltName: Full=Neu5Ac-binding protein; DE Flags: Precursor; GN Name=siaP; OrderedLocusNames=HI_0146; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP FUNCTION, CHARACTERIZATION, SUBUNIT, AND MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=16262798; DOI=10.1111/j.1365-2958.2005.04901.x; RA Severi E., Randle G., Kivlin P., Whitfield K., Young R., Moxon R., RA Kelly D., Hood D., Thomas G.H.; RT "Sialic acid transport in Haemophilus influenzae is essential for RT lipopolysaccharide sialylation and serum resistance and is dependent RT on a novel tripartite ATP-independent periplasmic transporter."; RL Mol. Microbiol. 58:1173-1185(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-329 IN COMPLEX WITH SIALIC RP ACID ANALOG. RX PubMed=16702222; DOI=10.1074/jbc.M603463200; RA Mueller A., Severi E., Mulligan C., Watts A.G., Kelly D.J., RA Wilson K.S., Wilkinson A.J., Thomas G.H.; RT "Conservation of structure and mechanism in primary and secondary RT transporters exemplified by SiaP, a sialic acid binding virulence RT factor from Haemophilus influenzae."; RL J. Biol. Chem. 281:22212-22222(2006). CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic CC (TRAP) transport system SiaPT involved in the uptake of sialic CC acid. This protein specifically binds sialic acid with high CC affinity. {ECO:0000269|PubMed:16262798}. CC -!- SUBUNIT: The complex comprises the extracytoplasmic solute CC receptor protein SiaP, and the fused transmembrane protein SiaT. CC {ECO:0000269|PubMed:16262798, ECO:0000269|PubMed:16702222}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- MASS SPECTROMETRY: Mass=34165; Mass_error=2; Method=Electrospray; CC Range=24-329; Evidence={ECO:0000269|PubMed:16262798}; CC -!- MISCELLANEOUS: Is essential for lipopolysaccharide (LPS) CC sialylation and serum resistance. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 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; L42023; AAC21818.1; -; Genomic_DNA. DR PIR; H64143; H64143. DR RefSeq; NP_438315.1; NC_000907.1. DR RefSeq; WP_005694430.1; NC_000907.1. DR PDB; 2CEX; X-ray; 2.20 A; A/B/C/D=24-329. DR PDB; 2CEY; X-ray; 1.70 A; A=24-329. DR PDB; 2V4C; X-ray; 1.70 A; A=24-329. DR PDB; 2WX9; X-ray; 1.37 A; A=24-329. DR PDB; 2WYK; X-ray; 1.50 A; A=24-329. DR PDB; 2WYP; X-ray; 1.50 A; A=24-329. DR PDB; 2XA5; X-ray; 1.09 A; A=24-329. DR PDB; 2XWI; X-ray; 2.20 A; A=24-329. DR PDB; 2XWK; X-ray; 1.49 A; A=24-329. DR PDB; 2XWO; X-ray; 1.54 A; A=24-329. DR PDB; 2XWV; X-ray; 1.05 A; A=24-329. DR PDB; 2XXK; X-ray; 1.48 A; A=24-329. DR PDB; 3B50; X-ray; 1.40 A; A=24-329. DR PDBsum; 2CEX; -. DR PDBsum; 2CEY; -. DR PDBsum; 2V4C; -. DR PDBsum; 2WX9; -. DR PDBsum; 2WYK; -. DR PDBsum; 2WYP; -. DR PDBsum; 2XA5; -. DR PDBsum; 2XWI; -. DR PDBsum; 2XWK; -. DR PDBsum; 2XWO; -. DR PDBsum; 2XWV; -. DR PDBsum; 2XXK; -. DR PDBsum; 3B50; -. DR ProteinModelPortal; P44542; -. DR SMR; P44542; 24-329. DR STRING; 71421.HI0146; -. DR TCDB; 2.A.56.1.3; the tripartite atp-independent periplasmic transporter (trap-t) family. DR EnsemblBacteria; AAC21818; AAC21818; HI_0146. DR GeneID; 951056; -. DR KEGG; hin:HI0146; -. DR PATRIC; 20188783; VBIHaeInf48452_0148. DR eggNOG; ENOG4108ERU; Bacteria. DR eggNOG; COG1638; LUCA. DR OMA; PYYDEYL; -. DR OrthoDB; EOG65BDH9; -. DR PhylomeDB; P44542; -. DR EvolutionaryTrace; P44542; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR InterPro; IPR004682; TRAP_DctP. DR InterPro; IPR018389; TRAP_DctP/TeaA. DR Pfam; PF03480; DctP; 1. DR PIRSF; PIRSF006470; DctB; 1. DR TIGRFAMs; TIGR00787; dctP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Periplasm; Reference proteome; KW Signal; Sugar transport; Transport. FT SIGNAL 1 23 {ECO:0000305}. FT CHAIN 24 329 Sialic acid-binding periplasmic protein FT SiaP. FT /FTId=PRO_0000031816. FT BINDING 90 90 Sialic acid. FT BINDING 150 150 Sialic acid. FT BINDING 170 170 Sialic acid. FT BINDING 210 210 Sialic acid. FT STRAND 26 31 {ECO:0000244|PDB:2XWV}. FT HELIX 39 54 {ECO:0000244|PDB:2XWV}. FT TURN 55 57 {ECO:0000244|PDB:2XWV}. FT STRAND 58 64 {ECO:0000244|PDB:2XWV}. FT TURN 66 69 {ECO:0000244|PDB:2XWV}. FT HELIX 72 80 {ECO:0000244|PDB:2XWV}. FT STRAND 86 89 {ECO:0000244|PDB:2XWV}. FT HELIX 91 96 {ECO:0000244|PDB:2XWV}. FT HELIX 99 105 {ECO:0000244|PDB:2XWV}. FT TURN 107 109 {ECO:0000244|PDB:2XWV}. FT HELIX 113 121 {ECO:0000244|PDB:2XWV}. FT HELIX 124 137 {ECO:0000244|PDB:2XWV}. FT STRAND 139 156 {ECO:0000244|PDB:2XWV}. FT HELIX 161 164 {ECO:0000244|PDB:2XWV}. FT STRAND 168 171 {ECO:0000244|PDB:2XWV}. FT HELIX 175 184 {ECO:0000244|PDB:2XWV}. FT STRAND 187 190 {ECO:0000244|PDB:2XWV}. FT HELIX 193 195 {ECO:0000244|PDB:2XWV}. FT HELIX 196 201 {ECO:0000244|PDB:2XWV}. FT STRAND 204 211 {ECO:0000244|PDB:2XWV}. FT HELIX 212 217 {ECO:0000244|PDB:2XWV}. FT HELIX 220 222 {ECO:0000244|PDB:2XWV}. FT STRAND 225 228 {ECO:0000244|PDB:2XWV}. FT STRAND 234 242 {ECO:0000244|PDB:2XWV}. FT HELIX 243 246 {ECO:0000244|PDB:2XWV}. FT HELIX 251 285 {ECO:0000244|PDB:2XWV}. FT STRAND 289 291 {ECO:0000244|PDB:2XWV}. FT HELIX 296 301 {ECO:0000244|PDB:2XWV}. FT HELIX 303 325 {ECO:0000244|PDB:2XWV}. SQ SEQUENCE 329 AA; 36513 MW; 4E369E0D51DA5F93 CRC64; MMKLTKLFLA TAISLGVSSA VLAADYDLKF GMNAGTSSNE YKAAEMFAKE VKEKSQGKIE ISLYPSSQLG DDRAMLKQLK DGSLDFTFAE SARFQLFYPE AAVFALPYVI SNYNVAQKAL FDTEFGKDLI KKMDKDLGVT LLSQAYNGTR QTTSNRAINS IADMKGLKLR VPNAATNLAY AKYVGASPTP MAFSEVYLAL QTNAVDGQEN PLAAVQAQKF YEVQKFLAMT NHILNDQLYL VSNETYKELP EDLQKVVKDA AENAAKYHTK LFVDGEKDLV TFFEKQGVKI THPDLVPFKE SMKPYYAEFV KQTGQKGESA LKQIEAINP // ID SOHB_HAEIN Reviewed; 353 AA. AC P45315; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Probable protease SohB; DE EC=3.4.21.-; GN Name=sohB; OrderedLocusNames=HI_1682; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Possible protease. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S49 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; L42023; AAC23328.1; -; Genomic_DNA. DR PIR; D64136; D64136. DR RefSeq; NP_439824.1; NC_000907.1. DR RefSeq; WP_005694402.1; NC_000907.1. DR ProteinModelPortal; P45315; -. DR STRING; 71421.HI1682; -. DR MEROPS; S49.002; -. DR EnsemblBacteria; AAC23328; AAC23328; HI_1682. DR GeneID; 950509; -. DR KEGG; hin:HI1682; -. DR PATRIC; 20192115; VBIHaeInf48452_1761. DR eggNOG; ENOG4105ERU; Bacteria. DR eggNOG; COG0616; LUCA. DR KO; K04774; -. DR OMA; MMACIGE; -. DR OrthoDB; EOG6P5ZHQ; -. DR PhylomeDB; P45315; -. DR Proteomes; UP000000579; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002142; Peptidase_S49. DR InterPro; IPR013703; Peptidase_S49_N_proteobac. DR Pfam; PF01343; Peptidase_S49; 1. DR Pfam; PF08496; Peptidase_S49_N; 1. DR SUPFAM; SSF52096; SSF52096; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Membrane; Protease; KW Reference proteome; Serine protease; Transmembrane; KW Transmembrane helix. FT CHAIN 1 353 Probable protease SohB. FT /FTId=PRO_0000171449. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT ACT_SITE 181 181 Nucleophile. {ECO:0000250}. FT ACT_SITE 233 233 Proton donor/acceptor. {ECO:0000250}. SQ SEQUENCE 353 AA; 39872 MW; 4C2E6D75B0F88070 CRC64; MLNDILTGYG IFILEILTIL LLILAVVGLI ISYRQHNKSK VGELEIKDLS EEFNEQVRLL RDFNLSEEEQ KQRTKAEKKA EKQNAKKRKE KLKKGETLED EKKACVYVLD FCGDISASET TALREEISAI LNVAKSEDEV LLRLESPGGI VHNYGFAASQ LSRLKQKGIK LTVAVDKVAA SGGYMMACVA DKIVSAPFAV IGSIGVVAQI PNVHRLLKKH DVDVDVMTAG EFKRTVTVLG ENTEKGKQKF QQELEETHKL FKQFVSQNRP CLDIDKIATG EHWFGQQAIA LQLVDEISTS DDLILEKMKE KQVLNVKYRL KKSLIKKFGR QAEESAINII HRYSTKQSRD FMY // ID SLMA_HAEIN Reviewed; 218 AA. AC P29280; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 104. DE RecName: Full=Nucleoid occlusion factor SlmA {ECO:0000255|HAMAP-Rule:MF_01839}; GN Name=slmA {ECO:0000255|HAMAP-Rule:MF_01839}; GN OrderedLocusNames=HI_0955; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-218. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1542653; DOI=10.1073/pnas.89.5.1626; RA Chandler M.S.; RT "The gene encoding cAMP receptor protein is required for competence RT development in Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1626-1630(1992). CC -!- FUNCTION: Required for nucleoid occlusion (NO) phenomenon, which CC prevents Z-ring formation and cell division over the nucleoid. CC Acts as a DNA-associated cell division inhibitor that binds CC simultaneously chromosomal DNA and FtsZ, and disrupts the assembly CC of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed CC on non-Ter regions of the chromosome, preventing FtsZ CC polymerization at these regions. {ECO:0000255|HAMAP- CC Rule:MF_01839}. CC -!- SUBUNIT: Homodimer. Interacts with FtsZ. {ECO:0000255|HAMAP- CC Rule:MF_01839}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_01839}. CC -!- SIMILARITY: Belongs to the nucleoid occlusion factor SlmA family. CC {ECO:0000255|HAMAP-Rule:MF_01839}. CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_01839}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22616.1; -; Genomic_DNA. DR EMBL; M77207; AAA24951.1; -; Genomic_DNA. DR PIR; D64162; D64162. DR RefSeq; NP_439116.1; NC_000907.1. DR RefSeq; WP_005648000.1; NC_000907.1. DR ProteinModelPortal; P29280; -. DR STRING; 71421.HI0955; -. DR EnsemblBacteria; AAC22616; AAC22616; HI_0955. DR GeneID; 949937; -. DR KEGG; hin:HI0955; -. DR PATRIC; 20190569; VBIHaeInf48452_0997. DR eggNOG; ENOG4105EC0; Bacteria. DR eggNOG; COG1309; LUCA. DR KO; K05501; -. DR OMA; RNPGITR; -. DR OrthoDB; EOG6G7R3C; -. DR PhylomeDB; P29280; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0043565; F:sequence-specific DNA binding; 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:0010974; P:negative regulation of barrier septum assembly; IEA:InterPro. DR Gene3D; 1.10.357.10; -; 1. DR HAMAP; MF_01839; NO_factor_SlmA; 1. DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR023769; NO_SlmA. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR InterPro; IPR011075; Tet_transcr_reg_TetR-rel_C. DR Pfam; PF00440; TetR_N; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF48498; SSF48498; 1. DR PROSITE; PS01081; HTH_TETR_1; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 218 Nucleoid occlusion factor SlmA. FT /FTId=PRO_0000198971. FT DOMAIN 30 90 HTH tetR-type. {ECO:0000255|HAMAP- FT Rule:MF_01839}. FT DNA_BIND 53 72 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_01839}. SQ SEQUENCE 218 AA; 25577 MW; E17BD6600891B7D0 CRC64; MVEEQLSLSG VEEIAPKIET PKIEKRTVKE RRQQVLTVLI HMLHSERGME RMTTARLAKE VGVSEAALYR YFPSKTKMFE ALIEHIESTL LSRITASMRN ETQTMNRIHD ILQTILDFAR KNPGLTRVLT GHALMFEEAQ LQARVAQFFD RLEMQFVNIL QMRKLREGRA FNVDERIIAS HLVTLCEGQF MRYVRTNFRL NSSQSFEQQW RFIEPLFA // ID SLT_HAEIN Reviewed; 593 AA. AC P44888; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Putative soluble lytic murein transglycosylase; DE EC=4.2.2.n1; DE AltName: Full=Peptidoglycan lytic exotransglycosylase; DE Flags: Precursor; GN Name=slt; OrderedLocusNames=HI_0829; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of CC muropeptides during cell elongation and/or cell division (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Exolytic cleavage of the (1->4)-beta- CC glycosidic linkage between N-acetylmuramic acid (MurNAc) and N- CC acetylglucosamine (GlcNAc) residues in peptidoglycan, from either CC the reducing or the non-reducing ends of the peptidoglycan chains, CC with concomitant formation of a 1,6-anhydrobond in the MurNAc CC residue. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the transglycosylase Slt 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; L42023; AAC22487.1; -; Genomic_DNA. DR PIR; C64097; C64097. DR RefSeq; NP_438989.1; NC_000907.1. DR RefSeq; WP_010869063.1; NC_000907.1. DR ProteinModelPortal; P44888; -. DR STRING; 71421.HI0829; -. DR EnsemblBacteria; AAC22487; AAC22487; HI_0829. DR GeneID; 949843; -. DR KEGG; hin:HI0829; -. DR PATRIC; 20190313; VBIHaeInf48452_0870. DR eggNOG; ENOG4107SC1; Bacteria. DR eggNOG; COG0741; LUCA. DR KO; K08309; -. DR OMA; QWFELAV; -. DR OrthoDB; EOG6S52QZ; -. DR PhylomeDB; P44888; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-EC. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro. DR Gene3D; 1.10.1240.20; -; 1. DR Gene3D; 1.25.20.10; -; 1. DR InterPro; IPR023346; Lysozyme-like_dom. DR InterPro; IPR016026; Lytic_TGlyclase_suprhlx_U/L. DR InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L. DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U. DR InterPro; IPR000189; Transglyc_AS. DR InterPro; IPR008258; Transglycosylase_SLT_dom_1. DR Pfam; PF01464; SLT; 1. DR Pfam; PF14718; SLT_L; 1. DR SUPFAM; SSF48435; SSF48435; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation; Complete proteome; Lyase; Periplasm; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 593 Putative soluble lytic murein FT transglycosylase. FT /FTId=PRO_0000032780. FT REGION 440 529 Slt-type domain. FT ACT_SITE 453 453 {ECO:0000305}. SQ SEQUENCE 593 AA; 68691 MW; 774DDD3D38217CEE CRC64; MKKVALISLC IFTALSAFAD SPNTATASIN LEQEKQNWEL AQHQDYLKRL KQREVFLQVE GLLKSAVKKQ QFSEATQNIT KTLIDSLQGY PLQYDLLARF WETKIAFLQN DDIQGRQQAI NELNALVQQN YPFVTPAFQA LLQKLSTLNE QQTSATSDNA KENNRVQKEQ NQVENPKQLA EIVRKSDPNT LDKTVLIDAF PRYLKTLPEQ MNNLSFESYQ KWANTWQLSE DEIKQWKIAF LNRFFDNENT DFQKWRDEQI RQLQTDNLTE RRLRMAIWQK TELTSWLNLL SAESKSKQEW RYWEAKQDIL KNTKKLTALS KERGFYPMLA ATQLKQAYQL NVPIAPSFTQ AEQLPFKQVF AMITELRELG RNGLAKQRWR ILLDNVDFTT QLKLSEYAKN QQWFELAVDA SIVAKAWDYL SLRLPNAYSE YFNAALQNLN ISKTFAMAIA RQESAWNPMA QSSANARGLM QLLPSTAKLT AENNQLPYQG EQDLFKPLNN ILLGTAHLNE LNGKYPNNRI LIAAAYNAGA NRVGKWLSRA SGKLALDEFV ASIPFYETRG YVQNVVAYDF YYQILQNKEN PQIFSQEELN RLY // ID SRMB_HAEIN Reviewed; 439 AA. AC P44701; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=ATP-dependent RNA helicase SrmB {ECO:0000255|HAMAP-Rule:MF_00967}; DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00967}; GN Name=srmB {ECO:0000255|HAMAP-Rule:MF_00967}; GN OrderedLocusNames=HI_0422; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the CC 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated CC ATP hydrolysis and RNA unwinding activity. {ECO:0000255|HAMAP- CC Rule:MF_00967}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00967}. CC -!- SUBUNIT: Interacts with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00967}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00967}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. SrmB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00967}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00967}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00967}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22078.1; -; Genomic_DNA. DR PIR; H64066; H64066. DR RefSeq; NP_438583.1; NC_000907.1. DR RefSeq; WP_005693742.1; NC_000907.1. DR ProteinModelPortal; P44701; -. DR STRING; 71421.HI0422; -. DR EnsemblBacteria; AAC22078; AAC22078; HI_0422. DR GeneID; 949526; -. DR KEGG; hin:HI0422; -. DR PATRIC; 20189397; VBIHaeInf48452_0442. DR eggNOG; ENOG4105C1J; Bacteria. DR eggNOG; COG0513; LUCA. DR KO; K05590; -. DR OMA; DCRSVEM; -. DR OrthoDB; EOG6GBMBM; -. DR PhylomeDB; P44701; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00967; DEAD_helicase_SrmB; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR028621; DEAD_helicase_SrmB. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. 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; PS00039; DEAD_ATP_HELICASE; 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; Cytoplasm; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; Ribosome biogenesis. FT CHAIN 1 439 ATP-dependent RNA helicase SrmB. FT /FTId=PRO_0000055110. FT DOMAIN 35 209 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00967}. FT DOMAIN 237 387 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00967}. FT NP_BIND 48 55 ATP. {ECO:0000255|HAMAP-Rule:MF_00967}. FT MOTIF 4 32 Q motif. FT MOTIF 157 160 DEAD box. SQ SEQUENCE 439 AA; 49805 MW; 7543942CE35B20C4 CRC64; MNLSQFEQFD LSPELLKALE KKGYSRPTAI QMEAIPAAME ESDVLGSAPT GTGKTAAFLL PALQHLLDYP RRKPGPPRIL VLTPTRELAM QVAEQAEELA QFTHLNIATI TGGVAYQNHG DVFNTNQDLV VATPGRLLQY IKEENFDCRS VEMLIFDEAD RMLQMGFGQD AEKIAAETRW RKQTLLFSAT LEGELLVDFA ERLLNDPVKV DAEPSRRERK KINQWYYHAD SNEHKIKLLA RFIETEEVTR GIVFIRRRED ARELSETLRK RGIRSAYLEG EMAQTQRNNA IDKLKSGIVT VLVATDVAAR GIDIDDVSHV MNFDLPYSAD TYLHRIGRTA RAGKKGTAVS FVEAHDYKLL GKIKRYTEEI LKARILAGLE PRTKPPKDGE VKSVSKKQKA RIKEKREEKK KTEAKKKVKL RHKDTKNIGK RRKPSNSNV // ID SMF_HAEIN Reviewed; 373 AA. AC P43862; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Protein smf; DE AltName: Full=DNA-processing chain A; GN Name=smf; Synonyms=dprA; OrderedLocusNames=HI_0985; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7768823; RA Karudapuram S., Zhao X., Barcak G.J.; RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a RT gene required for chromosomal but not plasmid DNA transformation."; RL J. Bacteriol. 177:3235-3240(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential for efficient chromosomal DNA transformation CC but not required for plasmid transformation. CC {ECO:0000269|PubMed:7768823}. CC -!- SIMILARITY: Belongs to the smf 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; U18657; AAA70111.1; -; Genomic_DNA. DR EMBL; L42023; AAC22646.1; -; Genomic_DNA. DR PIR; D64106; D64106. DR RefSeq; NP_439148.1; NC_000907.1. DR RefSeq; WP_005693325.1; NC_000907.1. DR ProteinModelPortal; P43862; -. DR STRING; 71421.HI0985; -. DR EnsemblBacteria; AAC22646; AAC22646; HI_0985. DR GeneID; 949984; -. DR KEGG; hin:HI0985; -. DR PATRIC; 20190631; VBIHaeInf48452_1028. DR eggNOG; ENOG4105C79; Bacteria. DR eggNOG; COG0758; LUCA. DR KO; K04096; -. DR OMA; GEYWAKH; -. DR OrthoDB; EOG6DG2TK; -. DR PhylomeDB; P43862; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009294; P:DNA mediated transformation; IEA:InterPro. DR InterPro; IPR003488; DprA. DR Pfam; PF02481; DNA_processg_A; 1. DR TIGRFAMs; TIGR00732; dprA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 373 Protein smf. FT /FTId=PRO_0000209158. SQ SEQUENCE 373 AA; 41640 MW; 26E0335372EFE61F CRC64; MNDITYTLLR LMQVPKLGGV GIDKILSNIT LNELLNYDDV AFRQMGWGAI QIRRWFKPEA KFIEPALVWS QKEGNHLVNY FSPFYPFLLK QTASFPPLLF VKGNLTALSQ RQMAMVGSRY CTTYGEYWAK HFATELSLAG FTITSGLALG IDGHCHQAVV NIQGQTIAVL GSGLEQIYPS KHQRLSAQII ENNGALVSEF LPNQAPIAAN FPRRNRIISG LSVGTLVVEA TEKSGSLITA RYALEQNREV FAVPGNIQNK SSQGCHRLIK QGAMLVENAK DILETLYQHS IHSQTEIDFD QIAVPNYTPP PDPRRLVEAP SHPKLYSRIG YTPVSIDDLA EEFNLSVDVL LVQLLDLELQ DLIISENGLY KRV // ID SODM_HAEIN Reviewed; 215 AA. AC P43725; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 110. DE RecName: Full=Superoxide dismutase [Mn]; DE EC=1.15.1.1; GN Name=sodA; OrderedLocusNames=HI_1088; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B; RX PubMed=7934846; DOI=10.1111/j.1365-2958.1993.tb00954.x; RA Kroll J.S., Langford P.R., Saah J.R., Loynds B.M.; RT "Molecular and genetic characterization of superoxide dismutase in RT Haemophilus influenzae type b."; RL Mol. Microbiol. 10:839-848(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP PROTEIN SEQUENCE OF 2-6. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological CC systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase 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; X73832; CAA52054.1; -; Genomic_DNA. DR EMBL; L42023; AAC22745.1; -; Genomic_DNA. DR PIR; C64182; C64182. DR PIR; S39871; S39871. DR RefSeq; NP_439245.1; NC_000907.1. DR RefSeq; WP_005693413.1; NC_000907.1. DR ProteinModelPortal; P43725; -. DR SMR; P43725; 2-207. DR STRING; 71421.HI1088; -. DR EnsemblBacteria; AAC22745; AAC22745; HI_1088. DR GeneID; 950093; -. DR KEGG; hin:HI1088; -. DR PATRIC; 20190841; VBIHaeInf48452_1133. DR eggNOG; ENOG4105CK4; Bacteria. DR eggNOG; COG0605; LUCA. DR KO; K04564; -. DR OMA; ILGMDVW; -. DR OrthoDB; EOG63NMNT; -. DR PhylomeDB; P43725; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR PANTHER; PTHR11404; PTHR11404; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF46609; SSF46609; 1. DR SUPFAM; SSF54719; SSF54719; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Manganese; KW Metal-binding; Oxidoreductase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10675023}. FT CHAIN 2 215 Superoxide dismutase [Mn]. FT /FTId=PRO_0000160038. FT METAL 27 27 Manganese. {ECO:0000250}. FT METAL 83 83 Manganese. {ECO:0000250}. FT METAL 170 170 Manganese. {ECO:0000250}. FT METAL 174 174 Manganese. {ECO:0000250}. FT CONFLICT 208 215 TAHSNCAK -> STL (in Ref. 1). FT {ECO:0000305}. SQ SEQUENCE 215 AA; 24110 MW; 80FAC9F1C0D59D25 CRC64; MSYTLPELGY AYNALEPHFD AQTMEIHHSK HHQAYVNNAN AALEGLPAEL VEMYPGHLIS NLDKIPAEKR GALRNNAGGH TNHSLFWKSL KKGTTLQGAL KDAIERDFGS VDAFKAEFEK AAATRFGSGW AWLVLTAEGK LAVVSTANQD NPLMGKEVAG CEGFPLLGLD VWEHAYYLKF QNRRPDYIKE FWNVVNWDFV AERFEQKTAH SNCAK // ID SOTB_HAEIN Reviewed; 396 AA. AC P44535; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Probable sugar efflux transporter {ECO:0000255|HAMAP-Rule:MF_00517}; GN Name=sotB {ECO:0000255|HAMAP-Rule:MF_00517}; GN OrderedLocusNames=HI_0135; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the efflux of sugars. The physiological role CC may be the reduction of the intracellular concentration of toxic CC sugars or sugar metabolites. {ECO:0000255|HAMAP-Rule:MF_00517}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00517}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00517}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. SotB CC (TC 2.A.1.2) family. {ECO:0000255|HAMAP-Rule:MF_00517}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21806.1; -; Genomic_DNA. DR PIR; E64143; E64143. DR RefSeq; NP_438304.1; NC_000907.1. DR RefSeq; WP_005694422.1; NC_000907.1. DR ProteinModelPortal; P44535; -. DR STRING; 71421.HI0135; -. DR EnsemblBacteria; AAC21806; AAC21806; HI_0135. DR GeneID; 951043; -. DR KEGG; hin:HI0135; -. DR PATRIC; 20188757; VBIHaeInf48452_0137. DR eggNOG; ENOG4105F27; Bacteria. DR eggNOG; COG2814; LUCA. DR KO; K03445; -. DR OMA; LVMRISP; -. DR OrthoDB; EOG6TJ7VJ; -. DR PhylomeDB; P44535; -. DR Proteomes; UP000000579; 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:0015144; F:carbohydrate transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00517; MFS_SotB; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR023495; Sugar_effux_transptr_put. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 396 Probable sugar efflux transporter. FT /FTId=PRO_0000209327. FT TRANSMEM 15 35 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 51 71 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 84 104 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 109 129 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 137 157 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 168 188 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 209 229 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 245 265 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 273 293 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 297 317 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 333 353 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. FT TRANSMEM 365 385 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00517}. SQ SEQUENCE 396 AA; 43360 MW; B7994F2F9E9339C8 CRC64; MSLYLKAEKI QSWRVLIMAC AGFIFNTTEF VPVAMLSDIA QSFDMQTADT GLMMTVYAWT VLIMSLPAML ATGNMERKSL LIKLFIIFIV GHILSVIAWN FWILLLARMC IALAHSVFWS ITASLVMRIS PKHKKTQALG MLAIGTALAT ILGLPIGRIV GQLVGWRVTF GIIAVLALSI MFLIIRLLPN LPSKNAGSIA SLPLLAKRPL LLWLYVTTAI VISAHFTAYT YIEPFMIDVG HLDPNFATAV LLVFGFSGIA ASLLFNRLYR FAPTKFIVVS MSLLMFSLLL LLFSTKTIIA MFSLVFIWGI GISCIGLSLQ MRVLKLAPDA TDVATAIYSG IFNAGIGAGA LFGNLATTYL GLNEIGYTGA ALGLIGFIIF ITTHLKYRHT FLLQNK // ID SPOT_HAEIN Reviewed; 677 AA. AC P43811; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=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=HI_1741; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. 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; L42023; AAC23388.1; -; Genomic_DNA. DR PIR; F64139; F64139. DR RefSeq; NP_439885.2; NC_000907.1. DR ProteinModelPortal; P43811; -. DR STRING; 71421.HI1741; -. DR EnsemblBacteria; AAC23388; AAC23388; HI_1741. DR GeneID; 950884; -. DR KEGG; hin:HI1741; -. DR PATRIC; 20192253; VBIHaeInf48452_1824. DR eggNOG; ENOG4105CWR; Bacteria. DR eggNOG; COG0317; LUCA. DR KO; K01139; -. DR OMA; NIWTEEL; -. DR OrthoDB; EOG6SV551; -. DR UniPathway; UPA00908; UER00886. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005618; C:cell wall; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008728; F:GTP diphosphokinase activity; IBA:GO_Central. DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central. DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IBA:GO_Central. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR004811; RelA/Spo_fam. DR InterPro; IPR007685; RelA_SpoT. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF13291; ACT_4; 1. DR Pfam; PF13328; HD_4; 1. DR Pfam; PF04607; RelA_SpoT; 1. DR Pfam; PF02824; TGS; 1. DR SMART; SM00471; HDc; 1. DR SMART; SM00954; RelA_SpoT; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00691; spoT_relA; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Reference proteome. FT CHAIN 1 677 Guanosine-3',5'-bis(diphosphate) 3'- FT pyrophosphohydrolase. FT /FTId=PRO_0000166571. FT DOMAIN 18 117 HD. FT DOMAIN 601 675 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 677 AA; 76726 MW; FB12CE3C33A18B93 CRC64; MIARDAHEGQ FRSSGEPYIT HPVAVASIIA QLHLDHEAVM AALLHDVIED TPYTEEQLKE EFGASVAEIV DGVSKLDKLK FRTRQEAQVE NFRKMILAMT RDIRVVLIKL ADRTHNMRTL GSLRPDKRRR IAKETLEIYC PLAHRLGIEH IKNELEDLSF QAMHPHRYEV LKKLVDVARS NRQDLIERIS QEIKVRLENS GIFARVWGRE KHLYKIYQKM RIKDQEFHSI MDIYAFRVIV KNVDDCYRVL GQMHNLYKPR PGRVKDYIAV PKANGYQSLQ TSMIGPKGVP VEVHIHTEDM EQVAEMGITA HWVYKENGKN DSTTAQIRVQ RWLQSLVEIQ QSVGNSFEFI ENVKSEFFPK EIYVFTPKGR IVELPMGATA VDFAYAVHSD VGNTCVGVTV EHKPYPLSKA LESGQTVNII TDPNAHPEVA WLNFVVTARA KTRIRHYLKQ RCEEDAVKLG EVELNVALQP HNLGDFSIQQ IRTVLDALAL SSLDELLREI GLGNQSASMI AHQFVGVPLE SANTKNLEFE SKILTIAPMQ VGKTQFAQCC HPILGDPIVG CCTEKNTVVV HHQHCASLKN ACRQSLAKWD NVQSAVNFEA ELQIEILNEQ NALLSLMTAI SASESSLQNI WTEELENNLL LVILQVCVKD IKHLANIVHR IKGITGVVNV KRNINEL // ID SSPB_HAEIN Reviewed; 150 AA. AC P45206; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Stringent starvation protein B homolog; DE AltName: Full=Adapter protein SspB; DE AltName: Full=Specificity-enhancing factor SspB; GN Name=sspB; OrderedLocusNames=HI_1440; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Enhances recognition of ssrA-tagged proteins by the CC ClpX-ClpP protease; the ssrA degradation tag (AANDENYALAA) is CC added trans-translationally to proteins that are stalled on the CC ribosome, freeing the ribosome and targeting stalled peptides for CC degradation. SspB activates the ATPase activity of ClpX. Seems to CC act in concert with SspA in the regulation of several proteins CC during exponential and stationary-phase growth (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: Also stimulates degradation of the N-terminus of RseA CC (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in CC a non-ssrA-mediated fashion. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SspB 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; L42023; AAC23089.1; -; Genomic_DNA. DR PIR; D64123; D64123. DR RefSeq; NP_439592.1; NC_000907.1. DR RefSeq; WP_005650453.1; NC_000907.1. DR PDB; 1OU8; X-ray; 1.60 A; A/B=1-111. DR PDB; 1OU9; X-ray; 1.80 A; A/B/C=1-129. DR PDB; 1OUL; X-ray; 2.20 A; A/B=1-129. DR PDB; 1TWB; X-ray; 1.90 A; A/B=1-110. DR PDB; 1ZSZ; X-ray; 2.00 A; A=1-110, B=1-111, C=1-129. DR PDBsum; 1OU8; -. DR PDBsum; 1OU9; -. DR PDBsum; 1OUL; -. DR PDBsum; 1TWB; -. DR PDBsum; 1ZSZ; -. DR ProteinModelPortal; P45206; -. DR SMR; P45206; 1-122. DR STRING; 71421.HI1440; -. DR EnsemblBacteria; AAC23089; AAC23089; HI_1440. DR GeneID; 950343; -. DR KEGG; hin:HI1440; -. DR PATRIC; 20191585; VBIHaeInf48452_1502. DR eggNOG; ENOG4105KB2; Bacteria. DR eggNOG; COG2969; LUCA. DR KO; K03600; -. DR OMA; NDFISFT; -. DR OrthoDB; EOG6X6RFF; -. DR PhylomeDB; P45206; -. DR EvolutionaryTrace; P45206; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.30.30.220; -; 1. DR InterPro; IPR007481; SspB. DR Pfam; PF04386; SspB; 1. DR PIRSF; PIRSF005276; SspB; 1. DR SUPFAM; SSF101738; SSF101738; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 150 Stringent starvation protein B homolog. FT /FTId=PRO_0000072220. FT HELIX 9 22 {ECO:0000244|PDB:1OU8}. FT STRAND 27 32 {ECO:0000244|PDB:1OU8}. FT STRAND 33 35 {ECO:0000244|PDB:1OUL}. FT HELIX 42 44 {ECO:0000244|PDB:1OU8}. FT STRAND 46 48 {ECO:0000244|PDB:1OUL}. FT STRAND 49 53 {ECO:0000244|PDB:1OU8}. FT TURN 56 58 {ECO:0000244|PDB:1OU8}. FT STRAND 60 64 {ECO:0000244|PDB:1OU8}. FT STRAND 66 75 {ECO:0000244|PDB:1OU8}. FT STRAND 78 85 {ECO:0000244|PDB:1OU8}. FT HELIX 86 88 {ECO:0000244|PDB:1OU8}. FT STRAND 89 94 {ECO:0000244|PDB:1OU8}. FT TURN 95 97 {ECO:0000244|PDB:1OU8}. FT STRAND 100 102 {ECO:0000244|PDB:1OU8}. FT HELIX 107 109 {ECO:0000244|PDB:1OU8}. SQ SEQUENCE 150 AA; 17168 MW; E8A2E3BD550732A1 CRC64; MEYKSSPKRP YLLRAYYDWL VDNSFTPYLV VDATYLGVNV PVEYVKDGQI VLNLSASATG NLQLTNDFIQ FNARFKGVSR ELYIPMGAAL AIYARENGDG VMFEPEEIYD ELNIEPDTEQ PTGFYEAVDK PKKREEKKKT KSVSHLRIVD // ID SSTT_HAEIN Reviewed; 414 AA. AC P45246; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Serine/threonine transporter SstT {ECO:0000255|HAMAP-Rule:MF_01582}; DE AltName: Full=Na(+)/serine-threonine symporter {ECO:0000255|HAMAP-Rule:MF_01582}; GN Name=sstT {ECO:0000255|HAMAP-Rule:MF_01582}; GN OrderedLocusNames=HI_1545; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the import of serine and threonine into the CC cell, with the concomitant import of sodium (symport system). CC {ECO:0000255|HAMAP-Rule:MF_01582}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01582}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01582}. CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter CC (TC 2.A.23) family. {ECO:0000255|HAMAP-Rule:MF_01582}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23195.1; -; Genomic_DNA. DR PIR; H64128; H64128. DR RefSeq; NP_439694.1; NC_000907.1. DR RefSeq; WP_010869240.1; NC_000907.1. DR ProteinModelPortal; P45246; -. DR STRING; 71421.HI1545; -. DR EnsemblBacteria; AAC23195; AAC23195; HI_1545. DR GeneID; 950408; -. DR KEGG; hin:HI1545; -. DR PATRIC; 20191815; VBIHaeInf48452_1616. DR eggNOG; ENOG4107QV7; Bacteria. DR eggNOG; COG3633; LUCA. DR KO; K07862; -. DR OMA; GFVFPTE; -. DR OrthoDB; EOG63Z78S; -. DR PhylomeDB; P45246; -. DR Proteomes; UP000000579; 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:0022889; F:serine transmembrane transporter activity; IEA:InterPro. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR GO; GO:0015565; F:threonine efflux transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.10.3860.10; -; 1. DR HAMAP; MF_01582; Ser_Thr_transp_SstT; 1. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR023025; Ser_Thr_transp_SstT. DR PANTHER; PTHR11958; PTHR11958; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; SSF118215; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 414 Serine/threonine transporter SstT. FT /FTId=PRO_0000202120. FT TRANSMEM 22 42 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 54 74 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 89 109 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 148 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 189 209 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 223 243 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 305 325 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 337 357 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. SQ SEQUENCE 414 AA; 43341 MW; CD976418CD5BA0AE CRC64; MNTSRLFSLL FQGGLVKRIA AGLVLGIVVA LISAPLQETI GFNLAEKVGV LGTIFVKALR AVAPILIFFL VMAALANRKI GTKSNMKEII VLYLLGTFLA AFVAVIAGFA FPTEVVLAAK EDSSSAPQAV GQVLLTLILN VVDDPLNAIF KANFIGVLAW SIGLGLALRH ASDATKNVLS DFAEGVSKIV HVIISFAPFG VFGLVAETLS DKGLVALGGY VQLLAVLIGT MLFTAFVVNP ILVYWKIRRN PYPLVWTCVR ESGVTAFFTR SSAANIPVNI ELAKRLNLDE ETYSVSIPLG ANINMAGAAI TITILTLAAV HTLGLEVSFV SALLLSIVAA LCACGASGVA GGSLLLIPLA CSLFGISDDV AAQMIGVGFI IGILQDSTET ALNSSTDVLF TAAVCMEEER KNAA // ID SPRT_HAEIN Reviewed; 156 AA. AC P44119; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Protein SprT; GN Name=sprT; OrderedLocusNames=HI_1173; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion. {ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SprT family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SprT-like domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22826.1; -; Genomic_DNA. DR PIR; B64021; B64021. DR RefSeq; NP_439331.1; NC_000907.1. DR RefSeq; WP_010869145.1; NC_000907.1. DR STRING; 71421.HI1173; -. DR EnsemblBacteria; AAC22826; AAC22826; HI_1173. DR GeneID; 950125; -. DR KEGG; hin:HI1173; -. DR PATRIC; 20191025; VBIHaeInf48452_1225. DR eggNOG; ENOG4105GPY; Bacteria. DR eggNOG; COG3091; LUCA. DR KO; K02742; -. DR OMA; QPHGEEW; -. DR OrthoDB; EOG661H7V; -. DR PhylomeDB; P44119; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00746; SprT; 1. DR InterPro; IPR006640; SprT-like_domain. DR InterPro; IPR023483; Uncharacterised_SprT. DR Pfam; PF10263; SprT-like; 1. DR SMART; SM00731; SprT; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 156 Protein SprT. FT /FTId=PRO_0000213270. FT DOMAIN 11 152 SprT-like. FT ACT_SITE 66 66 {ECO:0000250}. FT METAL 65 65 Zinc. {ECO:0000255}. FT METAL 69 69 Zinc. {ECO:0000255}. SQ SEQUENCE 156 AA; 18684 MW; BBEF66F0585C465A CRC64; MQRKLNQSLL LAEAYFKRKF TMPEVNYELR GIKAGVAYLQ KNEIKFNRTL LQENTDEFIR QVVPHELAHL IVYQMFGRVK PHGKEWQLVM NEIFKLPADT CHQFDIKNVQ GKTFEYRCAC QTHFLTIRRH NKIMKENIEY LCKKCRGKLV FVDDEE // ID SRP54_HAEIN Reviewed; 462 AA. AC P44518; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. 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=HI_0106; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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. Interaction with FtsY leads to the transfer of the RNC CC complex to the Sec translocase for insertion into the membrane, CC the hydrolysis of GTP by both Ffh and FtsY, and the dissociation CC of the SRP-FtsY complex into the individual components. CC {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. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. 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; L42023; AAC21784.1; -; Genomic_DNA. DR PIR; H64048; H64048. DR RefSeq; NP_438280.1; NC_000907.1. DR RefSeq; WP_005693814.1; NC_000907.1. DR ProteinModelPortal; P44518; -. DR SMR; P44518; 2-431. DR STRING; 71421.HI0106; -. DR EnsemblBacteria; AAC21784; AAC21784; HI_0106. DR GeneID; 951009; -. DR KEGG; hin:HI0106; -. DR PATRIC; 20188679; VBIHaeInf48452_0109. DR eggNOG; ENOG4105CB9; Bacteria. DR eggNOG; COG0541; LUCA. DR KO; K03106; -. DR OMA; MLPGMGQ; -. DR OrthoDB; EOG62K1ZH; -. DR PhylomeDB; P44518; -. DR Proteomes; UP000000579; 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 1 462 Signal recognition particle protein. FT /FTId=PRO_0000101156. FT NP_BIND 107 114 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 190 194 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 248 251 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. SQ SEQUENCE 462 AA; 50843 MW; 16AC32089A158F7A CRC64; MFENLSDRLS KTLRNITGKG RLTEDNIKET LREVRMALLE ADVALPVVRE FIAKVKESAL GEEVNKSLTP GQEFLKIVQR ELEKAMGEAN ESLNLATQPP AVILMAGLQG AGKTTSVGKL AKFLRERHKK KVLVVSADVY RPAAIKQLET LAQSVGVDFF PSDVKQNPVD IAKSALADAK LKFYDVLIVD TAGRLHVDTE MMDEIKQVHA ALNPIETLFT VDAMTGQDAA NTAKAFNEAL PLTGVILTKV DGDARGGAAL SIRQITGKPI KFLGVGEKTE ALEPFHPDRV ASRILGMGDV LSLIEDLERS VDREKAEKMA QKFKKGDDFT LDDFREQLIE MKKMGGMMSM LEKLPGAKNL SEHVKNQVDD KMFVKMEAII NSMTLKERAN PDIIKGSRRR RIALGSGTQV QDVNKLLKQF DEMQRMMKKM RKGGMAKMMR GMQGLMGGGL GGLGGLGGMF KR // ID SSPA_HAEIN Reviewed; 212 AA. AC P45207; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Stringent starvation protein A homolog; GN Name=sspA; OrderedLocusNames=HI_1441; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-212. RG New York structural genomix research consortium (NYSGXRC); RT "Structure of stringent starvation protein a homolog from Haemophilus RT influenzae."; RL Submitted (MAR-2010) to the PDB data bank. CC -!- FUNCTION: Forms an equimolar complex with the RNA polymerase CC holoenzyme (RNAP) but not with the core enzyme. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23090.1; -; Genomic_DNA. DR PIR; E64123; E64123. DR RefSeq; NP_439593.1; NC_000907.1. DR RefSeq; WP_005650452.1; NC_000907.1. DR PDB; 3LYK; X-ray; 2.10 A; A/B=12-212. DR PDBsum; 3LYK; -. DR ProteinModelPortal; P45207; -. DR SMR; P45207; 4-203. DR STRING; 71421.HI1441; -. DR DNASU; 950832; -. DR EnsemblBacteria; AAC23090; AAC23090; HI_1441. DR GeneID; 950832; -. DR KEGG; hin:HI1441; -. DR PATRIC; 20191587; VBIHaeInf48452_1503. DR eggNOG; ENOG4107MKT; Bacteria. DR eggNOG; COG0625; LUCA. DR KO; K03599; -. DR OMA; LLMHRIQ; -. DR OrthoDB; EOG6MWN8X; -. DR PhylomeDB; P45207; -. DR EvolutionaryTrace; P45207; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0001000; F:bacterial-type RNA polymerase core enzyme binding; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SUPFAM; SSF47616; SSF47616; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 212 Stringent starvation protein A homolog. FT /FTId=PRO_0000185880. FT DOMAIN 9 87 GST N-terminal. FT DOMAIN 92 212 GST C-terminal. FT STRAND 12 15 {ECO:0000244|PDB:3LYK}. FT HELIX 20 32 {ECO:0000244|PDB:3LYK}. FT STRAND 37 40 {ECO:0000244|PDB:3LYK}. FT HELIX 48 53 {ECO:0000244|PDB:3LYK}. FT STRAND 61 64 {ECO:0000244|PDB:3LYK}. FT STRAND 67 71 {ECO:0000244|PDB:3LYK}. FT HELIX 72 82 {ECO:0000244|PDB:3LYK}. FT HELIX 93 109 {ECO:0000244|PDB:3LYK}. FT HELIX 111 119 {ECO:0000244|PDB:3LYK}. FT HELIX 122 138 {ECO:0000244|PDB:3LYK}. FT HELIX 140 145 {ECO:0000244|PDB:3LYK}. FT STRAND 146 148 {ECO:0000244|PDB:3LYK}. FT STRAND 151 153 {ECO:0000244|PDB:3LYK}. FT HELIX 156 169 {ECO:0000244|PDB:3LYK}. FT TURN 170 172 {ECO:0000244|PDB:3LYK}. FT HELIX 180 191 {ECO:0000244|PDB:3LYK}. FT HELIX 194 199 {ECO:0000244|PDB:3LYK}. SQ SEQUENCE 212 AA; 24290 MW; 8BC4DC08CFAFF115 CRC64; MSSASSKRSV MTLFSNKDDI YCHQVKIVLA EKGVLYENAE VDLQALPEDL MELNPYGTVP TLVDRDLVLF NSRIIMEYLD ERFPHPPLMQ VYPVSRAKDR LLMLRIEQDW YPTLAKAENG TEKEKTSALK QLKEELLGIA PIFQQMPYFM NEEFGLVDCY VAPLLWKLKH LGVEFTGTGS KAIKAYMERV FTRDSFLQSV GEAAPKNLMD DK // ID SSRP_HAEIN Reviewed; 161 AA. AC P44967; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, 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}; GN OrderedLocusNames=HI_0981; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11805338; DOI=10.1073/pnas.012602299; RA Akerley B.J., Rubin E.J., Novick V.L., Amaya K., Judson N., RA Mekalanos J.J.; RT "A genome-scale analysis for identification of genes required for RT growth or survival of Haemophilus influenzae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:966-971(2002). 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 disrupted. CC {ECO:0000269|PubMed:11805338}. 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; L42023; AAC22643.1; -; Genomic_DNA. DR PIR; B64106; B64106. DR RefSeq; NP_439144.1; NC_000907.1. DR RefSeq; WP_005647965.1; NC_000907.1. DR ProteinModelPortal; P44967; -. DR STRING; 71421.HI0981; -. DR EnsemblBacteria; AAC22643; AAC22643; HI_0981. DR GeneID; 950039; -. DR KEGG; hin:HI0981; -. DR PATRIC; 20190623; VBIHaeInf48452_1024. DR eggNOG; ENOG4108UH4; Bacteria. DR eggNOG; COG0691; LUCA. DR KO; K03664; -. DR OMA; FLLNAHI; -. DR OrthoDB; EOG6HXJ9P; -. DR PhylomeDB; P44967; -. DR Proteomes; UP000000579; 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 1 161 SsrA-binding protein. FT /FTId=PRO_0000102957. SQ SEQUENCE 161 AA; 18433 MW; 58223CA1E3443529 CRC64; MTKKKVKPNS NTIALNKRAR HDYFIEDEIE AGLELQGWEV KSMRAGKANI SDSYVIFKNG EAFLFGASIQ PLNVASTHIV CDPTRTRKLL LNKRELASLF GKANRDGFTI VALSLYWKSA WAKVKIGLAK GKKQQDKRDD IKEREWKVTK DRIMKNAHRR S // ID SURA_HAEIN Reviewed; 313 AA. AC P44721; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Putative peptidyl-prolyl cis-trans isomerase SurA; DE Short=PPIase SurA; DE EC=5.2.1.8; DE AltName: Full=Chaperone SurA homolog; DE AltName: Full=Rotamase SurA; DE Flags: Precursor; GN Name=surA; OrderedLocusNames=HI_0458; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Chaperone involved in the folding of extracytoplasmic CC proteins. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00278}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22116.1; -; Genomic_DNA. DR PIR; F64069; F64069. DR RefSeq; NP_438619.1; NC_000907.1. DR RefSeq; WP_005693706.1; NC_000907.1. DR ProteinModelPortal; P44721; -. DR STRING; 71421.HI0458; -. DR EnsemblBacteria; AAC22116; AAC22116; HI_0458. DR GeneID; 949829; -. DR KEGG; hin:HI0458; -. DR PATRIC; 20189471; VBIHaeInf48452_0478. DR eggNOG; ENOG4105DBD; Bacteria. DR eggNOG; COG0760; LUCA. DR KO; K03771; -. DR OMA; RANIQYF; -. DR OrthoDB; EOG6M9DS4; -. DR PhylomeDB; P44721; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR InterPro; IPR023058; PPIase_PpiC_CS. DR InterPro; IPR015391; SurA_N. DR InterPro; IPR027304; Trigger_fact/SurA_dom. DR Pfam; PF00639; Rotamase; 1. DR Pfam; PF09312; SurA_N; 1. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS01096; PPIC_PPIASE_1; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Isomerase; Periplasm; KW Reference proteome; Rotamase; Signal. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 313 Putative peptidyl-prolyl cis-trans FT isomerase SurA. FT /FTId=PRO_0000025543. FT DOMAIN 167 267 PpiC. {ECO:0000255|PROSITE- FT ProRule:PRU00278}. SQ SEQUENCE 313 AA; 34670 MW; EAE2A7C352302450 CRC64; MKMKKFVLRS FLLATLGCVA FTSMAQAEER VVATVDGIPV LESQVRANMG KKGDRQSAID KIIDDILVQK AVQESGVKID PREIDHIVED TAARNGLTYG QFLDALDYQG ISLNTFRQQI ANQMVMGAVR NKAIQESIDV TREEVVALGQ KMLDEAKSQG TAQKVTGKEY EVRHILLKLN PLLNDAQAKK QLAKIRSDII AGKTTFADAA LKYSKDYLSG ANGGSLGYAF PETYAPQFAQ TVVKSKQGVI SAPFKTEFGW HILEVTGVRD GDLTAEAYTQ KAYERLVNTQ LQDATNDWVK ALRKRANIQY FNK // ID SPPA_HAEIN Reviewed; 615 AA. AC P45243; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Protease 4; DE EC=3.4.21.-; DE AltName: Full=Endopeptidase IV; DE AltName: Full=Protease IV; DE AltName: Full=Signal peptide peptidase; GN Name=sppA; OrderedLocusNames=HI_1541; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Digests cleaved signal peptides in vitro, its in vivo CC function is unknown. This activity is necessary to maintain proper CC secretion of mature proteins across the membrane (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S49 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; L42023; AAC23191.1; -; Genomic_DNA. DR PIR; F64128; F64128. DR RefSeq; NP_439690.1; NC_000907.1. DR RefSeq; WP_005693566.1; NC_000907.1. DR ProteinModelPortal; P45243; -. DR STRING; 71421.HI1541; -. DR PRIDE; P45243; -. DR EnsemblBacteria; AAC23191; AAC23191; HI_1541. DR GeneID; 950404; -. DR KEGG; hin:HI1541; -. DR PATRIC; 20191807; VBIHaeInf48452_1612. DR eggNOG; ENOG4105D07; Bacteria. DR eggNOG; COG0616; LUCA. DR KO; K04773; -. DR OMA; YLYCLTC; -. DR OrthoDB; EOG6P5ZHQ; -. DR PhylomeDB; P45243; -. DR Proteomes; UP000000579; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro. DR Gene3D; 3.90.226.10; -; 4. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR004634; Pept_S49_pIV. DR InterPro; IPR004635; Pept_S49_SppA. DR InterPro; IPR002142; Peptidase_S49. DR Pfam; PF01343; Peptidase_S49; 2. DR PIRSF; PIRSF001217; Protease_4_SppA; 1. DR SUPFAM; SSF52096; SSF52096; 4. DR TIGRFAMs; TIGR00705; SppA_67K; 1. DR TIGRFAMs; TIGR00706; SppA_dom; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Protease; Reference proteome; Serine protease; KW Transmembrane; Transmembrane helix. FT CHAIN 1 615 Protease 4. FT /FTId=PRO_0000171439. FT TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TOPO_DOM 39 615 Periplasmic. {ECO:0000255}. FT ACT_SITE 201 201 Proton donor/acceptor. {ECO:0000250}. FT ACT_SITE 405 405 Nucleophile. {ECO:0000250}. SQ SEQUENCE 615 AA; 68057 MW; 60BE52496CFAAA3E CRC64; MFQVLKFCWK VLCFIRDLVM NVVFLGFVLL LVAIISFSSG GKKSTALTSE GALLLNLDGY LADNRDETLR WQDALSELNG EHVPRKISTF DVVFAIQQAE DDPKIKGLVL DLNYFEGADL PALDFIGGAI SHFKDAGKPV IAYADNYSQG QYYLASFADE IYLNSIGSVD IHGLSQENLY FKEMLDKLAV TPHIFRVGTY KSAVEPFLRN DMSAEAKANM QRWLGEMWNN YVLSVSENRN IKKDRILPNA KQYLAELKAL KGNSTAYAQQ RGLVTDVVTR LDLDKKLSAL FGKGSDGKAN LIEFDDYLTQ LPDRLEHYNV PNKIAVVNVE GTIIDGESDE ENAGGDTIAR ILRKAHDDNS VKAVILRVNS PGGSAFASEI IRQETENLQK IGKPVIVSMG AMAASGGYWI SSTADYIIAD SNTITGSIGI FTMFPTFENS IKKIGVHADG VSTTELANTS AFSPLAKPVQ DIYQTEIEHG YDRFLEIVSK GRQLSKTQVD KLAQGQVWLG SDAFQNGLVD EIGSFNEAVN KAEQLVNQRQ DTAVQDFSVE WFTDDNVSLI STLLSDTKKG AQEQLVKWLG LPAPIQKLQK ELNILTKFND PKGQYLYCLN CGKVK // ID SUCC_HAEIN Reviewed; 389 AA. AC P45101; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558}; DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558}; GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; GN OrderedLocusNames=HI_1196; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC succinate from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00558}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22850.1; -; Genomic_DNA. DR PIR; C64189; C64189. DR RefSeq; NP_439352.1; NC_000907.1. DR RefSeq; WP_005694249.1; NC_000907.1. DR ProteinModelPortal; P45101; -. DR SMR; P45101; 1-388. DR STRING; 71421.HI1196; -. DR PRIDE; P45101; -. DR EnsemblBacteria; AAC22850; AAC22850; HI_1196. DR GeneID; 950149; -. DR KEGG; hin:HI1196; -. DR PATRIC; 20191071; VBIHaeInf48452_1248. DR eggNOG; ENOG4105CMV; Bacteria. DR eggNOG; COG0045; LUCA. DR KO; K01903; -. DR OMA; YIESGCD; -. DR OrthoDB; EOG644ZT0; -. DR PhylomeDB; P45101; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.261; -; 1. DR HAMAP; MF_00558; Succ_CoA_beta; 1. DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS. DR InterPro; IPR005809; Succ_CoA_synthase_bsu. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR PANTHER; PTHR11815; PTHR11815; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01016; sucCoAbeta; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 389 Succinyl-CoA ligase [ADP-forming] subunit FT beta. FT /FTId=PRO_0000102835. FT DOMAIN 9 244 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00558}. FT NP_BIND 35 108 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 197 197 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 199 199 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. SQ SEQUENCE 389 AA; 42164 MW; 37926FFAF4CD6AA6 CRC64; MNLHEYQAKQ LFEHYGLPVK NGAVCQSVED VDLVLAQLSG GKWAAKCQVH AGGRGKAGGV KLVQDVEEAR AFAEKWLGQR LVTFQTDKLG QPVNQIYFEE TCDIDKEFYL SAVVDRTSQK VVFIASSEGG MNIEEVVQNS PHLLHKVTID PLFGGLPYQG RELAFKLGLS GTQNKQFTDI FMGLSRLFLE KDLSLLEVNP LVLTPQGNLV CLDAKISVDD NALFRHKDLL ALQDLTQNDA REAEAEKFQL NYVALEGDIG CMVNGAGLAM GTMDIVKLYG GKPANFLDVG GGATQERVAE AFKIILTDPS VKVILVNIFG GIVRCDLIAE GVIAAVNEVG VRVPVVVRLE GTNAEMGRQI LAESDVNILT AQSLQQAAEL AVNAAKGEH // ID SUCD_HAEIN Reviewed; 293 AA. AC P45102; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha; DE EC=6.2.1.5; DE AltName: Full=Succinyl-CoA synthetase subunit alpha; DE Short=SCS-alpha; GN Name=sucD; OrderedLocusNames=HI_1197; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha CC subunit 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; L42023; AAC22851.1; -; Genomic_DNA. DR PIR; D64189; D64189. DR RefSeq; NP_439353.1; NC_000907.1. DR RefSeq; WP_005694247.1; NC_000907.1. DR ProteinModelPortal; P45102; -. DR SMR; P45102; 2-289. DR STRING; 71421.HI1197; -. DR PRIDE; P45102; -. DR EnsemblBacteria; AAC22851; AAC22851; HI_1197. DR GeneID; 950515; -. DR KEGG; hin:HI1197; -. DR PATRIC; 20191073; VBIHaeInf48452_1249. DR eggNOG; ENOG4105CH8; Bacteria. DR eggNOG; COG0074; LUCA. DR KO; K01902; -. DR OMA; FEQDPQT; -. DR OrthoDB; EOG644ZT0; -. DR PhylomeDB; P45102; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central. DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 3.40.50.261; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR005810; CoA_lig_alpha. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001553; SucCS_alpha; 1. DR PRINTS; PR01798; SCOASYNTHASE. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01019; sucCoAalpha; 1. DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1. DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 293 Succinyl-CoA ligase [ADP-forming] subunit FT alpha. FT /FTId=PRO_0000102794. FT ACT_SITE 247 247 Tele-phosphohistidine intermediate. FT {ECO:0000250}. SQ SEQUENCE 293 AA; 30389 MW; E9C4AF5D3F3D9FE1 CRC64; MAILIDKNTK VICQGFTGGQ GTFHSEQALA YGTQLVGGVS PNKGGTTHLG LPVFNTVREA VENTGVTATV IYVPASFCKD AIIEAIDAGI QLIVCITEGI PTLDMLKVKQ KLNETGVVMI GPNCPGVITP DECKIGIMPA HIHKKGKVGI VSRSGTLTYE AVKQTTDEGF GQSTCVGIGG DPIPGSSFID ILERFQQDPE TEAIVMIGEI GGSAEEEAAI FIKDNVTKPV VAYIAGITAP KGKRMGHAGA IISGGKGTAV EKIAALEAAG VTCVKSLAEI GEALRKLLKS SKN // ID SUHB_HAEIN Reviewed; 267 AA. AC P44333; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Inositol-1-monophosphatase; DE Short=I-1-Pase; DE Short=IMPase; DE Short=Inositol-1-phosphatase; DE EC=3.1.3.25; GN Name=suhB; OrderedLocusNames=HI_0937; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the inositol monophosphatase 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; L42023; AAC22595.1; -; Genomic_DNA. DR PIR; F64103; F64103. DR RefSeq; NP_439097.1; NC_000907.1. DR RefSeq; WP_005693284.1; NC_000907.1. DR ProteinModelPortal; P44333; -. DR SMR; P44333; 1-258. DR STRING; 71421.HI0937; -. DR EnsemblBacteria; AAC22595; AAC22595; HI_0937. DR GeneID; 949915; -. DR KEGG; hin:HI0937; -. DR PATRIC; 20190531; VBIHaeInf48452_0978. DR eggNOG; ENOG4105ECY; Bacteria. DR eggNOG; COG0483; LUCA. DR KO; K01092; -. DR OMA; YILATNG; -. DR OrthoDB; EOG6QK4W4; -. DR PhylomeDB; P44333; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central. DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central. DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR InterPro; IPR022337; Inositol_monophosphatase_SuhB. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PRINTS; PR01959; SBIMPHPHTASE. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 267 Inositol-1-monophosphatase. FT /FTId=PRO_0000142562. FT REGION 86 89 Substrate binding. {ECO:0000250}. FT METAL 67 67 Magnesium 1. {ECO:0000250}. FT METAL 84 84 Magnesium 1. {ECO:0000250}. FT METAL 84 84 Magnesium 2. {ECO:0000250}. FT METAL 86 86 Magnesium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 87 87 Magnesium 2. {ECO:0000250}. FT METAL 212 212 Magnesium 2. {ECO:0000250}. FT BINDING 67 67 Substrate. {ECO:0000250}. FT BINDING 183 183 Substrate. {ECO:0000250}. FT BINDING 212 212 Substrate. {ECO:0000250}. SQ SEQUENCE 267 AA; 29500 MW; DF974E0DAB0CCEA6 CRC64; MNPMLNIAIR AARKAGNVIA KNYERRDAIE STQKGINDYV TNVDKASEAE IIEVIRKSYP DHTIITEETG AIEGKDSDVQ WIIDPLDGTR NFMTGLPHFS VSIAVRVKNR TEVGVVYDPI RNELFTAVRG EGAKLNEVRL RVDSKREIQG SILATGFPFK QPKLMPAQFA MMNALIEDAA DFRRTGSAAL DLCYVASNRI DGYFEMGLKA WDCAAGDLIV REAGGLVCDF DAGNSYLRSG NIIAAPSRVI KEMLNKIRPC LGAEFNH // ID SYA_HAEIN Reviewed; 874 AA. AC P43815; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036}; DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036}; DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036}; DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036}; GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; GN OrderedLocusNames=HI_0814; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22473.1; -; Genomic_DNA. DR PIR; I64095; I64095. DR RefSeq; NP_438974.1; NC_000907.1. DR RefSeq; WP_010869060.1; NC_000907.1. DR ProteinModelPortal; P43815; -. DR STRING; 71421.HI0814; -. DR EnsemblBacteria; AAC22473; AAC22473; HI_0814. DR GeneID; 950776; -. DR KEGG; hin:HI0814; -. DR PATRIC; 20190283; VBIHaeInf48452_0855. DR eggNOG; ENOG4105CIM; Bacteria. DR eggNOG; COG0013; LUCA. DR KO; K01872; -. DR OMA; FDFNCPR; -. DR OrthoDB; EOG6Q2SQ2; -. DR PhylomeDB; P43815; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF01411; tRNA-synt_2c; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR00980; TRNASYNTHALA. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF101353; SSF101353; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 874 Alanine--tRNA ligase. FT /FTId=PRO_0000075122. FT METAL 563 563 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 567 567 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 665 665 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. FT METAL 669 669 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. SQ SEQUENCE 874 AA; 96601 MW; A79D119E47916BB1 CRC64; MKTTAEIRQS FLDFFHSKGH QVVESSSLVP ENDPTLLFTN AGMNQFKDVF LGMDKRPYSR ATTAQRCVRP GGKHNDLENV GYTARHHTFF EMLGNFSFGD YFKQDAINFA WEYLTSPQWL GLPKEKLWVT VYETDDEAYN IWNKDVGVPA ERIIRIGDNK GSPYASDNFW AMGDTGPCGP CTEIFYDHGD HIWGGPPGSP EEDGDRYIEI WNVVFMQFNR LADGTMEKLP RPSVDTGMGL ERISAVLQHV NSNYEIDIFK TLIAKTAEIV GATDLTNKSL RVIADHIRSC AYLIADGVIP SNEGRGYVLR RIIRRAVRHG HLLGAKESFF YKLVPTLIDV MAEAGKDVKA KQTNVEKLLR LEEEQFARTL ERGLSLLDEA LSQVKDGILS GEVAFKLYDT YGFPLDLTAD VCRERNITID EQAFDRKMEA QRTRAQAASQ FGVDYNSVIR VDGETKFEGY TEVESQAKIT ALFYDGKSVE SIEAGQSAVV ILENTPFYAE SGGQIGDSGY LSTQSVTFNV KDTQKYGQVF GHIGELTQGS LKVGQSVNAI VDAKRRHNTS LNHSATHLLH AALRQILGLH VVQKGSLVSD KALRFDFAQP EAITKEQLSE IETLVNQKIR ANFPVQTDIM DIDSAKAKGA MALFGEKYGD KVRVLTMGDF SIELCGGIHA KRTGDIGLFK IITENAVAAG IRRIEAVTGQ NAIDWLHNQQ RILTQSADLL KSDVNTLAEK IQQLQDKAKK VEKELQGLKE KAAMQAGSYF VKSAVKINGV SVIAQQLDGI ETKSLRVMVD DLKNQLGSGV IAFASILDEK VNLVVGVTND LTAKIKAGEL VNLMAQQVGG KGGGRPDMAM AGGSQLENVT QAIKVAQDWL NKNL // ID SSB_HAEIN Reviewed; 168 AA. AC P44409; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984}; DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984}; GN Name=ssb; OrderedLocusNames=HI_0250; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=8063092; DOI=10.1016/0378-1119(94)90841-9; RA Jarosik G.P., Hansen E.J.; RT "Cloning and sequencing of the Haemophilus influenzae ssb gene RT encoding single-strand DNA-binding protein."; RL Gene 146:101-103(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays an important role in DNA replication, CC recombination and repair. Binds to ssDNA and to an array of CC partner proteins to recruit them to their sites of action during CC DNA metabolism. {ECO:0000255|HAMAP-Rule:MF_00984}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000255|HAMAP- CC Rule:MF_00984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21916.1; -; Genomic_DNA. DR EMBL; U04997; AAA60461.1; -; Genomic_DNA. DR PIR; E64057; E64057. DR RefSeq; NP_438419.1; NC_000907.1. DR RefSeq; WP_005694052.1; NC_000907.1. DR ProteinModelPortal; P44409; -. DR SMR; P44409; 3-111. DR STRING; 71421.HI0250; -. DR EnsemblBacteria; AAC21916; AAC21916; HI_0250. DR GeneID; 950657; -. DR KEGG; hin:HI0250; -. DR PATRIC; 20189025; VBIHaeInf48452_0265. DR eggNOG; ENOG4108UUM; Bacteria. DR eggNOG; COG0629; LUCA. DR KO; K03111; -. DR OMA; ENCARYL; -. DR OrthoDB; EOG6M9F32; -. DR PhylomeDB; P44409; -. DR Proteomes; UP000000579; Chromosome. 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:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00984; SSB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR PANTHER; PTHR10302; PTHR10302; 1. DR Pfam; PF00436; SSB; 1. DR PIRSF; PIRSF002070; SSB; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00621; ssb; 1. DR PROSITE; PS50935; SSB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW DNA replication; DNA-binding; Reference proteome. FT CHAIN 1 168 Single-stranded DNA-binding protein. FT /FTId=PRO_0000096048. FT DOMAIN 4 109 SSB. {ECO:0000255|HAMAP-Rule:MF_00984}. FT MOTIF 163 168 Important for interaction with partner FT proteins. {ECO:0000255|HAMAP- FT Rule:MF_00984}. FT VARIANT 118 119 YG -> FS (in strain: TN106). FT VARIANT 121 121 D -> E (in strain: TN106). FT VARIANT 124 125 GA -> SS (in strain: TN106). FT VARIANT 128 128 S -> P (in strain: TN106). FT VARIANT 151 151 A -> S (in strain: TN106). SQ SEQUENCE 168 AA; 18754 MW; 883DEE51E5623693 CRC64; MAGINKVIIV GHLGNDPEIR TMPNGDAVAN ISVATSESWN DRNTGERREV TEWHRIVFYR RQAEICGEYL RKGSQVYVEG RLKTRKWQDQ NGQDRYTTEI QGDVMQMLGG RNQNAGGYGN DMGGAPQSSY QARQTNNGNS YQSSRPAPQQ AAPQAEPPMD GFDDDIPF // ID SYC_HAEIN Reviewed; 459 AA. AC P43816; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. 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=HI_0078; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21753.1; -; Genomic_DNA. DR PIR; C64047; C64047. DR RefSeq; NP_438251.1; NC_000907.1. DR RefSeq; WP_005693844.1; NC_000907.1. DR ProteinModelPortal; P43816; -. DR SMR; P43816; 1-459. DR STRING; 71421.HI0078; -. DR EnsemblBacteria; AAC21753; AAC21753; HI_0078. DR GeneID; 950973; -. DR KEGG; hin:HI0078; -. DR PATRIC; 20188611; VBIHaeInf48452_0079. DR eggNOG; ENOG4105C8N; Bacteria. DR eggNOG; COG0215; LUCA. DR KO; K01883; -. DR OMA; HENEACQ; -. DR OrthoDB; EOG6RVFXC; -. DR PhylomeDB; P43816; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00041; Cys_tRNA_synth; 1. DR InterPro; IPR015803; Cys-tRNA-ligase. DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR. DR InterPro; IPR024909; Cys-tRNA/MSH_ligase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR032678; tRNA-synt_1_cat_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR10890; PTHR10890; 1. DR Pfam; PF09190; DALR_2; 1. DR Pfam; PF01406; tRNA-synt_1e; 1. DR PRINTS; PR00983; TRNASYNTHCYS. DR SMART; SM00840; DALR_2; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR TIGRFAMs; TIGR00435; cysS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 459 Cysteine--tRNA ligase. FT /FTId=PRO_0000159406. FT MOTIF 30 40 "HIGH" region. FT MOTIF 266 270 "KMSKS" region. FT METAL 28 28 Zinc. {ECO:0000250}. FT METAL 209 209 Zinc. {ECO:0000250}. FT METAL 234 234 Zinc. {ECO:0000250}. FT METAL 238 238 Zinc. {ECO:0000250}. FT BINDING 269 269 ATP. {ECO:0000250}. SQ SEQUENCE 459 AA; 52356 MW; 4718A779103980C0 CRC64; MLKIFNTLTR EKEIFKPIHE NKVGMYVCGV TVYDLCHIGH GRTFVCFDVI ARYLRSLGYD LTYVRNITDV DDKIIKRALE NKETCDQLVD RMVQEMYKDF DALNVLRPDF EPRATHHIPE IIEIVEKLIK RGHAYVADNG DVMFDVESFK EYGKLSRQDL EQLQAGARIE INEIKKNPMD FVLWKMSKEN EPSWASPWGA GRPGWHIECS AMNCKQLGEY FDIHGGGSDL MFPHHENEIA QSCCAHGGQY VNYWIHSGMI MVDKEKMSKS LGNFFTIRDV LNHYNAEAVR YFLLTAHYRS QLNYSEENLN LAQGALERLY TALRGTDQSA VAFGGENFVA TFREAMDDDF NTPNALSVLF EMAREINKLK TEDVEKANGL AARLRELGAI LGLLQQEPEK FLQAGSNDDE VAKIEALIKQ RNEARTAKDW SAADSARNEL TAMGIVLEDG PNGTTWRKQ // ID SYGA_HAEIN Reviewed; 302 AA. AC P43821; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Glycine--tRNA ligase alpha subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit; DE Short=GlyRS; GN Name=glyQ; OrderedLocusNames=HI_0927; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22586.1; -; Genomic_DNA. DR PIR; C64103; C64103. DR RefSeq; NP_439087.1; NC_000907.1. DR RefSeq; WP_005628151.1; NC_000907.1. DR ProteinModelPortal; P43821; -. DR SMR; P43821; 10-288. DR STRING; 71421.HI0927; -. DR EnsemblBacteria; AAC22586; AAC22586; HI_0927. DR GeneID; 950664; -. DR KEGG; hin:HI0927; -. DR PATRIC; 20190511; VBIHaeInf48452_0968. DR eggNOG; ENOG4107QIB; Bacteria. DR eggNOG; COG0752; LUCA. DR KO; K01878; -. DR OMA; LGSYYQF; -. DR OrthoDB; EOG661H9S; -. DR PhylomeDB; P43821; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR002310; Gly-tRNA_ligase_asu. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR TIGRFAMs; TIGR00388; glyQ; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 302 Glycine--tRNA ligase alpha subunit. FT /FTId=PRO_0000072841. SQ SEQUENCE 302 AA; 34471 MW; 96C36AC2CA878541 CRC64; MSTKFNVKTF QGMILALQEY WANQGCTIVQ PFDMEVGAGT SHPMTALRAL GPEPMAFAYV QPSRRPTDGR YGENPNRLQH YYQFQVVIKP SPDNIQELYL GSLEMLGFDP TKNDIRFVED NWENPTLGAW GLGWEVWLNG MEVTQFTYFQ QVGGLECKPV TGEVTYGLER LAMYIQGVDS VYDLVWSDGP LGKTTYGDVF HQNEVEQSTY NFEHANTDFL FYCFDQYEKE AQELLALEKP LPLPAYERIL KAAHSFNLLD ARKAISVTER QRYILRIRAL TKGVAEAYYA SREALGFPGC KK // ID SYFB_HAEIN Reviewed; 795 AA. AC P43820; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. 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=HI_1312; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22958.1; -; Genomic_DNA. DR PIR; I64115; I64115. DR RefSeq; NP_439463.1; NC_000907.1. DR RefSeq; WP_005694456.1; NC_000907.1. DR ProteinModelPortal; P43820; -. DR STRING; 71421.HI1312; -. DR BindingDB; P43820; -. DR EnsemblBacteria; AAC22958; AAC22958; HI_1312. DR GeneID; 950235; -. DR KEGG; hin:HI1312; -. DR PATRIC; 20191307; VBIHaeInf48452_1364. DR eggNOG; ENOG4105C6A; Bacteria. DR eggNOG; COG0072; LUCA. DR eggNOG; COG0073; LUCA. DR KO; K01890; -. DR OMA; MKFSEQW; -. DR OrthoDB; EOG6CCH1J; -. DR PhylomeDB; P43820; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.56.20; -; 1. DR Gene3D; 3.30.70.380; -; 1. DR Gene3D; 3.50.40.10; -; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF54991; SSF54991; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00472; pheT_bact; 1. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding. FT CHAIN 1 795 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000126892. FT DOMAIN 39 148 tRNA-binding. FT DOMAIN 401 476 B5. FT DOMAIN 701 794 FDX-ACB. FT METAL 454 454 Magnesium. {ECO:0000250}. FT METAL 460 460 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 463 463 Magnesium. {ECO:0000250}. FT METAL 464 464 Magnesium. {ECO:0000250}. SQ SEQUENCE 795 AA; 86747 MW; 470FE3F404F6673D CRC64; MKFSEQWVRE WVNPAVSTEQ LCEQITMLGL EVDGVEAVAG TFNGVVVGEV VECAQHPDAD KLRVTKVNVG GDRLLDIVCG APNCRQGLKV ACATEGAVLP GDFKIKKTKL RGQPSEGMLC SFSELGIDVE ADGIIELPLD APIGTDLREY LALDDNAIEI SLTPNRADCL SIAGIAREIG VVNKQLVNQL HFEAAPATIS DKVQIDLQAP EACPRYLLRV IKNVNVKAPS PMWMQEKLRR CGIRSIDPIV DITNYILLEF GQPMHAFDAA KVTQPVQVRF AKEGEELVLL DGSTAKLQSN TLLIADQNGP LAMAGIFGGA ASGVNSETKD VILESAFFAP LAIAGRARQY GLHTDASHRF ERGVDFELAR KAMERATALL LEICGGEAGE ICEASSETHL PKVNTVQLRR SKLDALLGHH IETGSVTEIF HRLGFDVTYA NDIWTVTSAS WRFDIEIEED LIEEVARIYG YNSIPNNAPL AHLCMREHKE SDLDLARIKT ALVDADYQEA ITYSFVDPKI QSLLHPHQEA LVLPNPISVE MSAMRVSLIS GLLGAVLYNQ NRQQSRVRLF ETGLRFVPDA NAEFGVRQEF VLSAVITGTA KSEHWAGKAE SVDFFDLKGD LESVLSLTEG GHRVRFVAKQ FDALHPGQSA AIELDGQEIG FIGAIHPSIS QKLGLNGKTF VFEILWNAIA ARNVVQAKEI SKFPANRRDL ALVVADSVPA GELIAACKQA GGEKLVQVNL FDVYQGVGVA EGYKSLAISL TVQDNEKTLE DEEINAVISA VLAEVKQRFN AELRD // ID SYH_HAEIN Reviewed; 423 AA. AC P43823; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 117. 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=HI_0369; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22027.1; -; Genomic_DNA. DR PIR; I64063; I64063. DR RefSeq; NP_438530.1; NC_000907.1. DR RefSeq; WP_005693795.1; NC_000907.1. DR ProteinModelPortal; P43823; -. DR SMR; P43823; 5-404. DR STRING; 71421.HI0369; -. DR EnsemblBacteria; AAC22027; AAC22027; HI_0369. DR GeneID; 950203; -. DR KEGG; hin:HI0369; -. DR PATRIC; 20189283; VBIHaeInf48452_0387. DR eggNOG; ENOG4105CUT; Bacteria. DR eggNOG; COG0124; LUCA. DR KO; K01892; -. DR OMA; CGGGNFK; -. DR OrthoDB; EOG6BPDH4; -. DR PhylomeDB; P43823; -. DR BRENDA; 6.1.1.21; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00127; His_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR015807; His-tRNA-ligase. DR InterPro; IPR004516; HisRS/HisZ. DR PANTHER; PTHR11476; PTHR11476; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00442; hisS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 423 Histidine--tRNA ligase. FT /FTId=PRO_0000136171. SQ SEQUENCE 423 AA; 47672 MW; 50C07AB84B6F6FD5 CRC64; MAKTIQAIRG MNDCAPTESP LWQWIEAQVR NVLNSYGYSE VRMPIVESTP LFARAIGEVT DVVSKEMYTF WDNDEQLTLR PEGTAGCVRA AIEHGWIYNN EQRLWYIGPM FRHERPQKGR YRQFHQVGVE VFGIANPEID AELIMLTYRL WKALGIDQHV TLQLNSIGSL EARANYRSAL VGFLENHQDL MSDEEKERLV RNPLRILDTK NPELQKVLDN APKLLDYLDD ESRTHFEQLC SLLDAVGIQY EINPKLVRGL DYYNKTVFEW VTSALGAQGT VCGGGRYDGL VEQLGGHATP SIGFAMGLER LVLLVQEVNP NVPAKSAVDI YVVYQGEGAT LAAFELAEKV RSELPHLNTM LHCSSGNFKK QFKRADKSGA TLALVIGESE VQNKQVVVKH LQGGTDQQTL DLVNIIDYLQ TQF // ID SURE_HAEIN Reviewed; 249 AA. AC P45681; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060}; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060}; GN Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; GN OrderedLocusNames=HI_0702; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on CC nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00060}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. CC {ECO:0000255|HAMAP-Rule:MF_00060}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22361.1; -; Genomic_DNA. DR PIR; T09407; T09407. DR RefSeq; NP_438861.1; NC_000907.1. DR RefSeq; WP_005694588.1; NC_000907.1. DR ProteinModelPortal; P45681; -. DR STRING; 71421.HI0702; -. DR EnsemblBacteria; AAC22361; AAC22361; HI_0702. DR GeneID; 949728; -. DR KEGG; hin:HI0702; -. DR PATRIC; 20190023; VBIHaeInf48452_0733. DR eggNOG; ENOG4105CV2; Bacteria. DR eggNOG; COG0496; LUCA. DR KO; K03787; -. DR OMA; KICRQAK; -. DR OrthoDB; EOG68WR45; -. DR PhylomeDB; P45681; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1210.10; -; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SSF64167; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 249 5'-nucleotidase SurE. FT /FTId=PRO_0000111814. FT METAL 8 8 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 9 9 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 39 39 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 91 91 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. SQ SEQUENCE 249 AA; 27340 MW; D10F280C95266757 CRC64; MRILVSNDDG FHAEGIQVLA TELRKIAEVI IVAPDRNRSA ASSSLTLVEP LRPRHLDNGD YCVNGTPADC VHLALNGFLS GQVDLVVSGI NAGCNMGDDT IYSGTLAAAL EGRHLGLPAI AVSLDGRQHY ETAARVVCDL IPKLQHQLLN PREIININVP DLPFEELKGY KVCRLGYRSS SVEVIKQRDP RDETIYWIGP SALPEDESEG TDFYAVKNGY VSITPIQADL TAYHSLLSLQ NWLDQEFTK // ID SYFA_HAEIN Reviewed; 329 AA. AC P43819; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. 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=HI_1311; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22957.1; -; Genomic_DNA. DR PIR; H64115; H64115. DR RefSeq; NP_439462.1; NC_000907.1. DR RefSeq; WP_005694457.1; NC_000907.1. DR ProteinModelPortal; P43819; -. DR SMR; P43819; 83-329. DR STRING; 71421.HI1311; -. DR BindingDB; P43819; -. DR ChEMBL; CHEMBL3671; -. DR EnsemblBacteria; AAC22957; AAC22957; HI_1311. DR GeneID; 950073; -. DR KEGG; hin:HI1311; -. DR PATRIC; 20191305; VBIHaeInf48452_1363. DR eggNOG; ENOG4105CSS; Bacteria. DR eggNOG; COG0016; LUCA. DR KO; K01889; -. DR OMA; KGTGWLE; -. DR OrthoDB; EOG6WX4QN; -. DR PhylomeDB; P43819; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR004188; Phe-tRNA_ligase_II_N. DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR010978; tRNA-bd_arm. DR Pfam; PF02912; Phe_tRNA-synt_N; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00468; pheS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 329 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126712. FT METAL 254 254 Magnesium. {ECO:0000250}. SQ SEQUENCE 329 AA; 38080 MW; 3BCC7172DB4FE3D6 CRC64; MQHLNELVEK AKLAIESIQD KSLTALDEIR VEYFGKKGHF TQLMQELRNV SAEERPAMGA KINEAKQAAL EFLNAKKTEW EQAELNSKLE KERVDVSLPG RKVETGGLHP VTMTINRVTK FFSELGFSVE NGPEIESDYY NFDALNIPKH HPARADHDTF WFNPELLLRT QTSGVQIRTM EKMQPPIRIM APGRVYRNDY DQTHTPMFHQ IELLYVDKKA NFTELKGLLH DFLRAFFEED LQVRFRPSYF PFTEPSAEVD VMGKNGKWLE VLGCGMVHPN VLRNVGIDPN EYSGFAVGMG VERLTMLRYN VTDLRSFFEN DLRFLKQFK // ID SYP_HAEIN Reviewed; 572 AA. AC P43830; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569}; DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569}; DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569}; GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; GN OrderedLocusNames=HI_0729; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SUBUNIT. RX PubMed=16087664; DOI=10.1074/jbc.M507550200; RA An S., Musier-Forsyth K.; RT "Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel RT synthetase.YbaK.tRNA ternary complex."; RL J. Biol. Chem. 280:34465-34472(2005). CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a CC two-step reaction: proline is first activated by ATP to form Pro- CC AMP and then transferred to the acceptor end of tRNA(Pro). As CC ProRS can inadvertently accommodate and process non-cognate amino CC acids such as alanine and cysteine, to avoid such errors it has CC two additional distinct editing activities against alanine. One CC activity is designated as 'pretransfer' editing and involves the CC tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other CC activity is designated 'posttransfer' editing and involves CC deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- CC tRNA(Pro) is not edited by ProRS, but is probably edited in trans CC by YbaK. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP- CC Rule:MF_01569}. CC -!- SUBUNIT: Homodimer. May form a tertiary complex with YbaK and t- CC RNA(Pro). {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the editing domain and the C-terminal anticodon-binding CC domain. {ECO:0000255|HAMAP-Rule:MF_01569}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22388.1; -; Genomic_DNA. DR PIR; C64089; C64089. DR RefSeq; NP_438888.1; NC_000907.1. DR RefSeq; WP_005693134.1; NC_000907.1. DR ProteinModelPortal; P43830; -. DR STRING; 71421.HI0729; -. DR PRIDE; P43830; -. DR EnsemblBacteria; AAC22388; AAC22388; HI_0729. DR GeneID; 949758; -. DR KEGG; hin:HI0729; -. DR PATRIC; 20190095; VBIHaeInf48452_0763. DR eggNOG; ENOG4105C90; Bacteria. DR eggNOG; COG0442; LUCA. DR KO; K01881; -. DR OMA; IQPAELW; -. DR OrthoDB; EOG6TTVMR; -. DR PhylomeDB; P43830; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR Gene3D; 3.90.960.10; -; 1. DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR002316; Pro-tRNA-ligase_IIa. DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type. DR InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1. DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom. DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 2. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF04073; tRNA_edit; 1. DR PIRSF; PIRSF001535; ProRS_1; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55826; SSF55826; 1. DR TIGRFAMs; TIGR00409; proS_fam_II; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 572 Proline--tRNA ligase. FT /FTId=PRO_0000139330. SQ SEQUENCE 572 AA; 63975 MW; 5BF0F81162368583 CRC64; MRTSQYLFST LKETPNDAQV VSHQLMLRAG MIRPMASGLY NWLPTGIRVL KKVEKVVREE MNKGGAIEVL MPVVQPAELW EESGRWDQYG PELLRFEDRG NRNFVLGPTH EEVITDLVRR EVSSYKQLPL NLYQIQTKFR DEVRPRFGVM RSREFIMKDA YSFHTTQESL QATYDVMYQV YSNIFNRLGL DFRAVQADTG SIGGSASHEF QVLASSGEDD VVFSTESDFA ANIELAEAIA IGERQAPTAE MCLVDTPNAK TIAELVEQFN LPIEKTVKTL IVKGADENQP LVALIIRGDH ELNEIKAQKH PLVADPLEFA DETEIKAKIG SGVGSLGAVN LNIPAIIDRT VALMSDFSCG ANIDGKHYFN VNWERDVAIP KVFDLRNVVE GDPSPDGKGT LQIKRGIEVG HIFQLGKKYS EAMKATVQGE DGKPLVMTMG CYGIGVTRVV ASAIEQHHDE RGIIWPSDEI APFTVAIVPM NMHKSEAVQK YAEELYRTLQ SQGVDVIFDD RKERPGVMFA DMELIGVPHM VVIGEKNLDN GEIEYKNRRT GEKEMISKDK LLSVLNEKLG NL // ID SYS_HAEIN Reviewed; 429 AA. AC P43833; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=HI_0110; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC21787.1; -; Genomic_DNA. DR PIR; I64048; I64048. DR RefSeq; NP_438284.1; NC_000907.1. DR RefSeq; WP_005693809.1; NC_000907.1. DR ProteinModelPortal; P43833; -. DR SMR; P43833; 1-428. DR STRING; 71421.HI0110; -. DR EnsemblBacteria; AAC21787; AAC21787; HI_0110. DR GeneID; 951014; -. DR KEGG; hin:HI0110; -. DR PATRIC; 20188689; VBIHaeInf48452_0114. DR eggNOG; ENOG4105CGR; Bacteria. DR eggNOG; COG0172; LUCA. DR KO; K01875; -. DR OMA; NTVRESI; -. DR OrthoDB; EOG61KBH9; -. DR PhylomeDB; P43833; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000579; 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 1 429 Serine--tRNA ligase. FT /FTId=PRO_0000122057. FT NP_BIND 266 268 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT NP_BIND 353 356 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. FT REGION 235 237 Serine binding. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 289 289 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. FT BINDING 389 389 Serine. {ECO:0000255|HAMAP- FT Rule:MF_00176}. SQ SEQUENCE 429 AA; 47722 MW; 763967DFCD9838ED CRC64; MIDPNLLRNN LAEVAEKLKV KRNFMLDTEK LTALEDQRKN LQVTTENLQA ERNARSKAIG AAKARGEDIA PLLAEMDDMG NQLTEAKAQL DAVLAEINQI ALSIPNLPAD EVPLGKDDTE NKEILRWGTP RTFDFEVKDH ITLGEEANGL DFAAGAKLAG ARFAVMKGQI AKMHRALAQF MLDLHTEQHG YLETYVPYLV NHATLYGTGQ LPKFGEDLFH TLALEGEQPY ALIPTAEVPV TNLVRDVIID EAELPIKMTA HTPCFRSEAG SYGRDTRGLI RMHQFDKVEM VQIVDPDKSM EALEELTGHA EKVLQLLNLP YRKVLLCTGD MGFGSCKTYD LEVWVPAQNT YREISSCSNM WDFQARRMQA RCKAKGDKKT RLVHTLNGSG LAVGRTLVAV LENYQNADGS ITVPEELRPY MGGLDVIGK // ID SYE_HAEIN Reviewed; 480 AA. AC P43818; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. 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}; GN OrderedLocusNames=HI_0274; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00022}; CC Note=Binds 1 zinc ion per subunit. {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; L42023; AAC21940.1; -; Genomic_DNA. DR PIR; B64059; B64059. DR RefSeq; NP_438443.1; NC_000907.1. DR RefSeq; WP_005668173.1; NC_000907.1. DR ProteinModelPortal; P43818; -. DR STRING; 71421.HI0274; -. DR EnsemblBacteria; AAC21940; AAC21940; HI_0274. DR GeneID; 949397; -. DR KEGG; hin:HI0274; -. DR PATRIC; 20189077; VBIHaeInf48452_0289. DR eggNOG; ENOG4105C20; Bacteria. DR eggNOG; COG0008; LUCA. DR KO; K01885; -. DR OMA; QLCYMPL; -. DR OrthoDB; EOG6DRPF7; -. DR PhylomeDB; P43818; -. DR Proteomes; UP000000579; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 480 Glutamate--tRNA ligase. FT /FTId=PRO_0000119572. FT MOTIF 21 31 "HIGH" region. FT MOTIF 248 252 "KMSKS" region. FT METAL 110 110 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}. FT METAL 112 112 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}. FT METAL 137 137 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}. FT METAL 139 139 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}. FT BINDING 251 251 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}. SQ SEQUENCE 480 AA; 54875 MW; ABE5A203F9CF700F CRC64; MKLDAPFNLD PNVKVRTRFA PSPTGYLHVG GARTALYSWL YAKHNNGEFV LRIEDTDLER STPEATAAII EGMEWLNLPW EHGPYYQTKR FDRYNQVIDE MIEQGLAYRC YCTKEHLEEL RHTQEQNKEK PRYDRHCLHD HNHSPDEPHV VRFKNPTEGS VVFDDAVRGR IEISNSELDD LIIRRTDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILKAIGA PIPTYAHVSM INGDDGQKLS KRHGAVSVMQ YRDDGYLPEA LINYLVRLGW GHGDQEIFSR EEMINYFELD HVSKSASAFN TEKLQWLNQH YIRELPPEYV AKHLEWHYKD QGIDTSNGPA LTEIVTMLAE RCKTLKEMAR SSRYFFEEFE TFDEAAAKKH FKGNAAEALA KVKEKLTALS SWDLHSIHEA IEQTAAELEV GMGKVGMPLR VAVTGSGQSP SMDVTLVGIG RDRVLARIQR AIDFIHAQNA // ID SYQ_HAEIN Reviewed; 557 AA. AC P43831; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Glutamine--tRNA ligase; DE EC=6.1.1.18; DE AltName: Full=Glutaminyl-tRNA synthetase; DE Short=GlnRS; GN Name=glnS; OrderedLocusNames=HI_1354; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamine + tRNA(Gln) = AMP + CC diphosphate + L-glutaminyl-tRNA(Gln). 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; L42023; AAC23001.1; -; Genomic_DNA. DR PIR; G64118; G64118. DR RefSeq; NP_439505.1; NC_000907.1. DR RefSeq; WP_010869190.1; NC_000907.1. DR ProteinModelPortal; P43831; -. DR SMR; P43831; 18-555. DR STRING; 71421.HI1354; -. DR EnsemblBacteria; AAC23001; AAC23001; HI_1354. DR GeneID; 950274; -. DR KEGG; hin:HI1354; -. DR PATRIC; 20191393; VBIHaeInf48452_1407. DR eggNOG; ENOG4105CX6; Bacteria. DR eggNOG; COG0008; LUCA. DR KO; K01886; -. DR OMA; KWLGFEW; -. DR OrthoDB; EOG6DRPF7; -. DR PhylomeDB; P43831; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 2.40.240.10; -; 2. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00126; Gln_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004514; Gln-tRNA-synth. DR InterPro; IPR022861; Gln_tRNA_ligase_bac. 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; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF50715; SSF50715; 1. DR TIGRFAMs; TIGR00440; glnS; 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 1 557 Glutamine--tRNA ligase. FT /FTId=PRO_0000195837. FT MOTIF 42 52 "HIGH" region. FT MOTIF 277 281 "KMSKS" region. FT BINDING 280 280 ATP. {ECO:0000250}. SQ SEQUENCE 557 AA; 64078 MW; 4FF1452D57A29F72 CRC64; MMSHTETSLG AENTRTHNFI TQIIDEDLAS GKHKSVHTRF PPEPNGYLHI GHAKSICLNF GLAKEYQGLC NLRFDDTNPV KEDVEYVDSI KADVEWLGFK WEGEPRYASD YFDALYGYAV ELIKKGLAYV DELSPDEMRE YRGTLTEPGK NSPYRDRTIE ENLALFEKMK NGEFAEGKAS LRAKIDMASP FMVMREPVIY RIKFSSHHQT GDKWCIYPMY DFTHCISDAI ERITHSICTL EFQDNRRLYD WVLENISIER PLPHQYEFSR LNLEGTLTSK RKLLKLVNDE IVDGWNDPRM PTISGLRRRG YTPASLREFC RRIGVTKQDN VVEYSALEAC IREDLNENAP RAMAVIDPVR VVIENFESEA VLTAPNHPNR PELGERQLPF TKELYIDRAD FREEANKQYK RLVLGKEVRL RNAYVIKAER VEKDANGEIT TIFCTYDPET LGKNPADGRK VKGVIHWVSA VNNHPAEFRL YDRLFTVPNP GAEDDIESVL NPNSLVIKQG FVEQSLANAE AEKGYQFERE GYFCADSKDS RPEHLVFNLT VSLKEGF // ID SYR_HAEIN Reviewed; 577 AA. AC P43832; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 116. 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=HI_1583; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23231.1; -; Genomic_DNA. DR PIR; A64131; A64131. DR RefSeq; NP_439728.1; NC_000907.1. DR RefSeq; WP_005693602.1; NC_000907.1. DR ProteinModelPortal; P43832; -. DR STRING; 71421.HI1583; -. DR PRIDE; P43832; -. DR EnsemblBacteria; AAC23231; AAC23231; HI_1583. DR GeneID; 950446; -. DR KEGG; hin:HI1583; -. DR PATRIC; 20191899; VBIHaeInf48452_1657. DR eggNOG; ENOG4105C75; Bacteria. DR eggNOG; COG0018; LUCA. DR KO; K01887; -. DR OMA; HVGHIRN; -. DR OrthoDB; EOG6JB13C; -. DR PhylomeDB; P43832; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.30.1360.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR11956; PTHR11956; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF55190; SSF55190; 1. DR TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 577 Arginine--tRNA ligase. FT /FTId=PRO_0000151564. FT MOTIF 122 132 "HIGH" region. SQ SEQUENCE 577 AA; 64732 MW; 56B2B799C25FFF14 CRC64; MNIQSILSDK IKQAMILAGA DQSCDALIRQ SGKPQFGDYQ ANGIMAAAKK LGLNPREFAQ KVLDNLQLSD IAEKLEIAGP GFINIFLNPT WLTTEISAAL SHKNLGIQAT NKQTVVIDYS SPNVAKEMHV GHLRSTIIGD AVARTLEFLG HNVIRANHVG DWGTQFGMLI AYLEKMQNEH ASEMELQDLE AFYREAKKHY DEDEVFAEKA RNYVVKLQSG DEYCRTMWKR LVDITMQQNQ HNYARLNVTL TEKDVMGESL YNPMLPSIVK DLKKQGLAVE NDGALVVYLD EFKNKDGDPM GVIVQKKDGG FLYTTTDIAA AKYRYETLKA NRALVFSDTR QSQHMQQAWL ITRKAGYVPD SFSLEHKNFG MMLGKDGKPF KTRTGGTVKL ADLLDEAIER ATVLINEKNT NLSNDEKEAV IEAVGIGAVK YADLSKNRTT DYVFDWDNML SFEGNTAPYM QYAYTRIRSI FNKTDINSTA LLAAPLTIKD DKERTLAIKL LQFEEAVQTV GKEGTPHVLC AYLYELAGIF SSFYEHCPIL NAEDESIKLS RLKLALLTEK TLKQGLTLLG IKTVEKM // ID T1MH_HAEIN Reviewed; 443 AA. AC Q57168; O05053; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Putative type I restriction enzyme HindVIIP M protein; DE Short=M.HindVIIP; DE EC=2.1.1.72; GN OrderedLocusNames=HI_1287; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Methylation of specific adenine residues; required for CC both restriction and modification activities. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. 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; L42023; AAC22936.1; -; Genomic_DNA. DR PIR; G64114; G64114. DR RefSeq; NP_439439.2; NC_000907.1. DR ProteinModelPortal; Q57168; -. DR STRING; 71421.HI1287; -. DR REBASE; 3426; M.HindI. DR EnsemblBacteria; AAC22936; AAC22936; HI_1287. DR GeneID; 950217; -. DR KEGG; hin:HI1287; -. DR PATRIC; 20191257; VBIHaeInf48452_1339. DR eggNOG; ENOG4105CVR; Bacteria. DR eggNOG; COG0286; LUCA. DR KO; K03427; -. DR OMA; YADVPGF; -. DR OrthoDB; EOG6VQPSK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 443 Putative type I restriction enzyme FT HindVIIP M protein. FT /FTId=PRO_0000088027. FT REGION 117 122 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 146 148 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 173 173 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 443 AA; 49732 MW; 70573FBFFA78594C CRC64; MPASARWQAL QEVSILNTGA ELPWGGKFSG VAKLIDDAFD AIEKDNEKLK GVLQRISGYA VNEDTLRGLI ILFSDTHFTR PTYNGEPVHL GAKDILGHVY EYFLSRFAQA EGKRSGQYFT PKSIVSLIVE MLEPYSGRVY DPAMGSGGFF VQTERFITAH QGNINNVSIY GQEFNPTTWK LAAMNMAIRG IDYDFGKYNA DSFTQPQHID KKMDFIMANP HFNDKEWWNE SLADDPRWAY GTPPKGNANF AWLQHMIYHL SPNGKIALLL ANGSMSSQTN NEGEIRKAII NADLVECMVA LPGQLFTNTK IPACIWFLNR NKKRKGEVLF IDARQIGYMK DRVLRDFTAD DIAKIADTLH AWQTSDGYED QAAFCKSATL EEIKNNDFVL TPGRYVGTAE QEDDGVPFAE KMQNLTALLK EQFAKSAELE AEIKKNLGGL GYE // ID T1RH_HAEIN Reviewed; 1055 AA. AC O05052; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 09-DEC-2015, entry version 113. DE RecName: Full=Putative type I restriction enzyme HindVIIP R protein; DE EC=3.1.21.3; GN OrderedLocusNames=HI_1285; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase CC activities, but not for modification. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give random CC double-stranded fragments with terminal 5'-phosphates; ATP is CC simultaneously hydrolyzed. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22934.1; -; Genomic_DNA. DR PIR; F64114; F64114. DR RefSeq; NP_439437.1; NC_000907.1. DR RefSeq; WP_005694526.1; NC_000907.1. DR ProteinModelPortal; O05052; -. DR STRING; 71421.HI1285; -. DR REBASE; 1149; HindI. DR DNASU; 950228; -. DR EnsemblBacteria; AAC22934; AAC22934; HI_1285. DR GeneID; 950228; -. DR KEGG; hin:HI1285; -. DR PATRIC; 20191253; VBIHaeInf48452_1337. DR eggNOG; ENOG4105DZR; Bacteria. DR eggNOG; COG0610; LUCA. DR KO; K01153; -. DR OMA; IRYFVLF; -. DR OrthoDB; EOG62G5HP; -. DR PhylomeDB; O05052; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR021810; DUF3387. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR. DR Pfam; PF11867; DUF3387; 1. DR Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00348; hsdR; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Hydrolase; KW Nucleotide-binding; Reference proteome; Restriction system. FT CHAIN 1 1055 Putative type I restriction enzyme FT HindVIIP R protein. FT /FTId=PRO_0000077262. FT DOMAIN 287 468 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. SQ SEQUENCE 1055 AA; 120710 MW; C5BEF298E7E05C67 CRC64; MLNENDIEQL TLQRLQSLGW EYRYGKDLPV HEGKFARGDL SGVVFVEQLR EAVRKLNPQL PESAVDSVVK SATKSDIGDL VVRNQTFYKL LRDGVRVEYT QNGEQKIEMV RLVDFEHWGN NRFVAVNQLE IRSRKGGKRI PDIIGFVNGL PLVVFELKNP LRESADLLQA FNQFETYKDE IAELFVYNQA LIISDGIVAR LGSLSADFQR FTPWKVVDEK NKSARLYFDD ELQSLLNGLM QPEDLLDYIR YFVLFERDSV GKTIKKIAAY HQYYGVNEAV DSTIWATSEK GDRRIGVMWH TQGSGKSISM LFYAGKLLAQ PELKNPTIVV VTDRNDLDGQ LFQTFSSGKD LIKQTPQQVE DRDQLRQLLA QNEVGGVFFT TIQKFALNEE ESRFPILNER NNIIVISDEA HRSQYGFTQK LHNGKFQTGY ARHLRDALPN ASFIGFTGTP ISLEDKDTQD VFGRYVSIYD LQDAVEDGAT VPIVYDDARQ IRLNKKDHDA LFAEIDALLE EEPSTSLRLR EKLLGSQERL IELAADFVQH FAKRNEVVDS KAMMVVSSRQ ICVDLYNQII ALHPEWHSDN INEGAIKIVM TGSASDTPEM QKHIYSKQEK QTLERRFKDP NDPLKVVIVR DMWLTGFDAP CCNTMYLDKP MKGHNLMQAI ARVNRVFANK SRENGGLIVD YVGLAKELRA ATQQYTNSTG KGQLAEDVQS VFFKMKEQLE FIRTLFATPI EGKTFDVQAA LEKDNPNDLL MAIRFAANHI LSLDQLSFDG KAHEQHWFNK KETEPRKKAF LKTAGLVKKG YMLCGTLAEV EPYNQEIAFY DAVRAILTKR EQKGTGTNER QILLKKLVNQ TVYSEGVIDL FDLLEKPQPQ ISLLSEEFLQ TVKNSPTKNL WVSAMERYLA SEIKVKSGTN LTLQKDFERR LKEALNQYHN HNLTVVEILD ELFKMSQDFQ ERLALGKKLG LTKEELAFYE ALSQNQSAKD LMGDEVLSKL AKEITETLRK SVTIDWQYKE AVRARIRLLV RRALQKYKYP PDKQEEAVTY VIKQAEEIAE DLTGL // ID SYD_HAEIN Reviewed; 588 AA. AC P43817; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 121. 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}; GN OrderedLocusNames=HI_0317; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC21981.1; -; Genomic_DNA. DR PIR; E64061; E64061. DR RefSeq; NP_438483.1; NC_000907.1. DR RefSeq; WP_005694347.1; NC_000907.1. DR ProteinModelPortal; P43817; -. DR SMR; P43817; 2-586. DR STRING; 71421.HI0317; -. DR EnsemblBacteria; AAC21981; AAC21981; HI_0317. DR GeneID; 949430; -. DR KEGG; hin:HI0317; -. DR PATRIC; 20189175; VBIHaeInf48452_0334. DR eggNOG; ENOG4105C9M; Bacteria. DR eggNOG; COG0173; LUCA. DR KO; K01876; -. DR OMA; YQLDVEM; -. DR OrthoDB; EOG68Q0NX; -. DR PhylomeDB; P43817; -. DR Proteomes; UP000000579; 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; IPR029351; GAD_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 2. DR PANTHER; PTHR22594:SF5; PTHR22594:SF5; 2. DR Pfam; PF02938; GAD; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF55261; SSF55261; 1. DR TIGRFAMs; TIGR00459; aspS_bact; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 588 Aspartate--tRNA ligase. FT /FTId=PRO_0000110880. FT NP_BIND 218 220 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 535 538 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 196 199 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 172 172 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 218 218 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 227 227 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 449 449 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 483 483 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 490 490 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. SQ SEQUENCE 588 AA; 66639 MW; C53850C75270395A CRC64; MMRTHYCGAL NRNNIGQDVT LSGWVHRRRD LGGLIFIDMR DRDGIVQVCF DPKYQDALTA AAGLRNEFCI QIKGEVIARP DNQINKNMAT GEVEVLAKEL RIYNASDVLP LDFNQNNTEE QRLKYRYLDL RRPEMAQRLK TRAKITSFVR RFMDDNGFLD IETPMLTKAT PEGARDYLVP SRVHKGKFYA LPQSPQLFKQ LLMMSGFDRY YQIVKCFRDE DLRADRQPEF TQIDVETSFL TAPEVREIME RMVHGLWLDT IGVDLGKFPV MTWQEAMRRF GSDKPDLRNP LEMVDVADIV KDVEFKVFNE PANNPNGRVA VIRVPNGAEI TRKQIDEYTQ FVGIYGAKGL AWAKVNDINA GLEGVQSPIA KFLNEDVWKG LAERVNAQTG DILFFGADKW QTTTDAMGAL RLKLGRDLGL TRLDEWQPLW VIDFPMFERD EEGNLAAMHH PFTSPKDFSP EQLEADPTSA VANAYDMVIN GYEVGGGSVR IFDPKMQQTV FRILGIDEEQ QREKFGFLLD ALKFGTPPHA GLAFGLDRLT MLLTGTENIR DVIAFPKTTA AACLMTEAPS FANPQALEEL AISVVKAE // ID SYK_HAEIN Reviewed; 502 AA. AC P43825; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=Lysine--tRNA ligase; DE EC=6.1.1.6; DE AltName: Full=Lysyl-tRNA synthetase; DE Short=LysRS; GN Name=lysS; Synonyms=lysU; OrderedLocusNames=HI_1211; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22865.1; -; Genomic_DNA. DR PIR; D64110; D64110. DR RefSeq; NP_439367.1; NC_000907.1. DR RefSeq; WP_010869153.1; NC_000907.1. DR ProteinModelPortal; P43825; -. DR SMR; P43825; 11-500. DR STRING; 71421.HI1211; -. DR EnsemblBacteria; AAC22865; AAC22865; HI_1211. DR GeneID; 950158; -. DR KEGG; hin:HI1211; -. DR PATRIC; 20191101; VBIHaeInf48452_1263. DR eggNOG; ENOG4105CRK; Bacteria. DR eggNOG; COG1190; LUCA. DR KO; K04567; -. DR OMA; DMMNLTE; -. DR OrthoDB; EOG69PQ2M; -. DR PhylomeDB; P43825; -. DR Proteomes; UP000000579; 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 1 502 Lysine--tRNA ligase. FT /FTId=PRO_0000152634. FT METAL 413 413 Magnesium 1. {ECO:0000250}. FT METAL 420 420 Magnesium 1. {ECO:0000250}. FT METAL 420 420 Magnesium 2. {ECO:0000250}. SQ SEQUENCE 502 AA; 56936 MW; DF281DF073A702B9 CRC64; MSEQEVKELD LNGEMLVRRE KLAALRAKGN AFPNKFRRDA LAQDLHNQYD AEDGEILKEK GIEVQVAGRI MTRRAMGKAT FITIQDMSGK IQLYVARDNL PEGVYKDDVG TWDLGDIVGI KGTLFKTKTD ELTVKTTEVQ LLTKALRPLP DKFHGLTDQE VRYRQRYLDL ISNEESRRTF IIRSKVVAGI REYFISKGFM EVETPMLQVI PGGASARPFV THHNALDVDM YLRIAPELYL KRLVVGGFER VFELNRNFRN EGVSVRHNPE FTMLEYYQAY ADYHDLMDNT EELLRKLAID ILGTTIVKYG DLEFDFGKPF ERITLHDATI KYGADKGIVK EDLYDFDRAK ATAERLGIEV QKSWGLGSIV NAIFEEVAEH HLIQPTFLNG SPAEISPLAR RNDENPEVTD RFELFIGGRE IGNGFSELND AEDQNERFDA QVAAKEAGDD EAMFKDEDFV VALEHGLPPT AGEGLGIDRL AMLYANAPSI RDVILFPAMR QK // ID SYL_HAEIN Reviewed; 861 AA. AC P43827; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=HI_0921; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22581.1; -; Genomic_DNA. DR PIR; H64102; H64102. DR RefSeq; NP_439081.1; NC_000907.1. DR RefSeq; WP_005693268.1; NC_000907.1. DR ProteinModelPortal; P43827; -. DR SMR; P43827; 228-413. DR STRING; 71421.HI0921; -. DR EnsemblBacteria; AAC22581; AAC22581; HI_0921. DR GeneID; 949390; -. DR KEGG; hin:HI0921; -. DR PATRIC; 20190497; VBIHaeInf48452_0962. DR eggNOG; ENOG4105C8T; Bacteria. DR eggNOG; COG0495; LUCA. DR KO; K01869; -. DR OMA; EGAHRFI; -. DR OrthoDB; EOG63Z74X; -. DR PhylomeDB; P43827; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 3. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; 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; 3. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 3. DR Pfam; PF13603; tRNA-synt_1_2; 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 1 861 Leucine--tRNA ligase. FT /FTId=PRO_0000152023. FT MOTIF 42 52 "HIGH" region. FT MOTIF 619 623 "KMSKS" region. FT BINDING 622 622 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. SQ SEQUENCE 861 AA; 97751 MW; EB93304F6B4C8FB7 CRC64; MQEQYRPDMI EPKVQQYWAE NKVFKAIKDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD VISRYQRMLG KNVLQPFGWD AFGLPAEGAA IKNKTAPAKW TYENIAYMKK QLQLLGFGFD WDREIATCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD TPVEQKEIPQ WFIKITDYAE QLLGGLDTLP QWPDMVKTMQ RNWIGRSEGV EITFDVANTN EKVAVYTTRP DTFYGVSYLG IAAAHPLASL AAQNNSELAA FIQEAKNAKV AEADLATMEK KGMATGLFAI HPLTGDKLPI WVANFVLMHY GTGAVMAVPA HDQRDFEFAQ KYSLPIKQVI APLADEEIDL TKQAFVEHGK LVNSDEFDGK NFDGAFNGIA DKLEKLGVGK RQVNYRLRDW GVSRQRYWGA PIPMLTLENG DVVPAPMEDL PIILPEDVVM DGVKSPINAD PNWAKTTFND APALKETDTF DTFMESSWYY ARYTCPQYQN GMLDAEEANY WLPVDQYIGG IEHATMHLLY FRFFHKLLRD AGFVTSEEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTQ VTLERDEKGR IIKATDPEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE SGVEGAKRFL GRVWNLVYQY QQNPAKTSLD LTALSAEQKV LRREVHKTIA KVSDDIGRRQ TFNTAIAAVM ELMNKLTKAS LDSEQDRAVM AEALSAVVRM LYPITPHICF ELWQALGNES AIDTAEWVKA DEAAMVEDEK LIVVQVNGKV RGKVTVATDA DEDTVKTIAF ADENVKKFID NQHIVKVIYV VGKLLNVVVK P // ID T2D5_HAEIN Reviewed; 334 AA. AC P44999; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Probable type-2 restriction enzyme HindVP; DE Short=R.HindVP; DE EC=3.1.21.4; DE AltName: Full=Endonuclease HindVP; DE AltName: Full=Type II restriction enzyme HindVP; GN Name=hindVRP; OrderedLocusNames=HI_1040; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22699.1; -; Genomic_DNA. DR PIR; B64109; B64109. DR RefSeq; NP_439199.1; NC_000907.1. DR RefSeq; WP_010869112.1; NC_000907.1. DR STRING; 71421.HI1040; -. DR REBASE; 2819; HindVP. DR EnsemblBacteria; AAC22699; AAC22699; HI_1040. DR GeneID; 950604; -. DR KEGG; hin:HI1040; -. DR PATRIC; 20190743; VBIHaeInf48452_1084. DR eggNOG; ENOG4108Q0R; Bacteria. DR eggNOG; ENOG4111645; LUCA. DR KO; K01155; -. DR OMA; WGKNQFN; -. DR OrthoDB; EOG6677SG; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR019044; Restrct_endonuc_II_HindVP. DR Pfam; PF09519; RE_HindVP; 2. PE 4: Predicted; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 334 Probable type-2 restriction enzyme FT HindVP. FT /FTId=PRO_0000077322. SQ SEQUENCE 334 AA; 38346 MW; 8CA1F88E76E730DD CRC64; MLYYVPRREK SYMNIKPHLF GLNRSNRDFS LRETWGKNQF NSSFPVSLCC YMSSKGILAN YLSIENAEIK CSSIDIKDVF EIEPENENTF FAFETSHSIK LTALPDHTTC DLTDADFGSE IVIRPDSIVY LACSLAEILK ESLANCMDIP NNVDHLDWSE PKQVIPLFPH ILSTLNNLCS RADTIQTPFL LQPVWKTLGK SPRLADNCLD IFIWSDVAFV KFILEISNLN VNVLSINRQT RTAIWLYKML VDIVKYGRFN HHKIIDLCSY NTKNDKAFAS SGMITNVFMK SERLERPIIM KSEIKNIILG GGQELLSPER RFDAIIYNSS ELFR // ID SYGB_HAEIN Reviewed; 688 AA. AC P43822; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Glycine--tRNA ligase beta subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase beta subunit; DE Short=GlyRS; GN Name=glyS; OrderedLocusNames=HI_0924; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22584.1; -; Genomic_DNA. DR PIR; B64103; B64103. DR RefSeq; NP_439084.1; NC_000907.1. DR RefSeq; WP_005693270.1; NC_000907.1. DR ProteinModelPortal; P43822; -. DR STRING; 71421.HI0924; -. DR EnsemblBacteria; AAC22584; AAC22584; HI_0924. DR GeneID; 949922; -. DR KEGG; hin:HI0924; -. DR PATRIC; 20190505; VBIHaeInf48452_0965. DR eggNOG; ENOG4105C38; Bacteria. DR eggNOG; COG0751; LUCA. DR KO; K01879; -. DR OMA; LPIPKRM; -. DR OrthoDB; EOG661H9S; -. DR PhylomeDB; P43822; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR015944; Gly-tRNA-synth_bsu. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF02092; tRNA_synt_2f; 1. DR PRINTS; PR01045; TRNASYNTHGB. DR SMART; SM00836; DALR_1; 1. DR TIGRFAMs; TIGR00211; glyS; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 688 Glycine--tRNA ligase beta subunit. FT /FTId=PRO_0000072904. SQ SEQUENCE 688 AA; 75613 MW; 67F9ACEF00A94184 CRC64; MTTQNFLVEI GTEELPPKAL KTLATSFADN VEAELNQAGL SFDKIEWFAA PRRLAVKVLN LATQQPSKEI EKRGPAVSAA FDAEGKPTKA AEGWARGCGI TVEQAERIAT DKGEWLIHRA KIEGQPTKNL LNDIVANALA KLPIPKPMRW ADKTVQFIRP VHTVTMLLGD ELIEGEILGV ASARTIRGHR FLGEKEFYIQ HADQYPQLLR EKGSVVADFN ERKAEILAKS QAKATALGGV ADIEESLLEE VTSLVEYPNV LAAKFEEHFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH FIFVSNINPE DPTAIIEGNE KVVRPRLTDA EFFFKTDLKQ KLVDRLPRLE TVLFQQQLGT LKDKTDRIEQ LAGEIAKQIG ADEAKAKRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD GEDEEVAVAL NEQYMPRFAG DELPKSLVAS AVALADKFDT LTGIFGIGQA PKGSADPFAL RRAALGALRI IVEKNLPLDL EDLVKKSAAL FGDKLTNQNV VADVVDFMLG RFRAWYQDEG IAVDVIQAVL ARRPTRPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKAGAAIGEI NLTACVEPAE KALAEAVLAL RTEVQPLIAQ GDYTTVLDKL ANLRAPVDSF FDNVMVNAED PALRQNRLAI LNTLQGLFLQ VADISVLQ // ID SYI_HAEIN Reviewed; 941 AA. AC P43824; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 17-FEB-2016, entry version 111. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; GN OrderedLocusNames=HI_0962; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As CC IleRS can inadvertently accommodate and process structurally CC similar amino acids such as valine, to avoid such errors it has CC two additional distinct tRNA(Ile)-dependent editing activities. CC One activity is designated as 'pretransfer' editing and involves CC the hydrolysis of activated Val-AMP. The other activity is CC designated 'posttransfer' editing and involves deacylation of CC mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP + CC diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02002}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02002}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- DOMAIN: IleRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated valine is CC translocated from the active site to the editing site, which CC sterically excludes the correctly activated isoleucine. The single CC editing site contains two valyl binding pockets, one specific for CC each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP- CC Rule:MF_02002}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Erroneous termination; Positions=30; Note=Translated as Leu.; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; S78633; S78633. DR ProteinModelPortal; P43824; -. DR OMA; PIPFFLH; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023585; Ile-tRNA-ligase_type1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR010663; Znf_FPG/IleRS. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00392; ileS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 941 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098395. FT MOTIF 59 69 "HIGH" region. FT MOTIF 603 607 "KMSKS" region. FT METAL 904 904 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 907 907 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 924 924 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT METAL 927 927 Zinc. {ECO:0000255|HAMAP-Rule:MF_02002}. FT BINDING 562 562 Aminoacyl-adenylate. {ECO:0000255|HAMAP- FT Rule:MF_02002}. FT BINDING 606 606 ATP. {ECO:0000255|HAMAP-Rule:MF_02002}. SQ SEQUENCE 941 AA; 106529 MW; 35B9C66B921B1DAF CRC64; MTVDYKNTLN LPETSFPMRG DLAKREPDKL KNWYEKNLYQ KIRKASKGKK SFILHDGPPY ANGNIHIGHA VNKILKDIII KSKTALGFDS PYIPGWDCHG LPIELKVEGL VGKPNEKISA AEFRQKCREY AAEQVEGQKK DFIRLGVLGD WDNPYLTMNF DTEANIIRTL GKVIENGHLY KGSKPVHWCL DCGSSLAEAE VEYEDKVSPS IYVRFPAESA DEIEAKFSAQ GRGQGKLSAI IWTTTPWTMP SNRAIAVNAD LEYNLVQLGD ERVILAAELV ESVAKAVGIE HIEILGSVKG DDLELSRFHH PFYDFTVPVI LGDHVTTDGG TGLVHTAPDH GLDDFIVGKQ YDLPMAGLVS NDGKFISTTE FFAGKGVFEA NPLVIEKLQE VGNLLKVEKI KHSYPHCWRH KTPIIFRATP QWFIGMETQG LRQQALGEIK QVRWIPDWGQ ARIEKMVENR PDWCISRQRT WGVPMTLFVH KETEELHPRT LDLLEEVAKR VERAGIQAWW DLDEKELLGA DAETYRKVPD TLDVWFDSGS TYSSVVANRL EFNGQDIDMY LEGSDQHRGW FMSSLMLSTA TDSKAPYKQV LTHGFTVDGQ GRKMSKSIGN IVTPQEVMDK FGGDILRLWV ASTDYTGEMT VSDEILKRAA DSYRRIRNTA RFLLANLNGF DPKRDLVKPE KMISLDRWAV ACALDAQNEI KDAYDNYQFH TVVQRLMRFC SVEMGSFYLD IIKDRQYTTK ADSLARRSCQ TALWHIAEAL VRWMAPILSF TADEIWQHLP QTESARAEFV FTEEFYQGLF GLGEDEKLDD AYWQQLIKVR SEVNRVLEIS RNNKEIGGGL EAEVTVYAND EYRALLAQLG NELRFVLITS KVDVKSLSEK PADLADSELE GIAVSVTRSN AEKCPRCWHY SDEIGVSPEH PTLCARCVEN VVGNGEVRYF A // ID TAL_HAEIN Reviewed; 317 AA. AC P45055; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 113. DE RecName: Full=Transaldolase; DE EC=2.2.1.2; GN Name=tal; Synonyms=talB; OrderedLocusNames=HI_1125; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D- CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative CC stage): step 2/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transaldolase family. 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; L42023; AAC22779.1; -; Genomic_DNA. DR PIR; D64167; D64167. DR RefSeq; NP_439282.1; NC_000907.1. DR RefSeq; WP_005693444.1; NC_000907.1. DR ProteinModelPortal; P45055; -. DR SMR; P45055; 2-313. DR STRING; 71421.HI1125; -. DR PRIDE; P45055; -. DR EnsemblBacteria; AAC22779; AAC22779; HI_1125. DR GeneID; 950099; -. DR KEGG; hin:HI1125; -. DR PATRIC; 20190923; VBIHaeInf48452_1174. DR eggNOG; ENOG4105CW3; Bacteria. DR eggNOG; COG0176; LUCA. DR KO; K00616; -. DR OMA; QIPEYSA; -. DR OrthoDB; EOG6G7R4D; -. DR PhylomeDB; P45055; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; ISS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00492; Transaldolase_1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR004730; Transaldolase_1. DR InterPro; IPR018225; Transaldolase_AS. DR PANTHER; PTHR10683; PTHR10683; 1. DR Pfam; PF00923; Transaldolase; 1. DR TIGRFAMs; TIGR00874; talAB; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Pentose shunt; Reference proteome; KW Schiff base; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 317 Transaldolase. FT /FTId=PRO_0000173599. FT ACT_SITE 132 132 Schiff-base intermediate with substrate. FT {ECO:0000250}. SQ SEQUENCE 317 AA; 34905 MW; E48A7E6DCABECF5A CRC64; MTTQLDSLRN MTVVVADTGD IDAIKKYQPQ DATTNPSLIL SASALPQYAP LIDEAVAYAK AQSADKAQQL IDAEDKLAVN IGLEILKIVP GRISTEVDAR LSYDTQATVE KARKLIALYN AAGISNDRIL IKIASTWQGI RAAEILEKEG INCNLTLLFS EAQARACAEA GVYLISPFVG RILDWYKANS DKKEYAPAED PGVISVTKIY NYYKEYGYNT VVMGASFRNV GEITELAGCD RLTIAPALLK ELQENSTALV RKLEYKGEVK AKPQPLTEAE FYWQHNSDAM AVEKLAEGIR KFAIDQEKLE TMLSAKL // ID SYM_HAEIN Reviewed; 682 AA. AC P43828; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 126. DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098}; DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098}; DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098}; GN Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; GN OrderedLocusNames=HI_1276; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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:0000255|HAMAP- CC Rule:MF_00098}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00098}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22924.1; -; Genomic_DNA. DR PIR; I64113; I64113. DR RefSeq; NP_439429.1; NC_000907.1. DR RefSeq; WP_005694519.1; NC_000907.1. DR ProteinModelPortal; P43828; -. DR SMR; P43828; 6-546. DR STRING; 71421.HI1276; -. DR BindingDB; P43828; -. DR ChEMBL; CHEMBL1641340; -. DR EnsemblBacteria; AAC22924; AAC22924; HI_1276. DR GeneID; 949809; -. DR KEGG; hin:HI1276; -. DR PATRIC; 20191231; VBIHaeInf48452_1327. DR eggNOG; ENOG4105CKH; Bacteria. DR eggNOG; COG0073; LUCA. DR eggNOG; COG0143; LUCA. DR KO; K01874; -. DR OMA; FWPAMLD; -. DR OrthoDB; EOG6CVV9B; -. DR PhylomeDB; P43828; -. DR Proteomes; UP000000579; 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:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 2.20.28.20; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR023458; Met-tRNA_ligase_1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR029038; MetRS_Zn. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF09334; tRNA-synt_1g; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF57770; SSF57770; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 682 Methionine--tRNA ligase. FT /FTId=PRO_0000139135. FT DOMAIN 580 682 tRNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_00098}. FT MOTIF 15 25 "HIGH" region. FT MOTIF 331 335 "KMSKS" region. FT METAL 146 146 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 149 149 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 159 159 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 162 162 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT BINDING 334 334 ATP. {ECO:0000255|HAMAP-Rule:MF_00098}. SQ SEQUENCE 682 AA; 77023 MW; 61F07EBDFD2A3CE2 CRC64; MTTQPRKILV TCALPYANGA IHLGHMLEHI QADIWVRFQR MRGNKIHFVC ADDAHGTPIM LNADKLGITP EELIAKAKAD HIRDFAGFNI SFDNYHSTHS EENKQLTAEI YNKLKANGFI KSKVISQLFD PEKNMFLPDR FVKGTCPKCK AEDQYGDNCE VCASTYSPMD LINPRSAVSG TTPIVKESEH FFFDLPAFEG MLKEWTRSGS LQSEIANKMQ EWFESDLQQW DISRDAPYFG FEIPGAKDKF FYVWLDAPIG YMASFKNLCN REGIDFNEFW AEGSDAELYH FIGKDIVYFH SLFWPAMLEG SGYRKPTNVF AHGYVTVDGA KMSKSRGTFI QASTYLNHID PECLRYYYAA KLNDRIEDLD FNLEDFVQRV NTDIVNKLVN LASRNAGFIA KRFEGKLADK LEDKSLFAEF TAQAEQIAAY YESREYNKTI REIMALTDKA NKYIDEKAPW VIAKEEGKEA ELQAVCSMGI ELFRVLMSYL KPVLPKLAER AETFLQAELR WDNIHQPLLG HTLAPFKALF SRLEKKQIDA VVEETKALFA AANKAAEKTE AKPTALSAVE PIAETITIDD FAKLDMRVAK VLKCEAVPES NKLLRFELDL GDHTRQVFSG IKAAYNKPEE LEGRFVIMVA NLAPRKMKFG VSEGMILSAG TGGSDLFLLS ADSGVTAGMQ VK // ID SYN_HAEIN Reviewed; 467 AA. AC P43829; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 2. DT 11-NOV-2015, entry version 109. 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}; GN OrderedLocusNames=HI_1302; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- SEQUENCE CAUTION: CC Sequence=AAC22949.1; 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; L42023; AAC22949.1; ALT_INIT; Genomic_DNA. DR PIR; B64115; B64115. DR RefSeq; NP_439453.2; NC_000907.1. DR RefSeq; WP_010869177.1; NC_000907.1. DR ProteinModelPortal; P43829; -. DR STRING; 71421.HI1302; -. DR EnsemblBacteria; AAC22949; AAC22949; HI_1302. DR GeneID; 950195; -. DR KEGG; hin:HI1302; -. DR PATRIC; 20191287; VBIHaeInf48452_1354. DR eggNOG; ENOG4105C5S; Bacteria. DR eggNOG; COG0017; LUCA. DR KO; K01893; -. DR OMA; WWYLDTR; -. DR OrthoDB; EOG6ZSP6X; -. DR PhylomeDB; P43829; -. DR Proteomes; UP000000579; 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; 2. DR PANTHER; PTHR22594:SF6; PTHR22594:SF6; 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 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 1 467 Asparagine--tRNA ligase. FT /FTId=PRO_0000176414. SQ SEQUENCE 467 AA; 52847 MW; 6EBCB823306F806C CRC64; MSKVASIVDV LQGKVAIGET VTVRGWVRTR RDSKAGLSFL AVYDGSCFDP IQAIINNDIE NYESEILRLT TGCSVIVTGK VVESPAEGQA VELQAEKVEV TGFVEDPDTY PMAAKRHSIE YLREVAHLRP RTNIIGAVAR VRHCLSQAIH RFFHEQGFYW VATPLITASD TEGAGEMFRV STLDLENLPR SENGKVDFSQ DFFGKESFLT VSGQLNGETY ACALSKIYTF GPTFRAENSN TTRHLAEFWM VEPEVAFATL ADNAKLAEDM LKYVFRAVLA ERKDDLQFFE KHVDKDVITR LENFVNSDFA QIDYTDAIDV LLKSGKKFEF PVSWGIDLSS EHERFLAEEY FKSPVVVKNY PKDIKAFYMR LNDDEKTVAA MDVLAPGIGE IIGGSQREER LEVLDKRMEE MGLNPDDYWW YRDLRKYGSV PHSGFGLGFE RLIVYVTGVQ NIRDVIPFPR APRNANF // ID SYW_HAEIN Reviewed; 334 AA. AC P43835; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 106. 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=HI_0637; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22296.1; -; Genomic_DNA. DR PIR; C64083; C64083. DR RefSeq; NP_438797.1; NC_000907.1. DR RefSeq; WP_005694505.1; NC_000907.1. DR ProteinModelPortal; P43835; -. DR SMR; P43835; 5-331. DR STRING; 71421.HI0637; -. DR PRIDE; P43835; -. DR EnsemblBacteria; AAC22296; AAC22296; HI_0637. DR GeneID; 949689; -. DR KEGG; hin:HI0637; -. DR PATRIC; 20189881; VBIHaeInf48452_0665. DR eggNOG; ENOG4105C31; Bacteria. DR eggNOG; COG0180; LUCA. DR KO; K01867; -. DR OMA; GWGQFKP; -. DR OrthoDB; EOG686NJQ; -. DR PhylomeDB; P43835; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type. DR PANTHER; PTHR10055; PTHR10055; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR TIGRFAMs; TIGR00233; trpS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 334 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136635. FT MOTIF 12 20 "HIGH" region. FT MOTIF 195 199 "KMSKS" region. FT BINDING 198 198 ATP. {ECO:0000250}. SQ SEQUENCE 334 AA; 37396 MW; 7A581383BFF1F7A1 CRC64; MAKPIVFSGV QPSGELTIGN YLGALRNWVK MQEDYECIFC VVDLHAITVR QDPVALRKAT LDVLALYLAC GIDPNKSTIF VQSHVPEHTQ LSWVLNCYTY FGEMSRMTQF KDKSARYAEN INVGLFDYPV LMAADILLYQ AKSVPVGDDQ KQHLEITRDI ANRFNALYGN IFTIPEIFIG KAGARIMSLQ DPEKKMSKSD DNRNNVVTLL EDPKSVAKKI KRAVTDSDEP PVVRYDVQNK AGVSNLLDIL SAVTDKPIAD LEKEFEGKMY GHLKTAVADE VSTLLASLQE RFHQYRNDET LLDNILRQGA EKARAKAQET LAKVYEAVGF VAAK // ID T1SI_HAEIN Reviewed; 385 AA. AC P71344; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Putative type I restriction enzyme specificity protein HI_0216; DE Short=S protein; GN OrderedLocusNames=HI_0216; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21883.1; -; Genomic_DNA. DR PIR; E64055; E64055. DR RefSeq; NP_438384.1; NC_000907.1. DR RefSeq; WP_005694081.1; NC_000907.1. DR ProteinModelPortal; P71344; -. DR STRING; 71421.HI0216; -. DR REBASE; 6051; S.HindORF215P. DR EnsemblBacteria; AAC21883; AAC21883; HI_0216. DR GeneID; 951125; -. DR KEGG; hin:HI0216; -. DR PATRIC; 20188935; VBIHaeInf48452_0224. DR eggNOG; ENOG41082EK; Bacteria. DR eggNOG; COG0732; LUCA. DR KO; K01154; -. DR OMA; ANNIQDY; -. DR OrthoDB; EOG6PKF94; -. DR Proteomes; UP000000579; 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 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repeat; KW Restriction system. FT CHAIN 1 385 Putative type I restriction enzyme FT specificity protein HI_0216. FT /FTId=PRO_0000198041. SQ SEQUENCE 385 AA; 44278 MW; AD6A5D037961E62F CRC64; MKNNRTFLEK LLEGSEVEWK PLDEVANIVN NARKPVKSSL RVSGNIPYYG ANNIQDYVEG YTHEGEFVLI AEDGSASLEN YSIQWAVGKF WANNHVHVVN GKEKLNNRFL YHYLTNMNFI PFLAGKERAK LTKAKLQQIP IPIPPLSVQT EIVKILDALT ALTSELTSEL TSELTSELIL RQKQYEYYRE KLLNIDEMNK VIELGDVGPV RMCKRILKNQ TASSGDIPFY KIGTFGKKPD AYISNELFQE YKQKYSYPKK GDILISASGT IGRTVIFDGE NSYFQDSNIV WIDNDETLVL NKYLYHFYKI AKWGIAEGGT IQRLYNDNLK KVKISIPPLK EQHRIVSILD KFETLTNSIT EGLPLAIEQS QKRYEYYREL LLNFS // ID T3RH_HAEIN Reviewed; 514 AA. AC P44105; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Putative type III restriction-modification system HindVIP enzyme res; DE EC=3.1.21.5; GN OrderedLocusNames=HI_1055; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC -!- SUBUNIT: Contains two different subunits: res and mod. CC {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; L42023; AAC22720.1; -; Genomic_DNA. DR PIR; F64019; F64019. DR ProteinModelPortal; P44105; -. DR STRING; 71421.HI1055; -. DR REBASE; 2820; HindVIP. DR EnsemblBacteria; AAC22720; AAC22720; HI_1055. DR PATRIC; 20190775; VBIHaeInf48452_1100. DR eggNOG; ENOG4107J0C; Bacteria. DR eggNOG; COG3421; LUCA. DR OMA; MNDRTSK; -. DR OrthoDB; EOG6H7FCV; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0015668; F:Type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Endonuclease; Helicase; Hydrolase; KW Nuclease; Nucleotide-binding; Reference proteome; Restriction system. FT CHAIN 1 514 Putative type III restriction- FT modification system HindVIP enzyme res. FT /FTId=PRO_0000077377. SQ SEQUENCE 514 AA; 59880 MW; F7801427DB3C23C2 CRC64; MRSIKRRKKM ANDKTLFDWV EDRKSTLEEM EQTDFFALPE FVERNLKYPF FEWQKSALEN FLIFDRTSKL KDFPDIKNRP THLLFNMATG AGKTMMMAAL ILYYFEKGYR HFLFFVNQNN IVDKTENNFT DPTHAKFLFT EKILQGDTVI PIRKVETFSP HSDGIEIKFT SIQKLYNDIH TEQENQTTLT DLHDLNLVML GDEAHHLNAQ TKGKKQGELD LEKEMNDRTS KAEIERKGWE HMVLELLLNK NGNPSENVLL EFTATLPENA EVQQKYADKI ITKFGLKEFL QKGYTKEINL VSSTLGKKER VLHALLFAWY RHQIALKYGI ANFKPVMLFR SKTIDESKAD YLAFLNWVEN VQAVDFSFLT TFLASLNDSD NANEQGKTRT EQALKFIQDN KFEFVHLADW VKQNYQKHNV IITNSETNKS KTEKTDSETE KLLNNLEAAD NPIRAIFTVD RLTEGWDVLN LFDIVRLYEG QNGGGSNKKS GKSCRHRIRK AVNWSWRALF SICV // ID T2D2_HAEIN Reviewed; 258 AA. AC P44413; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-DEC-2015, entry version 99. DE RecName: Full=Type-2 restriction enzyme HindII; DE Short=R.HindII; DE EC=3.1.21.4; DE AltName: Full=Endonuclease HindII; DE AltName: Full=Type II restriction enzyme HindII; GN Name=hindIIR; OrderedLocusNames=HI_0512; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Recognizes the double-stranded sequence GTYRAC and CC cleaves after Y-3. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22170.1; -; Genomic_DNA. DR PIR; E64073; E64073. DR RefSeq; NP_438670.1; NC_000907.1. DR RefSeq; WP_005693662.1; NC_000907.1. DR ProteinModelPortal; P44413; -. DR SMR; P44413; 2-258. DR STRING; 71421.HI0512; -. DR REBASE; 1150; HindII. DR EnsemblBacteria; AAC22170; AAC22170; HI_0512. DR GeneID; 950710; -. DR KEGG; hin:HI0512; -. DR PATRIC; 20189577; VBIHaeInf48452_0531. DR eggNOG; ENOG4106KR2; Bacteria. DR eggNOG; ENOG410YBKR; LUCA. DR KO; K01155; -. DR OMA; YINWAAA; -. DR OrthoDB; EOG6VMTKC; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.600.10; -; 1. DR InterPro; IPR011337; DNA_rep_MutH/RE_typeII. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR015307; Restrct_endonuc_II_HincII. DR Pfam; PF09226; Endonuc-HincII; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 258 Type-2 restriction enzyme HindII. FT /FTId=PRO_0000077320. SQ SEQUENCE 258 AA; 29929 MW; 6BE104A1D1B63238 CRC64; MSFIKPIYQD INSILIGQKV KRPKSGTLSG HAAGEPFEKL VYKFLKENLS DLTFKQYEYL NDLFMKKPAI IGHEARYKLF NSPTLLFLLS RGKAATENWS IENLFEEKQN DTADILLVKD QFYELLDVKT RNISKSAQAP NIISAYKLAQ TCAKMIDNKE FDLFDINYLE VDWELNGEDL VCVSTSFAEL FKSEPSELYI NWAAAMQIQF HVRDLDQGFN GTREEWAKSY LKHFVTQAEQ RAISMIDKFV KPFKKYIL // ID T2D3_HAEIN Reviewed; 300 AA. AC P43870; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 99. DE RecName: Full=Type-2 restriction enzyme HindIII; DE Short=R.HindIII; DE EC=3.1.21.4; DE AltName: Full=Endonuclease HindIII; DE AltName: Full=Type II restriction enzyme HindIII; GN Name=hindIIIR; OrderedLocusNames=HI_1393; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-26. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3; RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., RA Benner J.S., Wilson G.G.; RT "Cloning, analysis and expression of the HindIII R-M-encoding genes."; RL Gene 150:75-80(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Recognizes the double-stranded sequence AAGCTT and CC cleaves after A-1. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L15391; AAA61958.1; -; Genomic_DNA. DR EMBL; L42023; AAC23040.1; -; Genomic_DNA. DR PIR; H64121; H64121. DR RefSeq; NP_439547.1; NC_000907.1. DR PDB; 2E52; X-ray; 2.00 A; A/B/C/D=1-300. DR PDB; 3A4K; X-ray; 2.17 A; A/B/C/D=1-300. DR PDB; 3WVG; X-ray; 2.25 A; A/B/C/D=1-300. DR PDB; 3WVH; X-ray; 2.54 A; A/B/C/D=1-300. DR PDB; 3WVI; X-ray; 2.55 A; A/B/C/D=1-300. DR PDB; 3WVK; X-ray; 2.00 A; A/B/C/D=1-300. DR PDB; 3WVP; X-ray; 2.30 A; A/B/C/D=1-300. DR PDBsum; 2E52; -. DR PDBsum; 3A4K; -. DR PDBsum; 3WVG; -. DR PDBsum; 3WVH; -. DR PDBsum; 3WVI; -. DR PDBsum; 3WVK; -. DR PDBsum; 3WVP; -. DR ProteinModelPortal; P43870; -. DR SMR; P43870; 2-300. DR STRING; 71421.HI1393; -. DR BindingDB; P43870; -. DR ChEMBL; CHEMBL5004; -. DR REBASE; 1151; HindIII. DR EnsemblBacteria; AAC23040; AAC23040; HI_1393. DR GeneID; 950303; -. DR KEGG; hin:HI1393; -. DR PATRIC; 20191483; VBIHaeInf48452_1452. DR eggNOG; ENOG4105S7Q; Bacteria. DR eggNOG; ENOG4111XCG; LUCA. DR KO; K01155; -. DR OMA; DINMSSK; -. DR OrthoDB; EOG686NN8; -. DR EvolutionaryTrace; P43870; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR019043; Restrct_endonuc_II_HindIII. DR Pfam; PF09518; RE_HindIII; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Endonuclease; Hydrolase; Nuclease; Reference proteome; KW Restriction system. FT CHAIN 1 300 Type-2 restriction enzyme HindIII. FT /FTId=PRO_0000077321. FT HELIX 5 15 {ECO:0000244|PDB:2E52}. FT TURN 16 18 {ECO:0000244|PDB:2E52}. FT HELIX 21 33 {ECO:0000244|PDB:2E52}. FT HELIX 37 47 {ECO:0000244|PDB:2E52}. FT HELIX 59 78 {ECO:0000244|PDB:2E52}. FT STRAND 81 85 {ECO:0000244|PDB:2E52}. FT STRAND 89 91 {ECO:0000244|PDB:3WVK}. FT STRAND 94 103 {ECO:0000244|PDB:2E52}. FT STRAND 105 110 {ECO:0000244|PDB:2E52}. FT HELIX 122 125 {ECO:0000244|PDB:2E52}. FT HELIX 127 133 {ECO:0000244|PDB:2E52}. FT TURN 134 136 {ECO:0000244|PDB:2E52}. FT STRAND 137 144 {ECO:0000244|PDB:2E52}. FT HELIX 146 148 {ECO:0000244|PDB:2E52}. FT STRAND 151 153 {ECO:0000244|PDB:2E52}. FT HELIX 155 163 {ECO:0000244|PDB:2E52}. FT STRAND 165 169 {ECO:0000244|PDB:2E52}. FT HELIX 170 178 {ECO:0000244|PDB:2E52}. FT HELIX 190 193 {ECO:0000244|PDB:2E52}. FT HELIX 195 200 {ECO:0000244|PDB:2E52}. FT HELIX 205 207 {ECO:0000244|PDB:2E52}. FT HELIX 213 224 {ECO:0000244|PDB:2E52}. FT HELIX 228 261 {ECO:0000244|PDB:2E52}. FT HELIX 265 275 {ECO:0000244|PDB:2E52}. FT HELIX 278 293 {ECO:0000244|PDB:2E52}. FT HELIX 295 298 {ECO:0000244|PDB:2E52}. SQ SEQUENCE 300 AA; 34952 MW; 62F62AC4B18E841B CRC64; MKKSALEKLL SLIENLTNQE FKQATNSLIS FIYKLNRNEV IELVRSIGIL PEAIKPSSTQ EKLFSKAGDI VLAKAFQLLN LNSKPLEQRG NAGDVIALSK EFNYGLVADA KSFRLSRTAK NQKDFKVKAL SEWREDKDYA VLTAPFFQYP TTKSQIFKQS LDENVLLFSW EHLAILLQLD LEETNIFSFE QLWNFPKKQS KKTSVSDAEN NFMRDFNKYF MDLFKIDKDT LNQLLQKEIN FIEERSLIEK EYWKKQINII KNFTREEAIE ALLKDINMSS KIETIDSFIK GIKSNDRLYL // ID T1SH_HAEIN Reviewed; 459 AA. AC P44152; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative type-1 restriction enzyme HindVIIP specificity protein; DE Short=S.HindVIIP; DE AltName: Full=Type I restriction enzyme HindVIIP specificity protein; DE Short=S protein; GN OrderedLocusNames=HI_1286; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22935.1; -; Genomic_DNA. DR PIR; H64024; H64024. DR RefSeq; NP_439438.1; NC_000907.1. DR RefSeq; WP_005694527.1; NC_000907.1. DR STRING; 71421.HI1286; -. DR REBASE; 5608; S.HindI. DR EnsemblBacteria; AAC22935; AAC22935; HI_1286. DR GeneID; 950231; -. DR KEGG; hin:HI1286; -. DR PATRIC; 20191255; VBIHaeInf48452_1338. DR eggNOG; ENOG4105EKX; Bacteria. DR eggNOG; COG0732; LUCA. DR KO; K01154; -. DR OMA; NETTEYF; -. DR OrthoDB; EOG6JDWF1; -. DR PhylomeDB; P44152; -. DR Proteomes; UP000000579; 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 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repeat; KW Restriction system. FT CHAIN 1 459 Putative type-1 restriction enzyme FT HindVIIP specificity protein. FT /FTId=PRO_0000198040. SQ SEQUENCE 459 AA; 51402 MW; F925AACF03C88D96 CRC64; MSDWKEYSLG DISRNISRRF DFNAYPNVVF INTGDVLNNK FLHCEISNVK DLPGQAKKAI KKGDILYSEI RPGNGRYLFV DNDLDNYVVS TKFMVIEPNA NIVLPEFLFL LLISNETTEY FKMIAESRSG TFPQITFDSV SSLSLNIPDK ETQQKILDII TPLDDKIELN TQINQTLEQI AQALFKSWFV DFDPVRAKAQ ALSDGMSLEQ AELAAMQAIS GKTPEELTAL SQTQPDRYAE LAETAKAFPC EMVEVDGVEV DGVEVPRGWE MKALSDLGQI ICGKTPSKSN KEFYGDDVPF IKIPDMHNQV FITQTTDNLS VVGANYQSKK YIPAKSICVS CIATVGLVSM TSKPSHTNQQ INSIIPDDEQ SCEFLYLSLK QPSMTKYLKD LASGGTATLN LNTSTFSKIE IITPSKEIIY IFQKKVVSIF EKTLSNSIEN KRLTEIRDLL LPRLLNGEI // ID TADA_HAEIN Reviewed; 173 AA. AC P44931; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=tRNA-specific adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00972}; DE EC=3.5.4.33 {ECO:0000255|HAMAP-Rule:MF_00972}; GN Name=tadA {ECO:0000255|HAMAP-Rule:MF_00972}; GN OrderedLocusNames=HI_0906; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the CC wobble position 34 of tRNA(Arg2). {ECO:0000255|HAMAP- CC Rule:MF_00972}. CC -!- CATALYTIC ACTIVITY: Adenine(34) in tRNA + H(2)O = hypoxanthine(34) CC in tRNA + NH(3). {ECO:0000255|HAMAP-Rule:MF_00972}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00972}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00972}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000255|HAMAP-Rule:MF_00972}. 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; L42023; AAC22565.1; -; Genomic_DNA. DR PIR; C64161; C64161. DR RefSeq; NP_439066.1; NC_000907.1. DR RefSeq; WP_005693256.1; NC_000907.1. DR ProteinModelPortal; P44931; -. DR STRING; 71421.HI0906; -. DR EnsemblBacteria; AAC22565; AAC22565; HI_0906. DR GeneID; 949908; -. DR KEGG; hin:HI0906; -. DR PATRIC; 20190467; VBIHaeInf48452_0947. DR eggNOG; ENOG4108Z6B; Bacteria. DR eggNOG; COG0590; LUCA. DR KO; K11991; -. DR OMA; RIGRIFF; -. DR OrthoDB; EOG64FKGZ; -. DR PhylomeDB; P44931; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central. DR HAMAP; MF_00972; tRNA_aden_deaminase; 1. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR028883; tRNA_aden_deaminase. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR SUPFAM; SSF53927; SSF53927; 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; KW tRNA processing; Zinc. FT CHAIN 1 173 tRNA-specific adenosine deaminase. FT /FTId=PRO_0000171739. FT DOMAIN 9 121 CMP/dCMP-type deaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01083}. FT ACT_SITE 63 63 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00972}. FT METAL 61 61 Zinc; via pros nitrogen; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00972}. FT METAL 91 91 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00972}. FT METAL 94 94 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00972}. SQ SEQUENCE 173 AA; 19359 MW; 785E2CE532FB72DE CRC64; MDAAKVRSEF DEKMMRYALE LADKAEALGE IPVGAVLVDD ARNIIGEGWN LSIVQSDPTA HAEIIALRNG AKNIQNYRLL NSTLYVTLEP CTMCAGAILH SRIKRLVFGA SDYKTGAIGS RFHFFDDYKM NHTLEVTSGV LAEECSQKLS TFFQKRREEK KIEKALLKSL SDK // ID TAMB_HAEIN Reviewed; 1298 AA. AC Q57523; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Translocation and assembly module TamB; DE AltName: Full=Autotransporter assembly factor TamB; GN Name=tamB; OrderedLocusNames=HI_0696; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the translocation and assembly module (TAM) CC autotransporter assembly complex, which functions in translocation CC of autotransporters across the outer membrane. {ECO:0000250}. CC -!- SUBUNIT: Interacts with TamA. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TamB 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; L42023; AAC22356.1; -; Genomic_DNA. DR PIR; A64157; A64157. DR RefSeq; NP_438856.1; NC_000907.1. DR RefSeq; WP_005694581.1; NC_000907.1. DR STRING; 71421.HI0696; -. DR EnsemblBacteria; AAC22356; AAC22356; HI_0696. DR GeneID; 950032; -. DR KEGG; hin:HI0696; -. DR PATRIC; 20190013; VBIHaeInf48452_0728. DR eggNOG; ENOG4105MA0; Bacteria. DR eggNOG; COG2911; LUCA. DR KO; K09800; -. DR OMA; FPQAFNA; -. DR OrthoDB; EOG6GJBQK; -. DR PhylomeDB; Q57523; -. DR Proteomes; UP000000579; 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; IPR007452; TamB. DR Pfam; PF04357; TamB; 1. PE 1: Evidence at protein level; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1 1298 Translocation and assembly module TamB. FT /FTId=PRO_0000169831. FT TOPO_DOM 1 27 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 28 48 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000250}. FT TOPO_DOM 49 1298 Periplasmic. {ECO:0000250}. SQ SEQUENCE 1298 AA; 141223 MW; 2D905D8E6D9329E9 CRC64; MTEQIQPSET SPKSPEKPNK KHWVRKAVCI GSAVILVPVL GVAGALSFDA GQKSLIQLVD KMLDSFSVEQ VEGGLQNGLV LKNVRYQTAG IETHIAQARL QLDFGCLFSR EVCLRDFTLN KPTIAINTAL LPPSAPDNSK SGSMKRISLP ISINAENLVM QDLSVNIDQT SITLGNFKSA VSLNNEKGLT IAPTEINDIS VIAKKLSEVK SEPKAEQPNK PVDWAAIEQS LTPAFLGNVS EIILPFDLHI PEISGKNWQY QAVNEKGETL QSVEMSSLIA QADTVDNQLQ LQKLAVESSL GNLSSQGKLQ LDGDMPLDLT LKSHLEPLKS DGKEILPASD VDLTLSGSLK KSTALSLKTK GVLDAELNGN VQLAQDKMPL NLTLNVAKGQ YTFVNTMTPL KINDVTLKLT GDLLNYHAEL KGDVAGMNYI PASQVELNAD GKLYEVTVNK LGIDSLDGKS EFVGNANWKN GANWDIQADL EKMNIAFFVP VMPATLSGKL HSRGFAGSQG WQVEVPVADL NGMLSAKPIS LKGSATLNQN VLLTVPDLQI KYGENYLKAS GVLDDHSDFA LDINAPNLRG LWSDLKGRVK GRVAISGQIT TPNLDLDLTS SNLHLQGFQL AKASIKGHIN NASLSSGKLN IKAEQLHYGG NIKLHLLDLD LSGDEQNHKL ILKSQGEPVA ANLQINGHFD RTLEQWKGTI SQVKFETPIG DVKSNQAIAV SYDNKQTQAN IASHCWQNTD VELCFPQAFN AGKQGNIPFQ FKRVNLDLVN KLIEQNSLKG NLQVQGNVAW FTDKPFQFTA NVDGNHLAFS QKLDYRTFKL YIPKLTLNAD IQNNNLVLKT DINVHNQGRI VGDIHLNDLA KNRQLGGTLA IERLNLSIAN QLLTSGESVN GEVVSKLSFG GNLEKPLLNG DFNIRNIRTK LKSMPVNITD GDIALRFNDN RSTLQGKIKT VDSHLNLTGR ANWANIEHWT TELNAQANNF NVDIPSMAKL RFSPNITIKA NPKELNLSGT VDIPWARIKI DSLPDTAEPV SEDEVILNGP HKSKEELIKR EFAAKTKSGM EIRSDLRINI GKDVSLDAYG LKTNLDGLLS VKQDKGNLGL FGQINLTKGR YASFGQDLLI RKGLISFSGQ ATQPTLNIEA IRNPETMEDS KITAGVRVIG IADSPEVTIF SEPSKPQDQA LSYLLTGRSL ESSGEVGSTG SVGAALIGLG ISKSGKLVGS IGEVFGIQDL NLGTSGVGDK SKVTVSGNIT NRLQIKYGVG LFDGLAEVTL RYRLMPQLYF QSVSSTNQVF DLLYKFEF // ID TATA_HAEIN Reviewed; 89 AA. AC P57046; P44559; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236}; GN Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; GN OrderedLocusNames=HI_0187; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. TatA CC could form the protein-conducting channel of the Tat system. CC {ECO:0000255|HAMAP-Rule:MF_00236}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000255|HAMAP-Rule:MF_00236}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00236}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00236}. CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP- CC Rule:MF_00236}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_438355.1; NC_000907.1. DR RefSeq; WP_010868952.1; NC_000907.1. DR STRING; 71421.HI0187a; -. DR GeneID; 951097; -. DR KEGG; hin:HI0187a; -. DR PATRIC; 20188869; VBIHaeInf48452_0191. DR eggNOG; COG1826; LUCA. DR KO; K03116; -. DR OrthoDB; EOG6WQD34; -. DR PhylomeDB; P57046; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00236; TatA_E; 1. DR InterPro; IPR003369; TatA/B/E. DR InterPro; IPR006312; TatA/E. DR Pfam; PF02416; MttA_Hcf106; 1. DR TIGRFAMs; TIGR01411; tatAE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 89 Sec-independent protein translocase FT protein TatA. FT /FTId=PRO_0000097938. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00236}. SQ SEQUENCE 89 AA; 10005 MW; A4F99E244D1F8E89 CRC64; MFGLSPAQLI ILLVVILLIF GTKKLRNAGS DLGAAVKGFK KAMKEDEKVK DAEFKSIDNE TASAKKGKYK RERNRLNPCL ILVFQNLFY // ID SYT_HAEIN Reviewed; 643 AA. AC P43014; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 118. 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=HI_1367; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-443. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6; RA Chandler M.S., Smith R.A.; RT "Characterization of the Haemophilus influenzae topA locus: DNA RT topoisomerase I is required for genetic competence."; RL Gene 169:25-31(1996). 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; L42023; AAC23014.1; -; Genomic_DNA. DR EMBL; U20964; AAC43729.1; -; Genomic_DNA. DR PIR; H64119; H64119. DR RefSeq; NP_439518.1; NC_000907.1. DR RefSeq; WP_005693993.1; NC_000907.1. DR ProteinModelPortal; P43014; -. DR SMR; P43014; 2-642. DR STRING; 71421.HI1367; -. DR EnsemblBacteria; AAC23014; AAC23014; HI_1367. DR GeneID; 950281; -. DR KEGG; hin:HI1367; -. DR PATRIC; 20191421; VBIHaeInf48452_1421. DR eggNOG; ENOG4105C22; Bacteria. DR eggNOG; COG0441; LUCA. DR KO; K01868; -. DR OMA; FYYDFAY; -. DR OrthoDB; EOG61KBFJ; -. DR PhylomeDB; P43014; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00184; Thr_tRNA_synth; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF02824; TGS; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 643 Threonine--tRNA ligase. FT /FTId=PRO_0000100987. FT REGION 243 534 Catalytic. FT METAL 334 334 Zinc; catalytic. {ECO:0000250}. FT METAL 385 385 Zinc; catalytic. {ECO:0000250}. FT METAL 511 511 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 643 AA; 73712 MW; 3B67D928B6E085DE CRC64; MPIITLPDGS QRQFDRPVSV LEVAQDIGAG LAKATIAGRV NGERRDACYV IEQDATLEII TAKDEDGLEI IRHSCAHLLG HAIKQLFPDV KMAIGPTIEN GFYYDVDLDR SLTQEDIDAI EKRMLELAKT NYDVVKKRVT WQEARDTFEK RGEPYKMAIL DENIERTATP ALYHHLEYID MCRGPHVPNM RFCQHFKLQK VAGAYWRGDS KNKMLQRIYG TAWADKKQLA EYLTRLEEAA KRDHRKIGKA LDLYHMQEEA PGMVFWHNDG WTIFRELETF VRTKLKQYDY QEVKGPFMMD RVLWEKTGHW QNYADLMFTT QSENREYAIK PMNCPGHVQI FNQGLKSYRD LPIRMAEFGS CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE DQIESEVTSC IKMVYDIYST FGFTNIAVKL STRPENRIGS DEMWDRAEAG LAAALAHNGL EYEIQEGEGA FYGPKIEFAL RDCLGREWQC GTVQLDFALP GRLDATYVAE DNSRKTPVMI HRAILGSIER FIGIITEEYA GFFPAWLAPT QAVVMNITDS QADYVQKVAK QLSDVGLRVK TDLRNEKVGF KIREHTLRRV PYMLVCGDKE IAEGKVAVRT RKGADLGTFT VEEFAEILKN QVRSRELKLL NEE // ID SYY_HAEIN Reviewed; 401 AA. AC P43836; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007}; DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007}; DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007}; DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007}; GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007}; GN OrderedLocusNames=HI_1610; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000255|HAMAP- CC Rule:MF_02007}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_02007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23254.1; -; Genomic_DNA. DR PIR; D64132; D64132. DR RefSeq; NP_439752.1; NC_000907.1. DR RefSeq; WP_010869258.1; NC_000907.1. DR STRING; 71421.HI1610; -. DR EnsemblBacteria; AAC23254; AAC23254; HI_1610. DR GeneID; 950464; -. DR KEGG; hin:HI1610; -. DR PATRIC; 20191951; VBIHaeInf48452_1683. DR eggNOG; ENOG4105DA0; Bacteria. DR eggNOG; COG0162; LUCA. DR KO; K01866; -. DR OMA; DMFGKVM; -. DR OrthoDB; EOG6B09VR; -. DR PhylomeDB; P43836; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.290.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1. DR InterPro; 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; IPR024108; Tyr-tRNA-ligase_bac_2. DR PANTHER; PTHR11766; PTHR11766; 1. DR Pfam; PF01479; S4; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR00234; tyrS; 1. DR PROSITE; 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 1 401 Tyrosine--tRNA ligase. FT /FTId=PRO_0000055654. FT DOMAIN 334 394 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_02007}. FT MOTIF 42 51 "HIGH" region. FT MOTIF 226 230 "KMSKS" region. FT BINDING 229 229 ATP. {ECO:0000255|HAMAP-Rule:MF_02007}. SQ SEQUENCE 401 AA; 44776 MW; 42F1EE374A00EC20 CRC64; MTDINTVLAE LKRGTDEILS EADLIEKLKE NRPLKVKLGA DPTAPDIHLG HTVVLNKLRQ FQQLGHEVYF LIGDFTGMVG DPSGKNATRP PLSREDVLRN AETYKEQIYK ILDPQKTKIV FNSEWLSKLG TXGMIRLASN YTVARMLERD DFKKRFGNNQ PIAIHEFIYP LLQGYDSVAL DADVELGGTD QKFNLLVGRE LQKSAGKKPQ VAITLPLLVG LDGEKKMSKS LGNYIGVTEA PSDMFGKVMS ISDELMWDWY NLLSFRPLNE IAQLKSEVEN GKNPRDVKIL LAKELIARFH NEEAANAAEQ EFINRFQKGA MPDEMPEFTF SGEMGLATLL KEAGLVPSTS EAIRSAQQGG VKINGEKVDN VKDNAPKGTN VYQVGKRKFA RVRLNKVDTV K // ID SYV_HAEIN Reviewed; 954 AA. AC P43834; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 113. DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004}; DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004}; DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004}; DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004}; GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; GN OrderedLocusNames=HI_1391; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3; RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., RA Benner J.S., Wilson G.G.; RT "Cloning, analysis and expression of the HindIII R-M-encoding genes."; RL Gene 150:75-80(1994). 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; L42023; AAC23038.1; -; Genomic_DNA. DR EMBL; L15391; AAA61960.1; -; Genomic_DNA. DR PIR; G64121; G64121. DR RefSeq; NP_439545.1; NC_000907.1. DR RefSeq; WP_005693970.1; NC_000907.1. DR ProteinModelPortal; P43834; -. DR STRING; 71421.HI1391; -. DR EnsemblBacteria; AAC23038; AAC23038; HI_1391. DR GeneID; 950584; -. DR KEGG; hin:HI1391; -. DR PATRIC; 20191479; VBIHaeInf48452_1450. DR eggNOG; ENOG4105CA4; Bacteria. DR eggNOG; COG0525; LUCA. DR KO; K01873; -. DR OMA; SQYRFDL; -. DR OrthoDB; EOG644ZM1; -. DR PhylomeDB; P43834; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.380; -; 1. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 3. 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; 3. 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 1 954 Valine--tRNA ligase. FT /FTId=PRO_0000106225. FT COILED 883 953 {ECO:0000255|HAMAP-Rule:MF_02004}. FT MOTIF 48 58 "HIGH" region. FT MOTIF 560 564 "KMSKS" region. FT BINDING 563 563 ATP. {ECO:0000255|HAMAP-Rule:MF_02004}. SQ SEQUENCE 954 AA; 108826 MW; FE26264932F2F78A CRC64; MTQKFEMADR FNPSAVEQAL YQRWEESGYF KPSENENAPS YCIAIPPPNV TGSLHMGHAF QQTLMDTLIR FNRMEGHNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI WDWKAYSGGT ISQQMRRLGN SIDWERERFT MDDGLSNAVK EVFVRLHEEG LIYRGKRLVN WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANDAKTADGK DYLVVATTRP ETMLGDTAVA VHPEDERYQS LIGKTVVLPL ANREIPIIAD EYVDREFGTG VVKITPAHDF NDYEVGKRHN LPMVNVLTLN ANIRDEAEII GTDGKPLAGY EATIPADYRG LERFAARKKI VADFEALGLL DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLADVAI KAVEDGEIQF VPKQYENLYF SWMRDIQDWC ISRQLWWGHR IPAWYDAEGN VYVARNEEEV RSKYNLDSAV ELKQDEDVLD TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI AKATRKEFAE GIAAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRFVLT NEKLDLSQGE IEFSLADRWI QSEFNRTVET FRSSLSQYRF DLCANAIYEF TWNQFCDWYL ELTKPVFANG NAAQIRAASQ TLVHVLEKLL RLAHPLIPFI TEEIWQKVKG FVGITADSIM LQPFPQVEES GFDPEAEAEI EWLKEVIVAV RNIRAESNIA PSKGLDLLFR NLSAENAKIL EKQTALLKAM AKLDNVQVLA TNETAPLAVA KLVGNAELLV PMAGFINKEA ELARLTKEIE KYQNEVKRIE NKLSNEAFVA KAPEAVIAKE REKQAEYQSG LEKIQEQYKA IEAL // ID TATB_HAEIN Reviewed; 186 AA. AC P57047; P44559; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237}; GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; GN OrderedLocusNames=HI_0187.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. CC Together with TatC, TatB is part of a receptor directly CC interacting with Tat signal peptides. TatB may form an oligomeric CC binding site that transiently accommodates folded Tat precursor CC proteins before their translocation. {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000255|HAMAP-Rule:MF_00237}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00237}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP- CC Rule:MF_00237}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_438356.1; NC_000907.1. DR RefSeq; WP_005694100.1; NC_000907.1. DR STRING; 71421.HI0187b; -. DR GeneID; 951096; -. DR KEGG; hin:HI0187b; -. DR PATRIC; 20188871; VBIHaeInf48452_0192. DR eggNOG; COG1826; LUCA. DR KO; K03117; -. DR OMA; MGSAMDS; -. DR OrthoDB; EOG6WQD34; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00237; TatB; 1. DR InterPro; IPR018448; TatB. DR InterPro; IPR003998; TatB-like. DR PRINTS; PR01506; TATBPROTEIN. DR TIGRFAMs; TIGR01410; tatB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 186 Sec-independent protein translocase FT protein TatB. FT /FTId=PRO_0000192657. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00237}. SQ SEQUENCE 186 AA; 20430 MW; 7FD2166488CA057F CRC64; MFDIGFSELI LLMVLGLVVL GPKRLPIAIR TVMDWVKTIR GLAANVQNEL KQELKLQELQ DSIKKAESLN LQALSPELSK TVEELKAQAD KMKAELEDKA AQAGTTVEDQ IKEIKSAAEN AEKSQNAISV EEAAETLSEA ERTPTDLTAL ETHEKVELNT HLSSYYPPDD IEIAPASKSQ SSKTKS // ID TBPA_HAEIN Reviewed; 912 AA. AC P44970; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Probable transferrin-binding protein 1; DE Flags: Precursor; GN Name=tbpA; Synonyms=tbp1; OrderedLocusNames=HI_0994; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts as a transferrin receptor and is required for CC transferrin utilization. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor 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; L42023; AAC22656.1; -; Genomic_DNA. DR PIR; C64107; C64107. DR RefSeq; NP_439157.1; NC_000907.1. DR RefSeq; WP_005693337.1; NC_000907.1. DR ProteinModelPortal; P44970; -. DR STRING; 71421.HI0994; -. DR TCDB; 1.B.14.2.12; the outer membrane receptor (omr) family. DR EnsemblBacteria; AAC22656; AAC22656; HI_0994. DR GeneID; 950660; -. DR KEGG; hin:HI0994; -. DR PATRIC; 20190649; VBIHaeInf48452_1037. DR eggNOG; ENOG4108MVK; Bacteria. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; TFAYNRV; -. DR OrthoDB; EOG6HB9KP; -. DR PhylomeDB; P44970; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 3. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010916; TonB_box_CS. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010948; TonB_lacto/transferrin_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR TIGRFAMs; TIGR01776; TonB-tbp-lbp; 1. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 912 Probable transferrin-binding protein 1. FT /FTId=PRO_0000034776. FT MOTIF 50 57 TonB box. FT MOTIF 895 912 TonB C-terminal box. SQ SEQUENCE 912 AA; 103234 MW; 294C08991A652CC2 CRC64; MTKKPYFRLS IISCLLISCY VKAETQSIKD TKEAISSEVD TQSTEDSELE TISVTAEKVR DRKDNEVTGL GKIIKTSESI SREQVLNIRD LTRYDPGISV VEQGRGASSG YSIRGMDRNR VALLVDGLPQ TQSYVVQSPL VARSGYSGTG AINEIEYENV KAVEISKGGS SSEYGNGALA GSVTFQSKSA ADILEGDKSW GIQTKNAYSS KNKGFTHSLA VAGKQGGFEG LAIYTQRNSI ETQVHKDALK GVQSYNRLIA KPENQSAYFV MEDECPKGYD ECIPSAKPPA ILSTKKETVS VSDYTGANRI KPNPMKYESQ SWFLRGGYHF SEQHYIGGIF EFTQQKFDIR DMTFPAYLSP TEKGDLANRP FYPKQDYGAY QHIEDGRGVK YASGLYFDEH HRKQRVGIEY IYENKNKAGI IDKAVLSANQ QNIILDSYMR HTHCSLYPNP SKNCRPTLDK PYSYYRSDRN VYKEKHNMLQ LNLEKKIQQN WLTHQIVFNL GFDDFTSALQ HKDYLTRRVI ATADSISDKT GKTRRNGLRE YPYLYPKPKP YFAGEDHCNY QGSSSNYRDC KVRLIKGKNY YFAARNNMAL GKYVDLGLGI RYDVSRTKAN ESTISVGKFK NFSWNTGIVI KPTEWLDLSY RLSTGFRNPS FAEMYGWRYG GKNDEVYVGK FKPETSRNQE FGLALKGDFG NIEISHFSNA YRNLIAFAEE LSKNGTGKGN YGYHNAQNAK LVGVNITAQL DFNGLWKRIP YGWYATFAYN RVKVKDQKIN AGLASVSSYL FDAIQPSRYI IGLGYDHISN TWGVNATFTQ SKAKSQNELL GKRALGNNSR DVKSTRKLTR AWHILDVSGY YMANKNIMLR LGIYNLFNYR YVTWEAVRQT AQGAVNQHQN VGNYTRYAAS GRNYTLTLEM KF // ID TEHA_HAEIN Reviewed; 328 AA. AC P44741; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 103. DE RecName: Full=Tellurite resistance protein TehA homolog; GN Name=tehA; OrderedLocusNames=HI_0511; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 15-328, SUBUNIT, SUBCELLULAR RP LOCATION, TRANSMEMBRANE TOPOLOGY, AND MUTAGENESIS OF GLY-29 AND RP PHE-276. RX PubMed=20981093; DOI=10.1038/nature09487; RA Chen Y.H., Hu L., Punta M., Bruni R., Hillerich B., Kloss B., Rost B., RA Love J., Siegelbaum S.A., Hendrickson W.A.; RT "Homologue structure of the SLAC1 anion channel for closing stomata in RT leaves."; RL Nature 467:1074-1080(2010). CC -!- FUNCTION: Ion channel involved in potassium tellurite resistance. CC {ECO:0000305}. CC -!- SUBUNIT: Homotrimer. Each subunit forms a channel. CC {ECO:0000269|PubMed:20981093}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate CC transporter (TDT) 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; L42023; AAC22169.1; -; Genomic_DNA. DR PIR; D64073; D64073. DR RefSeq; NP_438669.1; NC_000907.1. DR RefSeq; WP_010868994.1; NC_000907.1. DR PDB; 3M71; X-ray; 1.20 A; A=15-328. DR PDB; 3M72; X-ray; 1.70 A; A=15-328. DR PDB; 3M73; X-ray; 1.15 A; A=15-328. DR PDB; 3M74; X-ray; 1.65 A; A=15-328. DR PDB; 3M75; X-ray; 1.60 A; A=15-328. DR PDB; 3M76; X-ray; 1.50 A; A=15-328. DR PDB; 3M77; X-ray; 1.50 A; A=15-328. DR PDB; 3M78; X-ray; 2.60 A; A=15-328. DR PDB; 3M7B; X-ray; 1.50 A; A=15-328. DR PDB; 3M7C; X-ray; 1.70 A; A=15-328. DR PDB; 3M7E; X-ray; 1.80 A; A=15-328. DR PDB; 3M7L; X-ray; 1.50 A; A=15-328. DR PDB; 4YCR; X-ray; 2.30 A; A=22-320. DR PDBsum; 3M71; -. DR PDBsum; 3M72; -. DR PDBsum; 3M73; -. DR PDBsum; 3M74; -. DR PDBsum; 3M75; -. DR PDBsum; 3M76; -. DR PDBsum; 3M77; -. DR PDBsum; 3M78; -. DR PDBsum; 3M7B; -. DR PDBsum; 3M7C; -. DR PDBsum; 3M7E; -. DR PDBsum; 3M7L; -. DR PDBsum; 4YCR; -. DR DIP; DIP-59222N; -. DR STRING; 71421.HI0511; -. DR TCDB; 2.A.16.1.2; the telurite-resistance/dicarboxylate transporter (tdt) family. DR DNASU; 950588; -. DR EnsemblBacteria; AAC22169; AAC22169; HI_0511. DR GeneID; 950588; -. DR KEGG; hin:HI0511; -. DR PATRIC; 20189575; VBIHaeInf48452_0530. DR eggNOG; COG1275; LUCA. DR KO; K03304; -. DR OMA; YFEEVRA; -. DR OrthoDB; EOG6P0709; -. DR PhylomeDB; P44741; -. DR EvolutionaryTrace; P44741; -. DR Proteomes; UP000000579; 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:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR GO; GO:0046690; P:response to tellurium ion; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011552; TehA/Mae1. DR InterPro; IPR004695; Voltage-dep_anion_channel. DR Pfam; PF03595; SLAC1; 1. DR TIGRFAMs; TIGR00816; tdt; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Cell inner membrane; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Reference proteome; Tellurium resistance; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 328 Tellurite resistance protein TehA FT homolog. FT /FTId=PRO_0000072480. FT TOPO_DOM 1 21 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 22 42 Helical. FT TOPO_DOM 43 49 Periplasmic. {ECO:0000305}. FT TRANSMEM 50 73 Helical. FT TOPO_DOM 74 93 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 94 112 Helical. FT TOPO_DOM 113 115 Periplasmic. {ECO:0000305}. FT TRANSMEM 116 141 Helical. FT TOPO_DOM 142 153 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 154 174 Helical. FT TOPO_DOM 175 176 Periplasmic. {ECO:0000305}. FT TRANSMEM 177 204 Helical. FT TOPO_DOM 205 208 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 209 232 Helical. FT TOPO_DOM 233 238 Periplasmic. {ECO:0000305}. FT TRANSMEM 239 262 Helical. FT TOPO_DOM 263 268 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 269 289 Helical. FT TOPO_DOM 290 294 Periplasmic. {ECO:0000305}. FT TRANSMEM 295 321 Helical. FT TOPO_DOM 322 328 Cytoplasmic. {ECO:0000305}. FT SITE 276 276 Important for gating; obstructs channel FT and prevents ion flux in the closed FT conformation. FT MUTAGEN 29 29 G->D: Blocks channel. Abolishes ion flux; FT when associated with A-276. FT {ECO:0000269|PubMed:20981093}. FT MUTAGEN 276 276 F->A,G: Constitutively open channel. FT Abolishes ion flux; when associated with FT D-29. {ECO:0000269|PubMed:20981093}. FT MUTAGEN 276 276 F->L,V: No ion flux while channel is in FT closed conformation. FT {ECO:0000269|PubMed:20981093}. FT MUTAGEN 276 276 F->T: Small constitutive ion flux. FT {ECO:0000269|PubMed:20981093}. FT HELIX 25 28 {ECO:0000244|PDB:3M73}. FT HELIX 29 42 {ECO:0000244|PDB:3M73}. FT TURN 43 47 {ECO:0000244|PDB:3M73}. FT HELIX 51 79 {ECO:0000244|PDB:3M73}. FT HELIX 81 89 {ECO:0000244|PDB:3M73}. FT HELIX 93 98 {ECO:0000244|PDB:3M73}. FT HELIX 99 111 {ECO:0000244|PDB:3M73}. FT TURN 112 114 {ECO:0000244|PDB:3M73}. FT HELIX 116 137 {ECO:0000244|PDB:3M73}. FT HELIX 139 143 {ECO:0000244|PDB:3M73}. FT STRAND 145 147 {ECO:0000244|PDB:3M73}. FT HELIX 149 151 {ECO:0000244|PDB:3M73}. FT HELIX 154 156 {ECO:0000244|PDB:3M73}. FT HELIX 157 160 {ECO:0000244|PDB:3M73}. FT HELIX 162 173 {ECO:0000244|PDB:3M73}. FT HELIX 177 204 {ECO:0000244|PDB:3M73}. FT HELIX 209 212 {ECO:0000244|PDB:3M73}. FT HELIX 213 219 {ECO:0000244|PDB:3M73}. FT HELIX 220 232 {ECO:0000244|PDB:3M73}. FT TURN 233 235 {ECO:0000244|PDB:3M73}. FT HELIX 239 262 {ECO:0000244|PDB:3M73}. FT TURN 263 265 {ECO:0000244|PDB:3M73}. FT HELIX 269 274 {ECO:0000244|PDB:3M73}. FT HELIX 275 290 {ECO:0000244|PDB:3M73}. FT HELIX 295 321 {ECO:0000244|PDB:3M73}. SQ SEQUENCE 328 AA; 36934 MW; 8F5BA175AD817CE0 CRC64; MLHFAHIFQN KVHTMNITKP FPLPTGYFGI PLGLAALSLA WFHLENLFPA ARMVSDVLGI VASAVWILFI LMYAYKLRYY FEEVRAEYHS PVRFSFIALI PITTMLVGDI LYRWNPLIAE VLIWIGTIGQ LLFSTLRVSE LWQGGVFEQK STHPSFYLPA VAANFTSASS LALLGYHDLG YLFFGAGMIA WIIFEPVLLQ HLRISSLEPQ FRATMGIVLA PAFVCVSAYL SINHGEVDTL AKILWGYGFL QLFFLLRLFP WIVEKGLNIG LWAFSFGLAS MANSATAFYH GNVLQGVSIF AFVFSNVMIG LLVLMTIYKL TKGQFFLK // ID TEHB_HAEIN Reviewed; 286 AA. AC P45134; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Probable S-adenosyl-L-methionine-dependent methyltransferase TehB; DE EC=2.1.1.-; DE AltName: Full=Tellurite resistance protein TehB homolog; GN Name=tehB; OrderedLocusNames=HI_1275; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=16855256; DOI=10.1128/JB.00417-06; RA Whitby P.W., Vanwagoner T.M., Seale T.W., Morton D.J., Stull T.L.; RT "Transcriptional profile of Haemophilus influenzae: effects of iron RT and heme."; RL J. Bacteriol. 188:5640-5645(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Chen Y.-H., Hendrickson W.A.; RT "Crystal structure of TehB from Haemophilus influenzae."; RL Submitted (MAY-2010) to the PDB data bank. CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent CC methyltransferase. Plays a role in both resistance to oxidative CC damage and heme uptake/utilization. Also protects H.influenzae CC from tellurite exposure in vitro; however, since H.influenzae CC grows only in humans, it is unlikely to encounter tellurite in its CC natural environment, and it is thus probable that tellurite CC resistance does not represent a biologically relevant role of TehB CC (By similarity). {ECO:0000250}. CC -!- INDUCTION: Transcription is significantly up-regulated during CC growth in iron/heme-restricted conditions. CC {ECO:0000269|PubMed:16855256}. CC -!- SIMILARITY: Belongs to the TehB 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; L42023; AAC22923.1; -; Genomic_DNA. DR PIR; H64113; H64113. DR RefSeq; NP_439428.1; NC_000907.1. DR RefSeq; WP_005694518.1; NC_000907.1. DR PDB; 3M70; X-ray; 1.95 A; A=1-286. DR PDBsum; 3M70; -. DR ProteinModelPortal; P45134; -. DR STRING; 71421.HI1275; -. DR EnsemblBacteria; AAC22923; AAC22923; HI_1275. DR GeneID; 949980; -. DR KEGG; hin:HI1275; -. DR PATRIC; 20191229; VBIHaeInf48452_1326. DR eggNOG; ENOG41088CC; Bacteria. DR eggNOG; COG0500; LUCA. DR eggNOG; COG3615; LUCA. DR KO; K16868; -. DR OMA; LHKTDEN; -. DR OrthoDB; EOG6C2WG4; -. DR PhylomeDB; P45134; -. DR EvolutionaryTrace; P45134; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR GO; GO:0046690; P:response to tellurium ion; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR015392; DUF1971. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR015985; TehB-like_dom. DR InterPro; IPR004537; Tellurite-R_MeTrfase_TehB. DR InterPro; IPR014431; Tellurite-R_TehB-2. DR Pfam; PF09313; DUF1971; 1. DR Pfam; PF03848; TehB; 1. DR PIRSF; PIRSF005215; TehB; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00477; tehB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 286 Probable S-adenosyl-L-methionine- FT dependent methyltransferase TehB. FT /FTId=PRO_0000072482. FT REGION 175 176 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 128 128 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 133 133 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 149 149 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 191 191 S-adenosyl-L-methionine. {ECO:0000250}. FT TURN 2 4 {ECO:0000244|PDB:3M70}. FT STRAND 5 10 {ECO:0000244|PDB:3M70}. FT TURN 16 18 {ECO:0000244|PDB:3M70}. FT HELIX 21 24 {ECO:0000244|PDB:3M70}. FT STRAND 25 27 {ECO:0000244|PDB:3M70}. FT STRAND 34 42 {ECO:0000244|PDB:3M70}. FT STRAND 44 49 {ECO:0000244|PDB:3M70}. FT STRAND 55 61 {ECO:0000244|PDB:3M70}. FT STRAND 76 82 {ECO:0000244|PDB:3M70}. FT STRAND 86 94 {ECO:0000244|PDB:3M70}. FT HELIX 95 97 {ECO:0000244|PDB:3M70}. FT HELIX 98 103 {ECO:0000244|PDB:3M70}. FT HELIX 110 118 {ECO:0000244|PDB:3M70}. FT STRAND 123 128 {ECO:0000244|PDB:3M70}. FT HELIX 133 140 {ECO:0000244|PDB:3M70}. FT STRAND 144 150 {ECO:0000244|PDB:3M70}. FT HELIX 152 164 {ECO:0000244|PDB:3M70}. FT STRAND 169 173 {ECO:0000244|PDB:3M70}. FT HELIX 176 178 {ECO:0000244|PDB:3M70}. FT STRAND 185 190 {ECO:0000244|PDB:3M70}. FT HELIX 194 196 {ECO:0000244|PDB:3M70}. FT HELIX 199 201 {ECO:0000244|PDB:3M70}. FT HELIX 202 211 {ECO:0000244|PDB:3M70}. FT STRAND 213 225 {ECO:0000244|PDB:3M70}. FT STRAND 228 230 {ECO:0000244|PDB:3M70}. FT HELIX 244 248 {ECO:0000244|PDB:3M70}. FT TURN 249 251 {ECO:0000244|PDB:3M70}. FT STRAND 252 258 {ECO:0000244|PDB:3M70}. FT STRAND 261 267 {ECO:0000244|PDB:3M70}. FT STRAND 273 284 {ECO:0000244|PDB:3M70}. SQ SEQUENCE 286 AA; 33020 MW; 69D7647E97CC74FA CRC64; MKNELICYKQ MPVWTKDNLP QMFQEKHNTK VGTWGKLTVL KGKLKFYELT ENGDVIAEHI FTPESHIPFV EPQAWHRVEA LSDDLECTLG FYCKKEDYFS KKYNTTAIHG DVVDAAKIIS PCKVLDLGCG QGRNSLYLSL LGYDVTSWDH NENSIAFLNE TKEKENLNIS TALYDINAAN IQENYDFIVS TVVFMFLNRE RVPSIIKNMK EHTNVGGYNL IVAAMSTDDV PCPLPFSFTF AENELKEYYK DWEFLEYNEN MGELHKTDEN GNRIKMKFAT MLARKK // ID THIE_HAEIN Reviewed; 226 AA. AC P71350; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TPS {ECO:0000255|HAMAP-Rule:MF_00097}; DE EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_00097}; DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00097}; DE Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_00097}; GN Name=thiE {ECO:0000255|HAMAP-Rule:MF_00097}; GN OrderedLocusNames=HI_0417; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl CC pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate CC (TMP). {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate CC = diphosphate + thiamine phosphate + CO(2). {ECO:0000255|HAMAP- CC Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + CC thiamine phosphate + CO(2). {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00097}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00097}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00097}. CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00097}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22075.1; -; Genomic_DNA. DR PIR; A64152; A64152. DR RefSeq; NP_438579.1; NC_000907.1. DR RefSeq; WP_005693747.1; NC_000907.1. DR ProteinModelPortal; P71350; -. DR STRING; 71421.HI0417; -. DR EnsemblBacteria; AAC22075; AAC22075; HI_0417. DR GeneID; 949518; -. DR KEGG; hin:HI0417; -. DR PATRIC; 20189387; VBIHaeInf48452_0437. DR eggNOG; ENOG4108UV6; Bacteria. DR eggNOG; COG0352; LUCA. DR KO; K00788; -. DR OMA; QVREKHG; -. DR OrthoDB; EOG6W19NW; -. DR PhylomeDB; P71350; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IBA:GO_Central. DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00097; TMP_synthase; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022998; ThiaminP_synth_SF. DR InterPro; IPR003733; TMP_synthase. DR Pfam; PF02581; TMP-TENI; 1. DR SUPFAM; SSF51391; SSF51391; 1. DR TIGRFAMs; TIGR00693; thiE; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 226 Thiamine-phosphate synthase. FT /FTId=PRO_0000157016. FT REGION 46 50 HMP-PP binding. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT REGION 149 151 THZ-P binding. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT REGION 201 202 THZ-P binding. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT METAL 84 84 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT METAL 103 103 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 83 83 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 122 122 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 152 152 HMP-PP. {ECO:0000255|HAMAP- FT Rule:MF_00097}. FT BINDING 181 181 THZ-P; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00097}. SQ SEQUENCE 226 AA; 24730 MW; C5EB00DED081EEE7 CRC64; MKNIQKILPL YFVAGTQDCR HLGENLSENL LFVLKQALEG GITCFQFRDK GKFSLEHTPS AQKALAINCR DLCREYGVPF IVDDNVDLAL EIEADGIHVG QSDMPVQEIR AKTDKPLIIG WSVNRLDEAK IGENLAEIDY FGIGPIFPTQ SKENPKPTLG MAFIQTLRNA GITKPLVAIG GVKLAHVKTL REFGADGVAV ITAITHADNV QAATKALREA SDEYAK // ID T3MH_HAEIN Reviewed; 629 AA. AC P71366; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 98. DE RecName: Full=Putative type III restriction-modification system HindVIP enzyme mod; DE Short=M.HindVIP; DE EC=2.1.1.72; DE AltName: Full=HindVIP methyltransferase; GN OrderedLocusNames=HI_1056; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SUBUNIT: Contains two different subunits: res and mod. Mod is a CC homotetramer (By similarity). {ECO:0000250}. 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; L42023; AAC22721.1; -; Genomic_DNA. DR PIR; C64180; C64180. DR RefSeq; NP_439215.1; NC_000907.1. DR RefSeq; WP_010869119.1; NC_000907.1. DR ProteinModelPortal; P71366; -. DR STRING; 71421.HI1056; -. DR REBASE; 3701; M.HindVI. DR EnsemblBacteria; AAC22721; AAC22721; HI_1056. DR GeneID; 950036; -. DR KEGG; hin:HI1056; -. DR PATRIC; 20190777; VBIHaeInf48452_1101. DR eggNOG; ENOG4107QMH; Bacteria. DR eggNOG; COG2189; LUCA. DR KO; K07316; -. DR OMA; IHSEEFQ; -. DR OrthoDB; EOG65F8SN; -. DR PhylomeDB; P71366; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002295; D21N6_MeTrfase. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 629 Putative type III restriction- FT modification system HindVIP enzyme mod. FT /FTId=PRO_0000088033. SQ SEQUENCE 629 AA; 71845 MW; 93ADAD909DB41E84 CRC64; MAGKAPKKAK KFILNAIIVS QSVSQSVSQS VSQSVSQSVS QSVSQSVSQS VSQSVSQSVS QLYTKLTRKR QEIFFNQTLA FDEIDRLFDA KAFSKFSRYT ADGKQAVGEI KRHSDGTPAE NLIIKGNNLI ALHSLAKQFK GKVKLIYIDP PYNTGNDGFK YNDKFNHSTW LTFMKNRLEI AKTLLADDGV IFVQCDDIEQ AYLKILMDDI FDRDNFLNIV TVKTKIGGVS GSSEGKSLKD STEFINVFSK NRERLFLNPV YQKTEVNEFI KNYEDSGKSW KYTQVLIDLG EKILLEEKDG FKYYHYPNAQ MTSIVKFSQD QNLSKEIIYT EYSHKVYRTT NAQSSIRSKI IEDLYSIKNG IVSIEYIPQK GKNAGNLIEV FYNASNKDMF MFLSDMLIKE KNKYFYLQKV NTLWDDIQYN NLNKEGGYID FKNGKKPEAL LRRIIDMTTK EGDIVLDYHL GSGTTAAVAH KMNRQYIGIE QMDYIETLAV ERLKKVIDGE QGGISKAVNW QGGGEFVYAE LAPFNETAKQ QILACEDSDD IKTLFEDLCE RYFLKYNVSV KEFSQIIEEP EFQSLPLDEQ KQMVLEMLDL NQMYVSLSEM DDEQFAGCLN DDDKALSRAF YQAEKKDGE // ID THIL_HAEIN Reviewed; 328 AA. AC Q57190; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-MAY-2016, entry version 95. DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128}; GN Name=thiL {ECO:0000255|HAMAP-Rule:MF_02128}; GN OrderedLocusNames=HI_1305; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the CC active form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- CATALYTIC ACTIVITY: ATP + thiamine phosphate = ADP + thiamine CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine diphosphate from thiamine phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a CC direct, inline transfer of the gamma-phosphate of ATP to TMP CC rather than a phosphorylated enzyme intermediate. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22952.1; 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; L42023; AAC22952.1; ALT_INIT; Genomic_DNA. DR PIR; E64115; E64115. DR RefSeq; NP_439456.1; NC_000907.1. DR RefSeq; WP_010869178.1; NC_000907.1. DR ProteinModelPortal; Q57190; -. DR STRING; 71421.HI1305; -. DR EnsemblBacteria; AAC22952; AAC22952; HI_1305. DR GeneID; 950230; -. DR KEGG; hin:HI1305; -. DR PATRIC; 20191293; VBIHaeInf48452_1357. DR eggNOG; ENOG4105CG2; Bacteria. DR eggNOG; COG0611; LUCA. DR KO; K00946; -. DR OMA; GRHFFAD; -. DR OrthoDB; EOG6RRKQ4; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_02128; TMP_kinase; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR006283; ThiL. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR01379; thiL; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 328 Thiamine-monophosphate kinase. FT /FTId=PRO_0000096197. FT NP_BIND 121 122 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 30 30 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 30 30 Magnesium 4; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 45 45 Magnesium 4. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 46 46 Magnesium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 47 47 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 47 47 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 75 75 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 75 75 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 75 75 Magnesium 4. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 122 122 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 211 211 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 214 214 Magnesium 5. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 54 54 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 146 146 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT BINDING 213 213 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT BINDING 262 262 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 321 321 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. SQ SEQUENCE 328 AA; 36016 MW; DD0F666BD73A6056 CRC64; MAMGEFDLIK RYFQQQILVD DSVQLSIGDD CALVSVPENY QLAITTDTMV ENTHFLPTIS PEDLAYKAVA TNLSDLAAMG AQPKWVSLAL TLPNVDENWI STFSQSLLHT LKQYNVTLIG GDTTKGNLSI TITAQGFVEK NKGICRHKAQ IGDLIYVSST LGDSAAGLTQ ILLGKSAVDS DDVFLQQRHL RPTPRIELGQ ALIGIAHVAI DLSDGLISDL GHILERSQCS AEVELTALPL SSSILNKYDR TQAEQFALSG GEDYELCFTI PPEYKDELEL RLKKLNVPCT CIGKINEKCG DFSPRFLRDG KPVNITFSSG FDHFKESK // ID TAMA_HAEIN Reviewed; 578 AA. AC P44038; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Translocation and assembly module TamA; DE AltName: Full=Autotransporter assembly factor TamA; DE Flags: Precursor; GN Name=tama; OrderedLocusNames=HI_0698; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of the translocation and assembly module (TAM) CC autotransporter assembly complex, which functions in translocation CC of autotransporters across the outer membrane. {ECO:0000250}. CC -!- SUBUNIT: Interacts with TamB. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. CC -!- DOMAIN: Contains 3 N-terminal periplasmic polypeptide transport- CC associated (POTRA) domains and a C-terminal transmembrane region. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TamA 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; L42023; AAC22357.1; -; Genomic_DNA. DR PIR; B64012; B64012. DR RefSeq; NP_438857.1; NC_000907.1. DR RefSeq; WP_010869035.1; NC_000907.1. DR ProteinModelPortal; P44038; -. DR STRING; 71421.HI0698; -. DR EnsemblBacteria; AAC22357; AAC22357; HI_0698. DR GeneID; 950204; -. DR KEGG; hin:HI0698; -. DR PATRIC; 20190015; VBIHaeInf48452_0729. DR eggNOG; ENOG4105CFU; Bacteria. DR eggNOG; COG0729; LUCA. DR KO; K07278; -. DR OMA; ALRYWNN; -. DR OrthoDB; EOG6F81K6; -. DR PhylomeDB; P44038; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR000184; Bac_surfAg_D15. DR Pfam; PF01103; Bac_surface_Ag; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane beta strand. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 578 Translocation and assembly module TamA. FT /FTId=PRO_0000013947. SQ SEQUENCE 578 AA; 65812 MW; 34F9AC189C505876 CRC64; MKKKSLKLTA LFLALSCFPA FAEQTVDIEV QGIRGFRAVR NTDLNVNLIN KEEMDGSERY QHLVTKAVDR GLRVFGYYES SVRFERKQRQ GKRDLLIAHV TPGEPTKIAG TDVQIEGEAA QDENFNALRK NLPKDGVLVE HQTYDDYKTA ISRLALNRGY FDGNFKISRL EISPETHQAW WRMLFDSGVR YHYGNITFSH SQIRDDYLNN ILNIKSGDPY LMNNLSDLTS DFPSSNWFSS VLVQPNVNHK SKTVDVEIIL YPRKKNAMEL GVGFSTDGGV HGQIGWTKPW INSRGHSLRS NLYLSAPKQT LEATYRMPLL KNPLNYYYDF AVGWEGEKEN DTNTRVLTLS ALRYWNNAHG WQYFGGLRMR YDSFTQADIT DKTLLLYPTV GFTRTRLRGG SFATWGDVQK ITFDLSKRIW LSESSFIKVQ ASSAWVRTYA ENHRVVARAE IGYLHTKGIE KIPPTLRFFA GGDRSVRGYG YKKIAPKNRN GKLVGGSRLL TTSLEYQYQV YPNWWAATFA DSGLAADNYT AKELRYGTGV GVRWASPVGA IKFDIATPIR DKDNSKNIQF YIGLGTEI // ID TATC_HAEIN Reviewed; 256 AA. AC P44560; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000255|HAMAP-Rule:MF_00902}; GN Name=tatC {ECO:0000255|HAMAP-Rule:MF_00902}; GN OrderedLocusNames=HI_0188; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system CC that transports large folded proteins containing a characteristic CC twin-arginine motif in their signal peptide across membranes. CC Together with TatB, TatC is part of a receptor directly CC interacting with Tat signal peptides. {ECO:0000255|HAMAP- CC Rule:MF_00902}. CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC CC complex, containing multiple copies of TatA, TatB and TatC CC subunits, and a separate TatA complex, containing only TatA CC subunits. Substrates initially bind to the TatABC complex, which CC probably triggers association of the separate TatA complex to form CC the active translocon. {ECO:0000255|HAMAP-Rule:MF_00902}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00902}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00902}. CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP- CC Rule:MF_00902}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21857.1; -; Genomic_DNA. DR PIR; C64145; C64145. DR RefSeq; NP_438357.1; NC_000907.1. DR RefSeq; WP_005694099.1; NC_000907.1. DR STRING; 71421.HI0188; -. DR EnsemblBacteria; AAC21857; AAC21857; HI_0188. DR GeneID; 951098; -. DR KEGG; hin:HI0188; -. DR PATRIC; 20188873; VBIHaeInf48452_0193. DR eggNOG; ENOG4105DCX; Bacteria. DR eggNOG; COG0805; LUCA. DR KO; K03118; -. DR OMA; ATQIYKF; -. DR OrthoDB; EOG60SCQS; -. DR PhylomeDB; P44560; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-HAMAP. DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00902; TatC; 1. DR InterPro; IPR019820; Sec-indep_translocase_CS. DR InterPro; IPR002033; TatC. DR PANTHER; PTHR30371:SF0; PTHR30371:SF0; 1. DR Pfam; PF00902; TatC; 1. DR PRINTS; PR01840; TATCFAMILY. DR TIGRFAMs; TIGR00945; tatC; 1. DR PROSITE; PS01218; TATC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 256 Sec-independent protein translocase FT protein TatC. FT /FTId=PRO_0000098086. FT TRANSMEM 25 45 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 77 97 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 117 137 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 158 178 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 195 215 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 217 237 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00902}. SQ SEQUENCE 256 AA; 28734 MW; F69971A264928DCC CRC64; MSNVDESQPL ITHLVELRNR LLRCVICVVL VFVALVYFSN DIYHFVAAPL TAVMPKGATM IATNIQTPFF TPIKLTAIVA IFISVPYLLY QIWAFIAPAL YQHEKRMIYP LLFSSTILFY CGVAFAYYIV FPLVFSFFTQ TAPEGVTIAT DISSYLDFAL ALFLAFGVCF EVPIAIILLC WTGITTVKAL SEKRPYIIVA AFFIGMLLTP PDVFSQTLLA IPMCLLFELG LLVARFYQPK DDESAVKNND ESEKTQ // ID TCDA_HAEIN Reviewed; 261 AA. AC Q57097; O05009; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=tRNA threonylcarbamoyladenosine dehydratase; DE EC=6.1.-.-; DE AltName: Full=t(6)A37 dehydratase; GN Name=tcdA; OrderedLocusNames=HI_0118; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the ATP-dependent dehydration of CC threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic CC t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with CC adenine. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF 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; L42023; AAC21793.1; -; Genomic_DNA. DR PIR; C64049; C64049. DR RefSeq; NP_438290.1; NC_000907.1. DR RefSeq; WP_005694410.1; NC_000907.1. DR ProteinModelPortal; Q57097; -. DR STRING; 71421.HI0118; -. DR EnsemblBacteria; AAC21793; AAC21793; HI_0118. DR GeneID; 951021; -. DR KEGG; hin:HI0118; -. DR PATRIC; 20188721; VBIHaeInf48452_0122. DR eggNOG; ENOG4105CUZ; Bacteria. DR eggNOG; COG1179; LUCA. DR OMA; DMDDICV; -. DR OrthoDB; EOG628F8J; -. DR PhylomeDB; Q57097; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro. DR GO; GO:0061503; F:tRNA threonylcarbamoyladenosine dehydratase; IBA:GO_Central. DR GO; GO:0061504; P:cyclic threonylcarbamoyladenosine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR Pfam; PF00899; ThiF; 1. DR SUPFAM; SSF69572; SSF69572; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Membrane; Nucleotide-binding; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 261 tRNA threonylcarbamoyladenosine FT dehydratase. FT /FTId=PRO_0000120580. FT TRANSMEM 230 250 Helical. {ECO:0000255}. SQ SEQUENCE 261 AA; 28572 MW; 6829BCBFFB2C81F0 CRC64; MGITVMARID NYEQRFGGIG RLYTPDSLAR LRQAHICVIG IGGVGSWVVE ALARSGIGEL TLIDMDDICV TNINRQLPAM SGTIGKLKTE VMSERVKLIN PECTVNIIDD FISPENQSDY LNRGYDYVID AIDNVKTKAS LIAYCKRNKI NVITIGGAGG QTDPTQIQIA DLSKTIQDPL LAKVRSVLRK DYNFSQNPKR KFSIDAVFST QPLIFPQMTE GCSTSATMNC ANGFGAATMI TATFGFFAVS RVIDKLLKKK S // ID THIB_HAEIN Reviewed; 332 AA. AC P44984; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Thiamine-binding periplasmic protein; DE Flags: Precursor; GN Name=thiB; Synonyms=tbpA; OrderedLocusNames=HI_1019; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in CC thiamine import. {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ThiQ), two transmembrane proteins (ThiP) and a solute-binding CC protein (ThiB). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 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; L42023; AAC22678.1; -; Genomic_DNA. DR PIR; C64164; C64164. DR RefSeq; NP_439179.1; NC_000907.1. DR RefSeq; WP_005693356.1; NC_000907.1. DR ProteinModelPortal; P44984; -. DR SMR; P44984; 25-331. DR STRING; 71421.HI1019; -. DR EnsemblBacteria; AAC22678; AAC22678; HI_1019. DR GeneID; 949440; -. DR KEGG; hin:HI1019; -. DR PATRIC; 20190701; VBIHaeInf48452_1063. DR eggNOG; ENOG4105DP9; Bacteria. DR eggNOG; COG4143; LUCA. DR KO; K02064; -. DR OMA; HIVTANI; -. DR OrthoDB; EOG6D8BCG; -. DR PhylomeDB; P44984; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0030975; F:thiamine binding; IEA:InterPro. DR GO; GO:0048502; F:thiamine-transporting ATPase activity; IEA:InterPro. DR GO; GO:0015888; P:thiamine transport; IEA:InterPro. DR InterPro; IPR006061; SBP_1_CS. DR InterPro; IPR005948; Thi_ABC_peri-bd. DR InterPro; IPR005967; ThiB_ABC_peri-bd. DR TIGRFAMs; TIGR01254; sfuA; 1. DR TIGRFAMs; TIGR01276; thiB; 1. DR PROSITE; PS01037; SBP_BACTERIAL_1; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 332 Thiamine-binding periplasmic protein. FT /FTId=PRO_0000031706. SQ SEQUENCE 332 AA; 37272 MW; 90A27B35D0F9C741 CRC64; MKLLKLTLIS TALFSTAALA QAQQSVNVYS YDSFTSEWGA GPKVKQDFEK AHPQCAINFT PFESVGVLLN RVRLEGKKTK ADIVLGLDNF FLEQAEKTGI FAPNNVDLTQ LDLPTKWANK TFLPFDFGNY AFVYDKTKLQ NPPKSLKELV ERQDLSVIYQ DPRTSSVGRG LLVWMNAVYP ADKIQSAWKE LDKHTVTVGK GWSDTYGAFL KGEADLVLSY STSPLYHQLF EKKDNYAATD FAEGHITQVE LAARVANHPN QCADDFMAFL ISPTAQKHIV TANIMLPVIQ GEIEPHFDAL KVQQKTQTSI NPMVNTEQLK NWISTWQTTL TK // ID THID_HAEIN Reviewed; 269 AA. AC P44697; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49; DE EC=2.7.4.7; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; GN Name=thiD; OrderedLocusNames=HI_0416; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine = ADP + 4-amino-2-methyl-5- CC (diphosphomethyl)pyrimidine. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 2/3. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole: step 3/3. CC -!- SIMILARITY: Belongs to the ThiD 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; L42023; AAC22074.1; -; Genomic_DNA. DR PIR; I64151; I64151. DR RefSeq; NP_438578.1; NC_000907.1. DR RefSeq; WP_005693748.1; NC_000907.1. DR ProteinModelPortal; P44697; -. DR STRING; 71421.HI0416; -. DR EnsemblBacteria; AAC22074; AAC22074; HI_0416. DR GeneID; 949517; -. DR KEGG; hin:HI0416; -. DR PATRIC; 20189385; VBIHaeInf48452_0436. DR eggNOG; ENOG4105DWF; Bacteria. DR eggNOG; COG0351; LUCA. DR KO; K00941; -. DR OMA; FAFHCVH; -. DR OrthoDB; EOG6XWV53; -. DR PhylomeDB; P44697; -. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00138. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR004399; HMP/HMP-P_kinase. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF08543; Phos_pyr_kin; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1 269 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT /FTId=PRO_0000192019. FT BINDING 45 45 Substrate. {ECO:0000250}. SQ SEQUENCE 269 AA; 28295 MW; 2B72DE9C39D1BEB3 CRC64; MSNVKQVLTI AGSDSGGGAG IQADLKTFQM RGVFGTSAIT AVTAQNTLGV FDIHPIPLKT IQAQLEAVKN DFQIASCKIG MLGNAEIIEC VADFLADKPF GTLVLDPVMI AKGGAPLLQR QAVSALSQKL LPLADVITPN IPEAEALTGI AIVDDISIQQ AAKALQKQGA KNVIIKGGHS LNSQSELCQD WVLLADGRHF TLQSPRFNTP HTHGTGCTFS ACLTAELAKG EPLQSAVKTA KDFITAAISH PLNIGQGHGP TNHWAYSRL // ID TBPB_HAEIN Reviewed; 625 AA. AC P44971; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Probable transferrin-binding protein 2; DE Flags: Precursor; GN Name=tbpB; Synonyms=tbp2; OrderedLocusNames=HI_0995; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts as a transferrin receptor and is required for CC transferrin utilization. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22657.1; -; Genomic_DNA. DR PIR; D64107; D64107. DR RefSeq; NP_439158.1; NC_000907.1. DR RefSeq; WP_005693338.1; NC_000907.1. DR ProteinModelPortal; P44971; -. DR STRING; 71421.HI0995; -. DR TCDB; 1.B.14.2.12; the outer membrane receptor (omr) family. DR EnsemblBacteria; AAC22657; AAC22657; HI_0995. DR GeneID; 950797; -. DR KEGG; hin:HI0995; -. DR PATRIC; 20190651; VBIHaeInf48452_1038. DR OMA; VNQAAMV; -. DR OrthoDB; EOG6XHC16; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR001677; Solute-bd_prot_TBP-like. DR Pfam; PF01298; Lipoprotein_5; 1. DR SUPFAM; SSF56925; SSF56925; 3. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Receptor; Reference proteome; Signal. FT SIGNAL 1 17 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 18 625 Probable transferrin-binding protein 2. FT /FTId=PRO_0000018191. FT LIPID 18 18 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 18 18 S-diacylglycerol cysteine. {ECO:0000305}. SQ SEQUENCE 625 AA; 69031 MW; 52EFBC97B5ED4E9A CRC64; MKSVPLISGG LSLFLSACSG GGGSFDVDDV SNPSSSKPRY QDDTSNQRKK SNLEKLSIPS LGGGMKLVAQ NLRGREPSLL NEDGYIIFSS LSKIEDDFKK ENQSQEPTIG SIDEPSETNS PQNHHGQQYV YSGLYYIQSW RNFSNGKFYS GYYGYAYYFG KQTATTLPVN GEATYKGTWS FITATERGKN YSLFSNSSGQ GYSRRSAISE DIDLENDQNN GETGLISQFS ADFGTKKLKG ELFYTKRKTN NQNYEKKKLY DIDANIYSNR FRGKVKPTEK DSEEHPFTRE GTLEGGFYGP NGEELGGKFL AGDKKVFGVF SAKETEETKQ KTLPKETLID GKLTTFSTKK PDATTSTTAN AKTDATTNAE NFTTKDISSF GEADYLLIDN YPVPLLPETE NSGDFATSKH YEVRDKTYKV EACCKNLSYV KFGMYYEDNK KNNKNETEQY HQFLLGLRTA SSKIPTTGNV KYRGSWFGYI SDGETSYSTT GDKRQDKNAV AEFDVNFAEK TLKGSLKRAD SQNPVFSIEA NFKNGGNAFT GTATAKDLVI DGKNSQTKNT PINITTKVNG AFYGPNASEL GGYFTYNGKN PTDKNSPTAS SPSNSEKARA AVVFGAKKQV ETNNK // ID TDHA_HAEIN Reviewed; 744 AA. AC P44523; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=TonB-dependent heme receptor A; DE Flags: Precursor; GN Name=tdhA; OrderedLocusNames=HI_0113; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Heme receptor. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor 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; L42023; AAC21789.1; -; Genomic_DNA. DR PIR; B64049; B64049. DR RefSeq; NP_438287.1; NC_000907.1. DR RefSeq; WP_010868937.1; NC_000907.1. DR ProteinModelPortal; P44523; -. DR STRING; 71421.HI0113; -. DR EnsemblBacteria; AAC21789; AAC21789; HI_0113. DR GeneID; 951015; -. DR KEGG; hin:HI0113; -. DR PATRIC; 20188695; VBIHaeInf48452_0117. DR eggNOG; ENOG4105X58; Bacteria. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; KLVYRDQ; -. DR OrthoDB; EOG6C5RJM; -. DR PhylomeDB; P44523; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR011276; TonB_haem/Hb_rcpt. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_rcpt. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR TIGRFAMs; TIGR01785; TonB-hemin; 1. DR TIGRFAMs; TIGR01786; TonB-hemlactrns; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 744 TonB-dependent heme receptor A. FT /FTId=PRO_0000034762. SQ SEQUENCE 744 AA; 85044 MW; 74D94F72E41AEC31 CRC64; MNILINKRIF LLVTLVGIQL NVTAKQNSSN SNREELLPII VNTNDDSNKL PGRSVLKQKN IEQXQADNAA NLINILPGVN MAGGFRPGGQ TLNINGMGDA EDVRVQLDGA TKSFEKYQQG SIFIEPELLR RVTVDKGNYS PQYGNGGFAG TVKFETKDAR DFLQENQKIG GFLKYGNNSN NNQKTYSTAL VLQNEQKNID LLLFGSVRNA GDYKRPDNSK ILFSKNNQKT GLIKLNWQIS PEHLLTLSSV YGIHKGWEPF AAKRDILPKP SLSDIMRYGT DIAWKRKLVY RDQKDENYTL KYNYLPENNP WINLSTQFSY SKTTQNDMRP KEASSGLVGS LGNQSWITYS DLTFDINNTS TFNIKTTVHE LLFGLQWLKN TRNTLMYDKS KVRKADYNYG YFQPYYMPSG RQYTQAFYLQ DQIKWKNIIF STGVRYDHIN NIGQKNLALK YNDISAGHDY SQKNYNGWSY YLGLNYDVNH YLSLFTNFSK TWRAPVIDEQ YETQFKQSSV PATSLNLEKE MINQTRVGGI ITLNHLFQEN DAFQFRTTYF YNRGKNEIFK TRGVNCVGNA ADTNNKVCPK IIENYRNLPG YVIQGAELEA YYQSTYLFGE ITYSYVKGKR DTSPRNPWGK TSTWIAEIPP RKATTALGFN VPKYYLTVGW RAEFVRRQDR SPLSGDPKAS SWSLPASRGY SLHNLFLSWS PAKIKGMNVK ITVDNLFNRA YNPYLGELAS GTGRNIKFSL SQKF // ID THIX_HAEIN Reviewed; 167 AA. AC P43787; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Thioredoxin-like protein HI_1115; GN OrderedLocusNames=HI_1115; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22769.1; -; Genomic_DNA. DR PIR; G64183; G64183. DR RefSeq; NP_439272.1; NC_000907.1. DR RefSeq; WP_005693438.1; NC_000907.1. DR ProteinModelPortal; P43787; -. DR STRING; 71421.HI1115; -. DR EnsemblBacteria; AAC22769; AAC22769; HI_1115. DR GeneID; 950780; -. DR KEGG; hin:HI1115; -. DR PATRIC; 20190903; VBIHaeInf48452_1164. DR eggNOG; ENOG4105N2G; Bacteria. DR eggNOG; COG0526; LUCA. DR OMA; WLTRKKM; -. DR OrthoDB; EOG6QG8RK; -. DR PhylomeDB; P43787; -. DR Proteomes; UP000000579; 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:0016209; F:antioxidant activity; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR Pfam; PF00578; AhpC-TSA; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Disulfide bond; Membrane; KW Redox-active center; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 167 Thioredoxin-like protein HI_1115. FT /FTId=PRO_0000120180. FT TRANSMEM 10 27 Helical. {ECO:0000255}. FT DOMAIN 30 167 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 69 72 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 167 AA; 19034 MW; 1AF6FAF9AE5FD23E CRC64; MKIKKLLKNG LSLFLTFIVI TSILDFVRRP VVPEEINKIT LQDLQGNTFS LESLDQNKPT LLYFWGTWCG YCRYTSPAIN SLAKEGYQVV SVALRSGNEA DVNDYLSKND YHFTTVNDPK GEFAERWQIN VTPTIVLLSK GKMDLVTTGL TSYWGLKVRL FFAEFFG // ID TFOX_HAEIN Reviewed; 217 AA. AC P43779; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=DNA transformation protein TfoX; DE AltName: Full=Competence activator Sxy {ECO:0000303|PubMed:23663205}; DE AltName: Full=Protein Sxy; GN Name=tfoX; Synonyms=sxy; OrderedLocusNames=HI_0601; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7724607; DOI=10.1073/pnas.92.8.3616; RA Zulty J.J., Barcak G.J.; RT "Identification of a DNA transformation gene required for com101A+ RT expression and supertransformer phenotype in Haemophilus influenzae."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3616-3620(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd RC {ECO:0000303|PubMed:1653215}; RX PubMed=1653215; RA Redfield R.J.; RT "sxy-1, a Haemophilus influenzae mutation causing greatly enhanced RT spontaneous competence."; RL J. Bacteriol. 173:5612-5618(1991). RN [4] RP IDENTIFICATION OF TFOX AS SXY, AND VARIANT SXY-1. RX PubMed=7961436; RA Williams P.M., Bannister L.A., Redfield R.J.; RT "The Haemophilus influenzae sxy-1 mutation is in a newly identified RT gene essential for competence."; RL J. Bacteriol. 176:6789-6794(1994). RN [5] RP FUNCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd RC {ECO:0000303|PubMed:9244270}; RX PubMed=9244270; RA Karudapuram S., Barcak G.J.; RT "The Haemophilus influenzae dprABC genes constitute a competence- RT inducible operon that requires the product of the tfoX (sxy) gene for RT transcriptional activation."; RL J. Bacteriol. 179:4815-4820(1997). RN [6] RP INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15769466; DOI=10.1016/j.jmb.2005.01.012; RA Redfield R.J., Cameron A.D., Qian Q., Hinds J., Ali T.R., Kroll J.S., RA Langford P.R.; RT "A novel CRP-dependent regulon controls expression of competence genes RT in Haemophilus influenzae."; RL J. Mol. Biol. 347:735-747(2005). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=18761017; DOI=10.1016/j.jmb.2008.08.027; RA Cameron A.D., Redfield R.J.; RT "CRP binding and transcription activation at CRP-S sites."; RL J. Mol. Biol. 383:313-323(2008). RN [8] RP INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd RC {ECO:0000303|PubMed:17981840}; RX PubMed=17981840; DOI=10.1093/nar/gkm915; RA Cameron A.D., Volar M., Bannister L.A., Redfield R.J.; RT "RNA secondary structure regulates the translation of sxy and RT competence development in Haemophilus influenzae."; RL Nucleic Acids Res. 36:10-20(2008). RN [9] RP INDUCTION. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd RC {ECO:0000303|PubMed:23663205}; RX PubMed=23663205; DOI=10.1111/mmi.12245; RA Sinha S., Mell J., Redfield R.; RT "The availability of purine nucleotides regulates natural competence RT by controlling translation of the competence activator Sxy."; RL Mol. Microbiol. 88:1106-1119(2013). CC -!- FUNCTION: Required for DNA transformation (PubMed:1653215, CC PubMed:18761017). Positively regulates genes required for DNA CC transformation (late competence-specific genes) in association CC with CRP (PubMed:18761017). Required for expression of the dprABC CC operon (PubMed:9244270). {ECO:0000269|PubMed:1653215, CC ECO:0000269|PubMed:18761017, ECO:0000269|PubMed:9244270}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P43779-1; Sequence=Displayed; CC Name=Short; CC IsoId=P43779-2; Sequence=VSP_018799; CC -!- INDUCTION: Induced about 50-fold on moving from rich to starvation CC medium. By CRP and cAMP in starvation medium. Translation CC increased by depletion of extra- or intra-cellular purine CC nucleotides in starvation medium. High levels of purine CC nucleotides by contrast decrease its translation under the same CC condition. {ECO:0000269|PubMed:15769466, CC ECO:0000269|PubMed:17981840, ECO:0000269|PubMed:23663205}. CC -!- DISRUPTION PHENOTYPE: Loss of expression of the competence CC regulatory element (CRE) regulon required for development of CC competence. {ECO:0000269|PubMed:15769466, CC ECO:0000269|PubMed:18761017}. CC -!- SIMILARITY: Belongs to the TfoX 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; U13205; AAC43320.1; -; Genomic_DNA. DR EMBL; U13205; AAC43321.1; -; Genomic_DNA. DR EMBL; L42023; AAC22258.1; -; Genomic_DNA. DR PIR; B64080; B64080. DR RefSeq; NP_438758.1; NC_000907.1. [P43779-1] DR RefSeq; WP_010869017.1; NC_000907.1. DR ProteinModelPortal; P43779; -. DR STRING; 71421.HI0601; -. DR EnsemblBacteria; AAC22258; AAC22258; HI_0601. DR GeneID; 949645; -. DR KEGG; hin:HI0601; -. DR PATRIC; 20189759; VBIHaeInf48452_0622. DR eggNOG; COG3070; LUCA. DR KO; K07343; -. DR OMA; PNLSIKH; -. DR OrthoDB; EOG6716M8; -. DR PhylomeDB; P43779; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB. DR GO; GO:0071320; P:cellular response to cAMP; IMP:UniProtKB. DR GO; GO:0071415; P:cellular response to purine-containing compound; IEP:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB. DR GO; GO:0009290; P:DNA import into cell involved in transformation; IMP:UniProtKB. DR GO; GO:0030420; P:establishment of competence for transformation; IMP:UniProtKB. DR GO; GO:0045809; P:positive regulation of establishment of competence for transformation; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.1460.30; -; 1. DR InterPro; IPR007077; TfoX_C. DR InterPro; IPR007076; TfoX_N. DR InterPro; IPR026256; TfoX_Sxy. DR Pfam; PF04994; TfoX_C; 1. DR Pfam; PF04993; TfoX_N; 1. DR PIRSF; PIRSF028788; TfoX_Sxy; 1. PE 2: Evidence at transcript level; KW Activator; Alternative initiation; Competence; Complete proteome; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 217 DNA transformation protein TfoX. FT /FTId=PRO_0000022483. FT VAR_SEQ 1 39 Missing (in isoform Short). FT {ECO:0000305}. FT /FTId=VSP_018799. FT VARIANT 19 19 V -> I (in sxy-Long; causes a 100-fold to FT 1000-fold increase in spontaneous natural FT competence). FT CONFLICT 203 203 W -> L (in Ref. 1; AAC43320/AAC43321). FT {ECO:0000305}. SQ SEQUENCE 217 AA; 25074 MW; 4A6E30E64008CC3F CRC64; MNIKDEHIDS VCSLLDQLVG NVSFKNLFTG YGLFHKEETM FAIWQNKKLY LRGEGVLAIQ LTKLGCEPFT TNELNKRFVL SQYYALSDQI LRSNRLCRKL IILSIKQILE QKLECTLRKL NRLKDLPNLT IKHERALIKV GITNVAMLRE IGAENALVEL KKSGSGATLD FYWKLVCALQ NKNSQMLSQA EKERLLKKLN EVWRKNGLKG YRKLDDE // ID TGT_HAEIN Reviewed; 382 AA. AC P44594; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Queuine tRNA-ribosyltransferase; DE EC=2.4.2.29; DE AltName: Full=Guanine insertion enzyme; DE AltName: Full=tRNA-guanine transglycosylase; GN Name=tgt; OrderedLocusNames=HI_0244; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7- CC deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His CC and -Tyr). After this exchange, a cyclopentendiol moiety is CC attached to the 7-aminomethyl group of 7-deazaguanine, resulting CC in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + queuine = queuosine(34) CC in tRNA + guanine. CC -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7- CC carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21911.1; -; Genomic_DNA. DR PIR; A64057; A64057. DR RefSeq; NP_438414.1; NC_000907.1. DR RefSeq; WP_005645731.1; NC_000907.1. DR ProteinModelPortal; P44594; -. DR SMR; P44594; 1-368. DR STRING; 71421.HI0244; -. DR EnsemblBacteria; AAC21911; AAC21911; HI_0244. DR GeneID; 949369; -. DR KEGG; hin:HI0244; -. DR PATRIC; 20189013; VBIHaeInf48452_0259. DR eggNOG; ENOG4105C6U; Bacteria. DR eggNOG; COG0343; LUCA. DR KO; K00773; -. DR OMA; MGVGKPD; -. DR OrthoDB; EOG6SNDVG; -. DR PhylomeDB; P44594; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Metal-binding; KW Queuosine biosynthesis; Reference proteome; Transferase; KW tRNA processing; Zinc. FT CHAIN 1 382 Queuine tRNA-ribosyltransferase. FT /FTId=PRO_0000135481. FT ACT_SITE 93 93 Nucleophile. {ECO:0000250}. FT METAL 306 306 Zinc. {ECO:0000250}. FT METAL 308 308 Zinc. {ECO:0000250}. FT METAL 311 311 Zinc. {ECO:0000250}. FT METAL 337 337 Zinc. {ECO:0000250}. FT BINDING 94 94 Substrate. {ECO:0000250}. SQ SEQUENCE 382 AA; 43627 MW; ABD1DE67822EF583 CRC64; MKYELDKTSG NARRGRLVFE RPQGTFSVET PAFMPVGTYG TVKGMTPEEV RATGAEILLG NTFHLWLRPG QEVMRKHGDL HDFMQWHRPI LTDSGGFQVF SLGKLRKITE EGVKFQNPIN GERIFLSPEK SMEIQYDLGS DIVMIFDECT PYPATFDYAK KSMEMSLRWA KRSRDRFDEL GNKNALFGII QGGVFEELRK VSLEGLVNIG FDGYAVGGLA VGEPKEDMHR ILEYICPQIP ADKPRYLMGV GKPEDLVEGV RRGIDMFDCV MPTRNARNGH LFVTDGIVKI RNAKYRDDTS PLDPECDCYT CKNYTKAYLY HLDKCGEILG ARLNTIHNLR YYQRLMAEIR QAIEDDRFDD FVVEFYARMG KPVPPLQLAD KS // ID THIO_HAEIN Reviewed; 107 AA. AC P43785; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Thioredoxin; DE Short=Trx; GN Name=trxA; Synonyms=trxM; OrderedLocusNames=HI_0084; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21757.1; -; Genomic_DNA. DR PIR; E64047; E64047. DR RefSeq; NP_438257.1; NC_000907.1. DR RefSeq; WP_005693835.1; NC_000907.1. DR ProteinModelPortal; P43785; -. DR SMR; P43785; 23-107. DR STRING; 71421.HI0084; -. DR EnsemblBacteria; AAC21757; AAC21757; HI_0084. DR GeneID; 950983; -. DR KEGG; hin:HI0084; -. DR PATRIC; 20188623; VBIHaeInf48452_0085. DR eggNOG; ENOG4105K63; Bacteria. DR eggNOG; COG0526; LUCA. DR KO; K03671; -. DR OMA; MSEHIHY; -. DR OrthoDB; EOG6QG8RK; -. DR PhylomeDB; P43785; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. 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 1 107 Thioredoxin. FT /FTId=PRO_0000120107. FT DOMAIN 2 107 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT DISULFID 32 35 Redox-active. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. SQ SEQUENCE 107 AA; 11681 MW; 1725C8A244685477 CRC64; MSEVLHINDA DFESVVVNSD IPILLDFWAP WCGPCKMIAP VLDELAPEFA GKVKIVKMNV DDNQATPAQF GVRSIPTLLL IKNGQVVATQ VGALPKTQLA NFINQHI // ID TESB_HAEIN Reviewed; 286 AA. AC P44498; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Acyl-CoA thioesterase 2; DE EC=3.1.2.-; DE AltName: Full=Acyl-CoA thioesterase II; DE Short=TEII; GN Name=tesB; OrderedLocusNames=HI_0076; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Can hydrolyze a broad range of acyl-CoA thioesters. Its CC physiological function is not known (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the C/M/P thioester 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; L42023; AAC21752.1; -; Genomic_DNA. DR PIR; B64047; B64047. DR RefSeq; NP_438249.1; NC_000907.1. DR RefSeq; WP_005693846.1; NC_000907.1. DR ProteinModelPortal; P44498; -. DR SMR; P44498; 2-285. DR STRING; 71421.HI0076; -. DR EnsemblBacteria; AAC21752; AAC21752; HI_0076. DR GeneID; 950974; -. DR KEGG; hin:HI0076; -. DR PATRIC; 20188607; VBIHaeInf48452_0077. DR eggNOG; ENOG4105C29; Bacteria. DR eggNOG; COG1946; LUCA. DR KO; K10805; -. DR OMA; IYDVEIL; -. DR OrthoDB; EOG683SB1; -. DR PhylomeDB; P44498; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IEA:InterPro. DR GO; GO:0006637; P:acyl-CoA metabolic process; IEA:InterPro. DR Gene3D; 3.10.129.10; -; 2. DR InterPro; IPR003703; Acyl_CoA_thio. DR InterPro; IPR025652; Acyl_CoA_thio_II_dom. DR InterPro; IPR029069; HotDog_dom. DR PANTHER; PTHR11066; PTHR11066; 1. DR Pfam; PF02551; Acyl_CoA_thio; 2. DR SUPFAM; SSF54637; SSF54637; 2. DR TIGRFAMs; TIGR00189; tesB; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 286 Acyl-CoA thioesterase 2. FT /FTId=PRO_0000202146. FT ACT_SITE 58 58 {ECO:0000250}. FT ACT_SITE 204 204 {ECO:0000250}. SQ SEQUENCE 286 AA; 32406 MW; 529390BF7189CDD7 CRC64; MSDILNNLIH LLKLEKIDDL IFRGESQDLG FRQVFGGQVV AQALSAAMQV APEDRILHSC HAYFLAPGDS QYPIIYDVET LREGRNFSAL CVKAIQHKNT ICHVTASFQV PEKGFEHQNT MPNVGAPEDF TDENVMLQKV AQTLPEPLNE KFAAERPFEV RTKYLNNPFN GTKLPAEQYS WFKTNGETPL DIKIQQCLLA YFSDFHCILT ALHPHEKGFL QKGMKVATID HSIWFHRPFD LNHWHLHAIE SNNAFGGRGL AQGQIFSQDG QLIATTQQEG LIRFSE // ID THIM_HAEIN Reviewed; 265 AA. AC Q57233; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228}; DE EC=2.7.1.50 {ECO:0000255|HAMAP-Rule:MF_00228}; DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=TH kinase {ECO:0000255|HAMAP-Rule:MF_00228}; DE Short=Thz kinase {ECO:0000255|HAMAP-Rule:MF_00228}; GN Name=thiM {ECO:0000255|HAMAP-Rule:MF_00228}; GN OrderedLocusNames=HI_0415; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of CC 4-methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP- CC Rule:MF_00228}. CC -!- CATALYTIC ACTIVITY: ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = CC ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole. CC {ECO:0000255|HAMAP-Rule:MF_00228}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00228}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4- CC methylthiazole: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00228}. CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00228}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22073.1; -; Genomic_DNA. DR PIR; H64151; H64151. DR RefSeq; NP_438577.1; NC_000907.1. DR RefSeq; WP_005693750.1; NC_000907.1. DR ProteinModelPortal; Q57233; -. DR STRING; 71421.HI0415; -. DR EnsemblBacteria; AAC22073; AAC22073; HI_0415. DR GeneID; 949516; -. DR KEGG; hin:HI0415; -. DR PATRIC; 20189383; VBIHaeInf48452_0435. DR eggNOG; ENOG4105C4U; Bacteria. DR eggNOG; COG2145; LUCA. DR KO; K00878; -. DR OMA; SPVMAHA; -. DR OrthoDB; EOG628F8M; -. DR PhylomeDB; Q57233; -. DR UniPathway; UPA00060; UER00139. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_00228; Thz_kinase; 1. DR InterPro; IPR000417; Hyethyz_kinase. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF02110; HK; 1. DR PIRSF; PIRSF000513; Thz_kinase; 1. DR PRINTS; PR01099; HYETHTZKNASE. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR00694; thiM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 265 Hydroxyethylthiazole kinase. FT /FTId=PRO_0000156936. FT BINDING 43 43 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 119 119 ATP. {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 165 165 ATP. {ECO:0000255|HAMAP-Rule:MF_00228}. FT BINDING 192 192 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00228}. SQ SEQUENCE 265 AA; 27733 MW; C43B7ABED91A8BD6 CRC64; MLMQSIYLSK IREQNPLIHN ITNIVAANFS ANGLLALGAS PLMSANVEEM QEVPKISQAL VINIGTLIGK DREAMLQAGK TANEVGIPVV LDPVGVGATS YRRETIRELL AEVKFALIRG NAGELAAIAG ETWQAKGVDA GQGEVDLKAV AEKVAQRYGC TVLISGAVDI VSDGTQTATV HNGTSLFPKV TASGCLLSAV CAAFLAVSEG NYFSATLEAC VAYTIAGECA AQGLTTQVGQ FQIRLLDELA ALSPETIGQR GRINE // ID TIG_HAEIN Reviewed; 432 AA. AC P44837; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Trigger factor; DE Short=TF; DE EC=5.2.1.8; DE AltName: Full=PPIase; GN Name=tig; OrderedLocusNames=HI_0713; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22370.1; -; Genomic_DNA. DR PIR; C64088; C64088. DR RefSeq; NP_438871.1; NC_000907.1. DR RefSeq; WP_010869039.1; NC_000907.1. DR ProteinModelPortal; P44837; -. DR SMR; P44837; 1-432. DR STRING; 71421.HI0713; -. DR EnsemblBacteria; AAC22370; AAC22370; HI_0713. DR GeneID; 949736; -. DR KEGG; hin:HI0713; -. DR PATRIC; 20190049; VBIHaeInf48452_0745. DR eggNOG; ENOG4105DEA; Bacteria. DR eggNOG; COG0544; LUCA. DR KO; K03545; -. DR OMA; FRNDATK; -. DR OrthoDB; EOG63VBX3; -. DR PhylomeDB; P44837; -. DR Proteomes; UP000000579; 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 3: Inferred from homology; KW Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm; KW Isomerase; Reference proteome; Rotamase. FT CHAIN 1 432 Trigger factor. FT /FTId=PRO_0000179361. FT DOMAIN 161 246 PPIase FKBP-type. SQ SEQUENCE 432 AA; 48332 MW; C6DB71F502973096 CRC64; MSLNIETTQG LERRVAITVP TEIVSKAVRE EFKRAAKNVR VDGFRKGHVP AHIIEQRFGA SIRQDVLNDL LPRHFFNAVI AEKINIAGRP TFAIETFEEG KDLVFTATFE VYPEVKLQGL ENIKVEKPTV EITEADIDKM IDVLRKQQAT WAESQDVVKA DDRVTIDFVG SVDGEEFEGG KATDFVLFMG QGRMIPGFEE GIVGHKAGEQ FDIDVTFPAE YHAENLKGKA AKFAITLKKI ENMVLPELTD EFVAKFGPNT KSVADLRAEI RKNMERELKN ALVSRVKQQV INGLIEQNPI DVPVSAVEEE INVLRNQAAQ RFGGNAQQTA QLPRELFEAE ATRRVQVGLL FSEVIKSNEL KADEERAKAM IADIASAYEQ PAEVVEYYSK NEELMNNIRN VVLEEQAVDA VLAKAQVTEK VSSFDEIMNP QA // ID THIP_HAEIN Reviewed; 538 AA. AC P44985; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Thiamine transport system permease protein ThiP; GN Name=thiP; OrderedLocusNames=HI_1020; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in CC thiamine import. Probably responsible for the translocation of the CC substrate across the membrane (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ThiQ), two transmembrane proteins (ThiP) and a solute-binding CC protein (ThiB). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass 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; L42023; AAC22679.1; -; Genomic_DNA. DR PIR; D64164; D64164. DR RefSeq; NP_439180.1; NC_000907.1. DR RefSeq; WP_005693357.1; NC_000907.1. DR ProteinModelPortal; P44985; -. DR STRING; 71421.HI1020; -. DR EnsemblBacteria; AAC22679; AAC22679; HI_1020. DR GeneID; 950718; -. DR KEGG; hin:HI1020; -. DR PATRIC; 20190703; VBIHaeInf48452_1064. DR eggNOG; ENOG4106SMU; Bacteria. DR eggNOG; COG1178; LUCA. DR KO; K02063; -. DR OMA; WHDSYLW; -. DR OrthoDB; EOG6JDW8K; -. DR PhylomeDB; P44985; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0015888; P:thiamine transport; IEA:InterPro. DR Gene3D; 1.10.3720.10; -; 2. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005947; ThiP_ABC_transpt. DR Pfam; PF00528; BPD_transp_1; 2. DR SUPFAM; SSF161098; SSF161098; 2. DR TIGRFAMs; TIGR01253; thiP; 1. DR PROSITE; PS50928; ABC_TM1; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 538 Thiamine transport system permease FT protein ThiP. FT /FTId=PRO_0000060231. FT TRANSMEM 19 39 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 57 77 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 97 117 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 141 161 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 202 222 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 242 262 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 293 313 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 337 357 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 376 396 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 406 426 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 466 486 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 509 529 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 58 263 ABC transmembrane type-1 1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 333 528 ABC transmembrane type-1 2. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 538 AA; 60851 MW; D7B31D2A15BCD6E1 CRC64; MFSLFHHPQL RPRHYAGGVV VISFIILFYG GALSSIFALG GELQWRAWFT DDYLQHLILF SFGQALLSTV LSIFFGLLLA RALFYKPFLG KKWLLKLMSL TFVLPALVVI FGLIGIYGSS GWLAWLANLF GMSWQGHIYG LSGILIAHLF FNIPLAAQLF LQSLQSIPYQ QRQLAAQLNL QGWQFVKLVE WPVFRQQCLP TFSLIFMLCF TSFTVVLTLG GGPQYTTLET AIYQAILFEF DLPKAALFAM LQFVFCLILF SLTSRFSLSN QNGLSNSNIW FEKPKSAVKI FHILVLLVFV FFLFSPVLNI LISALSSSNL LTVWHNSQLW RALGYSLSIA PLSALLALTM AIALLLLSRR LEWLHYQKIS QFIINAGMVI LAIPILVLAM GLFLLLQDRD FSNIDLFIIV VFCNALSAMP FVLRILSAPF HNNMRYYENL CNSLGIVGWQ RFYLIEWKTL RAPLRYAFAL GLALSLGDFT AIALFGNQEF TSLPHLLYQQ LGNYRNQDAA VTAGILLLLC GILFAFIHTY RDADDLSK // ID TLDD_HAEIN Reviewed; 482 AA. AC P45297; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Metalloprotease TldD homolog; DE EC=3.4.-.-; GN Name=tldD; OrderedLocusNames=HI_1653; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable metalloprotease. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=345; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; I64173; I64173. DR STRING; 71421.HI1653; -. DR eggNOG; ENOG4105D1U; Bacteria. DR eggNOG; COG0312; LUCA. DR OMA; MVGNDLS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR025502; TldD. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. DR PIRSF; PIRSF004919; TldD; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metalloprotease; Protease; KW Reference proteome. FT CHAIN 1 482 Metalloprotease TldD homolog. FT /FTId=PRO_0000142359. SQ SEQUENCE 482 AA; 51715 MW; 047DF8680511F680 CRC64; MLNQVSNTLL TPSNLSTQTL LNIFDIMSHR NIDYADLYFQ LSQDESWVLE DGIIKEGSFH IDRGVGVRAV SGEKTGFAYA DQINLASLQQ CAEAVKGIAQ VKQGNLISPS AFNVVNPIAR YAAINPLESL TKEKKIELLH LVDRTARAED HRVTKVSASL SSVYEEVLIM ATDGTLAADI RPLVRLSISV LVEENGKRER GSCGSGGRFG LDWFFEVVDG DIRAVLFAKE AVRQALVNLS AVAAPAGLMP VVLGAGWPGV LLHEAVGHGL EGDFNRKESS LFTGKIGEQV TSPLCTIVDD GTIENRRGSL TIDDEGVPSQ CNVLIKDGIL QGYMQDKMNA RLMGVSTTGN GRRESYAHLP MPRMTNTYML AGQSQFDDLI ASVKQGIYAP HFGGGQVDIT SGKFVFSTSE AYLIEKGKIT KPVKGATLIG SGIEVMQKIS MVADKSELDL GIGVCGKEGQ SVPVGVGQPA LKIDEITVGG TN // ID TOLQ_HAEIN Reviewed; 228 AA. AC P43768; P94809; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Protein TolQ; GN Name=tolQ; OrderedLocusNames=HI_0385; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-228. RC STRAIN=1479; RX PubMed=8921895; DOI=10.1016/0378-1119(96)00338-1; RA Sen K., Sikkema D.J., Murphy T.F.; RT "Isolation and characterization of the Haemophilus influenzae tolQ, RT tolR, tolA and tolB genes."; RL Gene 178:75-81(1996). CC -!- FUNCTION: Involved in the TonB-independent uptake of proteins. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ExbB/TolQ 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; L42023; AAC22043.1; -; Genomic_DNA. DR EMBL; U32470; AAC44594.1; -; Genomic_DNA. DR PIR; I64064; I64064. DR RefSeq; NP_438546.1; NC_000907.1. DR RefSeq; WP_005649191.1; NC_000907.1. DR STRING; 71421.HI0385; -. DR EnsemblBacteria; AAC22043; AAC22043; HI_0385. DR GeneID; 950751; -. DR KEGG; hin:HI0385; -. DR PATRIC; 20189319; VBIHaeInf48452_0403. DR eggNOG; ENOG4105E02; Bacteria. DR eggNOG; COG0811; LUCA. DR KO; K03562; -. DR OMA; LESHLPF; -. DR OrthoDB; EOG67MF2K; -. DR PhylomeDB; P43768; -. DR BioCyc; RETL1328306-WGS:GSTH-3529-MONOMER; -. DR Proteomes; UP000000579; 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:0008565; F:protein transporter activity; IEA:InterPro. DR InterPro; IPR002898; MotA_ExbB_proton_chnl. DR InterPro; IPR014163; Tol-Pal_TolQ. DR Pfam; PF01618; MotA_ExbB; 1. DR TIGRFAMs; TIGR02796; tolQ; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 228 Protein TolQ. FT /FTId=PRO_0000145824. FT TRANSMEM 14 37 Helical. {ECO:0000255}. FT TRANSMEM 128 150 Helical. {ECO:0000255}. FT TRANSMEM 175 193 Helical. {ECO:0000255}. FT VARIANT 51 51 R -> H (in strain: 1479). FT VARIANT 110 110 M -> T (in strain: 1479). FT VARIANT 177 177 I -> V (in strain: 1479). FT VARIANT 208 208 G -> V (in strain: 1479). SQ SEQUENCE 228 AA; 25287 MW; 14AE319D2CB2A86B CRC64; MTAELNFLDL FLKASIVVQL VIVILISFSI ISWAIIIQRS RILTNALKEA RTFEDRFWSG EDLNKLYEGL SNRRDGLTGS EQIFCVGFKE FSRLKQVNPD APEAIIKGTM RAMNLAMNRE IESLENRVPF LATVASVSPY IGLFGTVWGI MHAFMALSGA KQATLQMVAP GIAEALIATA IGLFAAIPAV MAYNRLSLRV NAIEQDYGNF IDEFTTILHR QAFGKAPH // ID THIQ_HAEIN Reviewed; 215 AA. AC P44986; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 09-DEC-2015, entry version 115. DE RecName: Full=Thiamine import ATP-binding protein ThiQ {ECO:0000255|HAMAP-Rule:MF_01723}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01723}; GN Name=thiQ {ECO:0000255|HAMAP-Rule:MF_01723}; GN OrderedLocusNames=HI_1021; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in CC thiamine import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01723}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ThiQ), two transmembrane proteins (ThiP) and a solute-binding CC protein (ThiB). {ECO:0000255|HAMAP-Rule:MF_01723}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01723}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01723}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Thiamine CC importer (TC 3.A.1.19.1) family. {ECO:0000255|HAMAP- CC Rule:MF_01723}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01723}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22680.1; -; Genomic_DNA. DR PIR; E64164; E64164. DR RefSeq; NP_439181.1; NC_000907.1. DR RefSeq; WP_005647864.1; NC_000907.1. DR ProteinModelPortal; P44986; -. DR STRING; 71421.HI1021; -. DR EnsemblBacteria; AAC22680; AAC22680; HI_1021. DR GeneID; 950003; -. DR KEGG; hin:HI1021; -. DR PATRIC; 20190705; VBIHaeInf48452_1065. DR eggNOG; ENOG4107T0D; Bacteria. DR eggNOG; COG3840; LUCA. DR KO; K02062; -. DR OMA; KIEQAAC; -. DR OrthoDB; EOG6SNDS1; -. DR PhylomeDB; P44986; -. DR Proteomes; UP000000579; 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:0048502; F:thiamine-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015888; P:thiamine 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; IPR027417; P-loop_NTPase. DR InterPro; IPR005968; Thiamine_ABC_ThiQ. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01277; thiQ; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51288; THIQ; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 215 Thiamine import ATP-binding protein ThiQ. FT /FTId=PRO_0000093023. FT DOMAIN 2 215 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01723}. FT NP_BIND 32 39 ATP. {ECO:0000255|HAMAP-Rule:MF_01723}. SQ SEQUENCE 215 AA; 23727 MW; D05054D963434ACC CRC64; MIYLNNVILN DKTLPMCFNL SVNAGERVAI IGESGAGKST LLNLIAGFEF PAQGEIWLND KNHTRSAPYE RPVSMLFQEN NLFPHLTVQQ NLALGIKPSL KLTALEQEKI EQVACSVGLG DYLERLPNSL SGGQKQRVAL ARCLLRDKPI LLLDEPFSAL DQKLRVEMLA LIAKLCDEKD LTLLLVTHQP SELIGSIDQV LVVENGQISQ LQKGV // ID THRC_HAEIN Reviewed; 425 AA. AC P44503; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=Threonine synthase; DE Short=TS; DE EC=4.2.3.1; GN Name=thrC; OrderedLocusNames=HI_0087; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L- CC phosphohomoserine and the beta-addition of water to produce L- CC threonine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-homoserine + H(2)O = L-threonine + CC phosphate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 5/5. CC -!- SIMILARITY: Belongs to the threonine synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21765.1; -; Genomic_DNA. DR PIR; H64047; H64047. DR RefSeq; NP_438260.1; NC_000907.1. DR RefSeq; WP_005693831.1; NC_000907.1. DR ProteinModelPortal; P44503; -. DR SMR; P44503; 1-423. DR STRING; 71421.HI0087; -. DR PRIDE; P44503; -. DR EnsemblBacteria; AAC21765; AAC21765; HI_0087. DR GeneID; 950990; -. DR KEGG; hin:HI0087; -. DR PATRIC; 20188637; VBIHaeInf48452_0088. DR eggNOG; ENOG4105D98; Bacteria. DR eggNOG; COG0498; LUCA. DR KO; K01733; -. DR OMA; HGAIAYQ; -. DR OrthoDB; EOG65BDJX; -. DR PhylomeDB; P44503; -. DR UniPathway; UPA00050; UER00065. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central. DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.90.1380.10; -; 1. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR029144; Thr_synth_N. DR InterPro; IPR004450; Thr_synthase-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR Pfam; PF14821; Thr_synth_N; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00260; thrC; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Lyase; KW Pyridoxal phosphate; Reference proteome; Threonine biosynthesis. FT CHAIN 1 425 Threonine synthase. FT /FTId=PRO_0000185632. FT MOD_RES 105 105 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 425 AA; 46682 MW; 2CC222DD201F09E0 CRC64; MNLYNIKHPE EQVTFSQAVR QGLGRDQGLF FPEVIPQLNN INELLELPLV ERSQKILGAL IDGELPQATL DAMVKNAFTF PAPLEKVEEN IYALELFHGP TLAFKDFGGR FMAQALAAVR GDGKITILTA TSGDTGAAVA HAFYGLENIN VVILYPKGKI SPLQEKLFCT LGGNIRTVAI NADFDACQAL VKQAFDDVEL RQAIGLNSAN SINISRLLAQ VCYYFEAVAQ LPKEKRDNVV VSVPSGNFGN LTAGLIAKTL GLPIKRFVAS TNANDTVPRY LKSGNWDPKT TVATLSNAMD VSRPNNWPRV EELFKRNGWD LTDLGSGMLS DSETEDTLKA MQSKGYLCEP HGAIAYQVLK DQLKASETGI FLCTAHPAKF KESVERILGI QLPLPETLDK HNQLPLLSDE MDNDFAQLRA YLLKS // ID TOP1_HAEIN Reviewed; 868 AA. AC P43012; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 126. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; GN OrderedLocusNames=HI_1365; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6; RA Chandler M.S., Smith R.A.; RT "Characterization of the Haemophilus influenzae topA locus: DNA RT topoisomerase I is required for genetic competence."; RL Gene 169:25-31(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; U20964; AAC43727.1; -; Genomic_DNA. DR EMBL; L42023; AAC23012.1; -; Genomic_DNA. DR PIR; G64119; G64119. DR RefSeq; NP_439516.1; NC_000907.1. DR ProteinModelPortal; P43012; -. DR SMR; P43012; 3-598, 748-868. DR STRING; 71421.HI1365; -. DR PRIDE; P43012; -. DR EnsemblBacteria; AAC23012; AAC23012; HI_1365. DR GeneID; 950025; -. DR KEGG; hin:HI1365; -. DR PATRIC; 20191417; VBIHaeInf48452_1419. DR eggNOG; ENOG4105C73; Bacteria. DR eggNOG; COG0550; LUCA. DR eggNOG; COG0551; LUCA. DR KO; K03168; -. DR OMA; VVECDKC; -. DR OrthoDB; EOG6S7XQ9; -. DR Proteomes; UP000000579; 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; IPR013263; TopoI_Znr_bac. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 2. DR Pfam; PF08272; Topo_Zn_Ribbon; 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 1 868 DNA topoisomerase 1. FT /FTId=PRO_0000145149. FT DOMAIN 3 148 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ZN_FING 605 636 C4-type 1. FT ZN_FING 667 694 C4-type 2. FT ZN_FING 716 739 C4-type 3. FT REGION 198 203 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 325 325 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 117 117 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 117 117 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 119 119 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 33 33 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 174 174 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 175 175 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 178 178 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 190 190 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 327 327 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 513 513 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT CONFLICT 343 343 T -> S (in Ref. 2; AAC23012). FT {ECO:0000305}. SQ SEQUENCE 868 AA; 98144 MW; AAD604BDEBC75D20 CRC64; MSKSLVIVES PAKAKTINKY LGSQYVVKSS VGHIRDLPTV GSSTGEKAKP ISTKGMDAEE KAKIKAEKER NALVKRMGID PYHDWKANYQ ILPGKEKVVS ELKSLAKKAD HIYLATDLDR EGEAIAWHLR EVIGGNDDRF SRVVFNEITK NAIKQAFEKP EQLNMDRVNA QQTRRFLDRV VGFMVSPLLW KKVARGLSAG RVQSVAVKLL VEREREIKAF QPEEYWEVAV LTNNQNKQAI RLDVTDYKGK KFDPKNQKEA QSAVDFLNVS DYVVTDLETK PTSSRPRAPF ITSTLQQTAS TRLGFGVKKT MMLAQRLYEA GYITYMRTDS TNLSQDALNM ARTYIENHFG AQYLPEKPNF YSSKENAQEA HEAIRPSDIR ALPESLEGME KDAVRLYDLI WCQFLACQMP PAQYDSSTLT VTAGDYTLKA KGRILRFDGW TKVLPQIGKN PEDQELPSVT VSEKLALKEV QPTQHFTKPP ARFTEAALVK ELEKRGIGRP STYAAIISTI QERGYVRTEN RRFYAEKMGE IVTDRLNESF GELMNYDFTA NMEDTLDKIA SGSVNWKTEL NQFFKDFSSQ LSKAELDELE GGMRPNSLVE TDIKCPTCGR NMAIRTASTG VFLGCTGYAL PPKERCKTTI NLIPEAELLN VLDESSETKA LMDRKRCTKC GTAMDSYVID AHRKIHICGN NPNCDGYLIE EGSFKIKGYD GPVVECDKCG ADMHLKLGRF GKYMGCTNCD NTRKILKNGE VAPPKEEPVH FPELKCEKSD AYFVLRDGAS GVFMSAHNFP KSRETRPVKI AELVQYRERL PEKLAYLADA PQKDPEENEA IVRFSRKEKK QYVTSEKEGK ATKWIVDFTN GKWVERKK // ID TMCA_HAEIN Reviewed; 656 AA. AC P44140; P44141; P44142; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 11-MAY-2016, entry version 86. DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886}; DE EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886}; GN Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; GN OrderedLocusNames=HI_1254/HI_1255/HI_1256; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) CC at the wobble position of tRNA(Met), by using acetyl-CoA as an CC acetyl donor and ATP (or GTP). {ECO:0000255|HAMAP-Rule:MF_01886}. CC -!- CATALYTIC ACTIVITY: (Elongator tRNA(Met))-cytidine(34) + ATP + CC acetyl-CoA + H(2)O = (elongator tRNA(Met))-N(4)-acetylcytidine(34) CC + ADP + phosphate + CoA. {ECO:0000255|HAMAP-Rule:MF_01886}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}. CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. CC TmcA subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|HAMAP-Rule:MF_01886}. CC -!- CAUTION: Could be the product of a pseudogene. Three frameshifts CC produce three separate ORFs. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22904.1; Type=Frameshift; Positions=349, 389, 502; Evidence={ECO:0000305}; CC Sequence=AAC22910.1; Type=Frameshift; Positions=349, 389, 502; Evidence={ECO:0000305}; CC Sequence=AAC22911.1; Type=Frameshift; Positions=349, 389, 502; 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; L42023; AAC22904.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC22910.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC22911.1; ALT_FRAME; Genomic_DNA. DR PIR; E64023; E64023. DR PIR; F64023; F64023. DR PIR; G64023; G64023. DR STRING; 71421.HI1254; -. DR EnsemblBacteria; AAC22904; AAC22904; HI_1254. DR EnsemblBacteria; AAC22910; AAC22910; HI_1255. DR EnsemblBacteria; AAC22911; AAC22911; HI_1256. DR eggNOG; COG1444; LUCA. DR OrthoDB; EOG67T5F2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051392; F:tRNA N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-HAMAP. DR GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.630.30; -; 2. DR HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR007807; Helicase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032672; TmcA/NAT10/Kre33. DR InterPro; IPR013562; TmcA_N. DR InterPro; IPR033442; TmcA_tRNA_bind. DR InterPro; IPR024914; tRNA_acetyltr_TmcA. DR PANTHER; PTHR10925; PTHR10925; 2. DR Pfam; PF08351; DUF1726; 1. DR Pfam; PF13718; GNAT_acetyltr_2; 2. DR Pfam; PF05127; Helicase_RecD; 1. DR Pfam; PF17176; tRNA_bind_3; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 5: Uncertain; KW Acyltransferase; ATP-binding; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase; KW tRNA processing; tRNA-binding. FT CHAIN 1 656 tRNA(Met) cytidine acetyltransferase FT TmcA. FT /FTId=PRO_0000013891. FT DOMAIN 368 542 N-acetyltransferase. {ECO:0000255|HAMAP- FT Rule:MF_01886}. FT NP_BIND 167 176 ATP. {ECO:0000255|HAMAP-Rule:MF_01886}. FT REGION 474 476 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01886}. FT REGION 481 487 Acetyl-CoA binding. {ECO:0000255|HAMAP- FT Rule:MF_01886}. FT BINDING 145 145 ATP. {ECO:0000255|HAMAP-Rule:MF_01886}. FT BINDING 291 291 ATP. {ECO:0000255|HAMAP-Rule:MF_01886}. FT BINDING 510 510 Acetyl-CoA. {ECO:0000255|HAMAP- FT Rule:MF_01886}. SQ SEQUENCE 656 AA; 75162 MW; 9975F7685CB45303 CRC64; MPSRQLQILI RKTLPLVPDH VLIIGESGIA FSKATNLLGQ EFEHILFDGR NGIHLEALAI AAGTLKMGGT LCLVLSDWEN LSQQPDQDSL RWNGNQSAIA TPNFIYHFKQ CIERYHFPIL REESAVEFPT VFYSNEHHKN ATLAQQQIIE NILQAEQDIY FLTAKRGRGK SALLGMLANQ IQAPVYLTAP NKSAVHSVIE FSEGDIEFIA PDELALTLQT EPEFSQSAWL LVDEAAMIPL PLLQEYSRYF QHIVFSTTIH SYEGTGRGFE LKFKRKIHRT FQHFELKQPL RWQENDPLEH FIDDLLLLNA EDDFQHFDYS NITYNIEENA KNLSFPCLRG KVPEGPKGDL DIASLPQALE ALLTSKGSEG KYNRQFFFRD FYGLMTIAHY RTSPLDLRRL LDGKNQRFYF AEYQQNLLGA IWALEEGNMA DDELIIQIQQ GKRRPKGNLV PQALCFHENL SQACKLRSLR ISRIAVQPNW QQKGIGQNLM QAMENADVDF LSVSFGYTDE LAKFWQKCGF VLVHLGEHQE ASSGCYSAIA LKGISKEGLA LVDTAYKQFQ RNLPLSFHPF AINFEQNQLD WQLDDFDWMS LKNFANFHRT LFSSIPAMRR LLKLAGKENF PLISAYLTKK QFPINKKKGV ECLRLEIKQY LERGTL // ID TOLA_HAEIN Reviewed; 372 AA. AC P44678; P94810; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Protein TolA; GN Name=tolA; OrderedLocusNames=HI_0383; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1479; RX PubMed=8921895; DOI=10.1016/0378-1119(96)00338-1; RA Sen K., Sikkema D.J., Murphy T.F.; RT "Isolation and characterization of the Haemophilus influenzae tolQ, RT tolR, tolA and tolB genes."; RL Gene 178:75-81(1996). CC -!- FUNCTION: Involved in the TonB-independent uptake of proteins. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single- CC pass type II 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; L42023; AAC22041.1; -; Genomic_DNA. DR EMBL; U32470; AAC44596.1; -; Genomic_DNA. DR PIR; G64064; G64064. DR RefSeq; NP_438544.1; NC_000907.1. DR RefSeq; WP_005693785.1; NC_000907.1. DR ProteinModelPortal; P44678; -. DR STRING; 71421.HI0383; -. DR EnsemblBacteria; AAC22041; AAC22041; HI_0383. DR GeneID; 949487; -. DR KEGG; hin:HI0383; -. DR PATRIC; 20189315; VBIHaeInf48452_0401. DR eggNOG; COG3064; LUCA. DR KO; K03646; -. DR OMA; KTCTVSV; -. DR Proteomes; UP000000579; 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:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR014161; Tol-Pal_TolA. DR Pfam; PF06519; TolA; 1. DR TIGRFAMs; TIGR02794; tolA_full; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 372 Protein TolA. FT /FTId=PRO_0000072623. FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TOPO_DOM 30 372 Periplasmic. {ECO:0000255}. FT VARIANT 48 48 V -> A (in strain: 1479). FT VARIANT 142 142 K -> R (in strain: 1479). FT VARIANT 165 165 A -> P (in strain: 1479). FT VARIANT 190 190 A -> R (in strain: 1479). FT VARIANT 203 203 V -> A (in strain: 1479). FT VARIANT 227 227 D -> A (in strain: 1479). FT VARIANT 232 232 A -> AKAAAEAKAKA (in strain: 1479). FT VARIANT 234 234 T -> A (in strain: 1479). FT VARIANT 249 249 L -> F (in strain: 1479). FT VARIANT 254 254 I -> V (in strain: 1479). FT VARIANT 306 306 N -> S (in strain: 1479). FT VARIANT 323 323 T -> A (in strain: 1479). FT VARIANT 333 333 S -> P (in strain: 1479). SQ SEQUENCE 372 AA; 39831 MW; 266ECF05C6C95544 CRC64; MQNNRQKKGI NAFAISILLH FILFGLLILS SLYHTVEIMG GGEGEGDVIG AVIVDTGTAA QEWGRIQQQK KGQADKQKRP EPVVEEKPPE PNQEEIKHQQ EVQRQEELKR QQEQQRQQEI KKQQEQARQE ALEKQKQAEE AKAKQAAEAA KLKADAEAKR LAAAAKQAEE EAKAKAAEIA AQKAKQEAEA KAKLEAEAKA KAVAEAKAKA EAEAKAKAAA EAKAKADAEA KAATEAKRKA DQASLDDFLN GGDIGGGSAS KGGNTNKGGT QGSGAALGSG DGGKVGDQYA GVIKKEIQRR FLKDPNFAGK VCRIKIQLGR DGTILGYQKI SGSDDICSAA LSAVARTKKV PAAPSDEIYE KYKSPIIDFD IR // ID TOLB_HAEIN Reviewed; 427 AA. AC P44677; P94811; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Protein TolB; DE Flags: Precursor; GN Name=tolB; OrderedLocusNames=HI_0382; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1479; RX PubMed=8921895; DOI=10.1016/0378-1119(96)00338-1; RA Sen K., Sikkema D.J., Murphy T.F.; RT "Isolation and characterization of the Haemophilus influenzae tolQ, RT tolR, tolA and tolB genes."; RL Gene 178:75-81(1996). CC -!- FUNCTION: Involved in the TonB-independent uptake of proteins. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TolB 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; L42023; AAC22040.1; -; Genomic_DNA. DR EMBL; U32470; AAC44597.1; -; Genomic_DNA. DR PIR; F64064; F64064. DR RefSeq; NP_438543.1; NC_000907.1. DR RefSeq; WP_005693786.1; NC_000907.1. DR ProteinModelPortal; P44677; -. DR SMR; P44677; 27-425. DR STRING; 71421.HI0382; -. DR PRIDE; P44677; -. DR EnsemblBacteria; AAC22040; AAC22040; HI_0382. DR GeneID; 949486; -. DR KEGG; hin:HI0382; -. DR PATRIC; 20189313; VBIHaeInf48452_0400. DR eggNOG; ENOG4107R6Y; Bacteria. DR eggNOG; COG0823; LUCA. DR KO; K03641; -. DR OMA; VREPSWG; -. DR OrthoDB; EOG679T7X; -. DR PhylomeDB; P44677; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0017038; P:protein import; IEA:UniProtKB-HAMAP. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 3.40.50.10070; -; 1. DR HAMAP; MF_00671; TolB; 1. DR InterPro; IPR011659; PD40. DR InterPro; IPR014167; Tol-Pal_propeller_TolB. DR InterPro; IPR007195; TolB_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR Pfam; PF07676; PD40; 4. DR Pfam; PF04052; TolB_N; 1. DR SUPFAM; SSF52964; SSF52964; 1. DR TIGRFAMs; TIGR02800; propeller_TolB; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Protein transport; Reference proteome; KW Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 427 Protein TolB. FT /FTId=PRO_0000034656. FT VARIANT 6 6 R -> H (in strain: 1479). FT VARIANT 14 14 V -> I (in strain: 1479). FT VARIANT 17 19 VGS -> ITH (in strain: 1479). FT VARIANT 21 21 A -> V (in strain: 1479). FT VARIANT 79 79 R -> H (in strain: 1479). FT VARIANT 129 129 T -> A (in strain: 1479). FT VARIANT 160 160 A -> G (in strain: 1479). FT VARIANT 237 237 A -> T (in strain: 1479). FT VARIANT 322 322 S -> N (in strain: 1479). FT VARIANT 326 326 A -> V (in strain: 1479). FT VARIANT 328 328 A -> S (in strain: 1479). SQ SEQUENCE 427 AA; 44968 MW; 0882201AEE9254B9 CRC64; MKLLKRLVSV FAIVLAVGSN AFAGDEVRIV IDEGVDGARP IAVVPFVGSA PEDISKIVAD DLRNSGKFNP IAVSQMPQRP TSAAEVNPEA WSNIGIDAIV IGQVVPSGNG YSITYQLIDT VGASGTPGTV LMQNSYTVTN KWLRYGAHTV SDEVFEKLTA IRGAFRTRIA YVVQKNGGSQ PYEVRVADYD GYNQFIVNRS AQPIMSPAWS PDGQRLAYVS FENKKSQLVV QDLNSGARKV VASFQGHNGA PAFSPDGSRL AFASSRDGVL NIYVMGANGG TPTQLTSGAG NNTEPAWSPD GNSILFTSDR SGSPQVYRMD ASGGSATAVG GRGSAQISAD GKTLVMINGN NNVVKQDLTT GVSEVLSTSF LGESPSLSPN GIMIIYSSTQ GLGKVLQLVS ADGRFKASLP GSDGQVKFPA WSPYLTK // ID TONB_HAEIN Reviewed; 270 AA. AC P42872; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Protein TonB; GN Name=tonB; OrderedLocusNames=HI_0251; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi TN106; RX PubMed=8188372; RA Jarosik G.P., Sanders J.D., Cope L.D., Mueller-Eberhard U., RA Hansen E.J.; RT "A functional tonB gene is required for both utilization of heme and RT virulence expression by Haemophilus influenzae type b."; RL Infect. Immun. 62:2470-2477(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Interacts with outer membrane receptor proteins that CC carry out high-affinity binding and energy dependent uptake into CC the periplasmic space of specific substrates. It could act to CC transduce energy from the cytoplasmic membrane to specific energy- CC requiring processes in the outer membrane, resulting in the CC release into the periplasm of ligands bound by these outer CC membrane proteins. Required for heme utilization and virulence. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}; Periplasmic side CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TonB 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; U04996; AAA60460.1; -; Genomic_DNA. DR EMBL; L42023; AAC21917.1; -; Genomic_DNA. DR PIR; F64057; F64057. DR RefSeq; NP_438420.1; NC_000907.1. DR RefSeq; WP_010868966.1; NC_000907.1. DR ProteinModelPortal; P42872; -. DR STRING; 71421.HI0251; -. DR EnsemblBacteria; AAC21917; AAC21917; HI_0251. DR GeneID; 949372; -. DR KEGG; hin:HI0251; -. DR PATRIC; 20189027; VBIHaeInf48452_0266. DR eggNOG; ENOG4108DNJ; Bacteria. DR eggNOG; ENOG410ZYHZ; LUCA. DR KO; K03832; -. DR OMA; WNWNEPS; -. DR OrthoDB; EOG6P0754; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031992; F:energy transducer activity; IEA:InterPro. DR GO; GO:0015343; F:siderophore transmembrane transporter activity; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003538; TonB. DR InterPro; IPR006260; TonB_C. DR Pfam; PF03544; TonB_C; 1. DR PRINTS; PR01374; TONBPROTEIN. DR TIGRFAMs; TIGR01352; tonB_Cterm; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Repeat; Signal-anchor; KW Transmembrane; Transmembrane helix; Transport; Virulence. FT CHAIN 1 270 Protein TonB. FT /FTId=PRO_0000196197. FT TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 27 Helical; Signal-anchor. {ECO:0000255}. FT TOPO_DOM 28 270 Periplasmic. {ECO:0000255}. FT REPEAT 70 71 1. FT REPEAT 72 73 2. FT REPEAT 74 75 3. FT REPEAT 76 77 4. FT REGION 70 77 4 X 2 AA tandem repeats of E-P. FT COMPBIAS 58 90 Glu/Pro-rich. FT COMPBIAS 98 143 Glu/Lys/Pro-rich. FT VARIANT 17 17 A -> V (in strain: TN106). FT VARIANT 31 31 E -> K (in strain: TN106). FT VARIANT 66 66 D -> N (in strain: TN106). FT VARIANT 76 84 Missing (in strain: TN106). FT VARIANT 116 116 G -> E (in strain: TN106). FT VARIANT 120 120 G -> E (in strain: TN106). FT VARIANT 134 134 K -> Q (in strain: TN106). FT VARIANT 140 140 E -> D (in strain: TN106). FT VARIANT 146 146 E -> K (in strain: TN106). FT VARIANT 226 226 K -> R (in strain: TN106). SQ SEQUENCE 270 AA; 29193 MW; 4CDA54B46F7D10A0 CRC64; MQQTKRSLLG LLISLIAHGI VIGFILWNWN EPSDSANSAQ GDISTSISME LLQGMVLEEP APEPEDVQKE PEPEPEPGNV QKEPEPEKQE IVEDPTIKPE PKKIKEPEKE KPKPKGKPKG KPKNKPKKEV KPQKKPINKE LPKGDENIDS SANVNDKAST TSAANSNAQV AGSGTDTSEI AAYRSAIRRE IESHKRYPTR AKIMRKQGKV SVSFNVGADG SLSGAKVTKS SGDESLDKAA LDAINVSRSV GTRPAGFPSS LSVQISFTLQ // ID TRA_HAEIN Reviewed; 687 AA. AC O05069; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=Mu-like prophage FluMu transposase A; GN OrderedLocusNames=HI_1478; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This transposase is essential for integration, CC replication-transposition, and excision of Mu-like viral DNA. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH Mu-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; L42023; AAC23125.1; -; Genomic_DNA. DR PIR; B64126; B64126. DR RefSeq; NP_439629.1; NC_000907.1. DR RefSeq; WP_010869221.1; NC_000907.1. DR ProteinModelPortal; O05069; -. DR STRING; 71421.HI1478; -. DR PRIDE; O05069; -. DR EnsemblBacteria; AAC23125; AAC23125; HI_1478. DR GeneID; 950583; -. DR KEGG; hin:HI1478; -. DR PATRIC; 20191673; VBIHaeInf48452_1546. DR eggNOG; ENOG4106YXT; Bacteria. DR eggNOG; COG2801; LUCA. DR KO; K07497; -. DR OMA; GYQHNVF; -. DR OrthoDB; EOG6NKQWR; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.10.60; -; 2. DR Gene3D; 2.30.30.130; -; 1. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR003314; Mu-type_HTH. DR InterPro; IPR015126; Mu_I-gamma. DR InterPro; IPR004189; Phage_Mu_transposase. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR015378; Transposase-like_Mu_C. DR InterPro; IPR009004; Transposase_Mu_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02914; DDE_2; 1. DR Pfam; PF02316; HTH_Tnp_Mu_1; 1. DR Pfam; PF09039; HTH_Tnp_Mu_2; 1. DR Pfam; PF09299; Mu-transpos_C; 1. DR SUPFAM; SSF46689; SSF46689; 2. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF50610; SSF50610; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS51702; HTH_MU; 1. PE 3: Inferred from homology; KW Complete proteome; DNA excision; DNA integration; DNA recombination; KW DNA-binding; Reference proteome; Transposable element; Transposition. FT CHAIN 1 687 Mu-like prophage FluMu transposase A. FT /FTId=PRO_0000077585. FT DOMAIN 8 74 HTH Mu-type. {ECO:0000255|PROSITE- FT ProRule:PRU01039}. FT DNA_BIND 398 417 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU01039}. SQ SEQUENCE 687 AA; 78720 MW; AC3A34DFDB68CB24 CRC64; MDNQSLKTHY SVYELANLKL KTLPSAPKNI WEQAKRENWK SQKRQGRGGG LEYELASLPI EVQNELLLKT TPEQTAVALQ KIEETRPLAS NEVWQLWDEA SAKAQEQAKI KLGTMFAVAN LVESGVNVLD AFRLVCGKEN AERLKNNEKL LSVGSLKNWW YRVKDAPRQD WLPLMLNNSG KSSKNVAEID EAAWQFFKNF YYSREKPSLA HSYEVLKQAA QYNGWRIPSR SSLKRKMERD VPKTEEVFRR EGQYALSRLY PSQVRTVAML QAMEWINGDG YQHNVWVRFP DGEIKRPKTW LWQDVRTRKV LAARTDKSEN TDTIRLSLLD VISRYGLPKH LTIDNTRAAA NKKMTGGVKN RYRYQVNENE VQGIIPALGI ELHWTSIQFG KGRGQAKPIE RAFSHGGLGD YVDKHLLLRG AYAGANAYEK PDYDGKNGAE QPVDYATFLM ALEQGIQQWN NVGNRLTEIC AGKSSYAEAF ERDWAVAEKR PISQSQMRLL LTLHEEVRLN QDGTFYLNAG KIGTNKNRYE SLALIGTSHK RVVVRYDPAN LHDKVWVYAX TGEYLAEAEI TEKAGFGDQM AGREHNKAMR NWVKHTEKAA KERAKAEEME LSNYAPAVEF EERFLEMLPE PVKAPQTQAE EVEYEEVLDF NTVRKVPKAV EVEAEEISEF NRDWEKGLEL LKKSKGR // ID TKT_HAEIN Reviewed; 665 AA. AC P43757; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=Transketolase; DE Short=TK; DE EC=2.2.1.1; GN Name=tktA; OrderedLocusNames=HI_1023; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol CC group from sedoheptulose-7-phosphate to glyceraldehyde-3- CC phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. CC Catalyzes the transfer of a two-carbon ketol group from a ketose CC donor to an aldose acceptor, via a covalent intermediate with the CC cofactor thiamine pyrophosphate (By similarity). {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; L42023; AAC22683.1; -; Genomic_DNA. DR PIR; G64108; G64108. DR RefSeq; NP_439183.1; NC_000907.1. DR RefSeq; WP_010869107.1; NC_000907.1. DR ProteinModelPortal; P43757; -. DR SMR; P43757; 2-665. DR STRING; 71421.HI1023; -. DR PRIDE; P43757; -. DR EnsemblBacteria; AAC22683; AAC22683; HI_1023. DR GeneID; 949889; -. DR KEGG; hin:HI1023; -. DR PATRIC; 20190709; VBIHaeInf48452_1067. DR eggNOG; ENOG4105CV1; Bacteria. DR eggNOG; COG0021; LUCA. DR KO; K00615; -. DR OMA; WEVLYVE; -. DR OrthoDB; EOG6N3CRG; -. DR PhylomeDB; P43757; -. DR Proteomes; UP000000579; 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; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 2. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR Pfam; PF00456; Transketolase_N; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR SUPFAM; SSF52922; SSF52922; 1. DR TIGRFAMs; TIGR00232; tktlase_bact; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 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 1 665 Transketolase. FT /FTId=PRO_0000191858. FT NP_BIND 114 116 Thiamine pyrophosphate. {ECO:0000250}. FT ACT_SITE 413 413 Proton donor. {ECO:0000250}. FT METAL 155 155 Magnesium. {ECO:0000250}. FT METAL 185 185 Magnesium. {ECO:0000250}. FT METAL 187 187 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 26 26 Substrate. {ECO:0000250}. FT BINDING 66 66 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 156 156 Thiamine pyrophosphate; via amide FT nitrogen. {ECO:0000250}. FT BINDING 185 185 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 261 261 Substrate. {ECO:0000250}. FT BINDING 261 261 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 358 358 Substrate. {ECO:0000250}. FT BINDING 385 385 Substrate. {ECO:0000250}. FT BINDING 439 439 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 463 463 Substrate. {ECO:0000250}. FT BINDING 471 471 Substrate. {ECO:0000250}. FT BINDING 522 522 Substrate. {ECO:0000250}. FT SITE 26 26 Important for catalytic activity. FT {ECO:0000250}. FT SITE 261 261 Important for catalytic activity. FT {ECO:0000250}. SQ SEQUENCE 665 AA; 72718 MW; 71FB421179D7FCFB CRC64; MATRRQLANA IRVLAMDSVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPT NPKWADRDRF VLSNGHGSML IYSLLHLTGY DLSIEDLKQF RQLHSKTPGH PEYGYAPGVE TTTGPLGQGI TNAVGMAIAE KTLAGQFNRE GHEIVDHHTY VFLGDGCLME GISHEACSLA GTLGLGKLIA FYDDNNISID GHVDGWFSDD TAERFEAYGW QVIRNVDGHD AEQIRAATIL AQAEKGKPTL IICKTIIGFG SPNKSGSHDS HGAPLGDEEI DLTRKALGWE YAPFEIPAEY YAEWSAKEKG AAAEKSWEEK FAAYAKAYPE LAAEFKRRVS GELPTNWAAE SKAFIEKLQA NPASIASRKA SQNAIEAYAH VLPEFLGGSA DLASSNLTLW SGSKPIRAHE NVGGNYINYG VREFGMSAIM NGIALHGGFI PYGATFLMFY EYAHNAVRMA ALMKQRTLFV YTHDSIGLGE DGPTHQPVEQ TASLRLIPNL ETWRPCDQVE SAIAWQQAVE RQDGPSALIF TRQNLAQMDR TSAQLDAVKR GAYVLKDCDG TPELIFIATG SEVELAVQAA EALSAEGKKV RVVSMPSTNR FDKQDAAYRE SVLPAAVTKR VAIEAGIADF WYKYVGFNGR VIGMNSFGES APADQLFKLF GFTVENVVAK AKEIL // ID TOP3_HAEIN Reviewed; 651 AA. AC P43704; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=DNA topoisomerase 3 {ECO:0000255|HAMAP-Rule:MF_00953}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00953}; DE AltName: Full=DNA topoisomerase III {ECO:0000255|HAMAP-Rule:MF_00953}; GN Name=topB {ECO:0000255|HAMAP-Rule:MF_00953}; GN OrderedLocusNames=HI_0444; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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_00953}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000255|HAMAP- CC Rule:MF_00953}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00953}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00953}; CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00953}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00953}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22103.1; -; Genomic_DNA. DR PIR; G64068; G64068. DR RefSeq; NP_438605.1; NC_000907.1. DR RefSeq; WP_005693718.1; NC_000907.1. DR ProteinModelPortal; P43704; -. DR SMR; P43704; 1-612. DR STRING; 71421.HI0444; -. DR EnsemblBacteria; AAC22103; AAC22103; HI_0444. DR GeneID; 949541; -. DR KEGG; hin:HI0444; -. DR PATRIC; 20189441; VBIHaeInf48452_0464. DR eggNOG; ENOG4105C73; Bacteria. DR eggNOG; COG0550; LUCA. DR KO; K03169; -. DR OMA; YCYSETA; -. DR OrthoDB; EOG60CWM6; -. DR PhylomeDB; P43704; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 2.70.20.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR HAMAP; MF_00953; Topoisom_3_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; IPR005738; TopoIII. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 3. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01056; topB; 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; Topoisomerase. FT CHAIN 1 651 DNA topoisomerase 3. FT /FTId=PRO_0000145187. FT DOMAIN 1 134 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT REGION 194 199 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT ACT_SITE 337 337 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00953}. FT METAL 7 7 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00953}. FT METAL 103 103 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00953}. FT METAL 103 103 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT METAL 105 105 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT SITE 61 61 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT SITE 170 170 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT SITE 178 178 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT SITE 185 185 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. FT SITE 339 339 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00953}. SQ SEQUENCE 651 AA; 74067 MW; 73D1A25F0C6C4229 CRC64; MRLFIAEKPS LARAIADVLP KPHQRGDGFI KCGDNDVVTW CVGHLLEQAE PDAYDPKFKQ WRLEHLPIIP EKWQLLPRKE VKKQLSVVEK LIHQADTLVN AGDPDREGQL LVDEVFSYAN LSAEKRDKIL RCLISDLNPS AVEKAVKKLQ PNRNFIPLAT SALARARADW LYGINMTRAY TIRGRQTGYD GVLSVGRVQT PVLGLIVRRD LEIEHFQPKD FFEVQAWVNP ESKEEKTPEK STALFSALWQ PSKACEDYQD DDGRVLSKGL AEKVVKRITN QPAEVTEYKD VREKETAPLP YSLSALQIDA AKRFGMSAQA VLDTCQRLYE THRLITYPRS DCRYLPEEHF AERHNVLNAI STHCEAYQVL PNVILTEQRN RCWNDKKVEA HHAIIPTAKN RPVNLTQEER NIYSLIARQY LMQFCPDAEY RKSKITLNIA GGTFIAQARN LQTAGWKELL GKEDDTENQE PLLPIVKKGQ ILHCERGEVM SKKTQPPKPF TDATLLSAMT GIARFVQDKE LKKILRETDG LGTEATRAGI IELLFKRGFL TKKGRNIHST ETGRILIQAL PNIATQPDMT AHWESQLTDI SQKQATYQQF MHNLNQILPD LVRFVDLNAL RQLSRIKMIK SDRAKPKSAV KKSSKSNGET D // ID TRKA_HAEIN Reviewed; 458 AA. AC P71354; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Trk system potassium uptake protein TrkA; DE Short=K(+)-uptake protein TrkA; GN Name=trkA; OrderedLocusNames=HI_0625; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a potassium transport system. {ECO:0000250}. CC -!- DOMAIN: The RCK N-terminal domain binds NAD and possibly other CC effectors. This is expected to cause a conformation change that CC regulates potassium transport (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 2 RCK C-terminal domains. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 2 RCK N-terminal domains. 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; L42023; AAC22285.1; -; Genomic_DNA. DR RefSeq; NP_438785.1; NC_000907.1. DR RefSeq; WP_005694644.1; NC_000907.1. DR ProteinModelPortal; P71354; -. DR STRING; 71421.HI0625; -. DR EnsemblBacteria; AAC22285; AAC22285; HI_0625. DR GeneID; 949682; -. DR KEGG; hin:HI0625; -. DR PATRIC; 20189845; VBIHaeInf48452_0651. DR eggNOG; ENOG4105C1A; Bacteria. DR eggNOG; COG0569; LUCA. DR KO; K03499; -. DR OMA; IACQVAY; -. DR OrthoDB; EOG6ZH2G8; -. DR PhylomeDB; P71354; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central. DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006036; K_uptake_TrkA. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF02080; TrkA_C; 2. DR Pfam; PF02254; TrkA_N; 2. DR PRINTS; PR00335; KUPTAKETRKA. DR SUPFAM; SSF116726; SSF116726; 2. DR SUPFAM; SSF51735; SSF51735; 2. DR PROSITE; PS51202; RCK_C; 2. DR PROSITE; PS51201; RCK_N; 2. PE 3: Inferred from homology; KW Complete proteome; Ion transport; NAD; Potassium; Potassium transport; KW Reference proteome; Repeat; Transport. FT CHAIN 1 458 Trk system potassium uptake protein TrkA. FT /FTId=PRO_0000148715. FT DOMAIN 2 131 RCK N-terminal 1. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 143 227 RCK C-terminal 1. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. FT DOMAIN 234 356 RCK N-terminal 2. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 368 453 RCK C-terminal 2. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. FT NP_BIND 7 11 NAD 1. {ECO:0000250}. FT NP_BIND 73 74 NAD 1. {ECO:0000250}. FT NP_BIND 234 262 NAD 2. {ECO:0000255}. FT BINDING 30 30 NAD 1. {ECO:0000250}. FT BINDING 98 98 NAD 1; shared with dimeric partner. FT {ECO:0000250}. SQ SEQUENCE 458 AA; 50174 MW; E1FAB66AA1A221DA CRC64; MKIIILGAGQ VGTTLAENLV SEDNDITLVD NESPQLQTLQ EKHDLRVVQG SPSSPKVLRD AGAADADLMV AVTASDEINM VACQMGYTLF NTPTRIARIR NSEYLREKDK LFNNENIPID HLISPENLVT DEITRLIAYP GALQVAHFAN NRISIVVVKA YYGGALVGYA LSAFREHMPH IDCRIMSILR NGKPIRPQGS TIVEAGDEIT FICATEHIKA IMGELQRLEK PYKRVMIVGG GNVAFGVAKR LENSCTVKLI ERDSNRAQAL AEKLPKTLVF NGDASDQNLL FEEHIESVDV FLSLSSDDEA NIMSALLAKR LGAKKAMVLI QRIAYINLIQ GGTIDIAVSP QQVTISALLG HVRKGDVKNV ATLRHGIAEA IEIVAHGNVN TSNIVGRKIG ELRLPMGIII GALLRGNDVI IARRQVIIEE GDHIVIYLSD KKNVPEIEKL FQPSAFFI // ID TRMD_HAEIN Reviewed; 246 AA. AC P43912; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 117. 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=HI_0202; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND RP SUBUNIT. RX PubMed=12773376; DOI=10.1093/emboj/cdg269; RA Ahn H.J., Kim H.-W., Yoon H.-J., Lee B.I., Suh S.W., Yang J.K.; RT "Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA RT recognition."; RL EMBO J. 22:2593-2603(2003). 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:0000269|PubMed:12773376}. 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; L42023; AAC21871.1; -; Genomic_DNA. DR PIR; C64054; C64054. DR RefSeq; NP_438371.1; NC_000907.1. DR RefSeq; WP_005661387.1; NC_000907.1. DR PDB; 1UAJ; X-ray; 1.85 A; A=1-246. DR PDB; 1UAK; X-ray; 2.05 A; A=1-246. DR PDB; 1UAL; X-ray; 1.80 A; A=1-246. DR PDB; 1UAM; X-ray; 2.20 A; A=1-246. DR PDB; 3AXZ; X-ray; 2.25 A; A=1-246. DR PDB; 4MCB; X-ray; 1.94 A; A/B=1-246. DR PDB; 4MCC; X-ray; 1.95 A; A/B=1-246. DR PDB; 4MCD; X-ray; 1.55 A; A=1-246. DR PDB; 4YPW; X-ray; 2.31 A; A=1-246. DR PDB; 4YPX; X-ray; 1.89 A; A=1-246. DR PDB; 4YPY; X-ray; 1.90 A; A=1-246. DR PDB; 4YPZ; X-ray; 1.84 A; A=1-246. DR PDB; 4YQ0; X-ray; 1.76 A; A=1-246. DR PDB; 4YQ1; X-ray; 2.00 A; A=1-246. DR PDB; 4YQ2; X-ray; 2.65 A; A=1-246. DR PDB; 4YQ3; X-ray; 2.49 A; A=1-246. DR PDB; 4YQ4; X-ray; 1.89 A; A=1-246. DR PDB; 4YQ5; X-ray; 1.76 A; A=1-246. DR PDB; 4YQ6; X-ray; 1.90 A; A=1-246. DR PDB; 4YQ7; X-ray; 1.80 A; A=1-246. DR PDB; 4YQ8; X-ray; 1.94 A; A=1-246. DR PDB; 4YQ9; X-ray; 1.64 A; A=1-246. DR PDB; 4YQA; X-ray; 1.55 A; A=1-246. DR PDB; 4YQB; X-ray; 2.10 A; A=1-246. DR PDB; 4YQC; X-ray; 1.89 A; A=1-246. DR PDB; 4YQD; X-ray; 1.45 A; A=1-246. DR PDB; 4YQG; X-ray; 1.86 A; A=1-246. DR PDB; 4YQI; X-ray; 1.92 A; A=1-246. DR PDB; 4YQJ; X-ray; 1.94 A; A=1-246. DR PDB; 4YQK; X-ray; 1.83 A; A=1-246. DR PDB; 4YQL; X-ray; 2.40 A; A=1-246. DR PDB; 4YQN; X-ray; 2.20 A; A=1-246. DR PDB; 4YQO; X-ray; 1.68 A; A=1-246. DR PDB; 4YQP; X-ray; 2.60 A; A=1-246. DR PDB; 4YQQ; X-ray; 1.78 A; A=1-246. DR PDB; 4YQR; X-ray; 1.70 A; A=1-246. DR PDB; 4YQS; X-ray; 1.90 A; A=1-246. DR PDB; 4YQT; X-ray; 1.60 A; A=1-246. DR PDB; 4YVG; X-ray; 1.55 A; A=1-246. DR PDB; 4YVH; X-ray; 1.60 A; A=1-246. DR PDB; 4YVI; X-ray; 3.01 A; A/B=1-246. DR PDB; 4YVJ; X-ray; 2.90 A; A/B=1-246. DR PDB; 4YVK; X-ray; 3.00 A; A/B=1-246. DR PDBsum; 1UAJ; -. DR PDBsum; 1UAK; -. DR PDBsum; 1UAL; -. DR PDBsum; 1UAM; -. DR PDBsum; 3AXZ; -. DR PDBsum; 4MCB; -. DR PDBsum; 4MCC; -. DR PDBsum; 4MCD; -. DR PDBsum; 4YPW; -. DR PDBsum; 4YPX; -. DR PDBsum; 4YPY; -. DR PDBsum; 4YPZ; -. DR PDBsum; 4YQ0; -. DR PDBsum; 4YQ1; -. DR PDBsum; 4YQ2; -. DR PDBsum; 4YQ3; -. DR PDBsum; 4YQ4; -. DR PDBsum; 4YQ5; -. DR PDBsum; 4YQ6; -. DR PDBsum; 4YQ7; -. DR PDBsum; 4YQ8; -. DR PDBsum; 4YQ9; -. DR PDBsum; 4YQA; -. DR PDBsum; 4YQB; -. DR PDBsum; 4YQC; -. DR PDBsum; 4YQD; -. DR PDBsum; 4YQG; -. DR PDBsum; 4YQI; -. DR PDBsum; 4YQJ; -. DR PDBsum; 4YQK; -. DR PDBsum; 4YQL; -. DR PDBsum; 4YQN; -. DR PDBsum; 4YQO; -. DR PDBsum; 4YQP; -. DR PDBsum; 4YQQ; -. DR PDBsum; 4YQR; -. DR PDBsum; 4YQS; -. DR PDBsum; 4YQT; -. DR PDBsum; 4YVG; -. DR PDBsum; 4YVH; -. DR PDBsum; 4YVI; -. DR PDBsum; 4YVJ; -. DR PDBsum; 4YVK; -. DR ProteinModelPortal; P43912; -. DR SMR; P43912; 1-246. DR STRING; 71421.HI0202; -. DR EnsemblBacteria; AAC21871; AAC21871; HI_0202. DR GeneID; 951111; -. DR KEGG; hin:HI0202; -. DR PATRIC; 20188901; VBIHaeInf48452_0207. DR eggNOG; ENOG4105D6X; Bacteria. DR eggNOG; COG0336; LUCA. DR KO; K00554; -. DR OMA; YKGVDQR; -. DR OrthoDB; EOG6J48RZ; -. DR PhylomeDB; P43912; -. DR BRENDA; 2.1.1.228; 2529. DR EvolutionaryTrace; P43912; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GOC. DR Gene3D; 1.10.1270.20; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00605; TrmD; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR002649; tRNA_m1G_MeTrfase_bac. DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10. DR Pfam; PF01746; tRNA_m1G_MT; 1. DR PIRSF; PIRSF000386; tRNA_mtase; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00088; trmD; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 246 tRNA (guanine-N(1)-)-methyltransferase. FT /FTId=PRO_0000060385. FT REGION 133 138 S-adenosyl-L-methionine binding. FT ACT_SITE 169 169 Proton acceptor. {ECO:0000255}. FT BINDING 86 86 S-adenosyl-L-methionine. FT BINDING 113 113 S-adenosyl-L-methionine; via amide FT nitrogen. FT STRAND 1 6 {ECO:0000244|PDB:4YQD}. FT HELIX 10 13 {ECO:0000244|PDB:4YQD}. FT HELIX 14 17 {ECO:0000244|PDB:4YQD}. FT HELIX 20 27 {ECO:0000244|PDB:4YQD}. FT STRAND 30 36 {ECO:0000244|PDB:4YQD}. FT HELIX 38 41 {ECO:0000244|PDB:4YQD}. FT HELIX 64 78 {ECO:0000244|PDB:4YQD}. FT STRAND 83 88 {ECO:0000244|PDB:4YQD}. FT STRAND 91 93 {ECO:0000244|PDB:4YQD}. FT HELIX 96 102 {ECO:0000244|PDB:4YQD}. FT STRAND 106 111 {ECO:0000244|PDB:4YQD}. FT HELIX 120 126 {ECO:0000244|PDB:4YQD}. FT STRAND 128 136 {ECO:0000244|PDB:4YQD}. FT STRAND 139 141 {ECO:0000244|PDB:4YVH}. FT HELIX 142 153 {ECO:0000244|PDB:4YQD}. FT TURN 157 159 {ECO:0000244|PDB:4YQD}. FT HELIX 164 166 {ECO:0000244|PDB:4YVJ}. FT TURN 170 172 {ECO:0000244|PDB:4YVG}. FT STRAND 173 175 {ECO:0000244|PDB:4YVG}. FT STRAND 185 187 {ECO:0000244|PDB:4YQD}. FT HELIX 194 197 {ECO:0000244|PDB:4YQD}. FT HELIX 201 219 {ECO:0000244|PDB:4YQD}. FT HELIX 221 225 {ECO:0000244|PDB:4YQD}. FT HELIX 231 245 {ECO:0000244|PDB:4YQD}. SQ SEQUENCE 246 AA; 27543 MW; DEEF238159B1003D CRC64; MWIGVISLFP EMFKAITEFG VTGRAVKHNL LKVECWNPRD FTFDKHKTVD DRPYGGGPGM LMMVQPLRDA IHTAKAAAGE GAKVIYLSPQ GRKLDQGGVT ELAQNQKLIL VCGRYEGIDE RLIQTEIDEE WSIGDYVLTG GELPAMTLID AVARFIPGVL GKQASAEEDS FADGLLDCPH YTRPEVLEGL TVPPVLMSGH HEEIRKWRLK QSLQRTWLRR PELLEGLALT DEQRKLLKEA QAEHNS // ID TILS_HAEIN Reviewed; 430 AA. AC P44689; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. 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}; Synonyms=mesJ; GN OrderedLocusNames=HI_0404; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22063.1; -; Genomic_DNA. DR PIR; D64151; D64151. DR RefSeq; NP_438566.1; NC_000907.1. DR RefSeq; WP_005693764.1; NC_000907.1. DR ProteinModelPortal; P44689; -. DR STRING; 71421.HI0404; -. DR EnsemblBacteria; AAC22063; AAC22063; HI_0404. DR GeneID; 949503; -. DR KEGG; hin:HI0404; -. DR PATRIC; 20189359; VBIHaeInf48452_0423. DR eggNOG; ENOG4105D3U; Bacteria. DR eggNOG; COG0037; LUCA. DR KO; K04075; -. DR OMA; DRNFLRQ; -. DR OrthoDB; EOG6NKR0V; -. DR PhylomeDB; P44689; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1. DR InterPro; IPR012796; Lysidine-tRNA-synth_C. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR012094; tRNA_Ile_lys_synt. DR InterPro; IPR012795; tRNA_Ile_lys_synt_N. DR InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd. DR PANTHER; PTHR11807:SF2; PTHR11807:SF2; 1. DR Pfam; PF01171; ATP_bind_3; 1. DR Pfam; PF09179; TilS; 1. DR Pfam; PF11734; TilS_C; 1. DR SMART; SM00977; TilS_C; 1. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR02433; lysidine_TilS_C; 1. DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 430 tRNA(Ile)-lysidine synthase. FT /FTId=PRO_0000181701. FT NP_BIND 24 29 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 430 AA; 50053 MW; FFDC831DB67C1C6C CRC64; MDLLSDIEKQ LQKATAQAFL IALSGGLDST VLLSLFAKLC QKQPHLPPLS IRAIHIHHGL SPNADSWAKH CQDLCDQFQI PLIIERVQVD KTNGIEAGAR EARYQAIKKY LQTQEMLVTA HHLNDQTETF FLALKRGSGL KGLGAMQQQS VLFGMPILRP LLGFTRTQLE NYAQKEKLNW ITDESNEDNR YDRNFLRNEI LPELRERWAH FDLAVQRSAQ HCFEQQQLIN DLLSEIFTEH CQIKNQFKLC QFRQYSLAKQ TALLRMWLAE NQLEMPSKRQ LTQLINDVIF AKEEANPQFQ LVNKVIRRYQ DSLYLTKPFS DLTKCTLKLE QNTLNLPDDL GNLTVQENEH NLIFYWQDYS VTLEKTNLPI SIRFGYSGKV KHYPKRPRED IKKIWQELGV PPWERNRIPL IFYGNELKSA VGFFRVLKSS // ID TPX_HAEIN Reviewed; 165 AA. AC Q57549; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Probable thiol peroxidase; DE EC=1.11.1.-; GN Name=tpx; OrderedLocusNames=HI_0751; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Has antioxidant activity. Could remove peroxides or CC H(2)O(2) (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AhpC/TSA family. Tpx subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin 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; L42023; AAC22410.1; -; Genomic_DNA. DR PIR; G64090; G64090. DR RefSeq; NP_438910.1; NC_000907.1. DR RefSeq; WP_005693150.1; NC_000907.1. DR PDB; 1Q98; X-ray; 1.90 A; A/B=1-165. DR PDBsum; 1Q98; -. DR ProteinModelPortal; Q57549; -. DR SMR; Q57549; 2-165. DR STRING; 71421.HI0751; -. DR EnsemblBacteria; AAC22410; AAC22410; HI_0751. DR GeneID; 949774; -. DR KEGG; hin:HI0751; -. DR PATRIC; 20190145; VBIHaeInf48452_0788. DR eggNOG; ENOG4108V1J; Bacteria. DR eggNOG; COG2077; LUCA. DR KO; K11065; -. DR OMA; KFNAQAN; -. DR OrthoDB; EOG6NWBV8; -. DR PhylomeDB; Q57549; -. DR EvolutionaryTrace; Q57549; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00269; Tpx; 1. DR InterPro; IPR002065; Put_TPX. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR018219; Tpx_CS. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. DR PROSITE; PS01265; TPX; 1. PE 1: Evidence at protein level; KW 3D-structure; Antioxidant; Complete proteome; Oxidoreductase; KW Peroxidase; Reference proteome. FT CHAIN 1 165 Probable thiol peroxidase. FT /FTId=PRO_0000187880. FT DOMAIN 17 165 Thioredoxin. FT STRAND 3 5 {ECO:0000244|PDB:1Q98}. FT STRAND 8 10 {ECO:0000244|PDB:1Q98}. FT STRAND 12 14 {ECO:0000244|PDB:1Q98}. FT STRAND 27 29 {ECO:0000244|PDB:1Q98}. FT STRAND 35 37 {ECO:0000244|PDB:1Q98}. FT HELIX 38 41 {ECO:0000244|PDB:1Q98}. FT STRAND 44 50 {ECO:0000244|PDB:1Q98}. FT HELIX 61 72 {ECO:0000244|PDB:1Q98}. FT STRAND 76 84 {ECO:0000244|PDB:1Q98}. FT HELIX 86 89 {ECO:0000244|PDB:1Q98}. FT TURN 93 97 {ECO:0000244|PDB:1Q98}. FT STRAND 101 105 {ECO:0000244|PDB:1Q98}. FT HELIX 111 115 {ECO:0000244|PDB:1Q98}. FT TURN 124 127 {ECO:0000244|PDB:1Q98}. FT STRAND 132 136 {ECO:0000244|PDB:1Q98}. FT STRAND 140 147 {ECO:0000244|PDB:1Q98}. FT HELIX 157 162 {ECO:0000244|PDB:1Q98}. SQ SEQUENCE 165 AA; 17626 MW; 221DA969C76106CB CRC64; MTVTLAGNPI EVGGHFPQVG EIVENFILVG NDLADVALND FASKRKVLNI FPSIDTGVCA TSVRKFNQQA AKLSNTIVLC ISADLPFAQA RFCGAEGIEN AKTVSTFRNH ALHSQLGVDI QTGPLAGLTS RAVIVLDEQN NVLHSQLVEE IKEEPNYEAA LAVLA // ID TRKH_HAEIN Reviewed; 487 AA. AC P44843; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 98. DE RecName: Full=Trk system potassium uptake protein TrkH; GN Name=trkH; OrderedLocusNames=HI_0723; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Low-affinity potassium transport system. Interacts with CC Trk system potassium uptake protein TrkA and requires TrkE for CC transport activity (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. 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; L42023; AAC22381.1; -; Genomic_DNA. DR RefSeq; NP_438881.1; NC_000907.1. DR RefSeq; WP_005694630.1; NC_000907.1. DR STRING; 71421.HI0723; -. DR EnsemblBacteria; AAC22381; AAC22381; HI_0723. DR GeneID; 949570; -. DR KEGG; hin:HI0723; -. DR PATRIC; 20190069; VBIHaeInf48452_0755. DR eggNOG; ENOG4105D37; Bacteria. DR eggNOG; COG0168; LUCA. DR KO; K03498; -. DR OMA; YRHLLQW; -. DR OrthoDB; EOG63589N; -. DR PhylomeDB; P44843; -. DR Proteomes; UP000000579; 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:0005267; F:potassium channel activity; ISS:UniProtKB. DR GO; GO:0030955; F:potassium ion binding; ISS:UniProtKB. DR GO; GO:0022820; F:potassium ion symporter activity; IEA:InterPro. DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB. DR InterPro; IPR003445; Cat_transpt. DR InterPro; IPR004772; TrkH. DR Pfam; PF02386; TrkH; 1. DR PIRSF; PIRSF006247; TrkH; 1. DR TIGRFAMs; TIGR00933; 2a38; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion channel; KW Ion transport; Membrane; Potassium; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 487 Trk system potassium uptake protein TrkH. FT /FTId=PRO_0000070477. FT TOPO_DOM 1 2 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 3 29 Helical. {ECO:0000250}. FT TOPO_DOM 30 35 Periplasmic. {ECO:0000250}. FT TRANSMEM 36 57 Helical. {ECO:0000250}. FT TOPO_DOM 58 65 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 66 90 Helical. {ECO:0000250}. FT TOPO_DOM 91 ? Periplasmic. {ECO:0000250}. FT INTRAMEM ? 97 {ECO:0000250}. FT INTRAMEM 98 109 Helical; Pore-forming. {ECO:0000250}. FT INTRAMEM 110 115 {ECO:0000250}. FT TOPO_DOM 116 124 Periplasmic. {ECO:0000250}. FT TRANSMEM 125 150 Helical. {ECO:0000250}. FT TOPO_DOM 151 177 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 178 202 Helical. {ECO:0000250}. FT TOPO_DOM 203 205 Periplasmic. {ECO:0000250}. FT INTRAMEM 206 206 {ECO:0000250}. FT INTRAMEM 207 218 Helical; Pore-forming. {ECO:0000250}. FT INTRAMEM 219 224 {ECO:0000250}. FT TOPO_DOM 225 234 Periplasmic. {ECO:0000250}. FT INTRAMEM 235 250 Helical. {ECO:0000250}. FT INTRAMEM 251 ? {ECO:0000250}. FT TOPO_DOM ? 277 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 278 298 Helical. {ECO:0000250}. FT TOPO_DOM 299 ? Periplasmic. {ECO:0000250}. FT INTRAMEM ? 304 {ECO:0000250}. FT INTRAMEM 305 320 Helical; Pore-forming. {ECO:0000250}. FT INTRAMEM 321 326 {ECO:0000250}. FT TOPO_DOM 327 334 Periplasmic. {ECO:0000250}. FT INTRAMEM 335 346 Helical. {ECO:0000250}. FT INTRAMEM 347 359 Note=Loop between two helices. FT {ECO:0000250}. FT INTRAMEM 360 ? Helical. {ECO:0000250}. FT TOPO_DOM ? 393 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 394 421 Helical. {ECO:0000250}. FT TOPO_DOM 422 423 Periplasmic. {ECO:0000250}. FT INTRAMEM 424 425 {ECO:0000250}. FT INTRAMEM 426 436 Helical; Pore-forming. {ECO:0000250}. FT INTRAMEM 437 443 {ECO:0000250}. FT TOPO_DOM 444 455 Periplasmic. {ECO:0000250}. FT INTRAMEM 456 467 Helical. {ECO:0000250}. FT INTRAMEM 468 ? {ECO:0000250}. FT TOPO_DOM ? 487 Cytoplasmic. {ECO:0000250}. FT REGION 110 115 Selectivity filter part 1. {ECO:0000250}. FT REGION 219 224 Selectivity filter part 2. {ECO:0000250}. FT REGION 321 326 Selectivity filter part 3. {ECO:0000250}. FT REGION 438 443 Selectivity filter part 4. {ECO:0000250}. FT BINDING 111 111 Potassium ion; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 112 112 Potassium ion; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 221 221 Potassium ion; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 439 439 Potassium ion; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 487 AA; 53469 MW; 91A8F38C37F4540A CRC64; MRILSIIRII GILVMCFSGT MLVPAFVALI YGDGGGKAFM QAFMLSLIAG TLLWWPCHHH KQELRSRDGF LIVVAFWLVL GSLATLPLLL FDSPHLTIAS AVFEAFSGLT TTGATVMTGL DNLPKSILFY RQFLQWLGGM GIIVLAVAII PLLGIGGTQL YRAESSGPLK DQKSLPKISE VAKALWIIYA SLTVLCAIAY WLSGMNLFDA IGHSFSTISN GGFSTHDASI GYFNQASIYW VTTIFMLIGG VNFSLHISAF LALGKRNIWR NYWKDPEFRF FLTMQIIFIG IVSLSLYGYG LVSDINEAVT KGALQLTSMS MTAGYTIFDI DNLPPFIGLL LVISAVIGGC GGSTTGGLKA IRTLILWKQI DRELHSLIHP NLVQPIRIGK NRLAPRMIES IWAFFIIFIL VYWGCVFAVI LCGMNTFDAM GAVFATLTNA GPGLGFIHES FIGVPESAKL VFSFAMICGR LEMFSLIVLF IPSYWKK // ID TRPB_HAEIN Reviewed; 397 AA. AC P43760; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Tryptophan synthase beta chain; DE EC=4.2.1.20; GN Name=trpB; OrderedLocusNames=HI_1431; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23078.1; -; Genomic_DNA. DR PIR; I64122; I64122. DR RefSeq; NP_439580.1; NC_000907.1. DR RefSeq; WP_005693932.1; NC_000907.1. DR ProteinModelPortal; P43760; -. DR SMR; P43760; 4-388. DR STRING; 71421.HI1431; -. DR EnsemblBacteria; AAC23078; AAC23078; HI_1431. DR GeneID; 950336; -. DR KEGG; hin:HI1431; -. DR PATRIC; 20191557; VBIHaeInf48452_1488. DR eggNOG; ENOG4105CG0; Bacteria. DR eggNOG; COG0133; LUCA. DR KO; K01696; -. DR OMA; IPEMLYP; -. DR OrthoDB; EOG6GFGH7; -. DR PhylomeDB; P43760; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR006654; Trp_synth_beta. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR PANTHER; PTHR10314:SF3; PTHR10314:SF3; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 397 Tryptophan synthase beta chain. FT /FTId=PRO_0000098953. FT MOD_RES 88 88 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 397 AA; 43257 MW; C74C070862FDF32B CRC64; MSDTLLNPYF GEFGGMYVPE ILVPVLKQLE QAFVEAQNDP TFQAEFADLL KNYAGRPTAL TLCRNLTKGT KTKLYLKRED LLHGGAHKTN QVLGQILLAK RMGKTRIIAE TGAGQHGVAT ALACAMLDMP CRVYMGAKDV ERQSPNVFRM RLMGAEVIPV QKGSCSLKDA CCEAMRDWSA NYETTHYLLG TAAGPHPFPT IVREFQKMIG EETKRQILER EGRLPDTVIA AVGGGSNAIG MFADFIDESN VRLIGVEPAG KGIETGEHGA PLKHGTTGIY FGMKSPIMQD KDGQIEESYS ISAGLDFPSV GPQHAYLNEI GRADYVSITD EEALNAFQEL AKHEGIIPAL ESSHALAYAL KLIKQNPEKE QLLVVNLSGR GDKDIFTVDK ILNGGAN // ID TORZ_HAEIN Reviewed; 825 AA. AC P44798; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=Trimethylamine-N-oxide reductase; DE Short=TMAO reductase; DE Short=Trimethylamine oxidase; DE EC=1.7.2.3; DE Flags: Precursor; GN Name=torZ; Synonyms=bisC; OrderedLocusNames=HI_0643; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into CC trimethylamine; an anaerobic reaction coupled to energy-yielding CC reactions. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Trimethylamine + 2 (ferricytochrome c)-subunit CC + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + CC 2 H(+). CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC -!- CAUTION: Was originally assigned to be a biotin sulfoxide CC reductase hence the original gene designation of bisC. CC {ECO:0000305|PubMed:7542800}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22303.1; -; Genomic_DNA. DR PIR; H64083; H64083. DR RefSeq; NP_438803.1; NC_000907.1. DR RefSeq; WP_010869026.1; NC_000907.1. DR ProteinModelPortal; P44798; -. DR SMR; P44798; 46-823. DR STRING; 71421.HI0643; -. DR EnsemblBacteria; AAC22303; AAC22303; HI_0643. DR GeneID; 950790; -. DR KEGG; hin:HI0643; -. DR PATRIC; 20189901; VBIHaeInf48452_0672. DR eggNOG; ENOG4107QY8; Bacteria. DR eggNOG; COG0243; LUCA. DR KO; K07812; -. DR OMA; HGEQTHW; -. DR OrthoDB; EOG6NWBKD; -. DR PhylomeDB; P44798; -. DR BioCyc; RETL1328306-WGS:GSTH-4546-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR006658; BisC. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR00509; bisC_fam; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Molybdenum; Oxidoreductase; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1 40 Tat-type signal. {ECO:0000255|PROSITE- FT ProRule:PRU00648}. FT CHAIN 41 825 Trimethylamine-N-oxide reductase. FT /FTId=PRO_0000019166. FT METAL 187 187 Molybdenum. {ECO:0000250}. SQ SEQUENCE 825 AA; 91053 MW; 4254287D42B45E5B CRC64; MKKNNVNEQR RDFLKKTSLG VAGSALSGGM VGVVSKSAVA KEAEMKTVVT AAHWGSIGVV VQDGKVVKSG PAIEPAVPNE LQTVVADQLY SERRVKCPMV RKGFLANPGK SDTTMRGRDE WVRVSWDEAL DLVHNQLKRV RDEHGSTGIF AGSYGWFSCG SLHASRTLLQ RYMNATGGFV GHKGDYSTGA AQVIMPHVLG TIEVYEQQTS WESILESSDI IVLWSANPLT TMRIAWMSTD QKGIEYFKKF QASGKRIICI DPQKSETCQM LNAEWIPVNT ATDVPLMLGI AHTLVEQGKH DKDFLKKYTS GYAKFEEYLL GKTDGQPKTA EWAAKICGVP AETIKQLAAD FASKRTMLMG GWGMQRQRHG EQTHWMLVTL ASMLGQIGLP GGGFGLSYHY SNGGVPTATG GIIGSITASP SGKAGAKTWL DDTSKSAFPL ARIADVLLHP GKKIQYNGTE ITYPDIKAVY WAGGNPFVHH QDTNTLVKAF QKPDVVIVNE VNWTPTARMA DIVLPATTSY ERNDLTMAGD YSMMSVYPMK QVVPPQFEAK NDYDIFVELA KRAGVEEQYT EGKTEMEWLE EFYNAAFSAA RANRVAMPRF DKFWAENKPL SFEAGEAAKK WVRYGEFRED PLLNPLGTPS GKIEIFSDVV EKMNYNDCKG HPSWMEPEEF AGNVTEEYPL ALVTPHPYYR LHSQLAHTSL RQKYAVNDRE PVMIHPEDAA ARGIKDGDIV RIHSKRGQVL AGAAVTENII KGTVALHEGA WYDPMYLGES EKPLCKNGCA NVLTRDEGTS KLAQGNSPNT CIVQIEKFIG VAPEVTVFKQ PKQVA // ID TRPD_HAEIN Reviewed; 333 AA. AC P43858; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 114. DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211}; DE EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211}; GN Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; GN OrderedLocusNames=HI_1389; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield CC N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00211}; CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00211}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase CC family. {ECO:0000255|HAMAP-Rule:MF_00211}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23035.1; -; Genomic_DNA. DR PIR; E64121; E64121. DR RefSeq; NP_439542.1; NC_000907.1. DR RefSeq; WP_005693973.1; NC_000907.1. DR ProteinModelPortal; P43858; -. DR SMR; P43858; 3-331. DR STRING; 71421.HI1389; -. DR EnsemblBacteria; AAC23035; AAC23035; HI_1389. DR GeneID; 950894; -. DR KEGG; hin:HI1389; -. DR PATRIC; 20191473; VBIHaeInf48452_1447. DR eggNOG; ENOG4107QYG; Bacteria. DR eggNOG; COG0547; LUCA. DR KO; K00766; -. DR OMA; MIVLNAG; -. DR OrthoDB; EOG6D5G6B; -. DR PhylomeDB; P43858; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1030.10; -; 1. DR HAMAP; MF_00211; TrpD; 1. DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR TIGRFAMs; TIGR01245; trpD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glycosyltransferase; Magnesium; Metal-binding; KW Reference proteome; Transferase; Tryptophan biosynthesis. FT CHAIN 1 333 Anthranilate phosphoribosyltransferase. FT /FTId=PRO_0000154448. FT REGION 84 85 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 91 94 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 109 117 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT METAL 93 93 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 225 225 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 226 226 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 226 226 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 81 81 Anthranilate 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 81 81 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 89 89 Phosphoribosylpyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 112 112 Anthranilate 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 121 121 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 167 167 Anthranilate 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. SQ SEQUENCE 333 AA; 35625 MW; 80BFF7676E0494B9 CRC64; MQHNQLLEQL YSGHSLSTSE STALFNAVIQ GELSNEQIAA MLIALKVRGA NTEEISGAVA ASLQNAKAFP YPNYPFADIV GTGGNGQNTI NISTTSAIVA ASMGAKIAKH GNRSVSSKSG ASDVLTALSV NVNVTPEQAR QALDEIGVCF LFAQQYHSGF RHVAPVRAAL KTRTIFNILG PLINPARPTY HLLGVYAPEL VKTYAETAVA LEHQHSFVVH GSGLDEVALH GETQVAEIKN GKIEYFTLTP EDFGLKTQSL ESLRGGEPQE NAQYLTALLQ GKGKAEHANA VAANTALLLK LFGYDDLKQN VQNVLAHLVS GKAFETLQKL TTY // ID TOLR_HAEIN Reviewed; 139 AA. AC P43769; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Protein TolR; GN Name=tolR; OrderedLocusNames=HI_0384; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1479; RX PubMed=8921895; DOI=10.1016/0378-1119(96)00338-1; RA Sen K., Sikkema D.J., Murphy T.F.; RT "Isolation and characterization of the Haemophilus influenzae tolQ, RT tolR, tolA and tolB genes."; RL Gene 178:75-81(1996). CC -!- FUNCTION: Involved in the TonB-independent uptake of proteins. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ExbD/TolR 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; L42023; AAC22042.1; -; Genomic_DNA. DR EMBL; U32470; AAC44595.1; -; Genomic_DNA. DR PIR; H64064; H64064. DR RefSeq; NP_438545.1; NC_000907.1. DR RefSeq; WP_005649190.1; NC_000907.1. DR PDB; 2JWK; NMR; -; A/B=59-130. DR PDB; 2JWL; NMR; -; A/B=59-130. DR PDBsum; 2JWK; -. DR PDBsum; 2JWL; -. DR ProteinModelPortal; P43769; -. DR SMR; P43769; 59-130. DR STRING; 71421.HI0384; -. DR EnsemblBacteria; AAC22042; AAC22042; HI_0384. DR GeneID; 949489; -. DR KEGG; hin:HI0384; -. DR PATRIC; 20189317; VBIHaeInf48452_0402. DR eggNOG; COG0848; LUCA. DR KO; K03560; -. DR OMA; HINNINA; -. DR OrthoDB; EOG6D2KWK; -. DR PhylomeDB; P43769; -. DR EvolutionaryTrace; P43769; -. DR Proteomes; UP000000579; 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:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003400; ExbD. DR Pfam; PF02472; ExbD; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 139 Protein TolR. FT /FTId=PRO_0000129143. FT TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 13 37 Helical. {ECO:0000255}. FT TOPO_DOM 38 139 Periplasmic. {ECO:0000255}. FT STRAND 61 65 {ECO:0000244|PDB:2JWK}. FT STRAND 67 69 {ECO:0000244|PDB:2JWK}. FT STRAND 71 75 {ECO:0000244|PDB:2JWK}. FT STRAND 78 83 {ECO:0000244|PDB:2JWK}. FT HELIX 85 98 {ECO:0000244|PDB:2JWK}. FT STRAND 104 108 {ECO:0000244|PDB:2JWK}. FT HELIX 114 126 {ECO:0000244|PDB:2JWK}. SQ SEQUENCE 139 AA; 15258 MW; 3A4D8FB633AF854F CRC64; MARRQRKAIK SEINIVPFLD VLLVLVLIFM ATAPIISQSV QVELPDSVQS QEVSNEDKVP VILEVAGIGK YAISIGGERQ EGLTEEMVTQ LSRQEFDKDN NTLFLVGGAK EVPYEEVIKA LNLLHLAGIK SVGLMTNPI // ID TPIS_HAEIN Reviewed; 263 AA. AC P43727; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 111. 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=tpi; GN OrderedLocusNames=HI_0678; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 219-223. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22337.1; -; Genomic_DNA. DR PIR; G64085; G64085. DR RefSeq; NP_438838.1; NC_000907.1. DR RefSeq; WP_005661219.1; NC_000907.1. DR ProteinModelPortal; P43727; -. DR SMR; P43727; 3-262. DR STRING; 71421.HI0678; -. DR EnsemblBacteria; AAC22337; AAC22337; HI_0678. DR GeneID; 950739; -. DR KEGG; hin:HI0678; -. DR PATRIC; 20189973; VBIHaeInf48452_0708. DR eggNOG; ENOG4105CP7; Bacteria. DR eggNOG; COG0149; LUCA. DR KO; K01803; -. DR OMA; YHHESDE; -. DR OrthoDB; EOG66QM23; -. DR PhylomeDB; P43727; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; KW Reference proteome. FT CHAIN 1 263 Triosephosphate isomerase. FT /FTId=PRO_0000090226. FT REGION 10 12 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT REGION 242 243 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 104 104 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 176 176 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 182 182 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT BINDING 221 221 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00147}. SQ SEQUENCE 263 AA; 27287 MW; 6F6D53108CAA132B CRC64; MARRPLVMGN WKLNGSKAFT KELIEGLKAE LHDVTGCDVA IAPPVMYLGT AEAALSGCGC SCGGKSVIQL GAQNVDINVK GAFTGDISTE MLKDFGAKYI IIGHSERRTY HKESDEFVAK KFGALKEAGL VPVLCIGESE AENEAGKTEE VCARQIDAVI NALGVEAFNG AVIAYEPIWA IGTGKSATPA QAQAVHAFIR GHIAAKSQAV AEQVIIQYGG SVNDANAAEL FTQPDIDGAL VGGASLKAPA FAVIVKAAAA AKN // ID TRMA_HAEIN Reviewed; 363 AA. AC P31812; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 110. DE RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011}; DE EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; DE Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011}; DE AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011}; GN Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011}; GN OrderedLocusNames=HI_0848; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1438213; DOI=10.1073/pnas.89.21.10252; RA Tomb J.-F.; RT "A periplasmic protein disulfide oxidoreductase is required for RT transformation of Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10252-10256(1992). CC -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the CC formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, CC and that of position 341 (m5U341) in tmRNA (transfer-mRNA). CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(54) in tRNA = CC S-adenosyl-L-homocysteine + 5-methyluracil(54) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(341) in tmRNA CC = S-adenosyl-L-homocysteine + 5-methyluracil(341) in tmRNA. CC {ECO:0000255|HAMAP-Rule:MF_01011}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA M5U methyltransferase family. CC TrmA subfamily. {ECO:0000255|HAMAP-Rule:MF_01011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22505.1; -; Genomic_DNA. DR EMBL; M94205; AAA24958.1; -; Genomic_DNA. DR PIR; C64098; C64098. DR RefSeq; NP_439008.1; NC_000907.1. DR RefSeq; WP_005693197.1; NC_000907.1. DR ProteinModelPortal; P31812; -. DR SMR; P31812; 2-363. DR STRING; 71421.HI0848; -. DR EnsemblBacteria; AAC22505; AAC22505; HI_0848. DR GeneID; 949860; -. DR KEGG; hin:HI0848; -. DR PATRIC; 20190351; VBIHaeInf48452_0889. DR eggNOG; ENOG4107R9T; Bacteria. DR eggNOG; COG2265; LUCA. DR KO; K00557; -. DR OMA; IKMLEWA; -. DR OrthoDB; EOG6V4GKM; -. DR PhylomeDB; P31812; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01011; RNA_methyltr_TrmA; 1. DR InterPro; IPR030390; MeTrfase_TrmA_AS. DR InterPro; IPR030391; MeTrfase_TrmA_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR011869; TrmA_MeTrfase. DR InterPro; IPR010280; U5_MeTrfase_fam. DR Pfam; PF05958; tRNA_U5-meth_tr; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02143; trmA_only; 1. DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1. DR PROSITE; PS01230; TRMA_1; 1. DR PROSITE; PS01231; TRMA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 363 tRNA/tmRNA (uracil-C(5))- FT methyltransferase. FT /FTId=PRO_0000161864. FT ACT_SITE 321 321 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT ACT_SITE 355 355 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT BINDING 187 187 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 215 215 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01011}. FT BINDING 220 220 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 236 236 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT BINDING 296 296 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01011}. FT CONFLICT 42 42 R -> A (in Ref. 2; AAA24958). FT {ECO:0000305}. SQ SEQUENCE 363 AA; 42230 MW; 256346FD418E0E14 CRC64; MQLPISQYNE LLQKKLEKLT ALLHPFNAPD IQVFDSPTSH YRMRAEFRIW HEQDDFYHIM FDQATLQRYR VDEFPIASML INRMMQTLLP LLKQQEVLHK KLFQIDYLST LSNKIIVSLL YHKTLTEEWE SAAKNLKDLL EKQDFDVQII GRASKQKICF EQDYVDEVLP VNGRNYVYRQ VENSFTQPNA TVNCKMLEWA IDCTQNSEGD LLELYCGNGN FSIALAQNFR KVLATEIAKP SVAAAQFNIA ENKVDNLQII RMSAEEFTQA MNGVRAFNRL KGIDLKSYEC NTIFVDPPRA GLDPDTVKLV QNYDRILYIS CNPHTLCDNL VELSKTHRIE KAALFDQFPY TDHMESGLWL IRK // ID TRPG_HAEIN Reviewed; 193 AA. AC P71381; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE Short=ASII; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, GATase component; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; GN Name=trpG; OrderedLocusNames=HI_1388; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23034.1; -; Genomic_DNA. DR PIR; D64121; D64121. DR RefSeq; NP_439540.1; NC_000907.1. DR RefSeq; WP_005693974.1; NC_000907.1. DR ProteinModelPortal; P71381; -. DR SMR; P71381; 2-193. DR STRING; 71421.HI1388; -. DR EnsemblBacteria; AAC23034; AAC23034; HI_1388. DR GeneID; 950293; -. DR KEGG; hin:HI1388; -. DR PATRIC; 20191469; VBIHaeInf48452_1445. DR eggNOG; ENOG4105DDQ; Bacteria. DR eggNOG; COG0512; LUCA. DR KO; K01658; -. DR OMA; LPICAFQ; -. DR OrthoDB; EOG6M9F11; -. DR PhylomeDB; P71381; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glutamine amidotransferase; Lyase; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 193 Anthranilate synthase component 2. FT /FTId=PRO_0000056878. FT DOMAIN 3 193 Glutamine amidotransferase type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT REGION 57 59 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 134 135 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT ACT_SITE 84 84 Nucleophile; for GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 170 170 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 172 172 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT BINDING 88 88 Glutamine. FT {ECO:0000250|UniProtKB:P00900}. SQ SEQUENCE 193 AA; 21509 MW; 53FF77844D568B51 CRC64; MANILFLDNF DSFTYNLVDQ FRVLGHNVTI YRNDCDLEKL VETALNTPDT ILALSPGPGT PSEAGILLPL IERLKNQVPI IGVCLGHQAL IQAFGGKVVH AGEVLHGKVS RISHDNEAMF KDLANPMPVA RYHSLMGQDL PKEFIVNAEY NGIIMAIRHR DLPICAFQFH PESILTVQGS QLLQQSIEWL LNR // ID TORY_HAEIN Reviewed; 368 AA. AC P44799; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Cytochrome c-type protein TorY; GN Name=torY; OrderedLocusNames=HI_0644; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the anaerobic respiratory chain of CC trimethylamine-N-oxide reductase TorZ. Required for electron CC transfer to the TorZ terminal enzyme (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- PTM: Binds 5 heme groups per subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TorC/TorY 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; L42023; AAC22304.1; -; Genomic_DNA. DR PIR; I64083; I64083. DR RefSeq; NP_438804.2; NC_000907.1. DR ProteinModelPortal; P44799; -. DR STRING; 71421.HI0644; -. DR EnsemblBacteria; AAC22304; AAC22304; HI_0644. DR GeneID; 950598; -. DR KEGG; hin:HI0644; -. DR PATRIC; 20189903; VBIHaeInf48452_0673. DR eggNOG; ENOG4105CUW; Bacteria. DR eggNOG; COG3005; LUCA. DR KO; K07821; -. DR OMA; FNANQWI; -. DR OrthoDB; EOG6RNQDS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR009154; Membr-bd_4haem_cyt_TorC. DR InterPro; IPR011031; Multihaem_cyt. DR InterPro; IPR005126; NapC/NirT_cyt_c_N. DR Pfam; PF03264; Cytochrom_NNT; 1. DR PIRSF; PIRSF000014; 4_hem_cytch_TorC; 1. DR SUPFAM; SSF46626; SSF46626; 1. DR SUPFAM; SSF48695; SSF48695; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Electron transport; Heme; Iron; Membrane; Metal-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 368 Cytochrome c-type protein TorY. FT /FTId=PRO_0000108431. FT TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 9 25 Helical. {ECO:0000255}. FT TOPO_DOM 26 368 Periplasmic. {ECO:0000255}. FT METAL 43 43 Iron (heme 1 axial ligand). FT {ECO:0000250}. FT METAL 72 72 Iron (heme 2 axial ligand). FT {ECO:0000250}. FT METAL 132 132 Iron (heme 3 axial ligand). FT {ECO:0000250}. FT METAL 164 164 Iron (heme 4 axial ligand). FT {ECO:0000250}. FT METAL 320 320 Iron (heme 5 axial ligand). FT {ECO:0000250}. FT BINDING 39 39 Heme 1 (covalent). {ECO:0000250}. FT BINDING 42 42 Heme 1 (covalent). {ECO:0000250}. FT BINDING 68 68 Heme 2 (covalent). {ECO:0000250}. FT BINDING 71 71 Heme 2 (covalent). {ECO:0000250}. FT BINDING 128 128 Heme 3 (covalent). {ECO:0000250}. FT BINDING 131 131 Heme 3 (covalent). {ECO:0000250}. FT BINDING 160 160 Heme 4 (covalent). {ECO:0000250}. FT BINDING 163 163 Heme 4 (covalent). {ECO:0000250}. FT BINDING 316 316 Heme 5 (covalent). {ECO:0000250}. FT BINDING 319 319 Heme 5 (covalent). {ECO:0000250}. SQ SEQUENCE 368 AA; 41145 MW; F6656FDC9C1DBBA5 CRC64; MAMSKMKKIV TALCLVGVGV GALWGSQWIM HKTSTPEFCA SCHSMSYPQQ EWEGSSHFAN AKGVRAQCSD CHIPKEGWHY VKAKFIALKD LWYEAQGKIE NKEKYEAHRA EMAQRVWKDM KANDSETCRS CHSFDAMELS KQTKLAKQTH TEAQTNGQTC IDCHKGIVHF LPEVHGDQNT QKSSAVQGGT LSDGSAIFAT EMVKATNDKG NEVRLMPYAE LMQWKVDGDQ IQGTLHGWQQ VGAEAVVYQE LGKRITLALM DEDARNHVQV LKIVHDAVTD SDWKEISVAV NVAKEKMTSD LTTLNQYGNQ LNQTQCSGCH AAIGADHYTA NQWIGVVNSM KDRTSMKKDE VRALTIYLQR NAKDMAKQ // ID TRMB_HAEIN Reviewed; 246 AA. AC P44648; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057}; GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; GN OrderedLocusNames=HI_0340; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC22002.1; -; Genomic_DNA. DR PIR; F64148; F64148. DR RefSeq; NP_438504.1; NC_000907.1. DR RefSeq; WP_005694335.1; NC_000907.1. DR ProteinModelPortal; P44648; -. DR STRING; 71421.HI0340; -. DR EnsemblBacteria; AAC22002; AAC22002; HI_0340. DR GeneID; 949446; -. DR KEGG; hin:HI0340; -. DR PATRIC; 20189223; VBIHaeInf48452_0357. DR eggNOG; ENOG4105CZ1; Bacteria. DR eggNOG; COG0220; LUCA. DR KO; K03439; -. DR OMA; IKLGHGV; -. DR OrthoDB; EOG6K6VBC; -. DR PhylomeDB; P44648; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central. DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR Pfam; PF02390; Methyltransf_4; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00091; TIGR00091; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 246 tRNA (guanine-N(7)-)-methyltransferase. FT /FTId=PRO_0000171333. FT REGION 225 228 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT ACT_SITE 152 152 {ECO:0000250}. FT BINDING 77 77 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 102 102 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 129 129 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 152 152 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01057}. FT BINDING 156 156 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. FT BINDING 188 188 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01057}. SQ SEQUENCE 246 AA; 28053 MW; 1FF1DFD12FEC729D CRC64; MTQTFADQKR KTVETAEFTE DGRYKRKVRS FVLRTGRLSE FQRNMMNDNW GTLGLDYQTE PFDFAKIYGN DNPVVLEIGF GMGKSLVDMA FANPDKNYLG IEVHTPGVGA CIAYAVEKGV TNLRVICHDA TEILRDSIAD GALGGLQLFF PDPWHKAKHH KRRIVQPHFV TQVIQKLGEN GFIHMATDWE NYAEQMLEVL SANTDLVNTS KNGDYIPRPD FRPLTKFEAR GYKLGHGVWD LYFVKK // ID TRMN6_HAEIN Reviewed; 232 AA. AC P44702; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 03-NOV-2009, sequence version 2. DT 11-MAY-2016, entry version 100. DE RecName: Full=tRNA1(Val) (adenine(37)-N6)-methyltransferase; DE EC=2.1.1.223; DE AltName: Full=tRNA m6A37 methyltransferase; GN OrderedLocusNames=HI_0423; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Specifically methylates the adenine in position 37 of CC tRNA(1)(Val) (anticodon cmo5UAC). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(37) in CC tRNA(1)(Val) = S-adenosyl-L-homocysteine + N(6)-methyladenine(37) CC in tRNA(1)(Val). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. tRNA CC (adenine-N(6)-)-methyltransferase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22079.1; 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; L42023; AAC22079.1; ALT_INIT; Genomic_DNA. DR PIR; C64152; C64152. DR RefSeq; NP_438584.1; NC_000907.1. DR RefSeq; WP_005693741.1; NC_000907.1. DR ProteinModelPortal; P44702; -. DR STRING; 71421.HI0423; -. DR EnsemblBacteria; AAC22079; AAC22079; HI_0423. DR GeneID; 949527; -. DR KEGG; hin:HI0423; -. DR PATRIC; 20189399; VBIHaeInf48452_0443. DR eggNOG; ENOG4107S47; Bacteria. DR eggNOG; COG4123; LUCA. DR KO; K15460; -. DR OrthoDB; EOG66TGB2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0016430; F:tRNA (adenine-N6-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01872; tRNA_methyltr_YfiC; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR InterPro; IPR022882; tRNA_adenine-N6_MeTrfase. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 232 tRNA1(Val) (adenine(37)-N6)- FT methyltransferase. FT /FTId=PRO_0000169267. SQ SEQUENCE 232 AA; 26563 MW; 2384499D04EC9CC5 CRC64; MSRFTFKQFH INQNSCAMKV GTDGILLGAW ADVKHCKNIL DMGCGTGLLA LMLAQRTEEN CQIQAVELDP IAAKQAQENI NNSVWKNRIQ LTQVDIQHFL QTTEQTFDLI VANPPYFEQG IACKNEEREL ARYTKQSHLN WLEWAATRLS ENGRISFVLP YEAGKTLTKS TALFCIKQTN VITKIGKTPQ RMLLTFAKQP EVLMQDQLVI YDADNQYTEA FIELTKDFYL KF // ID TRPA_HAEIN Reviewed; 268 AA. AC P43759; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; GN OrderedLocusNames=HI_1432; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage CC of indoleglycerol phosphate to indole and glyceraldehyde 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23079.1; -; Genomic_DNA. DR PIR; A64123; A64123. DR RefSeq; NP_439581.1; NC_000907.1. DR RefSeq; WP_005693930.1; NC_000907.1. DR ProteinModelPortal; P43759; -. DR SMR; P43759; 3-268. DR STRING; 71421.HI1432; -. DR EnsemblBacteria; AAC23079; AAC23079; HI_1432. DR GeneID; 950337; -. DR KEGG; hin:HI1432; -. DR PATRIC; 20191559; VBIHaeInf48452_1489. DR eggNOG; ENOG4105F6H; Bacteria. DR eggNOG; COG0159; LUCA. DR KO; K01695; -. DR OMA; PVFICPP; -. DR OrthoDB; EOG6RVG0K; -. DR PhylomeDB; P43759; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00131; Trp_synth_alpha; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR018204; Trp_synthase_alpha_AS. DR InterPro; IPR002028; Trp_synthase_suA. DR Pfam; PF00290; Trp_syntA; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00262; trpA; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 268 Tryptophan synthase alpha chain. FT /FTId=PRO_0000098787. FT ACT_SITE 49 49 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. FT ACT_SITE 60 60 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. SQ SEQUENCE 268 AA; 28731 MW; E2FED02E50099E84 CRC64; MSRFETQFAT LNAKNEGAFV PFVTLCDPTF DRSFEIICTL VDNGADALEL GFPFSDPLLD GPVIQAANNR ALTAGHSSED SLKLLEKVRS KYPEIPISLL LCANLIFAKG LDAFYQRCAE VGVDAVLVAD IPLLAKGDYV QTAKKHGIQP VFICPPNADE KTIQGVAKNS EGYTYLVSRA GVTSAENQAH AANLDTLVEK LKAHNAPPIL QGFGIAQPEQ VKEALSLGTA GAISGSATVK IIERNLDNHE QCLAELAEFV QTMKAATK // ID TRPC_HAEIN Reviewed; 477 AA. AC P46451; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=Tryptophan biosynthesis protein TrpCF; DE Includes: DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; DE Includes: DE RecName: Full=N-(5'-phospho-ribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpC; OrderedLocusNames=HI_1389.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- FUNCTION: Bifunctional enzyme that catalyzes two sequential steps CC of tryptophan biosynthetic pathway. The first reaction is CC catalyzed by the isomerase, coded by the TrpF domain; the second CC reaction is catalyzed by the synthase, coded by the TrpC domain CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpC family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpF 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; L42023; AAC23036.1; -; Genomic_DNA. DR RefSeq; NP_439543.1; NC_000907.1. DR RefSeq; WP_005693972.1; NC_000907.1. DR ProteinModelPortal; P46451; -. DR SMR; P46451; 16-278. DR STRING; 71421.HI1389.1; -. DR EnsemblBacteria; AAC23036; AAC23036; HI_1389.1. DR GeneID; 950301; -. DR KEGG; hin:HI1389.1; -. DR PATRIC; 20191475; VBIHaeInf48452_1448. DR eggNOG; ENOG4105DK0; Bacteria. DR eggNOG; COG0134; LUCA. DR eggNOG; COG0135; LUCA. DR KO; K13498; -. DR OMA; SFILECK; -. DR OrthoDB; EOG6WT8JX; -. DR PhylomeDB; P46451; -. DR UniPathway; UPA00035; UER00042. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_00134_B; IGPS_B; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR001240; PRAI. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; SSF51366; 2. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Decarboxylase; Isomerase; Lyase; KW Multifunctional enzyme; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 477 Tryptophan biosynthesis protein TrpCF. FT /FTId=PRO_0000154279. FT REGION 13 275 Indole-3-glycerol phosphate synthase. FT REGION 276 477 N-(5'-phosphoribosyl)anthranilate FT isomerase. SQ SEQUENCE 477 AA; 53306 MW; B1435FAEFA24379E CRC64; MMITQDFTKP IDSATVLQKI VLDKAQWVKA KEKEFPLSQF KQNIQNSDRS FYDALAKGTH QKPAYILECK KASPSKGLIR AEFNLEEIAN VYKHYASAVS VLTDEKYFQG NFEFLPLVRD IVSQPVLCKD FMISEYQVYL ARYYQVDAIL LMLSVVNDET YRVLADLAHS LGMGVLTETS NEEEFERALA LGAKIIGVNN RNLHDLTVDL NRVVELTKKY ADCIPADVRI ISESGIYNHK QIHQLQKVAH GFLIGSSLMG NQDLNNAVRS VIFGENKVCG LTRAQDVKIV YENGALYGGL IFAEHSKRSV SLRQAQELVT AAPLRFVGVF QNQEIDFIVK IASQLQLYAV QLHGAETEAF ITALRQQLPK NTQIWKAISV NTEAQSAVDF TDDLNVDRYI FDSQTANQQG GTGKTFDWSL IPENLKHKII LAGGISPNNV EQAIAQGCLG LDLNSGVESS AGVKDQEKVR LVFNNIY // ID TRUD_HAEIN Reviewed; 339 AA. AC P44039; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=tRNA pseudouridine synthase D; DE EC=5.4.99.27; DE AltName: Full=tRNA pseudouridine(13) synthase; DE AltName: Full=tRNA pseudouridylate synthase D; DE AltName: Full=tRNA-uridine isomerase D; GN Name=truD; OrderedLocusNames=HI_0701; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 13 in transfer RNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(13) = tRNA pseudouridine(13). CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 TRUD 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; L42023; AAC22360.1; -; Genomic_DNA. DR PIR; C64012; C64012. DR RefSeq; NP_438860.1; NC_000907.1. DR RefSeq; WP_005694586.1; NC_000907.1. DR ProteinModelPortal; P44039; -. DR STRING; 71421.HI0701; -. DR EnsemblBacteria; AAC22360; AAC22360; HI_0701. DR GeneID; 949727; -. DR KEGG; hin:HI0701; -. DR PATRIC; 20190021; VBIHaeInf48452_0732. DR eggNOG; ENOG4106NZV; Bacteria. DR eggNOG; COG0585; LUCA. DR KO; K06176; -. DR OMA; LWLWVEK; -. DR OrthoDB; EOG6FRCSP; -. DR PhylomeDB; P44039; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01082; TruD; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001656; PsdUridine_synth_TruD. DR InterPro; IPR020119; PsdUridine_synth_TruD_CS. DR InterPro; IPR011760; PsdUridine_synth_TruD_insert. DR PANTHER; PTHR13326; PTHR13326; 1. DR Pfam; PF01142; TruD; 2. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1. DR PROSITE; PS50984; TRUD; 1. DR PROSITE; PS01268; UPF0024; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 339 tRNA pseudouridine synthase D. FT /FTId=PRO_0000152500. FT DOMAIN 155 311 TRUD. FT ACT_SITE 80 80 Nucleophile. {ECO:0000250}. SQ SEQUENCE 339 AA; 38548 MW; 335C5BFCED34CBC1 CRC64; MLEQLPYLAL KTPPKTTALL KAECADFIVK EHLGYEMSGD GEFVALYVRK TDCNTLFVGE KLAKFAGVSE RNMGYAGLKD RRAVTEQWFC LQMPGMETPD FSQFELDGVE ILTVTRHNRK IRTGSLEGNY FDILLRGAEE SDELKARLDF VANFGFPNYF TEQRFGRDGH NLTQALRWAQ GEIKVKDRKK RSFYLSAARS EIFNLVVAAR IEKSTINQVL PNDIVQLAGS HSWFKADEKE DLTALQVRLE NQDILLTAPL IGEDILAASE IENEIVNQHS AFDPLMKQER MKAARRPLLM KAKGFSWAFE PEGLRLKFYL PAGSYATALV RELVNYTEE // ID TSAB_HAEIN Reviewed; 236 AA. AC P43990; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB; GN Name=tsaB; OrderedLocusNames=HI_0388; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaD and TsaE; this reaction does CC not require ATP in vitro. TsaB seems to play an indirect role in CC the t(6)A biosynthesis pathway, possibly in regulating the core CC enzymatic function of TsaD (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22046.1; -; Genomic_DNA. DR PIR; H64006; H64006. DR RefSeq; NP_438549.1; NC_000907.1. DR RefSeq; WP_005693782.1; NC_000907.1. DR ProteinModelPortal; P43990; -. DR STRING; 71421.HI0388; -. DR EnsemblBacteria; AAC22046; AAC22046; HI_0388. DR GeneID; 950019; -. DR KEGG; hin:HI0388; -. DR PATRIC; 20189325; VBIHaeInf48452_0406. DR eggNOG; ENOG41072GX; Bacteria. DR eggNOG; COG1214; LUCA. DR KO; K14742; -. DR OMA; EPIYLRN; -. DR OrthoDB; EOG6D8B8B; -. DR PhylomeDB; P43990; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022496; T6A_YeaZ. DR Pfam; PF00814; Peptidase_M22; 1. DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Reference proteome; tRNA processing. FT CHAIN 1 236 tRNA threonylcarbamoyladenosine FT biosynthesis protein TsaB. FT /FTId=PRO_0000096991. SQ SEQUENCE 236 AA; 26084 MW; 79E8D313BF877D97 CRC64; MQNLTLLALD TSTEACSVAL LYRGEKTHIN ELAQRTHTKR ILPMIDEILA NSGLGLNQVD ALAFGRGPGS FTGVRVGAGI AQGLAFGADL PVIPISNLTA MAQAAFELHQ AENVVAAIDA RMNEVYFSQV VREKVRSDFG EFFQWREIIS EQVCSPEQAI NQLQNDNAFR VGTGWAAYSQ FTEKNLTGSD IALPNALYML ELAQVEYLQK HTISALEIEP IYLRNEVTWK KLPGRE // ID TRUA_HAEIN Reviewed; 269 AA. AC P45291; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171}; DE EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171}; GN Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; Synonyms=hisT; GN OrderedLocusNames=HI_1644; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in CC the anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_00171}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38- CC 40). {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA CC family. {ECO:0000255|HAMAP-Rule:MF_00171}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23291.1; -; Genomic_DNA. DR PIR; F64134; F64134. DR RefSeq; NP_439786.1; NC_000907.1. DR RefSeq; WP_005693653.1; NC_000907.1. DR ProteinModelPortal; P45291; -. DR SMR; P45291; 2-261. DR STRING; 71421.HI1644; -. DR EnsemblBacteria; AAC23291; AAC23291; HI_1644. DR GeneID; 950487; -. DR KEGG; hin:HI1644; -. DR PATRIC; 20192033; VBIHaeInf48452_1720. DR eggNOG; ENOG4105DI7; Bacteria. DR eggNOG; COG0101; LUCA. DR KO; K06173; -. DR OMA; PWRNVHH; -. DR OrthoDB; EOG6Z9B4R; -. DR PhylomeDB; P45291; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.580; -; 1. DR Gene3D; 3.30.70.660; -; 1. DR HAMAP; MF_00171; TruA; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001406; PsdUridine_synth_TruA. DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom. DR InterPro; IPR020095; PsdUridine_synth_TruA_C. DR InterPro; IPR020094; PsdUridine_synth_TruA_N. DR PANTHER; PTHR11142; PTHR11142; 1. DR Pfam; PF01416; PseudoU_synth_1; 2. DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00071; hisT_truA; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 269 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057388. FT ACT_SITE 51 51 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00171}. FT BINDING 109 109 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00171}. SQ SEQUENCE 269 AA; 30530 MW; 3F1A694C41AE3116 CRC64; MKIALGIEYN GQNYYGWQRQ EKVRSVQEEL EKALSHIANE KIEIFCAGRT DSGVSGTGQV VHFETNAVRP EKAWAFGTNA HLPDDIAVSW AKQVDDEFHA RFSATARRYR YILYCNKLRS AILAGGITHC HLDLDAEKMH QAGQCLLGEQ DFSSFRAAQC QSHTPWRNVH HLNVSRIGKY IIVDIQANAF VHHMVRNIVG SLIEVGTGNQ PIEWMQWLLE QKNRQLAAPT AKPDGLYLVD VIYPQKFDIP KRPIGPLFLE DGLLNRPLK // ID TRUC_HAEIN Reviewed; 239 AA. AC P44197; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 86. DE RecName: Full=tRNA pseudouridine synthase C; DE EC=5.4.99.26; DE AltName: Full=tRNA pseudouridine(65) synthase; DE AltName: Full=tRNA pseudouridylate synthase C; DE AltName: Full=tRNA-uridine isomerase C; GN Name=truC; OrderedLocusNames=HI_1435; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 65 in transfer RNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(65) = tRNA pseudouridine(65). CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23084.2; Type=Frameshift; Positions=160; 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; L42023; AAC23084.2; ALT_FRAME; Genomic_DNA. DR PIR; I64029; I64029. DR ProteinModelPortal; P44197; -. DR EnsemblBacteria; AAC23084; AAC23084; HI_1435. DR PATRIC; 20191571; VBIHaeInf48452_1495. DR OMA; QHVFPIH; -. DR OrthoDB; EOG6P070X; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR PROSITE; PS01129; PSI_RLU; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 239 tRNA pseudouridine synthase C. FT /FTId=PRO_0000162715. FT ACT_SITE 54 54 {ECO:0000250}. SQ SEQUENCE 239 AA; 27777 MW; 6D9409FD8E379CE4 CRC64; MLEILYQDGF LVAVNKPAGM LVHRSWLDPH ETQFVMQTLR DQIGQHVFPI HRLDRPTSGV LLFALSSEIA NLMCEQFEQK YVQKSYLAVV RGYLQGKERI DYPLKIQLDK IADKFSQEDK EPQEAITDYE GLKIVEMPYP AGRYQTARYS LVKLIPHTGR KHXLRXHMKH VFHPIXGDTQ YGDLHQNRAL MSHLGCSRLF LHSDSLSFIH PITKEQITIT AGLDEQWQQL MNQFGWENV // ID TYPA_HAEIN Reviewed; 616 AA. AC P44910; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=GTP-binding protein TypA/BipA homolog; GN Name=typA; OrderedLocusNames=HI_0864; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Not known; probably interacts with the ribosomes in a CC GTP dependent manner. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. TypA CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22523.1; -; Genomic_DNA. DR PIR; G64160; G64160. DR RefSeq; NP_439024.1; NC_000907.1. DR RefSeq; WP_005693211.1; NC_000907.1. DR ProteinModelPortal; P44910; -. DR STRING; 71421.HI0864; -. DR EnsemblBacteria; AAC22523; AAC22523; HI_0864. DR GeneID; 949876; -. DR KEGG; hin:HI0864; -. DR PATRIC; 20190383; VBIHaeInf48452_0905. DR eggNOG; ENOG4105CI3; Bacteria. DR eggNOG; COG1217; LUCA. DR KO; K06207; -. DR OMA; SMLFTIN; -. DR OrthoDB; EOG67HJSM; -. DR PhylomeDB; P44910; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; 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; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR006298; TypA_GTP-bd. DR PANTHER; PTHR23115:SF14; PTHR23115:SF14; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR TIGRFAMs; TIGR01394; TypA_BipA; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 616 GTP-binding protein TypA/BipA homolog. FT /FTId=PRO_0000091554. FT DOMAIN 8 204 tr-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT NP_BIND 17 24 GTP. {ECO:0000250}. FT NP_BIND 80 84 GTP. {ECO:0000250}. FT NP_BIND 134 137 GTP. {ECO:0000250}. SQ SEQUENCE 616 AA; 68470 MW; D4FCBD69621828C8 CRC64; MKNEIDIKKL RNIAIIAHVD HGKTTLVDKL LQQSGTFESA RGDVDERVMD SNDLEKERGI TILAKNTAIN WNDYRINIVD TPGHADFGGE VERVLSMVDS VLLVVDAFDG PMPQTRFVTQ KAFAHGLKPI VVINKVDRPG ARPDWVVDQV FDLFVNLGAS DEQLDFPIIY ASALNGVAGL EHEDLAEDMT PLFEAIVKHV EPPKVELDAP FQMQISQLDY NNYVGVIGIG RIKRGSIKPN QPVTIINSEG KTRQGRIGQV LGHLGLQRYE EDVAYAGDIV AITGLGELNI SDTICDINTV EALPSLTVDE PTVTMFFCVN TSPFAGQEGK YVTSRQILER LNKELVHNVA LRVEETPNPD EFRVSGRGEL HLSVLIENMR REGYELAVSR PKVIYRDIDG KKQEPYEQVT IDVEEQHQGS VMEALGIRKG EVRDMLPDGK GRVRLEYIIP SRGLIGFRGD FMTMTSGTGL LYSSFSHYDE IKGGEIGQRK NGVLISNATG KALGYALFGL QERGKLMIDA NIEVYEGQII GIHSRSNDLT VNCLQGKKLT NMRASGKDDA IVLTTPVKFS LEQAIEFIDD DELVEVTPES IRIRKKLLTE NDRKRANRTT TSTSTH // ID TYRR_HAEIN Reviewed; 318 AA. AC P44694; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 121. DE RecName: Full=Transcriptional regulatory protein TyrR; GN Name=tyrR; OrderedLocusNames=HI_0410; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION. RX PubMed=9226720; DOI=10.1006/prep.1997.0757; RA Zhu Q., Zhao S., Somerville R.L.; RT "Expression, purification, and functional analysis of the TyrR protein RT of Haemophilus influenzae."; RL Protein Expr. Purif. 10:237-246(1997). RN [3] RP STRUCTURE BY NMR OF 258-318. RX PubMed=11344327; DOI=10.1110/ps.45301; RA Wang Y., Zhao S., Somerville R.L., Jardetzky O.; RT "Solution structure of the DNA-binding domain of the TyrR protein of RT Haemophilus influenzae."; RL Protein Sci. 10:592-598(2001). CC -!- FUNCTION: Involved in transcriptional regulation of aromatic amino CC acid biosynthesis and transport. {ECO:0000269|PubMed:9226720}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 sigma-54 factor interaction domain. CC {ECO:0000255|PROSITE-ProRule:PRU00193}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22069.1; -; Genomic_DNA. DR PIR; C64066; C64066. DR RefSeq; NP_438572.1; NC_000907.1. DR RefSeq; WP_005693758.1; NC_000907.1. DR PDB; 1G2H; NMR; -; A=258-318. DR PDBsum; 1G2H; -. DR ProteinModelPortal; P44694; -. DR SMR; P44694; 258-318. DR STRING; 71421.HI0410; -. DR EnsemblBacteria; AAC22069; AAC22069; HI_0410. DR GeneID; 950074; -. DR KEGG; hin:HI0410; -. DR PATRIC; 20189371; VBIHaeInf48452_0429. DR eggNOG; ENOG4108JU8; Bacteria. DR eggNOG; COG3283; LUCA. DR KO; K03721; -. DR OMA; QDAESEM; -. DR OrthoDB; EOG6WHNMG; -. DR PhylomeDB; P44694; -. DR EvolutionaryTrace; P44694; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR030828; HTH_TypR. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002078; Sigma_54_int. DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1. DR Pfam; PF00158; Sigma54_activat; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR04381; HTH_TypR; 1. DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1. DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; ATP-binding; KW Complete proteome; Cytoplasm; DNA-binding; Nucleotide-binding; KW Reference proteome; Transcription; Transcription regulation; KW Two-component regulatory system. FT CHAIN 1 318 Transcriptional regulatory protein TyrR. FT /FTId=PRO_0000081343. FT DOMAIN 15 239 Sigma-54 factor interaction; truncated. FT {ECO:0000255|PROSITE-ProRule:PRU00193}. FT NP_BIND 43 50 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00193}. FT NP_BIND 101 110 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00193}. FT DNA_BIND 293 312 H-T-H motif. FT STRAND 271 274 {ECO:0000244|PDB:1G2H}. FT HELIX 277 289 {ECO:0000244|PDB:1G2H}. FT HELIX 293 299 {ECO:0000244|PDB:1G2H}. FT HELIX 305 312 {ECO:0000244|PDB:1G2H}. FT TURN 313 315 {ECO:0000244|PDB:1G2H}. SQ SEQUENCE 318 AA; 35954 MW; 5AB2AD8D994044F8 CRC64; MTISKFNPQK PFECFIVQSE AMKSAVENAK RFAMFDAPLL IQGETGSGKD LLAKACHYQS LRRDKKFIAV NCAGLPDEDA ESEMFGRKVG DSETIGFFEY ANKGTVLLDG IAELSLSLQA KLLRFLTDGS FRRVGEEKEH YANVRVICTS QVPLHLLVEQ GKVRADLFHR LNVLTINVPA LRDRMADIEP LAQGFLQEIS EELKIAKPTF DKDFLLYLQK YDWKGNVREL YNTLYRACSL VQDNHLTIES LNLALPQSAV ISLDEFENKT LDEIIGFYEA QVLKLFYAEY PSTRKLAQRL GVSHTAIANK LKQYGIGK // ID TRPE_HAEIN Reviewed; 518 AA. AC P43761; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 111. DE RecName: Full=Anthranilate synthase component 1; DE Short=AS; DE Short=ASI; DE EC=4.1.3.27; GN Name=trpE; OrderedLocusNames=HI_1387; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00897}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P00897}; CC -!- ENZYME REGULATION: Feedback inhibited by tryptophan. CC {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anthranilate synthase component I CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23033.1; -; Genomic_DNA. DR PIR; C64121; C64121. DR RefSeq; NP_439539.1; NC_000907.1. DR RefSeq; WP_005693976.1; NC_000907.1. DR ProteinModelPortal; P43761; -. DR STRING; 71421.HI1387; -. DR EnsemblBacteria; AAC23033; AAC23033; HI_1387. DR GeneID; 950300; -. DR KEGG; hin:HI1387; -. DR PATRIC; 20191467; VBIHaeInf48452_1444. DR eggNOG; ENOG4105CRQ; Bacteria. DR eggNOG; COG0147; LUCA. DR KO; K01657; -. DR OMA; MQDQDFT; -. DR OrthoDB; EOG6D5G6B; -. DR PhylomeDB; P43761; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR006805; Anth_synth_I_N. DR InterPro; IPR005257; Anth_synth_I_TrpE. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF04715; Anth_synt_I_N; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PIRSF; PIRSF001373; TrpE; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. DR TIGRFAMs; TIGR00565; trpE_proteo; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Magnesium; Metal-binding; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 518 Anthranilate synthase component 1. FT /FTId=PRO_0000154093. FT REGION 291 293 Tryptophan binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 328 329 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 483 485 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 361 361 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 498 498 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 41 41 Tryptophan. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 449 449 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 469 469 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 485 485 Chorismate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P00897}. SQ SEQUENCE 518 AA; 57522 MW; D597A7D56E921409 CRC64; MNIQTQAFIA VTAQPIPYYA DTTAIFNTLC QSNSNSLLLD SAEIGSKNSL QSLILVNAAV KITCLGHNVT FKALNNNGKQ VLKEIHPKLT ALGKVSAVNF EDEFSVQFLP LDNQLDEDSK LQSATIFDGL RVISSLYQHS QTPIFLGGLF AYDLVANFIP MDGITLKNDG INCPDYSFYL AEHLITIDHQ NQQATLKSFC FAQEEQVNIA KTSLSIAQKL KNIDHVLSIK AASDEVKTNF DDPEFTGIVK ALKHHINIGD VFQIVPSRRF SLACPNTLAS YAQLKQNNPS PYMFYMNDED FILFGASPES ALKYAPENRQ LEIYPIAGSR PRGFDAHGNI DPELDARLEL ELRLDHKEQA EHLMLVDLAR NDIARVCQSG TRKVAELMQV DRYSHIMHLV SRVVGKLRPE LDALHAYQAC MNMGTLTGAP KIKAMQLIYQ FEQQKRHSYG GAVGYLTSDG HFDTCIVIRS AFVQNGMAHV QAGCGEVLDS DPQMEADETR HKAAAVLKAI RQVNTQAK // ID TRUB_HAEIN Reviewed; 312 AA. AC P45142; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080}; DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080}; DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080}; GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01080}; GN OrderedLocusNames=HI_1289; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_01080}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(55) = tRNA pseudouridine(55). CC {ECO:0000255|HAMAP-Rule:MF_01080}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22938.1; -; Genomic_DNA. DR PIR; B64170; B64170. DR RefSeq; NP_439441.1; NC_000907.1. DR RefSeq; WP_010869174.1; NC_000907.1. DR ProteinModelPortal; P45142; -. DR SMR; P45142; 10-283. DR STRING; 71421.HI1289; -. DR EnsemblBacteria; AAC22938; AAC22938; HI_1289. DR GeneID; 950222; -. DR KEGG; hin:HI1289; -. DR PATRIC; 20191261; VBIHaeInf48452_1341. DR eggNOG; ENOG4105D0T; Bacteria. DR eggNOG; COG0130; LUCA. DR KO; K03177; -. DR OMA; YELQFIR; -. DR OrthoDB; EOG6358D3; -. DR PhylomeDB; P45142; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.130.10; -; 1. DR HAMAP; MF_01080; TruB_bact; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB. DR InterPro; IPR015240; tRNA_sdUridine_synth_fam1_C. DR InterPro; IPR032819; TruB_C. DR PANTHER; PTHR13767; PTHR13767; 1. DR Pfam; PF09157; TruB-C_2; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00431; TruB; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 312 tRNA pseudouridine synthase B. FT /FTId=PRO_0000121843. FT ACT_SITE 48 48 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01080}. SQ SEQUENCE 312 AA; 35085 MW; C423FAD92B6E0295 CRC64; MSRPRKRWRD VDGVFLLDKP QGMSSNDIMQ KVKRLFQANK AGHTGALDPL ATGMLPICLG EATKFSQFLL DADKRYLVTA KLGERTDTSD AEGQVVETRE VNLETQQILT ALEQFRGDIL QVPTMFSALK HNGKPLYEYA RQGITVEREA RPITIFELNF IEYNAPFLTL EVHCSKGTYI RTLVDDLGEV LGCGAHVTML RRTAVADYPV AEMMPINELQ LLAESFPLSE LDRLLLPTDT AVSKLPALHL DAEQSKAIGF GQRVKFANEQ QLSGQVRLFS AENLFLGVLN RREYYSPTTI NYTIRITSLP FL // ID TUSE_HAEIN Reviewed; 109 AA. AC P45184; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Sulfurtransferase TusE homolog; DE EC=2.8.1.-; GN Name=tusE; OrderedLocusNames=HI_1371; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be part of a sulfur-relay system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DsrC/TusE 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; L42023; AAC23018.1; -; Genomic_DNA. DR PIR; A64120; A64120. DR RefSeq; NP_439522.1; NC_000907.1. DR RefSeq; WP_005693989.1; NC_000907.1. DR ProteinModelPortal; P45184; -. DR STRING; 71421.HI1371; -. DR EnsemblBacteria; AAC23018; AAC23018; HI_1371. DR GeneID; 950285; -. DR KEGG; hin:HI1371; -. DR PATRIC; 20191429; VBIHaeInf48452_1425. DR eggNOG; ENOG4108Z0T; Bacteria. DR eggNOG; COG2920; LUCA. DR KO; K11179; -. DR OMA; EYNTSPA; -. DR OrthoDB; EOG60390T; -. DR PhylomeDB; P45184; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR025526; DsrC-like_dom. DR InterPro; IPR007453; DsrC/TusE. DR Pfam; PF04358; DsrC; 1. DR PIRSF; PIRSF006223; DsrC_TusE; 1. DR SUPFAM; SSF69721; SSF69721; 1. DR TIGRFAMs; TIGR03342; dsrC_tusE_dsvC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 109 Sulfurtransferase TusE homolog. FT /FTId=PRO_0000168791. FT ACT_SITE 108 108 Cysteine persulfide intermediate. FT {ECO:0000250}. SQ SEQUENCE 109 AA; 12336 MW; 32E3E25A02A4D3D0 CRC64; MLNINGIEVE TDKDGYLLHS QQWNEDAARA IAQLESIELT DAHWEVIYFV RDFYQEYNTS PAIRMLVKAM AEKLGADKGN SRYLQHLFPE GPAKQATKLA GLPKPAKCL // ID TRML_HAEIN Reviewed; 160 AA. AC P44868; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=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 TrmL {ECO:0000255|HAMAP-Rule:MF_01885}; GN Name=trmL {ECO:0000255|HAMAP-Rule:MF_01885}; GN OrderedLocusNames=HI_0766; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT. RX PubMed=12596263; DOI=10.1002/prot.10323; RA Lim K., Zhang H., Tempczyk A., Krajewski W., Bonander N., Toedt J., RA Howard A., Eisenstein E., Herzberg O.; RT "Structure of the YibK methyltransferase from Haemophilus influenzae RT (HI0766): a cofactor bound at a site formed by a knot."; RL Proteins 51:56-67(2003). CC -!- FUNCTION: Methylates the ribose at the nucleotide 34 wobble CC position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and CC tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S- CC adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. CC {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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01885, CC ECO:0000269|PubMed:12596263}. 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; L42023; AAC22424.1; -; Genomic_DNA. DR PIR; E64158; E64158. DR RefSeq; NP_438925.1; NC_000907.1. DR RefSeq; WP_005652354.1; NC_000907.1. DR PDB; 1J85; X-ray; 2.00 A; A=1-160. DR PDB; 1MXI; X-ray; 1.70 A; A=1-160. DR PDBsum; 1J85; -. DR PDBsum; 1MXI; -. DR ProteinModelPortal; P44868; -. DR SMR; P44868; 1-156. DR DIP; DIP-29173N; -. DR STRING; 71421.HI0766; -. DR EnsemblBacteria; AAC22424; AAC22424; HI_0766. DR GeneID; 949782; -. DR KEGG; hin:HI0766; -. DR PATRIC; 20190183; VBIHaeInf48452_0805. DR eggNOG; ENOG4108UIQ; Bacteria. DR eggNOG; COG0219; LUCA. DR KO; K03216; -. DR OMA; AGLDYWH; -. DR OrthoDB; EOG6RG038; -. DR PhylomeDB; P44868; -. DR EvolutionaryTrace; P44868; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. 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 GO; GO:0002131; P:wobble position cytosine ribose methylation; IBA:GO_Central. DR GO; GO:0002132; P:wobble position uridine ribose methylation; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 160 tRNA (cytidine(34)-2'-O)- FT methyltransferase. FT /FTId=PRO_0000159819. FT BINDING 78 78 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP-Rule:MF_01885, FT ECO:0000269|PubMed:12596263}. FT BINDING 100 100 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01885, FT ECO:0000269|PubMed:12596263}. FT BINDING 122 122 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01885, FT ECO:0000269|PubMed:12596263}. FT BINDING 130 130 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01885, FT ECO:0000269|PubMed:12596263}. FT STRAND 3 8 {ECO:0000244|PDB:1MXI}. FT HELIX 12 25 {ECO:0000244|PDB:1MXI}. FT STRAND 28 34 {ECO:0000244|PDB:1MXI}. FT HELIX 42 45 {ECO:0000244|PDB:1MXI}. FT TURN 46 48 {ECO:0000244|PDB:1J85}. FT HELIX 51 53 {ECO:0000244|PDB:1MXI}. FT STRAND 54 56 {ECO:0000244|PDB:1MXI}. FT STRAND 58 62 {ECO:0000244|PDB:1MXI}. FT HELIX 63 70 {ECO:0000244|PDB:1MXI}. FT STRAND 73 78 {ECO:0000244|PDB:1MXI}. FT STRAND 83 85 {ECO:0000244|PDB:1MXI}. FT HELIX 86 88 {ECO:0000244|PDB:1MXI}. FT STRAND 95 99 {ECO:0000244|PDB:1MXI}. FT TURN 102 104 {ECO:0000244|PDB:1MXI}. FT HELIX 108 111 {ECO:0000244|PDB:1MXI}. FT HELIX 116 118 {ECO:0000244|PDB:1MXI}. FT STRAND 119 121 {ECO:0000244|PDB:1MXI}. FT HELIX 133 147 {ECO:0000244|PDB:1MXI}. FT TURN 148 152 {ECO:0000244|PDB:1MXI}. SQ SEQUENCE 160 AA; 18401 MW; 0E09ADB31E575026 CRC64; MLDIVLYEPE IPQNTGNIIR LCANTGFRLH LIEPLGFTWD DKRLRRSGLD YHEFAEIKRH KTFEAFLESE KPKRLFALTT KGCPAHSQVK FKLGDYLMFG PETRGIPMSI LNEMPMEQKI RIPMTANSRS MNLSNSVAVT VYEAWRQLGY KGAVNLPEVK // ID TRMO_HAEIN Reviewed; 239 AA. AC P44740; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=tRNA (adenine(37)-N6)-methyltransferase {ECO:0000305}; DE EC=2.1.1.- {ECO:0000250|UniProtKB:P28634}; DE AltName: Full=tRNA (m6t6A37) methyltransferase; DE AltName: Full=tRNA methyltransferase O {ECO:0000250|UniProtKB:P28634}; GN Name=trmO {ECO:0000250|UniProtKB:P28634}; GN Synonyms=tsaA {ECO:0000250|UniProtKB:P28634}; GN OrderedLocusNames=HI_0510; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT. RG Northeast structural genomics consortium (NESG); RT "X-ray structure of yaeb from Haemophilus influenzae. Northeast RT structural genomics research consortium (nesgc) target ir47."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase CC responsible for the addition of the methyl group in the formation CC of N6-methyl-N6-threonylcarbamoyladenosine at position 37 CC (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The CC methyl group of m(6)t(6)A37 appears to slightly improve the CC efficiency of the tRNA decoding ability. Binds to tRNA. CC {ECO:0000250|UniProtKB:P28634}. CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}. CC -!- SIMILARITY: Contains 1 TsaA-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU01003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22168.1; -; Genomic_DNA. DR PIR; I64153; I64153. DR RefSeq; NP_438668.1; NC_000907.1. DR RefSeq; WP_005693665.1; NC_000907.1. DR PDB; 1XQB; X-ray; 2.85 A; A/B=1-239. DR PDBsum; 1XQB; -. DR ProteinModelPortal; P44740; -. DR SMR; P44740; 1-231. DR STRING; 71421.HI0510; -. DR EnsemblBacteria; AAC22168; AAC22168; HI_0510. DR GeneID; 949577; -. DR KEGG; hin:HI0510; -. DR PATRIC; 20189573; VBIHaeInf48452_0529. DR eggNOG; ENOG4108R96; Bacteria. DR eggNOG; COG1720; LUCA. DR OMA; FASRSTH; -. DR OrthoDB; EOG60SCKQ; -. DR PhylomeDB; P44740; -. DR EvolutionaryTrace; P44740; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB. DR GO; GO:0089715; F:tRNA m6t6A37 methyltransferase activity; ISS:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB. DR Gene3D; 2.40.30.70; -; 1. DR InterPro; IPR023370; TsaA-like. DR InterPro; IPR023368; UPF0066_cons_site. DR Pfam; PF01980; UPF0066; 1. DR SUPFAM; SSF118196; SSF118196; 1. DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1. DR PROSITE; PS01318; TSAA_1; 1. DR PROSITE; PS51668; TSAA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 239 tRNA (adenine(37)-N6)-methyltransferase. FT /FTId=PRO_0000155619. FT DOMAIN 6 147 TsaA-like. {ECO:0000255|PROSITE- FT ProRule:PRU01003}. FT REGION 23 25 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 64 65 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 127 130 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 92 92 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 102 102 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000250}. FT STRAND 4 6 {ECO:0000244|PDB:1XQB}. FT STRAND 10 13 {ECO:0000244|PDB:1XQB}. FT HELIX 19 21 {ECO:0000244|PDB:1XQB}. FT TURN 26 28 {ECO:0000244|PDB:1XQB}. FT STRAND 33 38 {ECO:0000244|PDB:1XQB}. FT TURN 40 42 {ECO:0000244|PDB:1XQB}. FT TURN 45 50 {ECO:0000244|PDB:1XQB}. FT HELIX 51 53 {ECO:0000244|PDB:1XQB}. FT STRAND 55 62 {ECO:0000244|PDB:1XQB}. FT HELIX 88 90 {ECO:0000244|PDB:1XQB}. FT STRAND 100 113 {ECO:0000244|PDB:1XQB}. FT STRAND 116 123 {ECO:0000244|PDB:1XQB}. FT STRAND 131 137 {ECO:0000244|PDB:1XQB}. FT HELIX 140 143 {ECO:0000244|PDB:1XQB}. FT STRAND 163 165 {ECO:0000244|PDB:1XQB}. FT HELIX 167 176 {ECO:0000244|PDB:1XQB}. FT TURN 177 179 {ECO:0000244|PDB:1XQB}. FT TURN 181 186 {ECO:0000244|PDB:1XQB}. FT STRAND 210 213 {ECO:0000244|PDB:1XQB}. FT STRAND 216 219 {ECO:0000244|PDB:1XQB}. FT STRAND 225 227 {ECO:0000244|PDB:1XQB}. SQ SEQUENCE 239 AA; 27214 MW; E63FE78E7706106E CRC64; MNDLTLSPIA IIHTPYKEKF SVPRQPNLVE DGVGIVELLP PYNSPEAVRG LEQFSHLWLI FQFDQIQQGK WQPTVRPPRL GGNQRVGVFA SRATHRPNPL GLSKVELRQV ECINGNIFLH LGAVDLVDGT PIFDIKPYIA YADSEPNAQS SFAQEKLPVK LTVEFTEQAK SAVKKREEKR PHLSRFIRQV LEQDPRPAYQ QGKPSDRIYG MSLYEFNVKW RIKAGTVNCV EVIEIEKDK // ID TSAE_HAEIN Reviewed; 158 AA. AC P44492; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE; GN Name=tsaE; Synonyms=yjeE; OrderedLocusNames=HI_0065; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APOPROEIN AND IN COMPLEX RP WITH MG-ADP, FUNCTION, ATPASE ACTIVITY, AND KINETIC PARAMETERS. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=12112691; DOI=10.1002/prot.10114; RA Teplyakov A., Obmolova G., Tordova M., Thanki N., Bonander N., RA Eisenstein E., Howard A.J., Gilliland G.L.; RT "Crystal structure of the YjeE protein from Haemophilus influenzae: a RT putative Atpase involved in cell wall synthesis."; RL Proteins 48:220-226(2002). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the CC N6 group of A37, together with TsaD and TsaB. TsaE seems to play CC an indirect role in the t(6)A biosynthesis pathway, possibly in CC regulating the core enzymatic function of TsaD (By similarity). CC Displays ATPase activity in vitro. {ECO:0000250, CC ECO:0000269|PubMed:12112691}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=38 uM for ATP {ECO:0000269|PubMed:12112691}; CC Note=kcat is 0.42 min(-1) for ATP hydrolysis.; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TsaE 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; L42023; AAC21743.1; -; Genomic_DNA. DR PIR; H64141; H64141. DR RefSeq; NP_438238.1; NC_000907.1. DR RefSeq; WP_005693857.1; NC_000907.1. DR PDB; 1FL9; X-ray; 2.50 A; A/B/C=1-158. DR PDB; 1HTW; X-ray; 1.70 A; A/B/C=1-158. DR PDBsum; 1FL9; -. DR PDBsum; 1HTW; -. DR ProteinModelPortal; P44492; -. DR SMR; P44492; 1-158. DR STRING; 71421.HI0065; -. DR EnsemblBacteria; AAC21743; AAC21743; HI_0065. DR GeneID; 950963; -. DR KEGG; hin:HI0065; -. DR PATRIC; 20188585; VBIHaeInf48452_0066. DR eggNOG; ENOG4105K8N; Bacteria. DR eggNOG; COG0802; LUCA. DR KO; K06925; -. DR OMA; EPHEAPD; -. DR OrthoDB; EOG6GBMHT; -. DR PhylomeDB; P44492; -. DR EvolutionaryTrace; P44492; -. DR Proteomes; UP000000579; 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:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003442; T6A_TsaE. DR Pfam; PF02367; TsaE; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00150; T6A_YjeE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; KW tRNA processing. FT CHAIN 1 158 tRNA threonylcarbamoyladenosine FT biosynthesis protein TsaE. FT /FTId=PRO_0000096208. FT NP_BIND 43 48 ATP. FT METAL 47 47 Magnesium. FT METAL 113 113 Magnesium. FT BINDING 11 11 ATP. FT BINDING 136 136 ATP; via carbonyl oxygen. FT STRAND 3 8 {ECO:0000244|PDB:1HTW}. FT HELIX 11 28 {ECO:0000244|PDB:1HTW}. FT STRAND 34 39 {ECO:0000244|PDB:1HTW}. FT HELIX 46 56 {ECO:0000244|PDB:1HTW}. FT TURN 67 69 {ECO:0000244|PDB:1HTW}. FT STRAND 71 76 {ECO:0000244|PDB:1HTW}. FT STRAND 79 85 {ECO:0000244|PDB:1HTW}. FT HELIX 94 97 {ECO:0000244|PDB:1HTW}. FT HELIX 100 104 {ECO:0000244|PDB:1HTW}. FT STRAND 105 107 {ECO:0000244|PDB:1HTW}. FT STRAND 109 114 {ECO:0000244|PDB:1HTW}. FT HELIX 115 118 {ECO:0000244|PDB:1HTW}. FT TURN 119 121 {ECO:0000244|PDB:1HTW}. FT STRAND 126 134 {ECO:0000244|PDB:1HTW}. FT STRAND 137 144 {ECO:0000244|PDB:1HTW}. FT HELIX 147 155 {ECO:0000244|PDB:1HTW}. SQ SEQUENCE 158 AA; 17970 MW; D148C82B95610FCD CRC64; MESLTQYIPD EFSMLRFGKK FAEILLKLHT EKAIMVYLNG DLGAGKTTLT RGMLQGIGHQ GNVKSPTYTL VEEYNIAGKM IYHFDLYRLA DPEELEFMGI RDYFNTDSIC LIEWSEKGQG ILPEADILVN IDYYDDARNI ELIAQTNLGK NIISAFSN // ID TRPR_HAEIN Reviewed; 101 AA. AC P44889; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Trp operon repressor homolog; GN Name=trpR; OrderedLocusNames=HI_0830; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is an aporepressor. When complexed with L- CC tryptophan it binds the operator region of the trp operon and CC prevents the initiation of transcription (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpR 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; L42023; AAC22488.1; -; Genomic_DNA. DR PIR; D64097; D64097. DR RefSeq; NP_438990.1; NC_000907.1. DR RefSeq; WP_005629736.1; NC_000907.1. DR ProteinModelPortal; P44889; -. DR STRING; 71421.HI0830; -. DR EnsemblBacteria; AAC22488; AAC22488; HI_0830. DR GeneID; 949844; -. DR KEGG; hin:HI0830; -. DR PATRIC; 20190315; VBIHaeInf48452_0871. DR eggNOG; ENOG4105R9M; Bacteria. DR eggNOG; COG2973; LUCA. DR KO; K03720; -. DR OMA; GQMSQRE; -. DR OrthoDB; EOG65TRW3; -. DR PhylomeDB; P44889; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.1270.10; -; 1. DR HAMAP; MF_00475; Trp_repressor; 1. DR InterPro; IPR000831; Trp_repress. DR InterPro; IPR013335; Trp_repress_bac. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR Pfam; PF01371; Trp_repressor; 1. DR PIRSF; PIRSF003196; Trp_repressor; 1. DR ProDom; PD012582; Trp_repress_bac; 1. DR SUPFAM; SSF48295; SSF48295; 1. DR TIGRFAMs; TIGR01321; TrpR; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 101 Trp operon repressor homolog. FT /FTId=PRO_0000196509. FT DNA_BIND 59 82 {ECO:0000250}. SQ SEQUENCE 101 AA; 11872 MW; 03592CCED4F6D824 CRC64; MYISRNLEQW NAFLQMLKIA FEENKAQEFL TLLLTADERD AVGLRLQIVS QLIDKNMPQR EIQQNLNTSA ATITRGSNMI KTMDPDFMQW MKQHLDLIEK N // ID TRXB_HAEIN Reviewed; 318 AA. AC P43788; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 115. DE RecName: Full=Thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9; GN Name=trxB; OrderedLocusNames=HI_1158; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22813.1; -; Genomic_DNA. DR PIR; G64186; G64186. DR RefSeq; NP_439316.1; NC_000907.1. DR RefSeq; WP_005693473.1; NC_000907.1. DR ProteinModelPortal; P43788; -. DR SMR; P43788; 5-315. DR STRING; 71421.HI1158; -. DR PRIDE; P43788; -. DR EnsemblBacteria; AAC22813; AAC22813; HI_1158. DR GeneID; 950118; -. DR KEGG; hin:HI1158; -. DR PATRIC; 20190993; VBIHaeInf48452_1209. DR eggNOG; ENOG4105C3M; Bacteria. DR eggNOG; COG0492; LUCA. DR KO; K00384; -. DR OMA; TDSGQVW; -. DR OrthoDB; EOG65XN2W; -. DR PhylomeDB; P43788; -. DR Proteomes; UP000000579; 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; -; 3. 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 1 318 Thioredoxin reductase. FT /FTId=PRO_0000166732. FT NP_BIND 36 43 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT NP_BIND 286 295 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT DISULFID 136 139 Redox-active. FT {ECO:0000250|UniProtKB:P0A9P4}. SQ SEQUENCE 318 AA; 34395 MW; 2BAEBC5DDE6020AA CRC64; MSDIKHAKLL ILGSGPAGYT AAIYAARANL KPVLVTGLQQ GGQLTTTDEI ENWPGDFEMT TGSGLMQRML QHAEKFETEI VFDHINRVDL SSRPFKLFGD VQNFTCDALI IATGASARYI GLPSEENYKG RGVSACATCD GFFYRNKPVG VIGGGNTAVE EALYLANIAS TVHLIHRRDS FRAEKILIDR LYKKVEEGKI VLHTDRTLDE VLGDNMGVTG LRLANTKTGE KEELKLDGLF VAIGHSPNTE IFQGQLELNN GYIVVKSGLD GNATATSVEG VFAAGDVMDH NYRQAITSAG TGCMAALDAE RYLDAQEA // ID TUSD_HAEIN Reviewed; 126 AA. AC P44762; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Sulfurtransferase TusD homolog; DE EC=2.8.1.-; GN Name=tusD; OrderedLocusNames=HI_0576; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be part of a sulfur-relay system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DsrE/TusD 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; L42023; AAC22234.1; -; Genomic_DNA. DR PIR; C64155; C64155. DR RefSeq; NP_438733.1; NC_000907.1. DR RefSeq; WP_005694173.1; NC_000907.1. DR ProteinModelPortal; P44762; -. DR STRING; 71421.HI0576; -. DR DNASU; 950688; -. DR EnsemblBacteria; AAC22234; AAC22234; HI_0576. DR GeneID; 950688; -. DR KEGG; hin:HI0576; -. DR PATRIC; 20189707; VBIHaeInf48452_0596. DR eggNOG; ENOG4108ZAT; Bacteria. DR eggNOG; COG1553; LUCA. DR KO; K07235; -. DR OMA; VFFYHDG; -. DR OrthoDB; EOG6BCSTH; -. DR PhylomeDB; P44762; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR InterPro; IPR017463; Sulphur_relay_TusD/DsrE. DR Pfam; PF02635; DrsE; 1. DR SUPFAM; SSF75169; SSF75169; 1. DR TIGRFAMs; TIGR03012; sulf_tusD_dsrE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 126 Sulfurtransferase TusD homolog. FT /FTId=PRO_0000214728. FT ACT_SITE 78 78 Cysteine persulfide intermediate. FT {ECO:0000250}. SQ SEQUENCE 126 AA; 13997 MW; A237D65A4C46D011 CRC64; MRYVIAVKSP IYGKQGAFLA YQFAESLIKK EHEISQIFFF QDGVSNGNAL VYPANDEVNL QKHWQMFSIT YNVPLHLCVA ASQRRGVVDN LTTPTTAHYN LAEGFTIAGL GEFIAASLNA DRVITL // ID TYRPA_HAEIN Reviewed; 400 AA. AC P44727; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Tyrosine-specific transport protein 1; DE AltName: Full=Tyrosine permease 1; GN Name=tyrP-A; OrderedLocusNames=HI_0477; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transporting tyrosine across the cytoplasmic CC membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 CC family. Mtr/TnaB/TyrP permease 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; L42023; AAC22135.1; -; Genomic_DNA. DR PIR; B64071; B64071. DR RefSeq; NP_438637.1; NC_000907.1. DR RefSeq; WP_005693687.1; NC_000907.1. DR STRING; 71421.HI0477; -. DR EnsemblBacteria; AAC22135; AAC22135; HI_0477. DR GeneID; 950656; -. DR KEGG; hin:HI0477; -. DR PATRIC; 20189507; VBIHaeInf48452_0496. DR eggNOG; ENOG4105E0U; Bacteria. DR eggNOG; COG0814; LUCA. DR KO; K03834; -. DR OMA; MFSYKVS; -. DR OrthoDB; EOG60394J; -. DR PhylomeDB; P44727; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002091; ArAA_permease. DR InterPro; IPR013061; Trp/try_permease_CS. DR InterPro; IPR013059; Trp_tyr_transpt. DR InterPro; IPR018227; Tryptophan/tyrosine_permease. DR Pfam; PF03222; Trp_Tyr_perm; 1. DR PRINTS; PR00166; AROAAPRMEASE. DR TIGRFAMs; TIGR00837; araaP; 1. DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 400 Tyrosine-specific transport protein 1. FT /FTId=PRO_0000093805. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 313 333 Helical. {ECO:0000255}. FT TRANSMEM 335 355 Helical. {ECO:0000255}. FT TRANSMEM 370 390 Helical. {ECO:0000255}. SQ SEQUENCE 400 AA; 42759 MW; CA43D5335F0F3DE7 CRC64; MNKTVGSTLL VAGTMIGAGM LAMPLTSAGI GFGFTLVLLL GLWALLTFSA LLFVELYQTA ESDAGIGTLA EQYFGKTGRI IATAVLIIFL YALIAAYISG GGSLLKDLLP ESFGDKVSVL LFTVIFGSFI VIGTHSVDKI NRVLFFVMLA AFAVVLSLML PEIKFDNLMA TPIDKALIIS ASPVFFTAFG FHGSIPSLNK YLDGNVKALR FSILVGSAIT LCAYILWQLS THGLLTQNEF LQILKEDATL NGLVKATFAI TGSNVIASAV KLFSTLALIT SFLGVGLGLL ECIEDLLKRS FNVTAGRISL GLLTFIPPLV FALFYPEGFI LALGYAGQMF AFYAVVLPVS LVWKARRAHA NLPYKVWGGN LTLIIVLVLG VLITSIPFAI RAGYLPFVVG // ID TSAC_HAEIN Reviewed; 183 AA. AC P44807; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852}; GN Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN; GN OrderedLocusNames=HI_0656; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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. Catalyzes the conversion of L-threonine, CC HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as CC the acyladenylate intermediate, with the release of diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01852}. CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|HAMAP- CC Rule:MF_01852}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22315.1; -; Genomic_DNA. DR PIR; B64156; B64156. DR RefSeq; NP_438816.1; NC_000907.1. DR RefSeq; WP_005694486.1; NC_000907.1. DR ProteinModelPortal; P44807; -. DR SMR; P44807; 4-181. DR STRING; 71421.HI0656; -. DR EnsemblBacteria; AAC22315; AAC22315; HI_0656. DR GeneID; 950161; -. DR KEGG; hin:HI0656; -. DR PATRIC; 20189927; VBIHaeInf48452_0685. DR eggNOG; ENOG4105EK0; Bacteria. DR eggNOG; COG0009; LUCA. DR KO; K07566; -. DR OMA; FGLGCNP; -. DR OrthoDB; EOG6C5RT4; -. DR PhylomeDB; P44807; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_01852; TsaC; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR023535; TC-AMP_synthase. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR PROSITE; PS51163; YRDC; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase; KW tRNA processing. FT CHAIN 1 183 Threonylcarbamoyl-AMP synthase. FT /FTId=PRO_0000202019. FT DOMAIN 1 183 YrdC-like. {ECO:0000255|HAMAP- FT Rule:MF_01852}. SQ SEQUENCE 183 AA; 20487 MW; 7B52523B5341D71D CRC64; MNREQIADAL RQNQVVAYPT EAVFGLGCNP QSESAVKKLL DLKQRPVEKG LILVAPSLDF FRPFVDFEQI NDEQLSRLQG KYERPTTWIV PAKSTTPHFL TGKFDSIAIR LCDHPSVKAL CELTGFALTS TSANLTGEPP CRTADEVRLQ FGSDFPVLNE MVGRAHNPSE IRDLRTNQLF RQG // ID TSAD_HAEIN Reviewed; 342 AA. AC P43764; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 110. 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=HI_0530; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22187.1; -; Genomic_DNA. DR PIR; H64074; H64074. DR RefSeq; NP_438688.1; NC_000907.1. DR RefSeq; WP_005694133.1; NC_000907.1. DR ProteinModelPortal; P43764; -. DR STRING; 71421.HI0530; -. DR DNASU; 950725; -. DR EnsemblBacteria; AAC22187; AAC22187; HI_0530. DR GeneID; 950725; -. DR KEGG; hin:HI0530; -. DR PATRIC; 20189613; VBIHaeInf48452_0549. DR eggNOG; ENOG4105CPM; Bacteria. DR eggNOG; COG0533; LUCA. DR KO; K01409; -. DR OMA; RDHVKRM; -. DR OrthoDB; EOG6K402S; -. DR PhylomeDB; P43764; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; 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 1 342 tRNA N6-adenosine FT threonylcarbamoyltransferase. FT /FTId=PRO_0000096964. FT REGION 134 138 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT METAL 111 111 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 115 115 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT METAL 305 305 Iron. {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 167 167 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. FT BINDING 180 180 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01445}. FT BINDING 277 277 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01445}. SQ SEQUENCE 342 AA; 36652 MW; C5F3A8F41D320DF2 CRC64; MKILGIETSC DETGVAIYDE EKGLIANQLY TQIALHADYG GVVPELASRD HIRKTAPLIK AALEEANLTA SDIDGIAYTS GPGLVGALLV GATIARSLAY AWNVPAIGVH HMEGHLLAPM LDDNSPHFPF VALLVSGGHT QLVRVDGVGK YEVIGESIDD AAGEAFDKTA KLLGLDYPGG AALSRLAEKG TPNRFTFPRP MTDRAGLDFS FSGLKTFAAN TVNQAIKNEG ELIEQTKADI AYAFQDAVVD TLAIKCKRAL KETGYKRLVI AGGVSANKKL RETLAHLMQN LGGEVFYPQP QFCTDNGAMI AYTGFLRLKQ GQHSDLAIDV KPRWAMAELP AI // ID TTCA_HAEIN Reviewed; 313 AA. AC Q57184; O05059; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=tRNA 2-thiocytidine biosynthesis protein TtcA {ECO:0000255|HAMAP-Rule:MF_01850}; GN Name=ttcA {ECO:0000255|HAMAP-Rule:MF_01850}; GN OrderedLocusNames=HI_1371.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for the thiolation of cytidine in position 32 CC of tRNA, to form 2-thiocytidine (s(2)C32). {ECO:0000255|HAMAP- CC Rule:MF_01850}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01850}. CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000255|HAMAP- CC Rule:MF_01850}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23019.1; -; Genomic_DNA. DR RefSeq; NP_439523.1; NC_000907.1. DR RefSeq; WP_005693987.1; NC_000907.1. DR ProteinModelPortal; Q57184; -. DR STRING; 71421.HI1371.1; -. DR EnsemblBacteria; AAC23019; AAC23019; HI_1371.1. DR GeneID; 950672; -. DR KEGG; hin:HI1371.1; -. DR PATRIC; 20191431; VBIHaeInf48452_1426. DR eggNOG; ENOG4105CB3; Bacteria. DR eggNOG; COG0037; LUCA. DR KO; K14058; -. DR OMA; IVQENTY; -. DR OrthoDB; EOG60KN2F; -. DR PhylomeDB; Q57184; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01850; TtcA; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 313 tRNA 2-thiocytidine biosynthesis protein FT TtcA. FT /FTId=PRO_0000168908. FT NP_BIND 50 55 ATP. {ECO:0000255|HAMAP-Rule:MF_01850}. FT MOTIF 125 128 CXXC. FT MOTIF 213 216 CXXC. SQ SEQUENCE 313 AA; 35703 MW; 646717CB802F7252 CRC64; MSELTQLAQQ EKKQTYNFNK LQKRLRRNVG NAIADFGMIE DGDKVMVCLS GGKDSYTLLD ILLNLQQSAP IKFDIVAVNL DQKQPGFPEH VLPEYLESIG VDYKIVQENT YGIVKEKIPE GKTTCSLCSR LRRGILYRTA TELGATKIAL GHHRDDMLAT LFLNMFYGGK IKSMPPKLIS DDGKQIVIRP LAYCKEKDIE KYAIAKEFPI IPCNLCGSQP NLQRQVVKEM LNTWDRQYPG RLETMFSAMQ NITLSHMCDP KLFDFKGIKH GQLIDGIEGD TAFDEERITP MQFEDEDQTD FSNKEMINFK EVN // ID TYRA_HAEIN Reviewed; 377 AA. AC P43902; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 124. DE RecName: Full=T-protein; DE Includes: DE RecName: Full=Chorismate mutase; DE Short=CM; DE EC=5.4.99.5; DE Includes: DE RecName: Full=Prephenate dehydrogenase; DE Short=PDH; DE EC=1.3.1.12; GN Name=tyrA; OrderedLocusNames=HI_1290; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Chorismate = prephenate. CC -!- CATALYTIC ACTIVITY: Prephenate + NAD(+) = 4-hydroxyphenylpyruvate CC + CO(2) + NADH. CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4- CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1. CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate CC biosynthesis; prephenate from chorismate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 chorismate mutase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00515}. CC -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00522}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22939.1; -; Genomic_DNA. DR PIR; H64114; H64114. DR RefSeq; NP_439442.1; NC_000907.1. DR RefSeq; WP_005694532.1; NC_000907.1. DR PDB; 2PV7; X-ray; 2.00 A; A/B=81-377. DR PDBsum; 2PV7; -. DR ProteinModelPortal; P43902; -. DR SMR; P43902; 92-370. DR STRING; 71421.HI1290; -. DR DNASU; 950220; -. DR EnsemblBacteria; AAC22939; AAC22939; HI_1290. DR GeneID; 950220; -. DR KEGG; hin:HI1290; -. DR PATRIC; 20191263; VBIHaeInf48452_1342. DR eggNOG; ENOG4105EHE; Bacteria. DR eggNOG; COG0287; LUCA. DR eggNOG; COG1605; LUCA. DR KO; K14187; -. DR OMA; LEQIQIW; -. DR OrthoDB; EOG618R0Z; -. DR PhylomeDB; P43902; -. DR BRENDA; 1.3.1.12; 2529. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00122; UER00961. DR EvolutionaryTrace; P43902; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central. DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0008977; F:prephenate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central. DR Gene3D; 1.20.59.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR008244; Chor_mut/prephenate_DH_T. DR InterPro; IPR002701; Chorismate_mutase. DR InterPro; IPR020822; Chorismate_mutase_type_II. DR InterPro; IPR011277; CM_T. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003099; Prephen_DH. DR Pfam; PF01817; CM_2; 1. DR Pfam; PF02153; PDH; 1. DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01799; CM_T; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS51176; PDH_ADH; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; Cytoplasm; KW Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Tyrosine biosynthesis. FT CHAIN 1 377 T-protein. FT /FTId=PRO_0000119197. FT DOMAIN 1 92 Chorismate mutase. {ECO:0000255|PROSITE- FT ProRule:PRU00515}. FT DOMAIN 101 364 Prephenate/arogenate dehydrogenase. FT {ECO:0000255|PROSITE-ProRule:PRU00522}. FT STRAND 103 106 {ECO:0000244|PDB:2PV7}. FT TURN 107 109 {ECO:0000244|PDB:2PV7}. FT HELIX 111 121 {ECO:0000244|PDB:2PV7}. FT TURN 122 124 {ECO:0000244|PDB:2PV7}. FT STRAND 127 130 {ECO:0000244|PDB:2PV7}. FT HELIX 135 137 {ECO:0000244|PDB:2PV7}. FT HELIX 138 142 {ECO:0000244|PDB:2PV7}. FT STRAND 146 150 {ECO:0000244|PDB:2PV7}. FT HELIX 154 156 {ECO:0000244|PDB:2PV7}. FT HELIX 157 164 {ECO:0000244|PDB:2PV7}. FT HELIX 165 167 {ECO:0000244|PDB:2PV7}. FT STRAND 172 176 {ECO:0000244|PDB:2PV7}. FT HELIX 182 191 {ECO:0000244|PDB:2PV7}. FT STRAND 193 201 {ECO:0000244|PDB:2PV7}. FT STRAND 214 221 {ECO:0000244|PDB:2PV7}. FT HELIX 223 225 {ECO:0000244|PDB:2PV7}. FT HELIX 227 235 {ECO:0000244|PDB:2PV7}. FT STRAND 239 242 {ECO:0000244|PDB:2PV7}. FT HELIX 245 255 {ECO:0000244|PDB:2PV7}. FT HELIX 257 270 {ECO:0000244|PDB:2PV7}. FT HELIX 277 282 {ECO:0000244|PDB:2PV7}. FT HELIX 286 299 {ECO:0000244|PDB:2PV7}. FT HELIX 303 310 {ECO:0000244|PDB:2PV7}. FT HELIX 317 335 {ECO:0000244|PDB:2PV7}. FT HELIX 339 353 {ECO:0000244|PDB:2PV7}. FT HELIX 356 370 {ECO:0000244|PDB:2PV7}. SQ SEQUENCE 377 AA; 43022 MW; 319722CFDFDE5791 CRC64; MSFMEALKDL RSEIDSLDRE LIQLFAKRLE LVSQVGKVKH QHGLPIYAPE REIAMLQARR LEAEKAGISA DLIEDVLRRF MRESYANENQ FGFKTINSDI HKIVIVGGYG KLGGLFARYL RASGYPISIL DREDWAVAES ILANADVVIV SVPINLTLET IERLKPYLTE NMLLADLTSV KREPLAKMLE VHTGAVLGLH PMFGADIASM AKQVVVRCDG RFPERYEWLL EQIQIWGAKI YQTNATEHDH NMTYIQALRH FSTFANGLHL SKQPINLANL LALSSPIYRL ELAMIGRLFA QDAELYADII MDKSENLAVI ETLKQTYDEA LTFFENNDRQ GFIDAFHKVR DWFGDYSEQF LKESRQLLQQ ANDLKQG // ID TUSA_HAEIN Reviewed; 79 AA. AC P44841; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Sulfurtransferase TusA homolog {ECO:0000255|HAMAP-Rule:MF_00413}; DE EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_00413}; GN Name=tusA {ECO:0000255|HAMAP-Rule:MF_00413}; GN OrderedLocusNames=HI_0721; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be part of a sulfur-relay system. CC {ECO:0000255|HAMAP-Rule:MF_00413}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00413}. CC -!- SIMILARITY: Belongs to the UPF0033 family. TusA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00413}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22379.1; 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; L42023; AAC22379.1; ALT_INIT; Genomic_DNA. DR PIR; D64157; D64157. DR RefSeq; NP_438879.2; NC_000907.1. DR RefSeq; WP_010869042.1; NC_000907.1. DR ProteinModelPortal; P44841; -. DR SMR; P44841; 5-78. DR STRING; 71421.HI0721; -. DR EnsemblBacteria; AAC22379; AAC22379; HI_0721. DR GeneID; 949741; -. DR KEGG; hin:HI0721; -. DR PATRIC; 20190065; VBIHaeInf48452_0753. DR eggNOG; ENOG41082K8; Bacteria. DR eggNOG; COG0425; LUCA. DR KO; K04085; -. DR OMA; SFCRFME; -. DR OrthoDB; EOG6QCD6D; -. DR PhylomeDB; P44841; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.110.40; -; 1. DR HAMAP; MF_00413; Thiourid_synth_A; 1. DR InterPro; IPR022931; Sulphurtransferase_TusA. DR InterPro; IPR001455; TusA-like. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS01148; UPF0033; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 79 Sulfurtransferase TusA homolog. FT /FTId=PRO_0000159038. FT ACT_SITE 17 17 Cysteine persulfide intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00413}. SQ SEQUENCE 79 AA; 9114 MW; 64890A0F3DE131EE CRC64; MSEISVTQTL DTLGLRCPEP VMLVRKNIRH LNDGEILLII ADDPATTRDI PSFCQFMDHT LLQCEVEKPP FKYWVKRGK // ID TYSY_HAEIN Reviewed; 283 AA. AC P44420; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 109. 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}; GN OrderedLocusNames=HI_0905; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22564.1; -; Genomic_DNA. DR PIR; G64101; G64101. DR RefSeq; NP_439065.1; NC_000907.1. DR RefSeq; WP_005648113.1; NC_000907.1. DR ProteinModelPortal; P44420; -. DR STRING; 71421.HI0905; -. DR EnsemblBacteria; AAC22564; AAC22564; HI_0905. DR GeneID; 949907; -. DR KEGG; hin:HI0905; -. DR PATRIC; 20190465; VBIHaeInf48452_0946. DR eggNOG; ENOG4105C0V; Bacteria. DR eggNOG; COG0207; LUCA. DR KO; K00560; -. DR OMA; IVYELLW; -. DR OrthoDB; EOG6K6V53; -. DR PhylomeDB; P44420; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000579; 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 1 283 Thymidylate synthase. FT /FTId=PRO_0000140963. FT ACT_SITE 160 160 {ECO:0000255|HAMAP-Rule:MF_00008}. SQ SEQUENCE 283 AA; 32460 MW; C1B6763651B1C233 CRC64; MKQYLELCRR IVSEGEWVAN ERTGKHCLTV INADLEYDVA NNQFPLITTR KSYWKAAIAE FLGYIRGYDN AADFRALGTK TWDANANENA AWLANPHRRG VDDMGRVYGV QGRAWRKPNG ETIDQLRKIV NNLTKGIDDR GEILTFFNPG EFDLGCLRPC MHTHTFSLVG DTLHLTSYQR SCDVPLGLNF NQIQVFTFLA LMAQITGKKA GKAYHKIVNA HIYEDQLELM RDVQLKREPF PLPKLEINPD IKTLEDLETW VTMDDFKVVG YQSHEPIKYP FSV // ID TUSC_HAEIN Reviewed; 119 AA. AC Q57194; O05026; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Protein TusC homolog; GN Name=tusC; OrderedLocusNames=HI_0576.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Could be part of a sulfur-relay system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DsrF/TusC 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; L42023; AAC22235.1; -; Genomic_DNA. DR RefSeq; NP_438734.1; NC_000907.1. DR RefSeq; WP_010869010.1; NC_000907.1. DR ProteinModelPortal; Q57194; -. DR STRING; 71421.HI0576.1; -. DR EnsemblBacteria; AAC22235; AAC22235; HI_0576.1. DR GeneID; 950759; -. DR KEGG; hin:HI0576.1; -. DR PATRIC; 20189709; VBIHaeInf48452_0597. DR eggNOG; ENOG4108ZKU; Bacteria. DR eggNOG; COG2923; LUCA. DR KO; K07236; -. DR OMA; MRNYIAT; -. DR OrthoDB; EOG6RVFZF; -. DR PhylomeDB; Q57194; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR InterPro; IPR017462; Sulphur_relay_TusC/DsrF. DR Pfam; PF02635; DrsE; 1. DR SUPFAM; SSF75169; SSF75169; 1. DR TIGRFAMs; TIGR03010; sulf_tusC_dsrF; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 119 Protein TusC homolog. FT /FTId=PRO_0000214886. SQ SEQUENCE 119 AA; 13659 MW; 7CC37D4C785991E0 CRC64; MKIAFLFRTS PHGTSISREG LDAILAATAF CEPNDIGIFF IDDGVLNLID NQQPEIIQQK DFIRTFKLLD LYDVEQRFIC TASLQKFKLD NRELILSCEK IDRSLLLEKL NQAGKLFTF // ID TYRPB_HAEIN Reviewed; 406 AA. AC P44747; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Tyrosine-specific transport protein 2; DE AltName: Full=Tyrosine permease 2; GN Name=tyrP-B; OrderedLocusNames=HI_0528; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in transporting tyrosine across the cytoplasmic CC membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 CC family. Mtr/TnaB/TyrP permease 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; L42023; AAC22185.1; -; Genomic_DNA. DR PIR; F64074; F64074. DR RefSeq; NP_438686.1; NC_000907.1. DR RefSeq; WP_010868997.1; NC_000907.1. DR STRING; 71421.HI0528; -. DR EnsemblBacteria; AAC22185; AAC22185; HI_0528. DR GeneID; 949591; -. DR KEGG; hin:HI0528; -. DR PATRIC; 20189609; VBIHaeInf48452_0547. DR eggNOG; ENOG4105E0U; Bacteria. DR eggNOG; COG0814; LUCA. DR KO; K03834; -. DR OMA; VWQLATH; -. DR OrthoDB; EOG60394J; -. DR PhylomeDB; P44747; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002091; ArAA_permease. DR InterPro; IPR013061; Trp/try_permease_CS. DR InterPro; IPR013059; Trp_tyr_transpt. DR InterPro; IPR018227; Tryptophan/tyrosine_permease. DR Pfam; PF03222; Trp_Tyr_perm; 1. DR PRINTS; PR00166; AROAAPRMEASE. DR TIGRFAMs; TIGR00837; araaP; 1. DR PROSITE; PS00594; AROMATIC_AA_PERMEASE_1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 406 Tyrosine-specific transport protein 2. FT /FTId=PRO_0000093806. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 183 203 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 335 355 Helical. {ECO:0000255}. FT TRANSMEM 376 396 Helical. {ECO:0000255}. SQ SEQUENCE 406 AA; 43476 MW; F83D979FEA62D428 CRC64; MLKNKTFGSA LIIAGTTIGA GMLAMPLTSA GMGFGYTLLL LVGLWALLVY SGLLFVEVYQ TADQLDDGVA TLAEKYFGVP GRIFATLSLL VLLYALSAAY ITGGGSLLSG LPTAFGMEAM SLKTAIIIFT VVLGSFVVVG TKGVDGLTRV LFIGKLIAFA FVLFMMLPKV ATDNLMALPL DYAFVVSAAP IFLTSFGFHV IMASVNSYLG GSVDKFRRAI LIGTAIPLAA YLVWQLATHG VLSQSEFVRI LQADPTLNGL VNATREITGS HFMGEVVRVF SSLALITSFL GVMLGVFEGL GDLFKRYHLP NNRFVLTIAA FLPPLVFALF YPEGFITALS YAGLLCAFYC LILPISLAWR TRIENPTLPY RVAGGNFALV LALLIGVVIM LIPFLIQWGY LPVVAG // ID UPPS_HAEIN Reviewed; 239 AA. AC P44938; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) {ECO:0000255|HAMAP-Rule:MF_01139}; DE EC=2.5.1.31 {ECO:0000255|HAMAP-Rule:MF_01139}; DE AltName: Full=Ditrans,polycis-undecaprenylcistransferase {ECO:0000255|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139}; DE Short=UDS {ECO:0000255|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139}; DE Short=UPP synthase {ECO:0000255|HAMAP-Rule:MF_01139}; GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; GN OrderedLocusNames=HI_0920; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to CC yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl CC diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of CC glycosyl carrier lipid in the biosynthesis of bacterial cell wall CC polysaccharide components such as peptidoglycan and CC lipopolysaccharide. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + 8 isopentenyl CC diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01139}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- SIMILARITY: Belongs to the UPP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01139}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22578.1; -; Genomic_DNA. DR PIR; E64161; E64161. DR RefSeq; NP_439080.1; NC_000907.1. DR RefSeq; WP_005655860.1; NC_000907.1. DR ProteinModelPortal; P44938; -. DR SMR; P44938; 11-233. DR STRING; 71421.HI0920; -. DR EnsemblBacteria; AAC22578; AAC22578; HI_0920. DR GeneID; 950624; -. DR KEGG; hin:HI0920; -. DR PATRIC; 20190495; VBIHaeInf48452_0961. DR eggNOG; ENOG4105CR3; Bacteria. DR eggNOG; COG0020; LUCA. DR KO; K00806; -. DR OMA; WNRPKLE; -. DR OrthoDB; EOG68H89T; -. DR PhylomeDB; P44938; -. DR BRENDA; 2.5.1.31; 2529. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1180.10; -; 1. DR HAMAP; MF_01139; ISPT; 1. DR InterPro; IPR001441; UPP_synth-like. DR InterPro; IPR018520; UPP_synth-like_CS. DR PANTHER; PTHR10291; PTHR10291; 1. DR Pfam; PF01255; Prenyltransf; 1. DR SUPFAM; SSF64005; SSF64005; 1. DR TIGRFAMs; TIGR00055; uppS; 1. DR PROSITE; PS01066; UPP_SYNTHASE; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Magnesium; Metal-binding; Peptidoglycan synthesis; Reference proteome; KW Transferase. FT CHAIN 1 239 Ditrans,polycis-undecaprenyl-diphosphate FT synthase ((2E,6E)-farnesyl-diphosphate FT specific). FT /FTId=PRO_0000123620. FT REGION 19 22 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 63 65 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 192 194 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT ACT_SITE 18 18 {ECO:0000255|HAMAP-Rule:MF_01139}. FT ACT_SITE 66 66 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 18 18 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 205 205 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 23 23 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 31 31 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 35 35 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 67 67 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 69 69 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 186 186 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. SQ SEQUENCE 239 AA; 27343 MW; 3A9002170C2FD6D7 CRC64; MIELDQTNIP KHVAIIMDGN GRWAKQKNKM RIFGHTNGVT AVRKAVAYAR QIGVEVLTLY AFSSENWSRP EQEISALMSL FMQALDREVK KLHKNNICLK IIGDVSRFSE TLQEKIKKAE NLTEKNTALT LNIAANYGGC WDIIQAAKQI AEKVKKEEMS VSDINNSTFQ HHLATQNAPP VDLLIRTSGE QRISNFLLWQ IAYAELYFSD VLWPDFNQLE FNRAIASYQQ RHRRFGGTE // ID URE1_HAEIN Reviewed; 572 AA. AC P44391; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953}; DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953}; DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953}; GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953}; GN OrderedLocusNames=HI_0539; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Urea + H(2)O = CO(2) + 2 NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953}; CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01953}; CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) CC from urea (urease route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01953}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC CC (alpha) subunits. Three heterotrimers associate to form the active CC enzyme. {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- SIMILARITY: Belongs to the urease family. {ECO:0000255|HAMAP- CC Rule:MF_01953}. CC -!- SIMILARITY: Contains 1 urease domain. {ECO:0000255|HAMAP- CC Rule:MF_01953}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22197.1; -; Genomic_DNA. DR PIR; H64075; H64075. DR RefSeq; NP_438697.1; NC_000907.1. DR RefSeq; WP_005694142.1; NC_000907.1. DR ProteinModelPortal; P44391; -. DR SMR; P44391; 5-572. DR STRING; 71421.HI0539; -. DR MEROPS; M38.982; -. DR EnsemblBacteria; AAC22197; AAC22197; HI_0539. DR GeneID; 950768; -. DR KEGG; hin:HI0539; -. DR PATRIC; 20189631; VBIHaeInf48452_0558. DR eggNOG; ENOG4105CQM; Bacteria. DR eggNOG; COG0804; LUCA. DR KO; K01428; -. DR OMA; FDSHIHF; -. DR OrthoDB; EOG6ND0GM; -. DR PhylomeDB; P44391; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_01953; Urease_alpha; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR011612; Urease_alpha_N_dom. DR InterPro; IPR017950; Urease_AS. DR InterPro; IPR005848; Urease_asu. DR InterPro; IPR017951; Urease_asu_c. DR InterPro; IPR029754; Urease_Ni-bd. DR Pfam; PF01979; Amidohydro_1; 1. DR Pfam; PF00449; Urease_alpha; 1. DR PRINTS; PR01752; UREASE. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 2. DR TIGRFAMs; TIGR01792; urease_alph; 1. DR PROSITE; PS01120; UREASE_1; 1. DR PROSITE; PS00145; UREASE_2; 1. DR PROSITE; PS51368; UREASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nickel; KW Reference proteome. FT CHAIN 1 572 Urease subunit alpha. FT /FTId=PRO_0000067542. FT DOMAIN 136 572 Urease. {ECO:0000255|HAMAP- FT Rule:MF_01953}. FT ACT_SITE 327 327 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01953}. FT METAL 141 141 Nickel 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 143 143 Nickel 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 224 224 Nickel 1; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 224 224 Nickel 2; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 253 253 Nickel 2; via pros nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 279 279 Nickel 2; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01953}. FT METAL 367 367 Nickel 1. {ECO:0000255|HAMAP- FT Rule:MF_01953}. FT BINDING 226 226 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01953}. FT MOD_RES 224 224 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_01953}. SQ SEQUENCE 572 AA; 61776 MW; 5E26396652BB6B43 CRC64; MALTISRAQY VATYGPTVGD KVRLGDTNLW ATIEQDLLTK GDECKFGGGK SVRDGMAQSG TATRDNPNVL DFVITNVMII DAKLGIIKAD IGIRDGRIVG IGQAGNPDTM DNVTPNMIIG ASTEVHNGAH LIATAGGIDT HIHFICPQQA QHAIESGVTT LIGGGTGPAD GTHATTCTPG AWYMERMFQA AEALPVNVGF FGKGNCSTLD PLREQIEAGA LGLKIHEDWG ATPAVIDSAL KVADEMDIQV AIHTDTLNES GFLEDTMKAI DGRVIHTFHT EGAGGGHAPD IIKAAMYSNV LPASTNPTRP FTKNTIDEHL DMLMVCHHLD KRVPEDVAFA DSRIRPETIA AEDILHDMGV FSIMSSDSQA MGRIGEVVIR TWQTADKMKM QRGELGNEGN DNFRIKRYIA KYTINPAIAH GIAEHIGSLE VGKIADIVLW KPMFFGVKPE VVIKKGFISY AKMGDPNASI PTPQPVFYRP MYGAQGLATA QTAVFFVSQA AEKADIRAKF GLHKETIAVK GCRNVGKKDL VHNDVTPNIT VDAERYEVRV DGELITCEPV DSVPLGQRYF LF // ID UREE_HAEIN Reviewed; 185 AA. AC P44394; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Urease accessory protein UreE {ECO:0000255|HAMAP-Rule:MF_00822}; GN Name=ureE {ECO:0000255|HAMAP-Rule:MF_00822}; GN OrderedLocusNames=HI_0538; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in urease metallocenter assembly. Binds nickel. CC Probably functions as a nickel donor during metallocenter CC assembly. {ECO:0000255|HAMAP-Rule:MF_00822}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00822}. CC -!- SIMILARITY: Belongs to the UreE family. {ECO:0000255|HAMAP- CC Rule:MF_00822}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22196.1; -; Genomic_DNA. DR PIR; G64075; G64075. DR RefSeq; NP_438696.1; NC_000907.1. DR RefSeq; WP_005688622.1; NC_000907.1. DR ProteinModelPortal; P44394; -. DR STRING; 71421.HI0538; -. DR EnsemblBacteria; AAC22196; AAC22196; HI_0538. DR GeneID; 949599; -. DR KEGG; hin:HI0538; -. DR PATRIC; 20189629; VBIHaeInf48452_0557. DR eggNOG; ENOG4105HFU; Bacteria. DR eggNOG; COG2371; LUCA. DR KO; K03187; -. DR OMA; DYVDLEW; -. DR OrthoDB; EOG647V3V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0018307; P:enzyme active site formation; IEA:InterPro. DR GO; GO:0006461; P:protein complex assembly; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0019627; P:urea metabolic process; IEA:InterPro. DR Gene3D; 3.30.70.790; -; 1. DR HAMAP; MF_00822; UreE; 1. DR InterPro; IPR012406; UreE. DR InterPro; IPR007864; UreE_C_dom. DR InterPro; IPR004029; UreE_N. DR Pfam; PF05194; UreE_C; 1. DR Pfam; PF02814; UreE_N; 1. DR PIRSF; PIRSF036402; Ureas_acces_UreE; 1. DR SMART; SM00988; UreE_N; 1. DR SUPFAM; SSF69287; SSF69287; 1. DR SUPFAM; SSF69737; SSF69737; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Nickel; Nickel insertion; KW Reference proteome. FT CHAIN 1 185 Urease accessory protein UreE. FT /FTId=PRO_0000067632. SQ SEQUENCE 185 AA; 21067 MW; AA2C4050FA026F5C CRC64; MKIINPILPI IENILGNLTA LQAEGKITTQ PIERVALQWY ESERNILRKT TNTGREVAFR LLKEGQRLKH DDVVFISDEL VIAIEILPSD VIVLSPKTLP EMARACYEIG NKHSPLFLDG DEVTLPYDKP MFEWLQAAGF HPQKAERRLS QALRANSAQG HGHSHSHSHD HHGYHHHGDG HWHKH // ID URK_HAEIN Reviewed; 213 AA. AC P44533; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. 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=HI_0132; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21804.1; -; Genomic_DNA. DR PIR; I64049; I64049. DR RefSeq; NP_438301.1; NC_000907.1. DR RefSeq; WP_005654445.1; NC_000907.1. DR ProteinModelPortal; P44533; -. DR STRING; 71421.HI0132; -. DR EnsemblBacteria; AAC21804; AAC21804; HI_0132. DR GeneID; 951039; -. DR KEGG; hin:HI0132; -. DR PATRIC; 20188751; VBIHaeInf48452_0134. DR eggNOG; ENOG4105DBI; Bacteria. DR eggNOG; COG0572; LUCA. DR KO; K00876; -. DR OMA; FNEELMF; -. DR OrthoDB; EOG6KMBCH; -. DR PhylomeDB; P44533; -. DR UniPathway; UPA00574; UER00637. DR UniPathway; UPA00579; UER00640. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043771; F:cytidine kinase activity; IBA:GO_Central. DR GO; GO:0004849; F:uridine kinase activity; IBA:GO_Central. DR GO; GO:0009224; P:CMP biosynthetic process; IBA:GOC. DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IBA:GO_Central. DR GO; GO:0043097; P:pyrimidine nucleoside salvage; IBA:GO_Central. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR 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 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_0000164474. FT NP_BIND 13 20 ATP. {ECO:0000255}. SQ SEQUENCE 213 AA; 24284 MW; 483B844ADA41E4D9 CRC64; MSNPSCIIIA ITGASASGKS SIASTVHKEL CNELGCQEIG IITEDSYYKD QSHLEMTERV KTNYDHPNSM DRDLLIQHLK NLKNGSAVDV PVYSYVEHTR TNETTHFTPK RIVILEGILL LTDERVRQLA DISVFVDTPL DICFIRRLQR DMEERGRSLQ SVIDQYRATV RPMFLQFIEP SKQYADIVIP RGGKNRIAIN MLKAQILHLL NQK // ID UNG_HAEIN Reviewed; 219 AA. AC P43731; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Uracil-DNA glycosylase; DE Short=UDG; DE EC=3.2.2.27; GN Name=ung; OrderedLocusNames=HI_0018; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC21696.1; -; Genomic_DNA. DR PIR; A64043; A64043. DR RefSeq; NP_438191.1; NC_000907.1. DR RefSeq; WP_005693885.1; NC_000907.1. DR ProteinModelPortal; P43731; -. DR SMR; P43731; 4-218. DR STRING; 71421.HI0018; -. DR EnsemblBacteria; AAC21696; AAC21696; HI_0018. DR GeneID; 950914; -. DR KEGG; hin:HI0018; -. DR PATRIC; 20188487; VBIHaeInf48452_0018. DR eggNOG; ENOG4105D5S; Bacteria. DR eggNOG; COG0692; LUCA. DR KO; K03648; -. DR OMA; KYTAFED; -. DR OrthoDB; EOG6MSS63; -. DR PhylomeDB; P43731; -. DR Proteomes; UP000000579; 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 1 219 Uracil-DNA glycosylase. FT /FTId=PRO_0000176100. FT ACT_SITE 61 61 Proton acceptor. {ECO:0000250}. SQ SEQUENCE 219 AA; 24848 MW; C270CC31F7B2E58A CRC64; MKNWTDVIGT EKAQPYFQHT LQQVHLARAS GKTIYPPQED VFNAFKYTAF EDVKVVILGQ DPYHGPNQAH GLAFSVKPEV AIPPSLLNIY KELTQDISGF QMPSNGYLVK WAEQGVLLLN TVLTVERGMA HSHANLGWER FTDKVIAVLN EHREKLVFLL WGSHAQKKGQ MIDRTRHLVL TAPHPSPLSA HRGFFGCRHF SKTNSYLESH GIKPIDWQI // ID URE3_HAEIN Reviewed; 100 AA. AC P44393; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739}; DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739}; DE AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739}; GN Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739}; GN OrderedLocusNames=HI_0541; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Urea + H(2)O = CO(2) + 2 NH(3). CC {ECO:0000255|HAMAP-Rule:MF_00739}. CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) CC from urea (urease route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00739}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC CC (alpha) subunits. Three heterotrimers associate to form the active CC enzyme. {ECO:0000255|HAMAP-Rule:MF_00739}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}. CC -!- SIMILARITY: Belongs to the urease gamma subunit family. CC {ECO:0000255|HAMAP-Rule:MF_00739}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22199.1; -; Genomic_DNA. DR PIR; A64076; A64076. DR RefSeq; NP_438699.1; NC_000907.1. DR RefSeq; WP_005694143.1; NC_000907.1. DR ProteinModelPortal; P44393; -. DR SMR; P44393; 1-99. DR STRING; 71421.HI0541; -. DR EnsemblBacteria; AAC22199; AAC22199; HI_0541. DR GeneID; 949600; -. DR KEGG; hin:HI0541; -. DR PATRIC; 20189635; VBIHaeInf48452_0560. DR eggNOG; ENOG4108YZ9; Bacteria. DR eggNOG; COG0831; LUCA. DR KO; K01430; -. DR OMA; ELMSYGT; -. DR OrthoDB; EOG69PQ9G; -. DR PhylomeDB; P44393; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.280.10; -; 1. DR HAMAP; MF_00739; Urease_gamma; 1. DR InterPro; IPR012010; Urease_gamma. DR InterPro; IPR002026; Urease_gamma/gamma-beta_su. DR Pfam; PF00547; Urease_gamma; 1. DR PIRSF; PIRSF001223; Urease_gamma; 1. DR ProDom; PD002319; Urease_gamma_reg; 1. DR SUPFAM; SSF54111; SSF54111; 1. DR TIGRFAMs; TIGR00193; urease_gam; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 100 Urease subunit gamma. FT /FTId=PRO_0000098014. SQ SEQUENCE 100 AA; 11097 MW; DB33B79DF6C84274 CRC64; MHLTSREQEK LMLFLAGELA AKRKARGVKL NYPETIAYIA SHLQEAAREG MSVAEVMQYG ATLLTVDDVM EGVAEMVHEV QIEATFPDGT KLVTVHNPIR // ID URED_HAEIN Reviewed; 261 AA. AC P44397; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Urease accessory protein UreD {ECO:0000255|HAMAP-Rule:MF_01384}; GN Name=ureD {ECO:0000255|HAMAP-Rule:MF_01384}; Synonyms=ureH; GN OrderedLocusNames=HI_0535; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for maturation of urease via the functional CC incorporation of the urease nickel metallocenter. CC {ECO:0000255|HAMAP-Rule:MF_01384}. CC -!- SUBUNIT: UreD, UreF and UreG form a complex that acts as a GTP- CC hydrolysis-dependent molecular chaperone, activating the urease CC apoprotein by helping to assemble the nickel containing CC metallocenter of UreC. The UreE protein probably delivers the CC nickel. {ECO:0000255|HAMAP-Rule:MF_01384}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01384}. CC -!- SIMILARITY: Belongs to the UreD family. {ECO:0000255|HAMAP- CC Rule:MF_01384}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22193.1; -; Genomic_DNA. DR PIR; D64075; D64075. DR RefSeq; NP_438693.1; NC_000907.1. DR RefSeq; WP_010869001.1; NC_000907.1. DR STRING; 71421.HI0535; -. DR DNASU; 949674; -. DR EnsemblBacteria; AAC22193; AAC22193; HI_0535. DR GeneID; 949674; -. DR KEGG; hin:HI0535; -. DR PATRIC; 20189623; VBIHaeInf48452_0554. DR eggNOG; ENOG4108XNJ; Bacteria. DR eggNOG; COG0829; LUCA. DR KO; K03190; -. DR OMA; QNINELG; -. DR OrthoDB; EOG690MJ6; -. DR PhylomeDB; P44397; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR HAMAP; MF_01384; UreD; 1. DR InterPro; IPR002669; UreD. DR Pfam; PF01774; UreD; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Nickel insertion; KW Reference proteome. FT CHAIN 1 261 Urease accessory protein UreD. FT /FTId=PRO_0000067623. SQ SEQUENCE 261 AA; 29088 MW; 6A64EFF0C407789F CRC64; MNSKLSLSTK LSSSGKTQLA EYFATPPFKV ITLPSYDDAW ANGLNAMQMS SSPGVLAGDL LEIDISLAKL TALSLNTQAF TRVQAMNEGD SAMQTTHILL AENSRLFYLP HPLVLHRDSV FKQQTQIEMG EQSELIYGEI VAIGRVLNDE RFAFRQFSSH LKIYALQNDG KKRPLVSDCI QWLPSKMNLT ALSQMENYSH QGSLTYLNLA KNNAEIKQQV QALQQQSTEE KDLLIGISQL NEYGLMVRVL GCRAEANSEI I // ID USPA_HAEIN Reviewed; 141 AA. AC P44880; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Universal stress protein A homolog; GN Name=uspA; OrderedLocusNames=HI_0815; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11738040; DOI=10.1016/S0969-2126(01)00680-3; RA Sousa M.C., McKay D.B.; RT "Structure of the universal stress protein of Haemophilus RT influenzae."; RL Structure 9:1135-1141(2001). CC -!- FUNCTION: Required for resistance to DNA-damaging agents. CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Unlike MJ0577, UspA shows no evidence of ATP CC binding activity. CC -!- SIMILARITY: Belongs to the universal stress protein A 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; L42023; AAC22474.1; -; Genomic_DNA. DR PIR; A64096; A64096. DR RefSeq; NP_438975.1; NC_000907.1. DR RefSeq; WP_005648375.1; NC_000907.1. DR PDB; 1JMV; X-ray; 1.85 A; A/B/C/D=1-141. DR PDBsum; 1JMV; -. DR ProteinModelPortal; P44880; -. DR SMR; P44880; 1-140. DR STRING; 71421.HI0815; -. DR EnsemblBacteria; AAC22474; AAC22474; HI_0815. DR GeneID; 949495; -. DR KEGG; hin:HI0815; -. DR PATRIC; 20190285; VBIHaeInf48452_0856. DR eggNOG; ENOG4108M6U; Bacteria. DR eggNOG; COG0589; LUCA. DR KO; K06149; -. DR OMA; SARQLMN; -. DR OrthoDB; EOG6RJV7M; -. DR PhylomeDB; P44880; -. DR EvolutionaryTrace; P44880; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR006015; Universal_stress_UspA. DR InterPro; IPR006016; UspA. DR Pfam; PF00582; Usp; 1. DR PIRSF; PIRSF006276; UspA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 141 Universal stress protein A homolog. FT /FTId=PRO_0000147400. FT STRAND 3 9 {ECO:0000244|PDB:1JMV}. FT HELIX 15 29 {ECO:0000244|PDB:1JMV}. FT STRAND 32 40 {ECO:0000244|PDB:1JMV}. FT HELIX 43 45 {ECO:0000244|PDB:1JMV}. FT HELIX 52 57 {ECO:0000244|PDB:1JMV}. FT HELIX 64 75 {ECO:0000244|PDB:1JMV}. FT STRAND 76 78 {ECO:0000244|PDB:1JMV}. FT STRAND 83 88 {ECO:0000244|PDB:1JMV}. FT HELIX 90 100 {ECO:0000244|PDB:1JMV}. FT STRAND 105 110 {ECO:0000244|PDB:1JMV}. FT HELIX 115 126 {ECO:0000244|PDB:1JMV}. FT STRAND 131 137 {ECO:0000244|PDB:1JMV}. SQ SEQUENCE 141 AA; 15758 MW; 6B8693E853E3E3ED CRC64; MYKHILVAVD LSEESPILLK KAVGIAKRHD AKLSIIHVDV NFSDLYTGLI DVNMSSMQDR ISTETQKALL DLAESVDYPI SEKLSGSGDL GQVLSDAIEQ YDVDLLVTGH HQDFWSKLMS STRQVMNTIK IDMLVVPLRD E // ID UUP1_HAEIN Reviewed; 647 AA. AC Q57242; O05056; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 99. DE RecName: Full=ABC transporter ATP-binding protein uup-1; GN Name=uup-A; OrderedLocusNames=HI_1300; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF CC family. EF3 subfamily. {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; L42023; AAC22945.1; -; Genomic_DNA. DR PIR; E64170; E64170. DR RefSeq; NP_439451.1; NC_000907.1. DR RefSeq; WP_005694468.1; NC_000907.1. DR ProteinModelPortal; Q57242; -. DR STRING; 71421.HI1300; -. DR EnsemblBacteria; AAC22945; AAC22945; HI_1300. DR GeneID; 950128; -. DR KEGG; hin:HI1300; -. DR PATRIC; 20191283; VBIHaeInf48452_1352. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR KO; K15738; -. DR OMA; FKGAFVV; -. DR OrthoDB; EOG6F297F; -. DR PhylomeDB; Q57242; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; 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; IPR032524; ABC_tran_C. DR InterPro; IPR032781; ABC_tran_Xtn. 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 Pfam; PF16326; ABC_tran_CTD; 1. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 647 ABC transporter ATP-binding protein uup- FT 1. FT /FTId=PRO_0000093030. FT DOMAIN 4 253 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 320 538 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 352 359 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 647 AA; 73268 MW; 85C949B0C0CF2B1B CRC64; MALISLTNGY LSFSDAPLLD HAELHIEPNE CVCLVGRNGA GKSTLLKIIA GDVLMDDGKI QYEKDLVVSR LEQDPPRNAQ GNIFDYVAEG VGHLTDLLKE YHQISVQLEE NYSDQILSQL EQVQAKLEHA DGWRFENKIN EVLLKLGLNP NTKLSALSGG WLRKAALARA LVCDPDVLLL DEPTNHLDVE AIEWLENFLL DFQGSIVFIS HDRSFIRKMA TRIVDLDRGQ LVSYPGNYDL YLTTKEENLR VEALQNELFD KRLAQEEVWI RQGIKARRTR NEGRVRALKV MREERRQRRD VMGTAKLQLD TSSRSGKIVF EMEDVSYEIA GKTLLKDFST TILRGDKIAL VGPNGCGKTT FIKLLLGEIQ PTSGKIRCGT KLEIAYFDQY RADLDPEKTV MDNVADGKQD IEINGVKRHV LGYLQDFLFP PKRAMTPVKA LSGGERNRLL LAKLLLKPNN LLILDEPTND LDVETLELLE EILTDYQGTL LIVSHDRQFI DNTATECYLF EGKGHLNKYV GGFFDAKQQQ ANFWASKAVE EQAKAKKSEP LKEESAVKND RTSKPKSVKL SYKEQRELEQ LPQLLEELET KITVLQAEIA DPAFFQQAHD ITDAKLKALA DTEAELETAF LRWEELEEKK NLVEGKA // ID UVRC_HAEIN Reviewed; 609 AA. AC P44489; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203}; DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203}; DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203}; GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; GN OrderedLocusNames=HI_0057; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrC both incises the 5' and 3' sides CC of the lesion. The N-terminal half is responsible for the 3' CC incision and the C-terminal half is responsible for the 5' CC incision. {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBUNIT: Interacts with UvrB in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}. CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00203}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21735.1; -; Genomic_DNA. DR PIR; F64045; F64045. DR RefSeq; NP_438230.1; NC_000907.1. DR RefSeq; WP_005693865.1; NC_000907.1. DR ProteinModelPortal; P44489; -. DR SMR; P44489; 554-608. DR STRING; 71421.HI0057; -. DR EnsemblBacteria; AAC21735; AAC21735; HI_0057. DR GeneID; 950955; -. DR KEGG; hin:HI0057; -. DR PATRIC; 20188567; VBIHaeInf48452_0057. DR eggNOG; ENOG4105CII; Bacteria. DR eggNOG; COG0322; LUCA. DR KO; K03703; -. DR OMA; LFPIRQC; -. DR OrthoDB; EOG6K13R9; -. DR PhylomeDB; P44489; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP. DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1440.10; -; 1. DR Gene3D; 4.10.860.10; -; 1. DR HAMAP; MF_00203; UvrC; 1. DR InterPro; IPR027299; GIY-YIG_dom. DR InterPro; IPR000305; GIY-YIG_SF. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR001943; UVR_dom. DR InterPro; IPR004791; UvrC. DR InterPro; IPR001162; UvrC_homol_region. DR Pfam; PF01541; GIY-YIG; 1. DR Pfam; PF02151; UVR; 1. DR Pfam; PF08459; UvrC_HhH_N; 1. DR SMART; SM00465; GIYc; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF46600; SSF46600; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF82771; SSF82771; 1. DR TIGRFAMs; TIGR00194; uvrC; 1. DR PROSITE; PS50164; GIY_YIG; 1. DR PROSITE; PS50151; UVR; 1. DR PROSITE; PS50165; UVRC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA excision; DNA repair; KW Excision nuclease; Reference proteome; SOS response. FT CHAIN 1 609 UvrABC system protein C. FT /FTId=PRO_0000138304. FT DOMAIN 13 91 GIY-YIG. {ECO:0000255|HAMAP- FT Rule:MF_00203}. FT DOMAIN 201 236 UVR. {ECO:0000255|HAMAP-Rule:MF_00203}. SQ SEQUENCE 609 AA; 69609 MW; 049DD9212349017A CRC64; MFDAKKFLTD VSHEPGVYRM YDDKDQVIYV GKAKDLKKRL SSYFRKNLSS KKTEALVASI HHIDTTLTSS ETEALLLEHN FIKLYQPRYN VLLRDDKSYP FILLTKERHQ RITSYRGSKK FAGEYFGPYP HAGAVRETLS LLQKLFPVRQ CENSVYSNRS RPCLQYQIGR CSAPCVQGYV SDEEYNQQVE LARLFLQGKD QQVLDYLIGK MEQASRNLDF EQAARYRDQI QAVRSVIEKQ FVSNERLDDM DIMSIAYQHG LACVQVMFIR QGKVLGNRSY FPKVPANTDL SELTETFVGQ FYLQGHQGRS IPNSIIVDRQ LAEKSELEQL LSEQAGRKVT IQESVKGDKS KYLQLAQVNA KAALNVQLKQ SSRMSERYQA LCDLLNLPKI KRMECFDISH TMGNQTVASC VVFNKEGPLK SDYRRFNIEG ITGGDDYAAM EQVLQKRYER DLEEDKIPDI IFIDGGKGQL NRALNVFQHL QVKWDKNRPH LIGVAKGVDR RAGQEVLIIS KQDREIHLPD DSLALHLIQH IRDESHNHAI SGHRKKRQKA FTQSGLETIE GVGAKRRQAL LKYLGGLQGV KKATLDEIAS VPGISPKLAE RIFETLKND // ID UDP_HAEIN Reviewed; 252 AA. AC P43770; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2003, sequence version 2. DT 11-NOV-2015, entry version 103. DE RecName: Full=Uridine phosphorylase; DE Short=UPase; DE Short=UrdPase; DE EC=2.4.2.3; GN Name=udp; OrderedLocusNames=HI_0280; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of CC uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- CC phosphate. The produced molecules are then utilized as carbon and CC energy sources or in the rescue of pyrimidine bases for nucleotide CC synthesis (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose CC 1-phosphate. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; uracil from uridine (phosphorylase route): step 1/1. CC -!- SUBUNIT: Homohexamer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21943.1; 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; L42023; AAC21943.1; ALT_INIT; Genomic_DNA. DR PIR; C64059; C64059. DR RefSeq; NP_438448.2; NC_000907.1. DR RefSeq; WP_010868970.1; NC_000907.1. DR ProteinModelPortal; P43770; -. DR SMR; P43770; 2-251. DR STRING; 71421.HI0280; -. DR EnsemblBacteria; AAC21943; AAC21943; HI_0280. DR GeneID; 950640; -. DR KEGG; hin:HI0280; -. DR PATRIC; 20189099; VBIHaeInf48452_0296. DR eggNOG; ENOG4108I5U; Bacteria. DR eggNOG; COG2820; LUCA. DR KO; K00757; -. DR OMA; GPSTSIC; -. DR OrthoDB; EOG676Z3T; -. DR PhylomeDB; P43770; -. DR UniPathway; UPA00574; UER00633. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1580; -; 1. DR InterPro; IPR018017; Nucleoside_phosphorylase. DR InterPro; IPR018016; Nucleoside_phosphorylase_CS. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR010058; Uridine_phosphorylase. DR PANTHER; PTHR21234; PTHR21234; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01718; Uridine-psphlse; 1. DR PROSITE; PS01232; PNP_UDP_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 252 Uridine phosphorylase. FT /FTId=PRO_0000063186. SQ SEQUENCE 252 AA; 27254 MW; 30A007A6A764DEF6 CRC64; MSGVFHLNLT KAQLKGATLA IVPGDPARSE RIAKQLDNPE FLTSTREFTS WLGYINGQPI VVCSTGIGGP STSICVEELA QLGVRTFLRI GTTGAIQPHI NVGDVLITTA AVRLDGASHH FVPLEYPAVA NFECTTALYN AAKAKGIEPY VGVTVSSDTF YPGQERYDTY SGKVYRNYQG LLKQWQDLNV MNYEMESSTL FTMCSALGLR AGMVAGVIVN RTQQEIPNEA TIKQTEEKAV SVVITAAQAL LS // ID UPP_HAEIN Reviewed; 208 AA. AC P43857; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. 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=HI_1228; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22881.1; -; Genomic_DNA. DR PIR; E64111; E64111. DR RefSeq; NP_439384.1; NC_000907.1. DR RefSeq; WP_005652947.1; NC_000907.1. DR ProteinModelPortal; P43857; -. DR SMR; P43857; 2-208. DR STRING; 71421.HI1228; -. DR PRIDE; P43857; -. DR EnsemblBacteria; AAC22881; AAC22881; HI_1228. DR GeneID; 950169; -. DR KEGG; hin:HI1228; -. DR PATRIC; 20191135; VBIHaeInf48452_1280. DR eggNOG; ENOG4105CZ5; Bacteria. DR eggNOG; COG0035; LUCA. DR KO; K00761; -. DR OMA; TIEGWCG; -. DR OrthoDB; EOG6HF5WX; -. DR PhylomeDB; P43857; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004849; F:uridine kinase activity; IBA:GO_Central. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IBA:GO_Central. DR GO; GO:0043097; P:pyrimidine nucleoside salvage; IBA:GO_Central. DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006223; P:uracil salvage; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01218_B; Upp_B; 1. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005765; Ura_phspho_trans. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01091; upp; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Glycosyltransferase; KW GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1 208 Uracil phosphoribosyltransferase. FT /FTId=PRO_0000120834. FT REGION 130 138 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT REGION 198 200 Uracil binding. {ECO:0000255|HAMAP- FT Rule:MF_01218}. FT BINDING 78 78 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 103 103 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 193 193 Uracil; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01218}. FT BINDING 199 199 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01218}. SQ SEQUENCE 208 AA; 22664 MW; 4FFCA1DB1421307D CRC64; MKLVEVKHPL VKHKLGVMRE AEIDTKKFRE LATEIGSLLT YEATSDLETE KVTINGWNGP VEIDRIKGKK VTVVPILRAG LGMMDGVLEH VPSARISVVG IYRNEETLEP VPYFQKLASD LEERLSIVVD PMLATGGSMI ATLDLLKAKG CKHIKVLVLV AAPEGIKALE AAHPDIELYC ASIDSHLNEQ GYIIPGLGDA GDKIFGTK // ID UVRA_HAEIN Reviewed; 943 AA. AC P44410; Q48151; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 120. DE RecName: Full=UvrABC system protein A {ECO:0000255|HAMAP-Rule:MF_00205}; DE Short=UvrA protein {ECO:0000255|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000255|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000255|HAMAP-Rule:MF_00205}; GN OrderedLocusNames=HI_0249; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=NTHi N187; RX PubMed=8921840; DOI=10.1016/0378-1119(96)00264-8; RA de la Morena M.L., Hendrixson D.R., St Geme J.W. III; RT "Isolation and characterization of the Haemophilus influenzae uvrA RT gene."; RL Gene 177:23-28(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71. RC STRAIN=NTHi TN106; RX PubMed=8063092; DOI=10.1016/0378-1119(94)90841-9; RA Jarosik G.P., Hansen E.J.; RT "Cloning and sequencing of the Haemophilus influenzae ssb gene RT encoding single-strand DNA-binding protein."; RL Gene 146:101-103(1994). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. UvrA is an ATPase and a DNA-binding CC protein. A damage recognition complex composed of 2 UvrA and 2 CC UvrB subunits scans DNA for abnormalities. When the presence of a CC lesion has been verified by UvrB, the UvrA molecules dissociate. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000255|HAMAP-Rule:MF_00205}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_00205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21915.1; -; Genomic_DNA. DR EMBL; U33877; AAC44592.1; -; Genomic_DNA. DR EMBL; U04997; AAA60462.1; -; Genomic_DNA. DR PIR; D64057; D64057. DR RefSeq; NP_438418.1; NC_000907.1. DR RefSeq; WP_005694053.1; NC_000907.1. DR ProteinModelPortal; P44410; -. DR SMR; P44410; 1-943. DR STRING; 71421.HI0249; -. DR EnsemblBacteria; AAC21915; AAC21915; HI_0249. DR GeneID; 949621; -. DR KEGG; hin:HI0249; -. DR PATRIC; 20189023; VBIHaeInf48452_0264. DR eggNOG; ENOG4105C5U; Bacteria. DR eggNOG; COG0178; LUCA. DR KO; K03701; -. DR OMA; GAIKGWD; -. DR OrthoDB; EOG6QK4PS; -. DR PhylomeDB; P44410; -. DR Proteomes; UP000000579; 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; 2. 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 1 943 UvrABC system protein A. FT /FTId=PRO_0000093053. FT DOMAIN 310 587 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT DOMAIN 607 937 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 31 38 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 253 280 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT NP_BIND 640 647 ATP. {ECO:0000255|HAMAP-Rule:MF_00205}. FT ZN_FING 740 766 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00205}. FT CONFLICT 163 163 V -> L (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 236 236 E -> D (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 425 425 R -> K (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 463 463 I -> M (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 514 514 E -> Q (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 661 661 A -> T (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 928 928 T -> E (in Ref. 2; AAC44592). FT {ECO:0000305}. FT CONFLICT 935 942 FLKPILEK -> PL (in Ref. 2; AAC44592). FT {ECO:0000305}. SQ SEQUENCE 943 AA; 104366 MW; 4DBA0DCFA602D465 CRC64; MENIDIRGAR THNLKNINLT IPRNKLVVIT GLSGSGKSSL AFDTLYAEGQ RRYVESLSAY ARQFLSLMEK PDVDSIEGLS PAISIEQKST SHNPRSTVGT ITEIYDYLRL LFARVGEPRC PDHNVPLTAQ TISQMVDKVL SLPEDSKMML LAPVVKNRKG EHVKILENIA AQGYIRARID GEICDLSDPP KLALQKKHTI EVVVDRFKVR SDLATRLAES FETALELSGG TAIVAEMDNP KAEELVFSAN FACPHCGYSV PELEPRLFSF NNPAGACPTC DGLGVQQYFD EDRVVQNPTI SLAGGAVKGW DRRNFYYYQM LTSLAKHYHF DVEAPYESLP KKIQHIIMHG SGKEEIEFQY MNDRGDVVIR KHPFEGILNN MARRYKETES MSVREELAKN ISNRPCIDCG GSRLRPEARN VYIGRTNLPI IAEKSIGETL EFFTALSLTG QKAQIAEKIL KEIRERLQFL VNVGLNYLSL SRSAETLSGG EAQRIRLASQ IGAGLVGVMY VLDEPSIGLH QRDNERLLNT LIHLRNLGNT VIVVEHDEDA IRAADHIIDI GPGAGVHGGQ VIAQGNADEI MLNPNSITGK FLSGADKIEI PKKRTALDKK KWLKLKGASG NNLKNVNLDI PVGLFTCVTG VSGSGKSTLI NDTLFPLAQN ALNRAEKTDY APYQSIEGLE HFDKVIDINQ SPIGRTPRSN PATYTGLFTP IRELFAGVPE ARARGYNPGR FSFNVRGGRC EACQGDGVLK VEMHFLPDVY VPCDQCKGKR YNRETLEIRY KGKTIHQVLD MTVEEAREFF DAIPMIARKL QTLMDVGLSY IRLGQSSTTL SGGEAQRVKL ATELSKRDTG KTLYILDEPT TGLHFADIKQ LLEVLHRLRD QGNTIVVIEH NLDVIKTADW IVDLGPEGGS GGGQIIATGT PEQVAKVTSS HTARFLKPIL EKP // ID UVRB_HAEIN Reviewed; 679 AA. AC P45125; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204}; DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204}; DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204}; GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; GN OrderedLocusNames=HI_1247; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and CC processing of DNA lesions. A damage recognition complex composed CC of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon CC binding of the UvrA(2)B(2) complex to a putative damaged site, the CC DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP CC binding by UvrB and probably causes local melting of the DNA CC helix, facilitating insertion of UvrB beta-hairpin between the DNA CC strands. Then UvrB probes one DNA strand for the presence of a CC lesion. If a lesion is found the UvrA subunits dissociate and the CC UvrB-DNA preincision complex is formed. This complex is CC subsequently bound by UvrC and the second UvrB is released. If no CC lesion is found, the DNA wraps around the other UvrB subunit that CC will check the other stand for damage. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for CC lesions. Interacts with UvrC in an incision complex. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|HAMAP-Rule:MF_00204}. CC -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP- CC Rule:MF_00204}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22897.1; -; Genomic_DNA. DR PIR; G64112; G64112. DR RefSeq; NP_439403.1; NC_000907.1. DR RefSeq; WP_005694308.1; NC_000907.1. DR ProteinModelPortal; P45125; -. DR SMR; P45125; 10-598, 636-676. DR STRING; 71421.HI1247; -. DR EnsemblBacteria; AAC22897; AAC22897; HI_1247. DR GeneID; 950196; -. DR KEGG; hin:HI1247; -. DR PATRIC; 20191173; VBIHaeInf48452_1299. DR eggNOG; ENOG4105CCW; Bacteria. DR eggNOG; COG0556; LUCA. DR KO; K03702; -. DR OMA; QEYVDRM; -. DR OrthoDB; EOG6B360R; -. DR PhylomeDB; P45125; -. DR Proteomes; UP000000579; 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 1 679 UvrABC system protein B. FT /FTId=PRO_0000138395. FT DOMAIN 31 414 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 436 589 Helicase C-terminal. {ECO:0000255|HAMAP- FT Rule:MF_00204}. FT DOMAIN 639 674 UVR. {ECO:0000255|HAMAP-Rule:MF_00204}. FT NP_BIND 44 51 ATP. {ECO:0000255|HAMAP-Rule:MF_00204}. FT MOTIF 97 120 Beta-hairpin. SQ SEQUENCE 679 AA; 77526 MW; 926DF16C1B21A0C3 CRC64; MSEKINTKPF ILHSDFRPSG DQPQAIEKLA ENLTDGLAHQ TLLGVTGSGK TFTIANVIAQ LNRPAMLLAP NKTLAAQLYA EMKAFFPENA VEYFVSYYDY YQPEAYVPSS DTFIEKDASI NDQIEQMRLS ATKSFLERRD TIVVASVSAI YGLGDPDSYL QMMLHLQQGA IIDQRQILAK LAELQYTRND QAFQRGTFRV RGEIIDIFPA ESDDRAVRIE LFDDEIERLS LFDPLTGSSF GAVPRFTIYP KTHYVTPRER ILDAIENIKK ELVSRREYFI KEHKLLEEQR ISQRTQFDIE MMNELGYCSG IENYSRYLSG RNEGEPPPTL FDYMPPDAIL IIDESHVTVP QIGGMYRGDR SRKETLVEYG FRLPSALDNR PLRFEEFERL APQTIYVSAT PGAYELEKSG SEIIDQVVRP TGLLDPLIEI RPVSIQVDDL LSEARQRADK NERVLVTTLT KKMAEDLTDY LDEHGIRVRY LHSDIDTVER VEIIRDLRLG EFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSERSL IQTIGRAARN LNGKAILYAD SITKSMEKAI TETNRRREKQ TKYNEEHGIV PQALNKKVGE LLDIGQGANQ KAKANKQRGK MAAEPTALYN APKNAKEYQQ QIKKLEQQMY KFAQDLEFEK AAAIRDQLHQ LREQFVFDN // ID UVRD_HAEIN Reviewed; 727 AA. AC Q02322; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 115. DE RecName: Full=DNA helicase II; DE EC=3.6.4.12; GN Name=uvrD; Synonyms=mutB; OrderedLocusNames=HI_1188; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8294031; DOI=10.1016/0378-1119(93)90444-8; RA Walter R.B., Morton K.A., Stuy J.H.; RT "The sequence of the Haemophilus influenzae mutB gene indicates it RT encodes a DNA helicase II-like protein."; RL Gene 136:35-40(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP CHARACTERIZATION. RX PubMed=3259573; RA Walter R.B., Stuy J.H.; RT "Isolation and characterization of a UV-sensitive mutator (mutB1) RT mutant of Haemophilus influenzae."; RL J. Bacteriol. 170:2537-2542(1988). CC -!- FUNCTION: May process damage occurring in non-replicating regions CC of DNA to produce recombinational intermediates for sister strand CC recombinational exchange. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-7817147, EBI-7817147; 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 -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator. 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; M99049; AAC36867.1; -; Unassigned_DNA. DR EMBL; L42023; AAC22841.1; -; Genomic_DNA. DR PIR; H64188; H64188. DR RefSeq; NP_439344.1; NC_000907.1. DR RefSeq; WP_010869148.1; NC_000907.1. DR ProteinModelPortal; Q02322; -. DR SMR; Q02322; 3-650. DR MINT; MINT-8361667; -. DR STRING; 71421.HI1188; -. DR PRIDE; Q02322; -. DR EnsemblBacteria; AAC22841; AAC22841; HI_1188. DR GeneID; 950076; -. DR KEGG; hin:HI1188; -. DR PATRIC; 20191055; VBIHaeInf48452_1240. DR eggNOG; ENOG4105C4R; Bacteria. DR eggNOG; COG0210; LUCA. DR KO; K03657; -. DR OMA; RLQIAFQ; -. DR OrthoDB; EOG64N9TW; -. DR PhylomeDB; Q02322; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR013986; DExx_box_DNA_helicase_dom. DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01075; uvrD; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 727 DNA helicase II. FT /FTId=PRO_0000102074. FT DOMAIN 9 290 UvrD-like helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00560}. FT DOMAIN 291 568 UvrD-like helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00617}. FT NP_BIND 33 38 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00560}. FT BINDING 288 288 ATP. {ECO:0000250}. FT CONFLICT 18 18 R -> A (in Ref. 1; AAC36867). FT {ECO:0000305}. FT CONFLICT 100 100 H -> R (in Ref. 1; AAC36867). FT {ECO:0000305}. FT CONFLICT 240 242 ILA -> FLP (in Ref. 1; AAC36867). FT {ECO:0000305}. FT CONFLICT 389 400 RQEIKDALAYLR -> LKKLKMRYAIFV (in Ref. 1; FT AAC36867). {ECO:0000305}. FT CONFLICT 459 460 ST -> QQ (in Ref. 1; AAC36867). FT {ECO:0000305}. FT CONFLICT 638 643 AELPRE -> GRITER (in Ref. 1; AAC36867). FT {ECO:0000305}. SQ SEQUENCE 727 AA; 83712 MW; 67FD98A7E455677E CRC64; MMDISELLDG LNDKQRERVA APLGNHLVLA GAGSGKTRVL THRIAWLIAV ENISEGSIMA VTFTNKAAAE MRHRIQSTLA KHAQHQLFGM WIGTFHSIAH RLLRAHHLDV GLPQDFQILD SEDQLRLIKR LLKLHNFDEK AFPPKQACWY INNKKDEGLR PNDIEDFNDR QEREWIKIYQ IYQDTCDRAG LVDFAELLIR VYELFEKKPL ILQRYQQRFQ HILVDEFQDT NKIQYKWIKI LAGKTGQVMI VGDDDQSIYG WRGAQIENIQ KFLKDFKAET IRLEQNYRST ANILNSANEL IANNSDRLGK NLWTEGEKGD PVGIYSAFNE LDEAKFVASQ IQDWVEHGGK LDDCAVLYRS NSQSRVIEEA LIRCQIPYRI YGGMRFFERQ EIKDALAYLR LINNRQDDAA FERVINTPTR GIGDRTLDIL RNLTRERQIT LWQAVQVATQ ENMLAGRAST ALLRFQELIN SLQLDTAEMP LFAQTDFVIK HSGLYEMYQQ EKGEKGEVRI ENLEELVTAT REFIKPDNAE EMTELTAFLT HASLEAGEEQ ASPHQSCVEM MTLHSAKGLE FPRVFMVGVE EGLFPSFRSF EEPGRLEEER RLAYVGITRA KKKLTISYAE SRRLYAKEER HLPSRFIAEL PRECIQEIRL RGTVTRAMNL AKVGSLSNTS AVENEWKMGQ KVKHEKFGFG TVINVEGSEN NTRLQIAFQA QGIKWLIAHL AKLEKVR // ID VG35_HAEIN Reviewed; 128 AA. AC P44228; P44229; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 11-NOV-2015, entry version 72. DE RecName: Full=Mu-like prophage FluMu protein gp35; GN OrderedLocusNames=HI_1506/HI_1507; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP STRUCTURE BY NMR, IDENTIFICATION, AND SUBUNIT. RX PubMed=17400915; DOI=10.1110/ps.072820907; RA Sari N., He Y., Doseeva V., Surabian K., Ramprakash J., Schwarz F., RA Herzberg O., Orban J.; RT "Solution structure of HI1506, a novel two-domain protein from RT Haemophilus influenzae."; RL Protein Sci. 16:977-982(2007). CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17400915}. CC -!- SIMILARITY: To phage Mu protein gp35. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23165.1; Type=Frameshift; Positions=68; Note=Produces two separate ORFs.; Evidence={ECO:0000305}; CC Sequence=AAC23166.1; Type=Frameshift; Positions=68; Note=Produces two separate ORFs.; 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; L42023; AAC23165.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC23166.1; ALT_FRAME; Genomic_DNA. DR PIR; D64033; D64033. DR PIR; E64033; E64033. DR PDB; 2OUT; NMR; -; A=1-67. DR PDBsum; 2OUT; -. DR STRING; 71421.HI1506; -. DR EnsemblBacteria; AAC23165; AAC23165; HI_1506. DR EnsemblBacteria; AAC23166; AAC23166; HI_1507. DR PATRIC; 20191735; VBIHaeInf48452_1576. DR OrthoDB; EOG60CWVK; -. DR EvolutionaryTrace; P44228; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:InterPro. DR InterPro; IPR025856; HeH/LEM_domain. DR InterPro; IPR011112; Rho_N. DR Pfam; PF12949; HeH; 1. DR SUPFAM; SSF68912; SSF68912; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 128 Mu-like prophage FluMu protein gp35. FT /FTId=PRO_0000077827. FT STRAND 7 10 {ECO:0000244|PDB:2OUT}. FT STRAND 20 22 {ECO:0000244|PDB:2OUT}. FT STRAND 26 30 {ECO:0000244|PDB:2OUT}. FT STRAND 34 36 {ECO:0000244|PDB:2OUT}. FT HELIX 37 43 {ECO:0000244|PDB:2OUT}. SQ SEQUENCE 128 AA; 13841 MW; 51CF32E9A1E8CE30 CRC64; MDKTFCVVVQ NRIKEGYRRA GFSFHLGDNS LAAVSESQLA QLKADPRLVV QITETGSQEG GEGLSKEPAG SDEQKQLRAD PPSTDLNTFT VEQLKAQLTE RGITFKQSAT KAELIALFAP ADGEKSEA // ID URE2_HAEIN Reviewed; 101 AA. AC P44392; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Urease subunit beta {ECO:0000255|HAMAP-Rule:MF_01954}; DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01954}; DE AltName: Full=Urea amidohydrolase subunit beta {ECO:0000255|HAMAP-Rule:MF_01954}; GN Name=ureB {ECO:0000255|HAMAP-Rule:MF_01954}; GN OrderedLocusNames=HI_0540; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Urea + H(2)O = CO(2) + 2 NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01954}. CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) CC from urea (urease route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01954}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC CC (alpha) subunits. Three heterotrimers associate to form the active CC enzyme. {ECO:0000255|HAMAP-Rule:MF_01954}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01954}. CC -!- SIMILARITY: Belongs to the urease beta subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01954}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22198.1; -; Genomic_DNA. DR PIR; I64075; I64075. DR RefSeq; NP_438698.1; NC_000907.1. DR RefSeq; WP_005687041.1; NC_000907.1. DR ProteinModelPortal; P44392; -. DR SMR; P44392; 1-101. DR STRING; 71421.HI0540; -. DR EnsemblBacteria; AAC22198; AAC22198; HI_0540. DR GeneID; 950763; -. DR KEGG; hin:HI0540; -. DR PATRIC; 20189633; VBIHaeInf48452_0559. DR eggNOG; ENOG4105KI2; Bacteria. DR eggNOG; COG0832; LUCA. DR KO; K01429; -. DR OMA; NGKVMGK; -. DR OrthoDB; EOG69PQ9G; -. DR PhylomeDB; P44392; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.10.150.10; -; 1. DR HAMAP; MF_01954; Urease_beta; 1. DR InterPro; IPR002019; Urease_beta. DR Pfam; PF00699; Urease_beta; 1. DR SUPFAM; SSF51278; SSF51278; 1. DR TIGRFAMs; TIGR00192; urease_beta; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1 101 Urease subunit beta. FT /FTId=PRO_0000067576. SQ SEQUENCE 101 AA; 11161 MW; DA7919DDA10F6C47 CRC64; MIPGEYQLAE GDILANVGRK TVKIEVTNSG DRPIQVGSHY HFFETNNALK FDRTLARGMR LNVPSGNAVR FEPGEVKSVE LVAFGGNQII YGFHNQIDGK L // ID UUP2_HAEIN Reviewed; 459 AA. AC P45167; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 93. DE RecName: Full=ABC transporter ATP-binding protein uup-2; GN Name=uup-B; OrderedLocusNames=HI_1342; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF CC family. EF3 subfamily. {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; L42023; AAC22987.1; -; Genomic_DNA. DR PIR; B64171; B64171. DR RefSeq; NP_439494.1; NC_000907.1. DR RefSeq; WP_010869185.1; NC_000907.1. DR ProteinModelPortal; P45167; -. DR STRING; 71421.HI1342; -. DR EnsemblBacteria; AAC22987; AAC22987; HI_1342. DR GeneID; 950264; -. DR KEGG; hin:HI1342; -. DR PATRIC; 20191369; VBIHaeInf48452_1395. DR eggNOG; COG0488; LUCA. DR OMA; ILENANF; -. DR OrthoDB; EOG6F297F; -. DR PhylomeDB; P45167; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; 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; IPR032524; ABC_tran_C. DR InterPro; IPR032781; ABC_tran_Xtn. 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 Pfam; PF16326; ABC_tran_CTD; 1. DR Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 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 1 459 ABC transporter ATP-binding protein uup- FT 2. FT /FTId=PRO_0000093031. FT DOMAIN 132 350 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 164 171 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 459 AA; 52467 MW; B4C1532C4EBCAA8E CRC64; MEAIEWLENF LLDFQGSIVF ISHDRSVIRK MATRIVDLDR GQLQSYLGNY DLYLTTKEEN LRVEALQNEL FDKRLAQEDV WIRQGIKARR TRNEGRVRAL KAMREERRQR REVMGTAKLQ LDTSSRSGKI VFEMEDVSYE IAGKTLLKDF STTILRGDKI ALVGPNGCGK TTFIKLLLGE IQPTSGKIRC GTKLEIAYFD QYRADLDPEK IVMDNVADGK QDIEINGVKR HVLGYLQEFL FPPKRAMTPV KALSGGERNR LLLAKLLLKP NNLLILDEPT NDLDVETLEL LEEILTDYQG TLLIVSHDRQ FIDNTATECY LFEGEGRLNK YVGGFFDAKQ QQANFWASKA VEEQAKAKKS EPLKEESAVK NDRTSKPKSV KLSYKEQREL EQLPQLLEEL ETKITTLQAE IADPAFFQQA HDITDAKLKA LADTEAELET AFLRWEELEE KKNLADGKA // ID VAPC2_HAEIN Reviewed; 132 AA. AC P71363; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Ribonuclease VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Toxin VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=HI_0947; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. Its cognate antitoxin is VapB2 (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22608.1; -; Genomic_DNA. DR PIR; B64104; B64104. DR RefSeq; NP_439108.1; NC_000907.1. DR RefSeq; WP_005651560.1; NC_000907.1. DR ProteinModelPortal; P71363; -. DR STRING; 71421.HI0947; -. DR EnsemblBacteria; AAC22608; AAC22608; HI_0947. DR GeneID; 950223; -. DR KEGG; hin:HI0947; -. DR PATRIC; 20190553; VBIHaeInf48452_0989. DR eggNOG; ENOG4105M0J; Bacteria. DR eggNOG; COG1487; LUCA. DR KO; K18828; -. DR OMA; REFQRVE; -. DR OrthoDB; EOG6ZWJH4; -. DR PhylomeDB; P71363; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 132 Ribonuclease VapC2. FT /FTId=PRO_0000077981. FT DOMAIN 4 130 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 7 7 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 98 98 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 132 AA; 15148 MW; A04CBBCCE407B65A CRC64; MLKYMLDTNI VIYVIKRRPL EILSRFNQNA GKMCVSSITV AELYYGAEKS EYPERNIAVI EDFLSRLTIL DYQPKHAAHF GNIKAELSKQ GKLIGENDIH IAAHARSEGL ILVSNNLREF ERVIALRTEN WV // ID VCOM_HAEIN Reviewed; 39 AA. AC P71390; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Mu-like prophage FluMu protein com; GN OrderedLocusNames=HI_1522.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the com 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; L42023; AAC23179.1; -; Genomic_DNA. DR RefSeq; NP_439672.1; NC_000907.1. DR RefSeq; WP_005693545.1; NC_000907.1. DR EnsemblBacteria; AAC23179; AAC23179; HI_1522.1. DR GeneID; 950388; -. DR KEGG; hin:HI1522.1; -. DR eggNOG; COG4416; LUCA. DR OrthoDB; EOG644ZXP; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019294; Translation_reg_Com. DR Pfam; PF10122; Mu-like_Com; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 39 Mu-like prophage FluMu protein com. FT /FTId=PRO_0000077660. SQ SEQUENCE 39 AA; 4449 MW; 03B2A846C72E3147 CRC64; MQSIKTIRCT FCNKLLAKVG TVGYLEIKCP RCKVINFTK // ID VG29_HAEIN Reviewed; 520 AA. AC P44225; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Mu-like prophage FluMu protein gp29; GN OrderedLocusNames=HI_1501; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp29. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23151.1; -; Genomic_DNA. DR PIR; A64033; A64033. DR RefSeq; NP_439651.1; NC_000907.1. DR RefSeq; WP_010869229.1; NC_000907.1. DR STRING; 71421.HI1501; -. DR EnsemblBacteria; AAC23151; AAC23151; HI_1501. DR GeneID; 950368; -. DR KEGG; hin:HI1501; -. DR PATRIC; 20191723; VBIHaeInf48452_1571. DR eggNOG; ENOG4105QIB; Bacteria. DR eggNOG; COG4383; LUCA. DR OMA; VDIGFRI; -. DR OrthoDB; EOG6PP9Q8; -. DR PhylomeDB; P44225; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009279; DUF935. DR Pfam; PF06074; DUF935; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 520 Mu-like prophage FluMu protein gp29. FT /FTId=PRO_0000077825. SQ SEQUENCE 520 AA; 58369 MW; 4268923B5AE46DF1 CRC64; MQSRILDIHG NPFRFEADMQ TESESRLMPL QYHYSDHPAS GLTPAKAARI LRAAEQGDLV AQAELAEDME EKDTHILSEL SKRRGAITAV DWQIKPPRNA TPEEQRDAEM LQEILEDAVW LDDCIFDATD AILKGFSSQE IEWEQGLVGG LKLIKNVHWR DPAWFMTPAY QRNSLRLRDG TPEGAEMQQF GWVKHVARAK TGYLSRIGLV RTLVWPFIFK NYSVRDFAEF LEIYGLPLRL GKYPEGATDK EKQTLLRAVM SIGHNAGGII PRGMELEFEK AADGSDSTFM AMIEWAEKSA SKAILGGTLT SQADGATSTN ALGNVHNDVR LEIRNADLKR LAATLTRDLV YPLYALNCKS FNDARRIPRF EFDVAESEDL NAFADGLNKL VDIGFRIPKQ WAHDKLQVPI ATENEEVLAK SFQNPTAYMH SKADGKMAVL SVQPDPEDLL DNLEPTAEDY QAVIDPLLKP VVEALQKGGY EFAQEKLAIL YAEMNDEELE TLLTRAIFVS DLLGRANAKR // ID VG38_HAEIN Reviewed; 63 AA. AC P44232; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Mu-like prophage FluMu protein gp38; GN OrderedLocusNames=HI_1510; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp38. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23157.1; -; Genomic_DNA. DR PIR; H64033; H64033. DR RefSeq; NP_439660.1; NC_000907.1. DR RefSeq; WP_005693531.1; NC_000907.1. DR STRING; 71421.HI1510; -. DR EnsemblBacteria; AAC23157; AAC23157; HI_1510. DR GeneID; 950834; -. DR KEGG; hin:HI1510; -. DR PATRIC; 20191743; VBIHaeInf48452_1580. DR eggNOG; ENOG4107BVY; Bacteria. DR eggNOG; ENOG410Z1N3; LUCA. DR OMA; YWLRRIK; -. DR OrthoDB; EOG6RG04W; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR024400; DUF2635. DR Pfam; PF10948; DUF2635; 1. DR ProDom; PD027295; PD027295; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 63 Mu-like prophage FluMu protein gp38. FT /FTId=PRO_0000077833. SQ SEQUENCE 63 AA; 7161 MW; B1B11A81352A1E67 CRC64; MPTFKIKPKT GLLIRDPETF ELLSESGEDK PKISYWLNHL KNGDVELVTE TTTKAKNSNK EQA // ID VG48_HAEIN Reviewed; 168 AA. AC P44241; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Mu-like prophage FluMu protein gp48; GN OrderedLocusNames=HI_1521; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp48 an E.coli YmfQ. 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; L42023; AAC23170.1; -; Genomic_DNA. DR PIR; H64034; H64034. DR RefSeq; NP_439670.2; NC_000907.1. DR STRING; 71421.HI1521; -. DR DNASU; 950386; -. DR EnsemblBacteria; AAC23170; AAC23170; HI_1521. DR GeneID; 950386; -. DR KEGG; hin:HI1521; -. DR PATRIC; 20191767; VBIHaeInf48452_1592. DR eggNOG; ENOG41061A0; Bacteria. DR eggNOG; COG3778; LUCA. DR OMA; EFVFIYE; -. DR OrthoDB; EOG6MD95C; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR018755; Phage_Mu_Gp48. DR Pfam; PF10076; DUF2313; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 168 Mu-like prophage FluMu protein gp48. FT /FTId=PRO_0000077848. SQ SEQUENCE 168 AA; 19820 MW; 2D41FEB8F7F754B1 CRC64; MLAVRCDQLV EVNSKAHTLI KERMPGQATL LLEEWEGFYG LPECGRQIVG KTLVQRQKQV QEKENEVGSN SKRFLEEIAT QAGFKVRVVN HYPHHCLRDC TYPLYEQANH WRIFMYTPAV SSIRYATCLD DVVKNLTIFE RNKELECLLK RYQYAHLEFV FIYEEETQ // ID URAA_HAEIN Reviewed; 414 AA. AC P45117; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Probable uracil permease; DE AltName: Full=Uracil transporter; GN Name=uraA; OrderedLocusNames=HI_1227; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transport of uracil in the cell. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the xanthine/uracil permease family. CC Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) 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; L42023; AAC22880.1; -; Genomic_DNA. DR PIR; D64111; D64111. DR RefSeq; NP_439383.1; NC_000907.1. DR RefSeq; WP_005694289.1; NC_000907.1. DR STRING; 71421.HI1227; -. DR DNASU; 950172; -. DR EnsemblBacteria; AAC22880; AAC22880; HI_1227. DR GeneID; 950172; -. DR KEGG; hin:HI1227; -. DR PATRIC; 20191133; VBIHaeInf48452_1279. DR eggNOG; ENOG4105C2W; Bacteria. DR eggNOG; COG2233; LUCA. DR KO; K02824; -. DR OMA; QTWGIAT; -. DR OrthoDB; EOG6Z3KKZ; -. DR PhylomeDB; P45117; -. DR Proteomes; UP000000579; 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:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006042; Xan_ur_permease. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR TIGRFAMs; TIGR00801; ncs2; 1. DR PROSITE; PS01116; XANTH_URACIL_PERMASE; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 414 Probable uracil permease. FT /FTId=PRO_0000165960. FT TOPO_DOM 1 14 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 15 38 Helical. {ECO:0000250}. FT TOPO_DOM 39 42 Periplasmic. {ECO:0000250}. FT TRANSMEM 43 62 Helical. {ECO:0000250}. FT TOPO_DOM 63 65 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 66 82 Discontinuously helical. {ECO:0000250}. FT TOPO_DOM 83 91 Periplasmic. {ECO:0000250}. FT TRANSMEM 92 112 Helical. {ECO:0000250}. FT TOPO_DOM 113 124 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 125 146 Helical. {ECO:0000250}. FT TOPO_DOM 147 155 Periplasmic. {ECO:0000250}. FT TRANSMEM 156 171 Helical. {ECO:0000250}. FT TOPO_DOM 172 178 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 179 199 Helical. {ECO:0000250}. FT TOPO_DOM 200 224 Periplasmic. {ECO:0000250}. FT TRANSMEM 225 248 Helical. {ECO:0000250}. FT TOPO_DOM 249 261 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 262 281 Helical. {ECO:0000250}. FT TRANSMEM 282 298 Discontinuously helical. {ECO:0000250}. FT TOPO_DOM 299 301 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 302 319 Helical. {ECO:0000250}. FT TOPO_DOM 320 332 Periplasmic. {ECO:0000250}. FT TRANSMEM 333 354 Helical. {ECO:0000250}. FT TOPO_DOM 355 365 Cytoplasmic. {ECO:0000250}. FT INTRAMEM 366 401 Discontinuously helical. {ECO:0000250}. FT TOPO_DOM 402 414 Cytoplasmic. {ECO:0000250}. FT BINDING 74 74 Uracil; via amide nitrogen. FT {ECO:0000250}. FT BINDING 241 241 Uracil. {ECO:0000250}. FT BINDING 290 290 Uracil. {ECO:0000250}. SQ SEQUENCE 414 AA; 43572 MW; 25361ABC22FE08B7 CRC64; MTNQIPPSLA ENQSKLKQSF VGLQMLFVAF GALVLVPLIT GLDSNTALLT AGVGTLLFQF CTGKQVPIFL ASSFAFIAPI QYGVQTWGIA TTMGGLAFTG LVYFALSTLV KLRGAEALQR FFPPVVVGPV IIIIGMGLAP IAVDMSLGKN SAYAYNDAVL VSMVTLLTTL SVAVFAKGLM KLIPIMFGIT AGYILCLFLG LINFQPVIDA PWFSLPKLTT PEFNLEAILY MLPIAIAPAV EHVGGIMAIS SVTGKDFLKK PGLHRTLLGD GIATAAASLV GGPPNTTYAE VTGAVMLTRN FNPNIMTWAA VWAIAISFCG KVGAFLSTIP TIVMGGIMML VFGSIAVVGM STLIRGKVDV TEARNLCIIS VVMTFGIGNM FVDVGNVSLK GISLCAIVAI ILNLVLPKAK NEVE // ID VAPD_HAEIN Reviewed; 91 AA. AC P71351; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Endoribonuclease VapD; DE EC=3.1.-.-; DE AltName: Full=Virulence-associated protein D; GN Name=vapD; OrderedLocusNames=HI_0450; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 76-80. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Cleaves ssRNA, mostly between U:A. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the VapD ribonuclease 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; L42023; AAC22108.1; -; Genomic_DNA. DR PIR; C64069; C64069. DR RefSeq; NP_438611.1; NC_000907.1. DR RefSeq; WP_005693712.1; NC_000907.1. DR STRING; 71421.HI0450; -. DR EnsemblBacteria; AAC22108; AAC22108; HI_0450. DR GeneID; 949544; -. DR KEGG; hin:HI0450; -. DR PATRIC; 20189455; VBIHaeInf48452_0470. DR eggNOG; ENOG4105K60; Bacteria. DR eggNOG; COG3309; LUCA. DR OMA; NMNEDMA; -. DR OrthoDB; EOG6XQ3QN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR016368; Virulence-assoc_VapD. DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2. DR Pfam; PF09827; CRISPR_Cas2; 1. DR PIRSF; PIRSF002882; VapD; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Hydrolase; Nuclease; KW Reference proteome; Virulence. FT CHAIN 1 91 Endoribonuclease VapD. FT /FTId=PRO_0000217271. SQ SEQUENCE 91 AA; 10543 MW; 70B23CDE28E083E7 CRC64; MYAIAFLVVK DTQDYHPKGV QQAYTDIGAV LAKFGFVRTQ GSLYINMNED MANLFQAMNA LKQLAWISQS VRDIRAFRIE QWSDFTDFIR N // ID VG36_HAEIN Reviewed; 141 AA. AC P44230; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=Mu-like prophage FluMu protein gp36; GN OrderedLocusNames=HI_1508; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp36. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23155.1; -; Genomic_DNA. DR PIR; F64033; F64033. DR RefSeq; NP_439658.1; NC_000907.1. DR RefSeq; WP_005693528.1; NC_000907.1. DR STRING; 71421.HI1508; -. DR EnsemblBacteria; AAC23155; AAC23155; HI_1508. DR GeneID; 950376; -. DR KEGG; hin:HI1508; -. DR PATRIC; 20191739; VBIHaeInf48452_1578. DR eggNOG; ENOG4105Y5J; Bacteria. DR eggNOG; COG4387; LUCA. DR OMA; LEEMTHR; -. DR OrthoDB; EOG6JTCCG; -. DR PhylomeDB; P44230; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009752; Phage_Mu_Gp36. DR Pfam; PF07030; DUF1320; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 141 Mu-like prophage FluMu protein gp36. FT /FTId=PRO_0000077829. SQ SEQUENCE 141 AA; 15873 MW; F282EFAC8442CAD2 CRC64; MVLYANRESL IKRYTLKVLE QIAWLPEAQS LDEAKVQEAL EDASQTIDSY LGGRYVLPLK TVPAVLERHC CYIARYFLEK NRATDQARQD YEDTIRFLEK VASGAISLGL SDDDETVESE NGAMMESAGS VWGRNTSKGF I // ID VPB_HAEIN Reviewed; 287 AA. AC P96343; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Mu-like prophage FluMu DNA transposition protein B; GN OrderedLocusNames=HI_1481; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: This protein is a non-specific DNA-binding and ATP- CC hydrolyzing protein essential for bacteriophage integration and CC replication. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23126.1; -; Genomic_DNA. DR PIR; C64126; C64126. DR RefSeq; NP_439632.1; NC_000907.1. DR RefSeq; WP_010869222.1; NC_000907.1. DR ProteinModelPortal; P96343; -. DR STRING; 71421.HI1481; -. DR EnsemblBacteria; AAC23126; AAC23126; HI_1481. DR GeneID; 950585; -. DR KEGG; hin:HI1481; -. DR PATRIC; 20191677; VBIHaeInf48452_1548. DR eggNOG; ENOG4108WTW; Bacteria. DR eggNOG; COG2842; LUCA. DR KO; K07132; -. DR OMA; HEYARLW; -. DR OrthoDB; EOG64R633; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 1.10.1180.10; -; 1. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR009084; B_transpositn_C. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13401; AAA_22; 1. DR Pfam; PF09077; Phage-MuB_C; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF47681; SSF47681; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA integration; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome; Transposition. FT CHAIN 1 287 Mu-like prophage FluMu DNA transposition FT protein B. FT /FTId=PRO_0000149719. FT DOMAIN 7 62 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 18 37 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT NP_BIND 98 105 ATP. {ECO:0000255}. SQ SEQUENCE 287 AA; 31488 MW; 5BAA47FE2BD03DC3 CRC64; MTLINKLKQH LSDSQITQAQ LAREAGVNAG ALSAYLNDNY KGNIADVEAK LAAYLEKKAV QAREFVEAPA FIETATSRQI FKTLEFAQIA NCLATVYGMS GVGKTKAIQE FAKSHANVWL VTASPSRSSL SEILYEIALE LGISDAPRRK GTLSRLIARK IKGTEGLLIV DEADHLPYEA LEELRIMQEE AGIGLVLVGN DKVYTRMKGG ISPSHEYARL WSRVAKNTSI QKTKKADTQA VAQAWGLETD EEALKVMQSI TETGGGLRIL TQTYACRNGS KRIWQVD // ID VPG2_HAEIN Reviewed; 138 AA. AC P45255; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Mu-like prophage FluMu G protein 2; GN OrderedLocusNames=HI_1568; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein G. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23215.1; -; Genomic_DNA. DR PIR; B64130; B64130. DR RefSeq; NP_439715.1; NC_000907.1. DR RefSeq; WP_005693592.1; NC_000907.1. DR STRING; 71421.HI1568; -. DR EnsemblBacteria; AAC23215; AAC23215; HI_1568. DR GeneID; 950426; -. DR KEGG; hin:HI1568; -. DR PATRIC; 20191861; VBIHaeInf48452_1639. DR eggNOG; ENOG4107XYH; Bacteria. DR eggNOG; COG5005; LUCA. DR OMA; AWKKLKI; -. DR OrthoDB; EOG6V7BR4; -. DR PhylomeDB; P45255; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006522; Phage_virion_morphogenesis. DR Pfam; PF05069; Phage_tail_S; 1. DR TIGRFAMs; TIGR01635; tail_comp_S; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Mu-like prophage FluMu G protein 2. FT /FTId=PRO_0000077684. SQ SEQUENCE 138 AA; 15204 MW; E8E55F140BF80E9F CRC64; MIEIEINNAQ EITSALERLA QATAHRAPLM RSIAGTMESA VAQNFEVGGR PAWKKLKIRQ GTPLVDTENL MASITSEYNN NEAIVGTNEP YAAIHQFGGK AGRGRKVAIP ARPFLILTPQ DEADILEDIQ DYFQLLIK // ID VPN_HAEIN Reviewed; 455 AA. AC P71389; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Mu-like prophage FluMu DNA circularization protein; GN OrderedLocusNames=HI_1515; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein N. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23161.1; -; Genomic_DNA. DR RefSeq; NP_439665.1; NC_000907.1. DR RefSeq; WP_010869234.1; NC_000907.1. DR STRING; 71421.HI1515; -. DR EnsemblBacteria; AAC23161; AAC23161; HI_1515. DR GeneID; 950381; -. DR KEGG; hin:HI1515; -. DR PATRIC; 20191753; VBIHaeInf48452_1585. DR eggNOG; ENOG4108NKR; Bacteria. DR eggNOG; COG4228; LUCA. DR OMA; RIVSHEY; -. DR OrthoDB; EOG6W19M8; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR InterPro; IPR009826; DNA_circ_N. DR Pfam; PF07157; DNA_circ_N; 1. DR ProDom; PD332323; DNA_circ_N; 1. PE 4: Predicted; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 455 Mu-like prophage FluMu DNA FT circularization protein. FT /FTId=PRO_0000077691. FT DNA_BIND 368 387 H-T-H motif. {ECO:0000255}. SQ SEQUENCE 455 AA; 50842 MW; B1999206C2C60DBB CRC64; MASKITGKGS FRGVPFLIEE EQGLDGGRRI VSHEYPLRDE GLTEDMGKRL RRYQVSCLVI GDDHLAQAEK LIDALEASGA GTLKHPYFGT IEVRVDDYRA KNSTNHQRVT RFDINFLPAI EKNAPEIAED TAYSVLSEYQ ATLNSLSDEF AEMVQDVSGF IESMVDNPLF RLADTTAAFI ENIFEGVANT VSGLTEVKDK ALSIKNRLSN LLLTPKVLAY ELQQLTRLNV RSAVNSQRQF VQHIVITDSI SSALGDLTAT KNEISKSTLD EMVTAKTNNV AETEILARQF KNLHEQEIFD ALMNKTTFLL KRLVLSTLAV EYGKAISDAV TESVAQKTVT EETIATLIES KTDVQRYIAE VDEQLEAVIL DNADAEQWTS YAALEQYRLT LMRDLQIRGE RLANAIEVKL NDTYPAILLE YRHTGNSKTW KRLALRNGIS HPLFCLGGTT LEVLQ // ID UREF_HAEIN Reviewed; 235 AA. AC P44395; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 11-NOV-2015, entry version 80. DE RecName: Full=Urease accessory protein UreF {ECO:0000255|HAMAP-Rule:MF_01385}; GN Name=ureF {ECO:0000255|HAMAP-Rule:MF_01385}; GN OrderedLocusNames=HI_0537; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for maturation of urease via the functional CC incorporation of the urease nickel metallocenter. CC {ECO:0000255|HAMAP-Rule:MF_01385}. CC -!- SUBUNIT: UreD, UreF and UreG form a complex that acts as a GTP- CC hydrolysis-dependent molecular chaperone, activating the urease CC apoprotein by helping to assemble the nickel containing CC metallocenter of UreC. The UreE protein probably delivers the CC nickel. {ECO:0000255|HAMAP-Rule:MF_01385}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01385}. CC -!- SIMILARITY: Belongs to the UreF family. {ECO:0000255|HAMAP- CC Rule:MF_01385}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22195.1; 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; L42023; AAC22195.1; ALT_INIT; Genomic_DNA. DR PIR; F64075; F64075. DR RefSeq; NP_438695.2; NC_000907.1. DR RefSeq; WP_005694141.1; NC_000907.1. DR STRING; 71421.HI0537; -. DR EnsemblBacteria; AAC22195; AAC22195; HI_0537. DR GeneID; 949598; -. DR KEGG; hin:HI0537; -. DR PATRIC; 20189627; VBIHaeInf48452_0556. DR eggNOG; ENOG4107Z51; Bacteria. DR eggNOG; COG0830; LUCA. DR KO; K03188; -. DR OMA; GEEQQLM; -. DR OrthoDB; EOG6DG2X9; -. DR PhylomeDB; P44395; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR HAMAP; MF_01385; UreF; 1. DR InterPro; IPR002639; UreF. DR Pfam; PF01730; UreF; 1. DR PIRSF; PIRSF009467; Ureas_acces_UreF; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Nickel insertion; KW Reference proteome. FT CHAIN 1 235 Urease accessory protein UreF. FT /FTId=PRO_0000067647. SQ SEQUENCE 235 AA; 26386 MW; 38C923A64E5B0E73 CRC64; MAQTLNRSLT DLGALLHLVD PTLPIGGFNH SNGLETFVQQ RVVESKATLE EYVQTQLLQN WIYNDGAYLS LAFDAMCEGN FDRLCELDWQ LSATKVARES REGSFKLGVR LLKIFIRYET HTLLTAYQQA IAEKRVQGYF PIVFAMVAQA MGLSKADTLY AFYYNAAVGV ITNGVKLIPL SQMDGQDILF DLRGSLVQAV ELSLDPDEEW LGAATLANDI RAMQHEVLYT RLYMS // ID USG_HAEIN Reviewed; 317 AA. AC P45201; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=USG-1 protein homolog; GN Name=usg; OrderedLocusNames=HI_1433; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23080.1; -; Genomic_DNA. DR PIR; B64123; B64123. DR RefSeq; NP_439582.1; NC_000907.1. DR RefSeq; WP_005693928.1; NC_000907.1. DR ProteinModelPortal; P45201; -. DR STRING; 71421.HI1433; -. DR EnsemblBacteria; AAC23080; AAC23080; HI_1433. DR GeneID; 950338; -. DR KEGG; hin:HI1433; -. DR PATRIC; 20191561; VBIHaeInf48452_1490. DR eggNOG; ENOG4105CM3; Bacteria. DR eggNOG; COG0136; LUCA. DR OMA; WSVADEQ; -. DR OrthoDB; EOG6K3ZZ1; -. DR PhylomeDB; P45201; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR Pfam; PF01118; Semialdhyde_dh; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 317 USG-1 protein homolog. FT /FTId=PRO_0000141403. SQ SEQUENCE 317 AA; 35414 MW; 8A2278C731B381A5 CRC64; MDATLNIAIA AEFELSEKIV ERLEQSALEI SKVSIVEIIP FEEEQNIRFR NKGVEQLSPN EVEWADFNYV FFAGKLEQVS HIAQAAEQGC IVIDMLGVCS ALSDVPVVVP TVNESQLLEL RQRNIVSLPD PQVSQLALTL APILQETNLN QVFVTSLLPA SYTDAETVTK LAGQTARLLN GIPLDEEETR LAFDVYPYQT PNLSNQLQRI FPQLDRATFH AIQVPVFYGL AQKVTALSDY DFDYQPQNSE LIALEETLIT PVLNGEQENG EESVKLHLSQ ISAVENGVEF WSVADEQRFN LALLSVKLLE GIYQQGY // ID USPE_HAEIN Reviewed; 309 AA. AC P44195; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 82. DE RecName: Full=Universal stress protein E homolog; GN Name=uspE; OrderedLocusNames=HI_1426; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Required for resistance to DNA-damaging agents. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the universal stress protein A family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23063.1; 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; L42023; AAC23063.1; ALT_INIT; Genomic_DNA. DR PIR; G64029; G64029. DR RefSeq; NP_439575.2; NC_000907.1. DR RefSeq; WP_010869209.1; NC_000907.1. DR ProteinModelPortal; P44195; -. DR STRING; 71421.HI1426; -. DR EnsemblBacteria; AAC23063; AAC23063; HI_1426. DR GeneID; 950328; -. DR KEGG; hin:HI1426; -. DR PATRIC; 20191547; VBIHaeInf48452_1483. DR eggNOG; ENOG4105Q9Y; Bacteria. DR eggNOG; COG0589; LUCA. DR KO; K14055; -. DR OMA; MAKYQNM; -. DR OrthoDB; EOG6SBT15; -. DR PhylomeDB; P44195; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 2. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR006016; UspA. DR Pfam; PF00582; Usp; 2. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 309 Universal stress protein E homolog. FT /FTId=PRO_0000147420. SQ SEQUENCE 309 AA; 35087 MW; C0016A9D991C840A CRC64; MKFKNILVVL NPSNEKQYAL ARAVRLVEEQ KNETKVKITA LLSVYDLSYE MSALLSSEER SEMHQQVIEK HRHAVQYYLD KYANPEIELQ SHIVWNSNEA DAINEEVENN NYDLVVKYTK DEEKLTSLIF TPIDWQLLRK CPIPVLMVRD GDWKHPRRIL VAVNVSGEQE YQDEFNQELV ETGISLAENL NRGNVHLVAA YPSAPINMAI DLPEFNTSGY ENGIRGQHLI NMKALRQKFG IDEDHTHVRE GFPEEVIPEV AKEIEAELVI LGTVGRTGLS AALLGNTAEH VISKLSCNLL GIKPSKKDD // ID VAPC1_HAEIN Reviewed; 134 AA. AC Q57122; O05016; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Ribonuclease VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Toxin VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=HI_0322; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Acts CC as an RNase, its toxic effect is neutralized by VapB1 antitoxin CC (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21985.1; -; Genomic_DNA. DR PIR; G64061; G64061. DR RefSeq; NP_438487.1; NC_000907.1. DR RefSeq; WP_010868975.1; NC_000907.1. DR ProteinModelPortal; Q57122; -. DR STRING; 71421.HI0322; -. DR EnsemblBacteria; AAC21985; AAC21985; HI_0322. DR GeneID; 949434; -. DR KEGG; hin:HI0322; -. DR PATRIC; 20189185; VBIHaeInf48452_0339. DR eggNOG; ENOG4105M0J; Bacteria. DR eggNOG; COG1487; LUCA. DR KO; K18828; -. DR OMA; WFACHAL; -. DR OrthoDB; EOG6ZWJH4; -. DR PhylomeDB; Q57122; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 134 Ribonuclease VapC1. FT /FTId=PRO_0000077910. FT DOMAIN 3 132 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 6 6 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 99 99 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 134 AA; 15726 MW; 7EC5014217A854F9 CRC64; MIYMLDTNII IYLMKNRPKI IAERVSQLLP NDRLVMSFIT YAELIKGAFG SQNYEQSIRA IELLTERVNV LYPNEQICLH YGKWANTLKK QGRPIGNNDL WFACHALSLN AVLITHNVKE FQRITDLQWQ DWTK // ID VG27_HAEIN Reviewed; 189 AA. AC P44223; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Mu-like prophage FluMu protein gp27; GN OrderedLocusNames=HI_1499; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp27. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23149.1; -; Genomic_DNA. DR PIR; H64032; H64032. DR RefSeq; NP_439649.1; NC_000907.1. DR RefSeq; WP_010869228.1; NC_000907.1. DR STRING; 71421.HI1499; -. DR EnsemblBacteria; AAC23149; AAC23149; HI_1499. DR GeneID; 950366; -. DR KEGG; hin:HI1499; -. DR PATRIC; 20191719; VBIHaeInf48452_1569. DR eggNOG; ENOG4108Z6H; Bacteria. DR eggNOG; ENOG4111QAG; LUCA. DR OMA; FVRTMAF; -. DR OrthoDB; EOG66HVJD; -. DR PhylomeDB; P44223; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR021874; Phage_Mu_Gp27. DR Pfam; PF11985; DUF3486; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 189 Mu-like prophage FluMu protein gp27. FT /FTId=PRO_0000077821. SQ SEQUENCE 189 AA; 21016 MW; 63F36035CC7F811E CRC64; MNDKTTRGRA SKVDLLPPNI KSTLTMMLRD KQYSQAEILE EINNIIADSG LDESMQLSKT GLNRFASKME RFGKKIREAR EVAEVWTKQL VEAPQSDIGK LLMEAVKTMA FDLTLNADEA VANDPKFLNQ LALIANRIEQ AQSISEERER KVRKEVAQQA ADTAEKVISQ AGLSADTVAQ IKQQILGIA // ID VG46_HAEIN Reviewed; 135 AA. AC P44239; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Mu-like prophage FluMu protein gp46; GN OrderedLocusNames=HI_1519; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp46. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23169.1; -; Genomic_DNA. DR PIR; F64034; F64034. DR RefSeq; NP_439668.1; NC_000907.1. DR RefSeq; WP_005693540.1; NC_000907.1. DR STRING; 71421.HI1519; -. DR EnsemblBacteria; AAC23169; AAC23169; HI_1519. DR GeneID; 950384; -. DR KEGG; hin:HI1519; -. DR PATRIC; 20191763; VBIHaeInf48452_1590. DR eggNOG; ENOG4105WR6; Bacteria. DR eggNOG; COG4381; LUCA. DR OMA; LIDDGHC; -. DR OrthoDB; EOG622PQM; -. DR PhylomeDB; P44239; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010877; Phage_Mu_Gp46. DR Pfam; PF07409; GP46; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 135 Mu-like prophage FluMu protein gp46. FT /FTId=PRO_0000077841. SQ SEQUENCE 135 AA; 14965 MW; 81D586FD1C0E0D19 CRC64; MSDLALTWHN GEGDLVLGTE SLLLDDSLTN AIIISLFTDL RVEGERGWWG DSYNDGFQTG SKLWTLSRAK QLPEILDDAQ LYASQALQWL VDDGVAKSVQ VIASNPQMSV LLLEILVVLP DGSTEQRTFR ANWSL // ID VGAM_HAEIN Reviewed; 169 AA. AC O05070; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Mu-like prophage FluMu host-nuclease inhibitor protein gam; GN OrderedLocusNames=HI_1483; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Protects linear double-stranded DNA of Mu genome from CC exonuclease degradation. {ECO:0000250}. CC -!- SIMILARITY: To phage Mu protein gam. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23132.1; -; Genomic_DNA. DR PIR; D64126; D64126. DR RefSeq; NP_439634.1; NC_000907.1. DR RefSeq; WP_005693500.1; NC_000907.1. DR ProteinModelPortal; O05070; -. DR STRING; 71421.HI1483; -. DR EnsemblBacteria; AAC23132; AAC23132; HI_1483. DR GeneID; 950566; -. DR KEGG; hin:HI1483; -. DR PATRIC; 20191681; VBIHaeInf48452_1550. DR eggNOG; ENOG4105IKI; Bacteria. DR eggNOG; COG4396; LUCA. DR OMA; TWCEAHR; -. DR OrthoDB; EOG61CM15; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro. DR GO; GO:0042262; P:DNA protection; IEA:InterPro. DR InterPro; IPR009951; Host-nuc_inhib_Gam. DR Pfam; PF07352; Phage_Mu_Gam; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 169 Mu-like prophage FluMu host-nuclease FT inhibitor protein gam. FT /FTId=PRO_0000077640. SQ SEQUENCE 169 AA; 19193 MW; EC142FE852098006 CRC64; MATKVKSQAK LRFVSVEQVQ SAIKEIGDLS REHTRLATEM NDKIGATSEH YAPKLKALKE EIEPLQKAVQ EYCEANRDEL TEFGKTKTAN FVTGEVQWRQ RPPSVAIRGA EAVMEFLQRM GFDRFIRTRQ EINKEALLNE PEVAKGIAGV TIKQGLEDFV IKPFEQDAR // ID VPF_HAEIN Reviewed; 414 AA. AC P44226; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Mu-like prophage FluMu F protein; GN OrderedLocusNames=HI_1502; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in virion morphogenesis. {ECO:0000250}. CC -!- SIMILARITY: To phage Mu protein F. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23163.1; -; Genomic_DNA. DR PIR; B64033; B64033. DR RefSeq; NP_439652.1; NC_000907.1. DR RefSeq; WP_010869230.1; NC_000907.1. DR STRING; 71421.HI1502; -. DR EnsemblBacteria; AAC23163; AAC23163; HI_1502. DR GeneID; 950369; -. DR KEGG; hin:HI1502; -. DR PATRIC; 20191725; VBIHaeInf48452_1572. DR eggNOG; ENOG4108QUU; Bacteria. DR eggNOG; COG2369; LUCA. DR OMA; INKERTI; -. DR OrthoDB; EOG6SNDXQ; -. DR PhylomeDB; P44226; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006528; Phage_head_morphogenesis. DR Pfam; PF04233; Phage_Mu_F; 1. DR TIGRFAMs; TIGR01641; phageSPP1_gp7; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 414 Mu-like prophage FluMu F protein. FT /FTId=PRO_0000077681. SQ SEQUENCE 414 AA; 46495 MW; 1A86D2DA2EAE5F51 CRC64; MNITWNWYEQ LESAHARAFT VAKATKAEVL DTIRWATEQA IANGTGEREY IKKLEPMLKE LGWWGKAKDE NGNEVQLGSP RRLRTILRTN KITAYHAARY AQQMENVDEQ PYWRYVAVND SRTRASHLAL HGKIYRADDP IWQTMYPPND WGCRCRVEAL SEYAVQSRGL KISSSDGEME MEEAVVGIDK DTGEEIRTTV SKIKTDQGEM KVGAGWNYNV GSAAFGTDVA VLRKLQQVKN RELRQQTIQA INNSEARHKA FADWVLANLG KRGASARYMS AGLVTTEIAE AVTEITQGGK NAELVLVMSE KRLAHANSDK HHEGGVGLTA EEYASISRIV ANPSLVLWDT LEGHNNLIYI NQERTIQVIV DVPNKHSIKP KEKVDAIINA YKVDMNNVKR QLSGGNYVLL KGKL // ID VPL_HAEIN Reviewed; 487 AA. AC P44233; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Mu-like prophage FluMu tail sheath protein; GN OrderedLocusNames=HI_1511; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Major component of the tail. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the myoviridae tail sheath 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; L42023; AAC23158.1; -; Genomic_DNA. DR PIR; I64033; I64033. DR RefSeq; NP_439661.1; NC_000907.1. DR RefSeq; WP_005693532.1; NC_000907.1. DR STRING; 71421.HI1511; -. DR DNASU; 950573; -. DR EnsemblBacteria; AAC23158; AAC23158; HI_1511. DR GeneID; 950573; -. DR KEGG; hin:HI1511; -. DR PATRIC; 20191745; VBIHaeInf48452_1581. DR eggNOG; ENOG4105TKZ; Bacteria. DR eggNOG; COG4386; LUCA. DR OMA; TYTKDAQ; -. DR OrthoDB; EOG6TJ7X1; -. DR PhylomeDB; P44233; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007067; Tail_sheath. DR Pfam; PF04984; Phage_sheath_1; 1. DR PIRSF; PIRSF007349; Tsp_L; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 487 Mu-like prophage FluMu tail sheath FT protein. FT /FTId=PRO_0000077687. SQ SEQUENCE 487 AA; 53144 MW; EB81ECA37C1278A7 CRC64; MSISFNNIPS ALRVPLTYIE FDNTKAVSGP PTALHKVLML GTKLATGSAK AGEAVRVSAY AQAKTLFGRG SQLAEMVKTF KAHNSTLDLW VLPLDEAPSG AKATGSVQIT GTATQAGTFS LMIAGNNYKT AVTSGDTADV VAGKLQKLIA ADQDVPVVAT VAGNTITLTC RFKGETGNEI DLRCNYYSGE AFPEGLKATI TDMKNGAVNP DMSVAITGLG AEWWNYIINP FTDTESLNLL RADLVKRWGP LKQIDGICFM AKRGTHAEVT TFAEQRNDYL FSLLATHKAP QPAYLWASAY AAVVAGSLAI DPARPVQTLV MDLLPPSMSD RWDLPERNTL LYSGVSTYTV NAGSQPQVEA AITMYRKNAF GDNDESYLYV ETIATLSYLR YAIRSRITQK FPRHKLANDG TRIGPGQAIV TPKIIRNELL ALFTELEFAG LVEDFEQFNQ TLFVERDSNN PCRVNVLSNE NLVNQFRIYA HAIQFIL // ID UXUA_HAEIN Reviewed; 394 AA. AC P44488; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Mannonate dehydratase; DE EC=4.2.1.8; DE AltName: Full=D-mannonate hydro-lyase; GN Name=uxuA; OrderedLocusNames=HI_0055; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + CC H(2)O. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. CC -!- SIMILARITY: Belongs to the mannonate dehydratase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21733.1; -; Genomic_DNA. DR PIR; E64045; E64045. DR RefSeq; NP_438228.1; NC_000907.1. DR RefSeq; WP_010868927.1; NC_000907.1. DR ProteinModelPortal; P44488; -. DR STRING; 71421.HI0055; -. DR EnsemblBacteria; AAC21733; AAC21733; HI_0055. DR GeneID; 950950; -. DR KEGG; hin:HI0055; -. DR PATRIC; 20188563; VBIHaeInf48452_0055. DR eggNOG; ENOG4105CHZ; Bacteria. DR eggNOG; COG1312; LUCA. DR KO; K01686; -. DR OMA; EGDVDMY; -. DR OrthoDB; EOG6ZSP6Z; -. DR PhylomeDB; P44488; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0008927; F:mannonate dehydratase activity; IBA:GO_Central. DR GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00106; UxuA; 1. DR InterPro; IPR004628; Man_deHydtase. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF03786; UxuA; 1. DR PIRSF; PIRSF016049; Man_dehyd; 1. DR SUPFAM; SSF51658; SSF51658; 2. DR TIGRFAMs; TIGR00695; uxuA; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Lyase; Manganese; Reference proteome. FT CHAIN 1 394 Mannonate dehydratase. FT /FTId=PRO_0000170675. SQ SEQUENCE 394 AA; 45205 MW; CFE4DCE635AAAB0C CRC64; MEQAWRWYGP KDPVSLSDIR QAGATGIVTA LHHIPNGEIW GIEEIKKRKT EIENAGLSWS VVESVPVHEE IKTQTGNYQK WINNYKQTLR NLAQCGIDTV CYNFMPVLDW TRTDLAYELP DGSKALRFDH IAFAAFELHI LKRPDAEKTY NQEEQVAART YYDNMSEQDI AQLTRNIIAG LPGAEEGYTL DEFQTQLDRY KDISSEKFRT HLAYFLNEIV PVAQEIGIKM AIHPDDPPRP ILGLPRIVST IEDMQWFVET QPLPANGFTM CTGSYGVRSD NDLVKMTEQF ADRIYFAHLR STQREGNPLT FHEAAHLEGD VDMFNVVKAL LNEEYRRLNQ GETRLIPMRP DHGHQILDDL RKKTNPGYSA IGRLKGLAEF RGLEMALKKV YFNK // ID UXUR_HAEIN Reviewed; 266 AA. AC P44487; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=Uxu operon regulator; GN Name=uxuR; OrderedLocusNames=HI_0054; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Repressor for the uxuRBA operon. {ECO:0000250}. 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; L42023; AAC21732.1; -; Genomic_DNA. DR PIR; D64045; D64045. DR RefSeq; NP_438227.2; NC_000907.1. DR ProteinModelPortal; P44487; -. DR STRING; 71421.HI0054; -. DR EnsemblBacteria; AAC21732; AAC21732; HI_0054. DR GeneID; 950951; -. DR KEGG; hin:HI0054; -. DR PATRIC; 20188561; VBIHaeInf48452_0054. DR eggNOG; ENOG4107YCY; Bacteria. DR eggNOG; COG2186; LUCA. DR KO; K13637; -. DR OMA; MNHVSSL; -. DR OrthoDB; EOG6S52JF; -. DR BioCyc; RETL1328306-WGS:GSTH-4314-MONOMER; -. DR Proteomes; UP000000579; 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 Gene3D; 1.20.120.530; -; 1. DR InterPro; IPR011711; GntR_C. DR InterPro; IPR008920; TF_FadR/GntR_C. DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07729; FCD; 1. DR Pfam; PF00392; GntR; 1. DR PRINTS; PR00035; HTHGNTR. DR SMART; SM00895; FCD; 1. DR SMART; SM00345; HTH_GNTR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48008; SSF48008; 1. DR PROSITE; PS50949; HTH_GNTR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 266 Uxu operon regulator. FT /FTId=PRO_0000050671. FT DOMAIN 23 91 HTH gntR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00307}. FT DNA_BIND 51 70 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00307}. SQ SEQUENCE 266 AA; 30919 MW; B54E86EBA120CDC0 CRC64; MSHITKIKNW NTNLRKNMEN IVNRTYTRIG QLLKQDISQG IYSIGDKLPT EREISEKFGV SRTIVREAMV MLEVEKLVEV KKGSGVYVVR TPESIHMEHS DLPDVGPFEL LQARQLLESS IAEFAALQAT KKDILNLKQI LNREKELLTQ NQDDYSADKD FHLALAEITQ NDVLVKLQEQ LWQYRFNSAM WAQLHSRILQ NDYHHLWIED HQTILSAIQK KNANEARKAM WQHLENVKVK LFELSDVEDP HFDGYLFNTN PVVVGI // ID VG16_HAEIN Reviewed; 185 AA. AC P71387; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Mu-like prophage FluMu protein gp16; GN OrderedLocusNames=HI_1488; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp16. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23133.1; -; Genomic_DNA. DR PIR; E64126; E64126. DR RefSeq; NP_439638.1; NC_000907.1. DR RefSeq; WP_010869224.1; NC_000907.1. DR STRING; 71421.HI1488; -. DR DNASU; 950788; -. DR EnsemblBacteria; AAC23133; AAC23133; HI_1488. DR GeneID; 950788; -. DR KEGG; hin:HI1488; -. DR PATRIC; 20191693; VBIHaeInf48452_1556. DR eggNOG; ENOG4105ZIA; Bacteria. DR eggNOG; COG4382; LUCA. DR OMA; LIHIARN; -. DR OrthoDB; EOG654P35; -. DR PhylomeDB; P71387; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009363; Phage_Mu_Gp16. DR Pfam; PF06252; DUF1018; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 185 Mu-like prophage FluMu protein gp16. FT /FTId=PRO_0000077812. SQ SEQUENCE 185 AA; 20955 MW; 23C80042B2F22449 CRC64; MSEKAKLIQL IHIGKQQLNM DEFSYREMVK RLTNKTSSTK CTVVELLKIL HEMQQKGAKV KHFAKRGTKP TAYSPATGEV KVKSEIAHKI RAVWIQMGKH GFLADPSXKA LNSYMRKVMN KGKSVLALNV GALNSNDASR FLEILKKWHK RVMLKRLAEK YGCITSAETG YDELCLVFKN YQGVA // ID VG41_HAEIN Reviewed; 127 AA. AC P44235; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Mu-like prophage FluMu protein gp41; GN OrderedLocusNames=HI_1513; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp41. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23160.1; -; Genomic_DNA. DR PIR; B64034; B64034. DR RefSeq; NP_439663.1; NC_000907.1. DR RefSeq; WP_005693534.1; NC_000907.1. DR STRING; 71421.HI1513; -. DR EnsemblBacteria; AAC23160; AAC23160; HI_1513. DR GeneID; 950379; -. DR KEGG; hin:HI1513; -. DR PATRIC; 20191749; VBIHaeInf48452_1583. DR eggNOG; ENOG41062PQ; Bacteria. DR eggNOG; COG4518; LUCA. DR OMA; LATEMHD; -. DR OrthoDB; EOG6SJJR4; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019289; Phage_tail_Gp41_put. DR Pfam; PF10109; Phage_TAC_7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 127 Mu-like prophage FluMu protein gp41. FT /FTId=PRO_0000077835. SQ SEQUENCE 127 AA; 13978 MW; 77D94FC1CFDC0D36 CRC64; MKLMLETGLM FGEEAQLEVT MRELTTGDLL DAEMAAERLV MTPEGEAVLA KSPALFGYEL LRRQIASVGK INGPISMRQL RSLTTEDLNR ISLYAQSWES AKAEQVVSRG RLDTADQETG KDLSAVS // ID VG45_HAEIN Reviewed; 182 AA. AC P44238; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Mu-like prophage FluMu protein gp45; GN OrderedLocusNames=HI_1518; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp45. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23168.1; -; Genomic_DNA. DR PIR; E64034; E64034. DR RefSeq; NP_439667.1; NC_000907.1. DR RefSeq; WP_005693539.1; NC_000907.1. DR STRING; 71421.HI1518; -. DR EnsemblBacteria; AAC23168; AAC23168; HI_1518. DR GeneID; 950383; -. DR KEGG; hin:HI1518; -. DR PATRIC; 20191761; VBIHaeInf48452_1589. DR eggNOG; ENOG4105PZ7; Bacteria. DR eggNOG; COG4384; LUCA. DR OMA; KKFTIET; -. DR OrthoDB; EOG6SZ1MG; -. DR PhylomeDB; P44238; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR013046; GpV/Gp45. DR InterPro; IPR014462; Phage_Mu_Gp45. DR Pfam; PF06890; Phage_Mu_Gp45; 1. DR PIRSF; PIRSF012337; gp45; 1. DR TIGRFAMs; TIGR01644; phage_P2_V; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 182 Mu-like prophage FluMu protein gp45. FT /FTId=PRO_0000077839. SQ SEQUENCE 182 AA; 19774 MW; 4DB4BF8F773315FB CRC64; MQAINRIIAP LKRGLQLLVS RAVVSVVNDA YARQNLQLRL QSEEVADDVE RFQNYGHYSV PKAGEAIVVS VGGKRSHLVA VVVDDKSVRP AGLIAGDSVL YHLEGHQLRL TENGEAILSC KKFTIETDTL DCSAQQITFD SPQTTFTGNV DIMGISTATD HQSSGISGKN HDHEERVGKP VP // ID VPC_HAEIN Reviewed; 72 AA. AC P71388; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Mu-like prophage FluMu protein C; GN OrderedLocusNames=HI_1491; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Required for transcription of the phage late genes. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the c/mor transcriptional regulatory 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; L42023; AAC23135.1; -; Genomic_DNA. DR ProteinModelPortal; P71388; -. DR EnsemblBacteria; AAC23135; AAC23135; HI_1491. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR014875; Mor_transcription_activator. DR Pfam; PF08765; Mor; 1. DR SUPFAM; SSF46689; SSF46689; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 72 Mu-like prophage FluMu protein C. FT /FTId=PRO_0000062805. FT DNA_BIND 35 55 H-T-H motif. {ECO:0000250}. SQ SEQUENCE 72 AA; 8558 MW; 98E0268A8CA4BB45 CRC64; MAHYFGGKSF YLPAGDKIKE ALRDAQIYQE FNGKNVPDLI KKYRLSESTI YAILRNQRTL QRKRHQMDFN FS // ID VPS_HAEIN Reviewed; 623 AA. AC P44242; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Mu-like prophage FluMu defective tail fiber protein; GN OrderedLocusNames=HI_1522; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein S. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23178.1; -; Genomic_DNA. DR PIR; I64034; I64034. DR RefSeq; NP_439671.1; NC_000907.1. DR RefSeq; WP_005693543.1; NC_000907.1. DR STRING; 71421.HI1522; -. DR EnsemblBacteria; AAC23178; AAC23178; HI_1522. DR GeneID; 950387; -. DR KEGG; hin:HI1522; -. DR PATRIC; 20191769; VBIHaeInf48452_1593. DR eggNOG; ENOG4106IKR; Bacteria. DR eggNOG; ENOG410Y5DM; LUCA. DR OrthoDB; EOG6FJNMJ; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 623 Mu-like prophage FluMu defective tail FT fiber protein. FT /FTId=PRO_0000077694. SQ SEQUENCE 623 AA; 67678 MW; 5EE5A8E2818C0060 CRC64; MYHLDNDSGV STFALAPVKS TQRLWFTEGG HGNAISYPGA DWFNMVQAEL FSILDDAGIQ PDKGRLNQIS LAIRKLSEGK VEDFSQQLKQ ADGYKYIGRC KSVAELRTIR PTENGQRILV DAYYEGSTAG GGEFVADLQD LITPDDGGTC FVVPNNGGRW KRLFSSSLQD TDFGVIGGVA DDTTNLNAFL DALRTYKVKG YFTSRHYKTS AALNIAGVDI EGVLAGYKNK HGTRITGNGN HNIFEQMGGE LQHITYSLKN FALSGGIVGL KMTYAVNAVV ENVFIDNVER AFLLGDSQFV GPIWCSLKNC RGEGRISGLE IDGNKWANAN MFETCFFKGD EFAGSITAKG GIGAVSNHFV NTEFAGKGVG VKLGKNKSTA FDNCYFESEG PSLLIEDSTA DLALNNATFG SLTENNKTGK TSFIHHSLGT CNMSISSGYI YLAGNNQNNL AFIESDKPES LVVNMATPVK REIYTATGFK LFKNPDLPNK NSRVHYTSGY VCEFSSQNKN AELGNGDLTA YYNLNNSRCA VGLNLKIGSS TTKGTGQWQF RLPFQASGIG KYYLGQAIAI KADGSKLMTG VARIVGGSNQ VVAYFNNVNP ADATRPFEWT EGDRLDISIE YEI // ID UREG_HAEIN Reviewed; 225 AA. AC P44396; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Urease accessory protein UreG {ECO:0000255|HAMAP-Rule:MF_01389}; GN Name=ureG {ECO:0000255|HAMAP-Rule:MF_01389}; GN OrderedLocusNames=HI_0536; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Facilitates the functional incorporation of the urease CC nickel metallocenter. This process requires GTP hydrolysis, CC probably effectuated by UreG. {ECO:0000255|HAMAP-Rule:MF_01389}. CC -!- SUBUNIT: Homodimer. UreD, UreF and UreG form a complex that acts CC as a GTP-hydrolysis-dependent molecular chaperone, activating the CC urease apoprotein by helping to assemble the nickel containing CC metallocenter of UreC. The UreE protein probably delivers the CC nickel. {ECO:0000255|HAMAP-Rule:MF_01389}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389}. CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01389}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22194.1; -; Genomic_DNA. DR PIR; E64075; E64075. DR RefSeq; NP_438694.1; NC_000907.1. DR RefSeq; WP_005694139.1; NC_000907.1. DR ProteinModelPortal; P44396; -. DR STRING; 71421.HI0536; -. DR EnsemblBacteria; AAC22194; AAC22194; HI_0536. DR GeneID; 950530; -. DR KEGG; hin:HI0536; -. DR PATRIC; 20189625; VBIHaeInf48452_0555. DR eggNOG; ENOG4105E8T; Bacteria. DR eggNOG; COG0378; LUCA. DR KO; K03189; -. DR OMA; REDCSIN; -. DR OrthoDB; EOG6RC3T9; -. DR PhylomeDB; P44396; -. DR Proteomes; UP000000579; 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:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01389; UreG; 1. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004400; UreG. DR PANTHER; PTHR31715; PTHR31715; 1. DR Pfam; PF02492; cobW; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00101; ureG; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; GTP-binding; KW Nickel insertion; Nucleotide-binding; Reference proteome. FT CHAIN 1 225 Urease accessory protein UreG. FT /FTId=PRO_0000067665. FT NP_BIND 25 32 GTP. {ECO:0000255|HAMAP-Rule:MF_01389}. SQ SEQUENCE 225 AA; 24688 MW; 67EF1E467DADDD29 CRC64; MSNTVATMIN KRNIMRNYIK IGVAGPVGAG KTALIEKLTR EIASKYSVAV ITNDIYTQED AEFLTKNSLL PPERIMGVET GGCPHTAIRE DASMNLEAVD EMVTRFPDVE IVFIESGGDN LSATFSPDLA DVTIFVIDVA QGEKIPRKGG PGITRSDLLV INKTDLAPFV GADLSVMERD ARRMRNGQPF IFTNLMKKEN LDGVIGWIEK YALLKNVEEP ASLVR // ID VAPB1_HAEIN Reviewed; 78 AA. AC Q57534; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Antitoxin VapB1; GN Name=vapB1; OrderedLocusNames=HI_0321; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Neutralizes the effect of toxin VapC1 (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the VapB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SpoVT-AbrB domain. {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; L42023; AAC21984.1; -; Genomic_DNA. DR PIR; F64061; F64061. DR RefSeq; NP_438486.1; NC_000907.1. DR RefSeq; WP_005649046.1; NC_000907.1. DR ProteinModelPortal; Q57534; -. DR STRING; 71421.HI0321; -. DR EnsemblBacteria; AAC21984; AAC21984; HI_0321. DR GeneID; 949433; -. DR KEGG; hin:HI0321; -. DR PATRIC; 20189183; VBIHaeInf48452_0338. DR eggNOG; ENOG41084JJ; Bacteria. DR eggNOG; COG4456; LUCA. DR KO; K18829; -. DR OMA; RNDVAPQ; -. DR OrthoDB; EOG6KWZ2K; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR InterPro; IPR007159; SpoVT-AbrB_dom. DR Pfam; PF04014; MazE_antitoxin; 1. DR SMART; SM00966; SpoVT_AbrB; 1. DR PROSITE; PS51740; SPOVT_ABRB; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 78 Antitoxin VapB1. FT /FTId=PRO_0000077909. FT DOMAIN 3 44 SpoVT-AbrB. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. SQ SEQUENCE 78 AA; 9037 MW; 468D048ED7C5C720 CRC64; MLTKVFQSGN SQAVRIPMDF RFDVDTVEIF RKENGDVVLR PVSKKTDDFL ALFEGFDETF IQALEARDDL PPQERENL // ID VG28_HAEIN Reviewed; 508 AA. AC P44224; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Mu-like prophage FluMu protein gp28; GN OrderedLocusNames=HI_1500; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp28. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23150.1; -; Genomic_DNA. DR PIR; I64032; I64032. DR RefSeq; NP_439650.1; NC_000907.1. DR RefSeq; WP_005693520.1; NC_000907.1. DR STRING; 71421.HI1500; -. DR EnsemblBacteria; AAC23150; AAC23150; HI_1500. DR GeneID; 950367; -. DR KEGG; hin:HI1500; -. DR PATRIC; 20191721; VBIHaeInf48452_1570. DR eggNOG; ENOG4105CF2; Bacteria. DR eggNOG; COG4373; LUCA. DR OMA; EDFGRTG; -. DR OrthoDB; EOG693GK1; -. DR PhylomeDB; P44224; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR012036; Phage_Mu_Gp28. DR InterPro; IPR004921; Terminase_lsu. DR Pfam; PF03237; Terminase_6; 1. DR PIRSF; PIRSF007056; UCP007056; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 508 Mu-like prophage FluMu protein gp28. FT /FTId=PRO_0000077823. SQ SEQUENCE 508 AA; 57191 MW; 5BFC6833E2F1242B CRC64; MQTLPDLIPF DPNALLLGYQ KRWVADTSQL KIAEKSRRTG LTWAEAADDV MIASLAKSEG GSDVFYIGSN KEMAREFIDA CAMWAAQFNR AAGQIQEELF NDEDKDILTY VIYFASGFKI KALSSNPKNL RGMQGVVCID EAAFHEKLAE VLKAALALTM WGAKVRLIST HNGVDNLFNQ LIQDSRAGRK SYSVHTITLD DACAEGLYQR ICQVSKQLWT PEKEAAWKAG LLRETATEDD ALEEYYCVPK ASSGAYIPRP MIERAATEGK AKLRFECDAK FMEWTEDERT VITSEFCLTQ LLPHLQALNP DRRHAFGVDF ARSADLSVYA VCAVQPDTAR HFDLTLEIKN CPYNQQKQIM LFMLANLPRL IGAAFDATGN GGYLAEAALI RYGSSMVEAV QLNEKWYREW MPKYKALYES GYIQIPKDEE IILDHGHIQV INGVPKIDKS RSKDKSGKRH GDSAVAYCMA VRASYMTGGE IDFIPLPDKH SDRSENDEFD DFISNWDW // ID VG42_HAEIN Reviewed; 631 AA. AC P44236; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Mu-like prophage FluMu protein gp42; GN OrderedLocusNames=HI_1514; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To phage Mu protein gp42. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23167.1; -; Genomic_DNA. DR PIR; C64034; C64034. DR RefSeq; NP_439664.1; NC_000907.1. DR RefSeq; WP_010869233.1; NC_000907.1. DR STRING; 71421.HI1514; -. DR EnsemblBacteria; AAC23167; AAC23167; HI_1514. DR GeneID; 950380; -. DR KEGG; hin:HI1514; -. DR PATRIC; 20191751; VBIHaeInf48452_1584. DR eggNOG; ENOG4108NYK; Bacteria. DR eggNOG; COG3941; LUCA. DR OMA; IANMANK; -. DR OrthoDB; EOG6HMXDN; -. DR Proteomes; UP000000579; 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; IPR013491; Caudovirus_tape_meas_N. DR TIGRFAMs; TIGR02675; tape_meas_nterm; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 631 Mu-like prophage FluMu protein gp42. FT /FTId=PRO_0000077837. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 385 405 Helical. {ECO:0000255}. FT TRANSMEM 455 475 Helical. {ECO:0000255}. FT TRANSMEM 495 515 Helical. {ECO:0000255}. FT TRANSMEM 543 563 Helical. {ECO:0000255}. SQ SEQUENCE 631 AA; 66208 MW; 34E234C986406DE2 CRC64; MMANNSTSFF VNLAGNVSQQ AARFSNSIAN MANKNVSSLN KVSRAISAVS KGFNGLGNIT IPIIGVGAAA GATMVGKSML RTAADFEMAK IRMKQTFGEQ GEAADAWLKK FATDTPMAFA DTQDAMMRLK TAGIDPMNGS LQALVDYNAK VGGDKANLDG YISAISKGFI KGKLSMEEIN PLLERNVKVF EILAKETGGK YTADQMQKML QEGKLGRKAI HALLRGMGRD AQGAAKEQMK TWDGLVSNLE DTWTSMQARF MEHGAFDALK KELGDFVEWL NEKIDDGTLD DFPKTVSDTL IEALKNLKEM AKDVKPVLES IGSVMSWVSE KAGGYGNLAK FMGALYLGNK VLRNDKVQTL GGWGWSGAKW GYNKIFNRKK GGAGGLADGV AGALGATVGV TPVYVTNFPM GFGGGGGGGY GYDVIEDGRD KDKKTQKKNK PPRPKRGRGS VRSPVAAVAA SAAAVPKVAA PVTTASSGVA RSVGNGVKSL GRGASKAVPY LGTGLAVAEG VTVLMDDTTN TKEKSEAIGS IAGATAGAIV GQALIPIPVV GAAVGSYLGG WLGEWLGSEV GEYLSDPEPI KNELNGTINI AVKASDQLIA TATQAKIQTN QQRDSLETAV QMGTLGMGGM W // ID VPG1_HAEIN Reviewed; 146 AA. AC O05072; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Mu-like prophage FluMu G protein 1; GN OrderedLocusNames=HI_1503; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein G. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23153.1; -; Genomic_DNA. DR PIR; H64126; H64126. DR RefSeq; NP_439653.1; NC_000907.1. DR RefSeq; WP_005693523.1; NC_000907.1. DR STRING; 71421.HI1503; -. DR EnsemblBacteria; AAC23153; AAC23153; HI_1503. DR GeneID; 950371; -. DR KEGG; hin:HI1503; -. DR PATRIC; 20191729; VBIHaeInf48452_1573. DR eggNOG; ENOG4105ZS4; Bacteria. DR eggNOG; COG5005; LUCA. DR OMA; HQLGTKK; -. DR OrthoDB; EOG6VMTPD; -. DR PhylomeDB; O05072; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006522; Phage_virion_morphogenesis. DR Pfam; PF05069; Phage_tail_S; 1. DR TIGRFAMs; TIGR01635; tail_comp_S; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Mu-like prophage FluMu G protein 1. FT /FTId=PRO_0000077683. SQ SEQUENCE 146 AA; 16410 MW; 3CBADF7F053E6467 CRC64; MHIEYKFDTS TIQQKFKKLA QVMDGRDITR KVAGVLRQEA EKFFDLEQAP TGEKWEDLDE DYKKYRYAAG HTGKILQIRG GRGLAGSLSL DYGDNYALIG AAEEYGGFHQ LGTTFMPARP FLGLGKDGVS EIKAILNREL SELTQE // ID VPM_HAEIN Reviewed; 118 AA. AC P44234; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Mu-like prophage FluMu tail tube protein; GN OrderedLocusNames=HI_1512; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein M. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23159.1; -; Genomic_DNA. DR PIR; A64034; A64034. DR RefSeq; NP_439662.1; NC_000907.1. DR RefSeq; WP_005693533.1; NC_000907.1. DR STRING; 71421.HI1512; -. DR EnsemblBacteria; AAC23159; AAC23159; HI_1512. DR GeneID; 950378; -. DR KEGG; hin:HI1512; -. DR PATRIC; 20191747; VBIHaeInf48452_1582. DR eggNOG; ENOG4105WMG; Bacteria. DR eggNOG; ENOG41123JG; LUCA. DR OMA; IAVECKE; -. DR OrthoDB; EOG6HXJ94; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019596; Phage_Mu_GpM_tail_tub. DR Pfam; PF10618; Tail_tube; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 118 Mu-like prophage FluMu tail tube protein. FT /FTId=PRO_0000077689. SQ SEQUENCE 118 AA; 12911 MW; 2F2F0F4BCA53B69E CRC64; MATQFQGSAI IRLNGKEWPS DNDGTLTPGG KERETVKGSR VYGFSEKPTE AMVECTVFNC AETDVMELQN ITNATVEFET DIGQVYLLPG AWTVETGTLS ADGKIKLKMA SIECKRVQ // ID VAPB2_HAEIN Reviewed; 77 AA. AC Q57120; O05037; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative antitoxin VapB2; GN Name=vapB2; OrderedLocusNames=HI_0948; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Neutralizes the effect of toxin VapC2 (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the VapB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SpoVT-AbrB domain. {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; L42023; AAC22609.1; -; Genomic_DNA. DR PIR; C64162; C64162. DR RefSeq; NP_439109.1; NC_000907.1. DR RefSeq; WP_005648011.1; NC_000907.1. DR STRING; 71421.HI0948; -. DR EnsemblBacteria; AAC22609; AAC22609; HI_0948. DR GeneID; 949840; -. DR KEGG; hin:HI0948; -. DR PATRIC; 20190555; VBIHaeInf48452_0990. DR eggNOG; ENOG4105VGJ; Bacteria. DR eggNOG; COG4456; LUCA. DR KO; K18829; -. DR OMA; VFTNNRS; -. DR OrthoDB; EOG654P8N; -. DR PhylomeDB; Q57120; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR InterPro; IPR007159; SpoVT-AbrB_dom. DR Pfam; PF04014; MazE_antitoxin; 1. DR PROSITE; PS51740; SPOVT_ABRB; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 77 Putative antitoxin VapB2. FT /FTId=PRO_0000219874. FT DOMAIN 4 46 SpoVT-AbrB. {ECO:0000255|PROSITE- FT ProRule:PRU01076}. SQ SEQUENCE 77 AA; 8881 MW; 50489BBE4678CD6D CRC64; MIEASVFMTN RSQAVRLPAE VRFSEEIKKL SVRVSGSDRI LSPLNQSWDS FFLNDQAVSD DFMNEREIAF QPEREAL // ID VG37_HAEIN Reviewed; 194 AA. AC P44231; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 65. DE RecName: Full=Mu-like prophage FluMu protein gp37; GN OrderedLocusNames=HI_1509; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein gp37. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23156.1; -; Genomic_DNA. DR PIR; G64033; G64033. DR RefSeq; NP_439659.2; NC_000907.1. DR STRING; 71421.HI1509; -. DR EnsemblBacteria; AAC23156; AAC23156; HI_1509. DR GeneID; 950377; -. DR KEGG; hin:HI1509; -. DR PATRIC; 20191741; VBIHaeInf48452_1579. DR eggNOG; ENOG41067KA; Bacteria. DR eggNOG; ENOG410Z8YA; LUCA. DR OMA; NLWSDTQ; -. DR OrthoDB; EOG60CWQJ; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR014972; Phage_Mu_Gp37. DR Pfam; PF08873; DUF1834; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 194 Mu-like prophage FluMu protein gp37. FT /FTId=PRO_0000077831. SQ SEQUENCE 194 AA; 21817 MW; 4FC24349AC1E2DDA CRC64; MGAQYLKRVY LMSVIAETNE ALLAKIKALC GDYLREVDTH PGQWDDSSVR RLVRNPPAVY VAWLGQQPNN NPHTVTARWG VFVVAEVLNG QRRNAVGIYQ IVETLTAGLH KQRIAPSGMF ELQTVQNLWS DTQSGMGVAV YGMYFNAVQP LPDMTSDDTL CDFKIYDHTF NQDKDEHTID GKTRLTVELP TQSD // ID VG47_HAEIN Reviewed; 355 AA. AC P44240; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Mu-like prophage FluMu protein gp47; GN OrderedLocusNames=HI_1520; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the Mu gp47/PBSX XkdT 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; L42023; AAC23162.1; -; Genomic_DNA. DR PIR; G64034; G64034. DR RefSeq; NP_439669.1; NC_000907.1. DR RefSeq; WP_005693541.1; NC_000907.1. DR STRING; 71421.HI1520; -. DR DNASU; 950385; -. DR EnsemblBacteria; AAC23162; AAC23162; HI_1520. DR GeneID; 950385; -. DR KEGG; hin:HI1520; -. DR PATRIC; 20191765; VBIHaeInf48452_1591. DR eggNOG; ENOG4108T86; Bacteria. DR eggNOG; COG3299; LUCA. DR OMA; ITHAINT; -. DR OrthoDB; EOG6G20M3; -. DR PhylomeDB; P44240; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006949; Baseplate_J-like. DR Pfam; PF04865; Baseplate_J; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 355 Mu-like prophage FluMu protein gp47. FT /FTId=PRO_0000077843. SQ SEQUENCE 355 AA; 38452 MW; D708248CB5871885 CRC64; MAFNTPTLST LIKQGEQQFQ YRFPTLKRHN VIGVINRICA ALSAGEHMHL DWLARQIIPT TAEEDYLIEY CLYKGIVRKQ ASTATGLVTV TAANDTTIPA GTVFEDTNTG LTFITTQETV VKAGTADIAV KCETTGVEGN LKAGTSLSLT SAILGLLPTA TVKVMSGGAD IESLSRLLAR LIYRVQYPPA GGASHDYIRW ATEVPGVTRA WCFERYYGGG TVGVAFACDE REDILPTPED IARVRAYIEG HKNEVTGQFE GMPANVELYV FAPQFQAVNF KIRLAPNTPT LRQAVRKSLA AYLANAGVGA LLYLSQIRAT VSNTAGEVDN SVIFPTADVQ LLSDNIAILG DIEWL // ID VPI_HAEIN Reviewed; 355 AA. AC O05073; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Mu-like prophage FluMu I protein; GN OrderedLocusNames=HI_1504; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Potential protease involved in virion morphogenesis. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase U35 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; L42023; AAC23154.1; -; Genomic_DNA. DR PIR; I64126; I64126. DR RefSeq; NP_439654.1; NC_000907.1. DR RefSeq; WP_005693524.1; NC_000907.1. DR STRING; 71421.HI1504; -. DR EnsemblBacteria; AAC23154; AAC23154; HI_1504. DR GeneID; 950372; -. DR KEGG; hin:HI1504; -. DR PATRIC; 20191731; VBIHaeInf48452_1574. DR eggNOG; ENOG4108TVE; Bacteria. DR eggNOG; COG4388; LUCA. DR OMA; YVPKATY; -. DR OrthoDB; EOG6K6VCN; -. DR PhylomeDB; O05073; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR012106; Phage_Mu_Gp1. DR Pfam; PF10123; Mu-like_Pro; 1. DR PIRSF; PIRSF016624; Mu_prophg_I; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome. FT CHAIN 1 355 Mu-like prophage FluMu I protein. FT /FTId=PRO_0000079188. SQ SEQUENCE 355 AA; 39026 MW; 0589E0370F7B8148 CRC64; MKAEKTSLAV LTAQLTSPDG WQQLLPKGEF RSRDGSPTDV AHWFIDGTIA QNLIHKARQL NQDLLVDYDH ETILKAKKGI DAGNVVAAGW FNADEIQWFD DETRQGLYIK PRWTPKAYQQ IKDGEFAFLS AVFPYDENGT PLELRMAALT NDPGITGMQR LAVLSATLNP QENVKMPESL RKLLAKLGVE IAEGVELTEE QANTALNALE TLQTDKTKAD EQVATLSAKN TEVDLSQYVP KATYDAVMSQ VAVLSAKTDD VEIDNHISKA RNEGRAVEAE VEYLKQFGKQ QGVAALSAML EKRPQIAVLS AQQTQTTKVE KPVEKGTAVL SAADKEAAKL LGISEQDYAK ELEAK // ID VPT_HAEIN Reviewed; 308 AA. AC P44227; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Mu-like prophage FluMu major head subunit; GN OrderedLocusNames=HI_1505; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage Mu protein T. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23164.1; -; Genomic_DNA. DR PIR; C64033; C64033. DR RefSeq; NP_439655.1; NC_000907.1. DR RefSeq; WP_005693526.1; NC_000907.1. DR STRING; 71421.HI1505; -. DR DNASU; 950373; -. DR EnsemblBacteria; AAC23164; AAC23164; HI_1505. DR GeneID; 950373; -. DR KEGG; hin:HI1505; -. DR PATRIC; 20191733; VBIHaeInf48452_1575. DR eggNOG; ENOG4105EFV; Bacteria. DR eggNOG; COG4397; LUCA. DR OMA; YFFDTDH; -. DR OrthoDB; EOG69973P; -. DR PhylomeDB; P44227; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR018774; Phage_Mu_GpT. DR Pfam; PF10124; Mu-like_gpT; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 308 Mu-like prophage FluMu major head FT subunit. FT /FTId=PRO_0000077696. SQ SEQUENCE 308 AA; 33811 MW; E7AC8F1E5F21EE58 CRC64; MANVTPDLVK ALFVGFGKNF KDGLAKAPSQ YTEIATVVKS TTASNTYAWL GQMPGLTEWI GDRTLTAIQS HGYSIVNKKW ANGVEIQRTD IEDDNVGVYS PLIEELGRAA GEKADELVFG ALTAGFKTAC YDGQYFFDTD HPVGANVDGT NQKSVSNITD DSTGVTEANA WYLLDCSRSL KPIIYQERKA PTPAQITDAN DEKVFMKDVF TYGVDSRSNV GYGFWQMAHA VKGKLTAENL WKAIEAMRAV RGDGDKRLAI RPTHIVVPPS LAQAATKLLE RELRAEDGVA VDNEFKRMNL KLIVGDYL // ID Y003_HAEIN Reviewed; 262 AA. AC P44447; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Putative phosphatase HI_0003; DE EC=3.1.3.-; GN OrderedLocusNames=HI_0003; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC21682.1; -; Genomic_DNA. DR PIR; I64139; I64139. DR RefSeq; NP_438176.1; NC_000907.1. DR RefSeq; WP_010868916.1; NC_000907.1. DR ProteinModelPortal; P44447; -. DR STRING; 71421.HI0003; -. DR EnsemblBacteria; AAC21682; AAC21682; HI_0003. DR GeneID; 950898; -. DR KEGG; hin:HI0003; -. DR PATRIC; 20188457; VBIHaeInf48452_0003. DR eggNOG; ENOG410667J; Bacteria. DR eggNOG; COG0561; LUCA. DR KO; K07024; -. DR OMA; KWVIYER; -. DR OrthoDB; EOG6K13W0; -. DR PhylomeDB; P44447; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0044283; P:small molecule biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 262 Putative phosphatase HI_0003. FT /FTId=PRO_0000054434. 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 212 212 Magnesium. {ECO:0000250}. FT BINDING 189 189 Phosphate. {ECO:0000250}. FT BINDING 215 215 Phosphate. {ECO:0000250}. SQ SEQUENCE 262 AA; 29354 MW; 2E9657AC4F2093DC CRC64; MMYKAVFSDF NGTLLTSQHT ISPRTVVVIK RLTANGIPFV PISARSPLGI LPYWKQLETN NVLVAFSGAL ILNQNLEPIY SVQIEPKDIL EINTVLAEHP LLGVNYYTNN DCHARDVENK WVIYERSVTK IEIHPFDEVA TRSPHKIQII GEAEEIIEIE VLLKEKFPHL SICRSHANFL EVMHKSATKG SAVRFLEDYF GVQTNEVIAF GDNFNDLDML EHVGLGVAMG NAPNEIKQAA NVVTATNNED GLALILEEKF PE // ID Y035_HAEIN Reviewed; 551 AA. AC P44472; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Putative transport protein HI_0035 {ECO:0000255|HAMAP-Rule:MF_01016}; GN OrderedLocusNames=HI_0035; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01016}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01016}. CC -!- SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. CC YidE subfamily. {ECO:0000255|HAMAP-Rule:MF_01016}. CC -!- SIMILARITY: Contains 2 RCK C-terminal domains. {ECO:0000255|HAMAP- CC Rule:MF_01016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21713.1; -; Genomic_DNA. DR PIR; I64140; I64140. DR RefSeq; NP_438208.1; NC_000907.1. DR RefSeq; WP_005693880.1; NC_000907.1. DR ProteinModelPortal; P44472; -. DR STRING; 71421.HI0035; -. DR EnsemblBacteria; AAC21713; AAC21713; HI_0035. DR GeneID; 950933; -. DR KEGG; hin:HI0035; -. DR PATRIC; 20188521; VBIHaeInf48452_0035. DR eggNOG; ENOG4105D0C; Bacteria. DR eggNOG; COG2985; LUCA. DR KO; K07085; -. DR OMA; IGNAQQK; -. DR OrthoDB; EOG6XDGX2; -. DR PhylomeDB; P44472; -. DR Proteomes; UP000000579; 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 GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR GO; GO:0043266; P:regulation of potassium ion transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.1450; -; 2. DR HAMAP; MF_01016; YidE; 1. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR023018; Transpt_YidE_put. DR InterPro; IPR006512; YidE_YbjL. DR Pfam; PF06826; Asp-Al_Ex; 2. DR Pfam; PF02080; TrkA_C; 1. DR SUPFAM; SSF116726; SSF116726; 2. DR TIGRFAMs; TIGR01625; YidE_YbjL_dupl; 2. DR PROSITE; PS51202; RCK_C; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 551 Putative transport protein HI_0035. FT /FTId=PRO_0000208801. FT TRANSMEM 4 24 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 28 48 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 65 85 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 95 115 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 157 177 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 370 390 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 402 424 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 438 458 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 463 483 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 492 512 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT TRANSMEM 529 549 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT DOMAIN 191 275 RCK C-terminal 1. {ECO:0000255|HAMAP- FT Rule:MF_01016}. FT DOMAIN 277 360 RCK C-terminal 2. {ECO:0000255|HAMAP- FT Rule:MF_01016}. SQ SEQUENCE 551 AA; 59014 MW; 4550021090CDFA1F CRC64; MSDIAITISL LALVAVIGLW IGHWKIRGVG LGIGGVLFGG IIVAHFTNQY GLKLDAHTLH FVQEFGLILF VYTIGIQVGP GFFSSLRKSG LKLNAFAILI ILLGSIAVVL VHKIADVPLD IALGIYSGAV TNTPALGAGQ QILAELGVPQ TTVTMGVSYA MAYPFGICGI LLAMWLIRLF FNVKVDDEAA RFNAESSQDK ESLHNISLKV TNQNLDGLTL IQIPGFSDEE VVCSRLKRDD MEIVPKASTE IRTNDILQLV GDDNSLAKMR LIIGHEVDAP TVAYSGEIRS ERVVVTNEKV LGKKIRALGI HQKYGVVISR LNRAGIELVP TGNTTLQFGD VLHMVGRSDV LNQAISVIGN AQQKLLQVQM LPVFIGIGLG VLVGSIPFYI PGFPVALKLG LAGGPLVVAL ILARIGTIGK LYWFMPPSAN LALREIGIVL FLAVVGLKSG GSFFDTLVNG SGLEWMGYGI FITFVPLIIV GTIARLYGKL NYLTICGLLA GSMTDPPALA FANEIKEDNG AAALSYATVY PLVMFLRIMS PQLLAVLLWA A // ID Y036_HAEIN Reviewed; 592 AA. AC Q57335; O05006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_0036; GN OrderedLocusNames=HI_0036; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC21714.1; -; Genomic_DNA. DR PIR; D64044; D64044. DR RefSeq; NP_438209.1; NC_000907.1. DR RefSeq; WP_005668011.1; NC_000907.1. DR ProteinModelPortal; Q57335; -. DR STRING; 71421.HI0036; -. DR EnsemblBacteria; AAC21714; AAC21714; HI_0036. DR GeneID; 950931; -. DR KEGG; hin:HI0036; -. DR PATRIC; 20188523; VBIHaeInf48452_0036. DR eggNOG; ENOG4105CQ0; Bacteria. DR eggNOG; COG4178; LUCA. DR KO; K02471; -. DR OMA; GDAYYRG; -. DR OrthoDB; EOG61KBCN; -. DR PhylomeDB; Q57335; -. DR Proteomes; UP000000579; 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; PF06472; ABC_membrane_2; 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 inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 592 Uncharacterized ABC transporter ATP- FT binding protein HI_0036. FT /FTId=PRO_0000093198. FT TRANSMEM 12 32 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 58 78 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 102 122 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 191 211 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 214 234 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 299 319 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 58 358 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 391 592 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 424 431 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 592 AA; 67904 MW; 6F2E91C0C0708237 CRC64; MDYSQEAITS LIWILQTLAI TSVVFSFGIF LLVRFTQWGK QFWMFAGGYL SPKRSIKPIL FFLLIVAMTL LSVRISLVNS EWYKNMYTSL QEFNEHVFWQ QMGLFCVIAA SSVSAALVSY YLEQRFVINW IEWLNEQLVN KWMAHRAYYK TQYLSENLDN PDQRIQQDVQ SYVKTTLSLS TGVIDAVTSM ISYTILLWGL AGPMIVLGVE IPHMMVFLVF GYVIFTTLIA FWLGRPLISL NFINERLNAN YRYSLIRIKE YAESIAFYAG EKVEKNQLYQ QFNAVIHNMW VIIFRTLKFS GFNLVVSQIS VVFPLLIQVG RYFEKQIKLG DLMQTLQVFG QLHANLSFFR STYDNFASYK ATLDRLTGFC YAIEKANNKS QTQIHNHPTD VIFKNLSIQN PLGHTLIKHL NITLPQGTSL LIQGKSGAGK TTLLRTIAGL WSYAEGEINC PTHNQLFLSQ KPYVPQGNLM SALAYPNNAD NISHTQAVEI LNKVQLGHLA EQLEKEQDWT RILSLGEQQR LAFARLILHK PAVAFLDEAT ASMDEGLEFS MYQLLQQELP QTTIISVGHR STLKTLHQQQ LILQDKGQWQ VL // ID Y040_HAEIN Reviewed; 258 AA. AC P43929; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0040; GN OrderedLocusNames=HI_0040; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21718.1; -; Genomic_DNA. DR PIR; A64000; A64000. DR RefSeq; NP_438213.1; NC_000907.1. DR RefSeq; WP_005657798.1; NC_000907.1. DR ProteinModelPortal; P43929; -. DR STRING; 71421.HI0040; -. DR EnsemblBacteria; AAC21718; AAC21718; HI_0040. DR GeneID; 950937; -. DR KEGG; hin:HI0040; -. DR PATRIC; 20188531; VBIHaeInf48452_0040. DR eggNOG; ENOG4105GXY; Bacteria. DR eggNOG; ENOG4111SWX; LUCA. DR OMA; WDIYFDF; -. DR OrthoDB; EOG61ZTFB; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.70.970; -; 1. DR InterPro; IPR006506; CHP01619. DR InterPro; IPR016097; DUF695. DR InterPro; IPR009671; RraB_dom. DR Pfam; PF05117; DUF695; 1. DR Pfam; PF06877; RraB; 1. DR PIRSF; PIRSF017962; UCP017962; 1. DR SUPFAM; SSF89946; SSF89946; 1. DR TIGRFAMs; TIGR01619; hyp_HI0040; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 258 Uncharacterized protein HI_0040. FT /FTId=PRO_0000077880. SQ SEQUENCE 258 AA; 30175 MW; 1D14384356128F52 CRC64; MDMANWQNYR STVNGMPAVF TANIEDVEKY HGKGLDKIVQ FTIDYQADDE TGLPSEVEYD KLINRVFKIL TQLTALPNVF FAGHFICNSQ IKIHFYCKHE NLIVETLQQI DFVKDINVQK DLIWDTYFDF LLASPLEIKL NATEELLDLL KSKGRNLSDT YLVEHSFHFD EEQKMFPFMD ELSLGDYSFT TLQYSAQAIQ FNEDDEPYFL VKLEQEISLE NSEIFEQVER FEKLAEQFSG EYIGWECDSL LDSNKPLN // ID XGPT_HAEIN Reviewed; 155 AA. AC P43859; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; DE EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903}; DE AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903}; DE Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903}; GN Name=gpt1 {ECO:0000255|HAMAP-Rule:MF_01903}; Synonyms=gptA; GN OrderedLocusNames=HI_0674; GN and GN Name=gpt2 {ECO:0000255|HAMAP-Rule:MF_01903}; Synonyms=gptB; GN OrderedLocusNames=HI_0692; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent CC hypoxanthine. CC -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose CC 1-diphosphate + xanthine. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01903}; CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; CC XMP from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01903}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01903}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01903}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. XGPT subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01903}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22334.1; -; Genomic_DNA. DR EMBL; L42023; AAC22352.1; -; Genomic_DNA. DR PIR; A64087; A64087. DR RefSeq; NP_438834.1; NC_000907.1. DR RefSeq; NP_438852.1; NC_000907.1. DR RefSeq; WP_005650775.1; NC_000907.1. DR ProteinModelPortal; P43859; -. DR SMR; P43859; 3-153. DR STRING; 71421.HI0692; -. DR PRIDE; P43859; -. DR EnsemblBacteria; AAC22334; AAC22334; HI_0674. DR EnsemblBacteria; AAC22352; AAC22352; HI_0692. DR GeneID; 949714; -. DR GeneID; 949722; -. DR KEGG; hin:HI0674; -. DR KEGG; hin:HI0692; -. DR PATRIC; 20189965; VBIHaeInf48452_0704. DR eggNOG; ENOG4105DYA; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00769; -. DR OMA; KAHFATV; -. DR OrthoDB; EOG6H1Q23; -. DR PhylomeDB; P43859; -. DR UniPathway; UPA00602; UER00658. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01903; XGPRT; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR023747; Xanthine_Guanine_PRibTrfase. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Glycosyltransferase; Magnesium; Membrane; Metal-binding; KW Purine salvage; Reference proteome; Transferase. FT CHAIN 1 155 Xanthine phosphoribosyltransferase. FT /FTId=PRO_0000139671. FT REGION 37 38 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT REGION 95 99 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01903}. FT METAL 92 92 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 95 95 Xanthine. {ECO:0000255|HAMAP- FT Rule:MF_01903}. FT BINDING 138 138 Xanthine; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01903}. SQ SEQUENCE 155 AA; 17325 MW; DE98F8651E83553C CRC64; MSEKYVVTWD MFQMHARRLS ERLLPASQWK GIIAVSRGGL FPAAVLAREL GLRHIETVCI ASYHDHNNQG ELQVLHAAQV PNGGEGFIVV DDLVDTGNTA RAIRQMYPNA KFVTVFAKPA GAELVDDYVI DIPQNTWIEQ PWDLGLTFVP PLSRK // ID XYLB_HAEIN Reviewed; 493 AA. AC P44401; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 90. DE RecName: Full=Xylulose kinase; DE Short=Xylulokinase; DE EC=2.7.1.17; GN Name=xylB; OrderedLocusNames=HI_1113; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + D-xylulose = ADP + D-xylulose 5- CC phosphate. CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22767.1; 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; L42023; AAC22767.1; ALT_INIT; Genomic_DNA. DR PIR; E64183; E64183. DR RefSeq; NP_439270.1; NC_000907.1. DR RefSeq; WP_005693437.1; NC_000907.1. DR ProteinModelPortal; P44401; -. DR STRING; 71421.HI1113; -. DR EnsemblBacteria; AAC22767; AAC22767; HI_1113. DR GeneID; 950087; -. DR KEGG; hin:HI1113; -. DR PATRIC; 20190899; VBIHaeInf48452_1162. DR eggNOG; ENOG4105CMG; Bacteria. DR eggNOG; COG1070; LUCA. DR KO; K00854; -. DR OMA; SYLPKPE; -. DR OrthoDB; EOG63RGRW; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central. DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central. DR GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR006000; Xylulokinase. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR TIGRFAMs; TIGR01312; XylB; 1. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase; KW Xylose metabolism. FT CHAIN 1 493 Xylulose kinase. FT /FTId=PRO_0000059550. SQ SEQUENCE 493 AA; 54804 MW; 0F7C72AEB26FEDD6 CRC64; MYIGIDCGTQ GTKAIVLDSV QKKVIGVGYA KHELITQSNG RREQQPNWWI EALQQALQIA LKQAKNSPHF SPNLVKGIGI SGQQHGLVML DKNDRPLYKA KLWCDTETAT ENDILIEKLG GQTAVFEKLG IICQTGYTAS KLSWFRQNYP DKFANIRKIM LPHDYLNYWL TGKFCTEFGD ASGSGYFDVV KREWKREVFK YLAPELNMDE VLPKLLSAEQ KIGVIKPEIA TLFGFNENVI VSTGGGDNMM GAIGTGNIRE GIATMSLGTS GTLYAYTQKP LLNLPPMIAN FCSSNNGWLP LVCVMNITSS NKQLMNLLNI DIEELNQLAQ QAPIGANGIT ILPFFNGERV PPLPNTKASI LGLDSSNFTR ENLCRAMMES ATFTLRYGLD LFRQAGLKTS QIRLIGGGAK SSFWRQMIAD VMNSEVVCLQ EEEAAALGGA IQAMWANGEG ELEFLCETFI HLDENSKAYP NLSQVKNYQN AYERYLTHLS QLY // ID XYLG_HAEIN Reviewed; 503 AA. AC P45046; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Xylose import ATP-binding protein XylG {ECO:0000255|HAMAP-Rule:MF_01722}; DE EC=3.6.3.17 {ECO:0000255|HAMAP-Rule:MF_01722}; GN Name=xylG {ECO:0000255|HAMAP-Rule:MF_01722}; GN OrderedLocusNames=HI_1110; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex XylFGH involved in CC xylose import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01722}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + monosaccharide(Out) = ADP + CC phosphate + monosaccharide(In). {ECO:0000255|HAMAP-Rule:MF_01722}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (XylG), two transmembrane proteins (XylH) and a solute-binding CC protein (XylF). {ECO:0000255|HAMAP-Rule:MF_01722}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01722}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01722}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Xylose CC importer (TC 3.A.1.2.4) family. {ECO:0000255|HAMAP-Rule:MF_01722}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|HAMAP-Rule:MF_01722}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22764.1; -; Genomic_DNA. DR PIR; B64183; B64183. DR RefSeq; NP_439267.1; NC_000907.1. DR RefSeq; WP_005693435.1; NC_000907.1. DR ProteinModelPortal; P45046; -. DR STRING; 71421.HI1110; -. DR EnsemblBacteria; AAC22764; AAC22764; HI_1110. DR GeneID; 950081; -. DR KEGG; hin:HI1110; -. DR PATRIC; 20190893; VBIHaeInf48452_1159. DR eggNOG; ENOG4105C2J; Bacteria. DR eggNOG; COG1129; LUCA. DR KO; K10545; -. DR OMA; LPGGRMH; -. DR OrthoDB; EOG6QK4RR; -. DR PhylomeDB; P45046; -. DR Proteomes; UP000000579; 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:0015614; F:D-xylose-importing ATPase activity; IEA:UniProtKB-HAMAP. 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; IPR013455; ABC_transptr_xylose_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR02633; xylG; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR PROSITE; PS51280; XYLG; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Repeat; KW Sugar transport; Transport. FT CHAIN 1 503 Xylose import ATP-binding protein XylG. FT /FTId=PRO_0000093125. FT DOMAIN 4 241 ABC transporter 1. {ECO:0000255|HAMAP- FT Rule:MF_01722}. FT DOMAIN 258 499 ABC transporter 2. {ECO:0000255|HAMAP- FT Rule:MF_01722}. FT NP_BIND 36 43 ATP. {ECO:0000255|HAMAP-Rule:MF_01722}. SQ SEQUENCE 503 AA; 55680 MW; B8D2FB066B83022C CRC64; MALLEMKHIT KKFGDVTALH NISIELEAGE ILSLCGENGS GKSTLMKILC GIYPCGDYSG DIYFSESELK ARNIRDTEEK GISIIHQELT LVKNMSVLEN IFLGNEITHK GLTADNEMYL RCKNLLQQVQ LDADPNTRVG ELGLGQQQLV EIAKALNKQV RLLILDEPTA SLTEKETEIL LNLIKDLKAH NIACIYISHK LNEVKAISDK ICVIRDGEHV GTKDASTMTE DDIITMMVGR EITSLYPHEP HEIKDEILRV ENLSAWHPIN THIKRVDNVS FSLHEGEILG VAGLVGSGRT DMVQCLFGSY EGKFEGNIFI NQKQVNIKNC AQAIEHKIVM VPEDRKKHGI VSIMGVGKNI TLSSLKSYCF GKMVVNEAKE EQIIGSAIKR LKVKTFSPDL PIGRLSGGNQ QKAILAKCLS LNPKILILDE PTRGIDVGAK YEIYKLINQL AQEGIAIIVI SSELPEVLGI SDRVLVMHQG KLKASLINTA LTQEQVMETA LKE // ID XYLH_HAEIN Reviewed; 375 AA. AC P45045; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Xylose transport system permease protein XylH; GN Name=xylH; OrderedLocusNames=HI_1109; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for D-xylose. Probably responsible for the translocation of the CC substrate across the membrane (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. AraH/RbsC 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; L42023; AAC22763.1; -; Genomic_DNA. DR PIR; A64183; A64183. DR RefSeq; NP_439266.1; NC_000907.1. DR RefSeq; WP_010869132.1; NC_000907.1. DR STRING; 71421.HI1109; -. DR EnsemblBacteria; AAC22763; AAC22763; HI_1109. DR GeneID; 950080; -. DR KEGG; hin:HI1109; -. DR PATRIC; 20190891; VBIHaeInf48452_1158. DR eggNOG; ENOG4108HWW; Bacteria. DR eggNOG; COG4214; LUCA. DR KO; K10544; -. DR OMA; SVNLQVY; -. DR OrthoDB; EOG61P6T8; -. DR PhylomeDB; P45045; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015749; P:monosaccharide transport; IBA:GOC. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Sugar transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 375 Xylose transport system permease protein FT XylH. FT /FTId=PRO_0000060237. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 271 291 Helical. {ECO:0000255}. FT TRANSMEM 319 339 Helical. {ECO:0000255}. FT TRANSMEM 348 368 Helical. {ECO:0000255}. SQ SEQUENCE 375 AA; 39510 MW; 21E9D6D343CF062F CRC64; MFKLKSVNLQ VYIMLIAIAV IMAFFSVATD GAYLSARNIS NLLRQTSITG XLAIGMVFVI ISAEIDLSVG SLMGLLGGFA AIADVWWGFP LPVTIIATIA LGLIFGIWNG WWVAYRKVPS FIVTLAGYLA FRGILIGLTN GTTVSPISGT MTVIGQGYLS DIAGVILGGI AVIGFVLWGN YQRRSRQQLQ LEVSALSKDF TKYALFAVIV LGAIYLLNDY RGIPFPVLVL AVLAILGLFL SRKTSFGRHV YAIGGNIDAA KLSGINVEKT KLIIFAMNGV LVAIAGLILS ARLGAGSPSA GQNAELDAIA ACVIGGASLA GGVGSVFGVV IGALIIASLD NGMSMLDVPT FWQYIVKGGI LLLAVWIDTS NKKKM // ID Y044_HAEIN Reviewed; 220 AA. AC P44477; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Uncharacterized protein HI_0044; GN OrderedLocusNames=HI_0044; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the BI1 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; L42023; AAC21722.1; -; Genomic_DNA. DR PIR; A64141; A64141. DR RefSeq; NP_438217.1; NC_000907.1. DR RefSeq; WP_005649826.1; NC_000907.1. DR STRING; 71421.HI0044; -. DR EnsemblBacteria; AAC21722; AAC21722; HI_0044. DR GeneID; 950935; -. DR KEGG; hin:HI0044; -. DR PATRIC; 20188539; VBIHaeInf48452_0044. DR eggNOG; ENOG4108MN8; Bacteria. DR eggNOG; COG0670; LUCA. DR KO; K19416; -. DR OMA; NIFLAIP; -. DR OrthoDB; EOG6PZXBH; -. DR PhylomeDB; P44477; -. DR Proteomes; UP000000579; 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:0043066; P:negative regulation of apoptotic process; IEA:InterPro. DR InterPro; IPR006213; Bax_inhbtr1_CS. DR InterPro; IPR006214; Bax_inhibitor_1-related. DR PANTHER; PTHR23291; PTHR23291; 1. DR PROSITE; PS01243; BI1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 220 Uncharacterized protein HI_0044. FT /FTId=PRO_0000179104. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. SQ SEQUENCE 220 AA; 24246 MW; FDE34BE90F3F915C CRC64; MQSRLIVDAQ KESLLSTHKV LRNTYFLLGL TMAFSAVVAF ISMSLNLPYP NIIVLLVGFY GLLFLTNKLA DRPAGILAAF AFTGFMGYTI GPILNMYVAR GMEDLIMLAF AGTAIVFFAC SAYVLTTKKD MSFLSSAMFA LFIVLLLGMV ASFFFQIPAL SVAISALFVV FSTMTILYET SNIIHGGETN YIRATVNIYV SIYNLFLSLL RLLSIFSSDE // ID Y052_HAEIN Reviewed; 328 AA. AC P71336; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Uncharacterized protein HI_0052; DE Flags: Precursor; GN OrderedLocusNames=HI_0052; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 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; L42023; AAC21730.1; -; Genomic_DNA. DR PIR; E64141; E64141. DR RefSeq; NP_438225.1; NC_000907.1. DR RefSeq; WP_005693870.1; NC_000907.1. DR ProteinModelPortal; P71336; -. DR STRING; 71421.HI0052; -. DR EnsemblBacteria; AAC21730; AAC21730; HI_0052. DR GeneID; 950947; -. DR KEGG; hin:HI0052; -. DR PATRIC; 20188557; VBIHaeInf48452_0052. DR eggNOG; ENOG4105GQU; Bacteria. DR eggNOG; COG1638; LUCA. DR OMA; CENMTET; -. DR OrthoDB; EOG63588M; -. DR PhylomeDB; P71336; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR004682; TRAP_DctP. DR InterPro; IPR018389; TRAP_DctP/TeaA. DR Pfam; PF03480; DctP; 1. DR PIRSF; PIRSF006470; DctB; 1. DR TIGRFAMs; TIGR00787; dctP; 1. PE 1: Evidence at protein level; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 328 Uncharacterized protein HI_0052. FT /FTId=PRO_0000031815. SQ SEQUENCE 328 AA; 37616 MW; 412112D790446F2F CRC64; MKSIKGLGKL LLASSILFSS SAFAKTIIKL GHYNSDIHPS HIALQEYFKK TIENETNHKY EIRLYPNNQL GGEDQIVNGL RNGTIEAGIT GLLLQNVDPI FGVWEWPYLF KDNQEAKKVL ESPIANKIGQ KMEKYGIKLL AYGMNGFRVI SSNKKLEKFD DFKGLRLRVP LNSLFVDWAK AMNINPQSMP LSEVFTALEQ KVIDGQENPY MLIKDSGLYE VQKYIIQSNH IFSPGLLQIS LKTWNKIPKE DQIIFEKAAK LYQEKEWELA IKTELEVKDY LAKHGNEIIV PSEAFKNDMV NASKVLYDSF YKKYDWAKDV VQKINEAK // ID Y083_HAEIN Reviewed; 71 AA. AC P43938; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0083; DE Flags: Precursor; GN OrderedLocusNames=HI_0083; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21762.1; -; Genomic_DNA. DR PIR; A64001; A64001. DR STRING; 71421.HI0083; -. DR EnsemblBacteria; AAC21762; AAC21762; HI_0083. DR PATRIC; 20188621; VBIHaeInf48452_0084. DR OMA; WIARRKS; -. DR OrthoDB; EOG6VTK2M; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 71 Uncharacterized protein HI_0083. FT /FTId=PRO_0000013949. SQ SEQUENCE 71 AA; 8074 MW; 0041E615FFBDD361 CRC64; MGVGLHGDHV GGELNSANAF TETLFKMDYN NPEHKEMMDL EGLKRWIARR KSLKLPSTRA NIKISDKKLP H // ID Y090_HAEIN Reviewed; 237 AA. AC P44506; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=UPF0001 protein HI_0090; GN OrderedLocusNames=HI_0090; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the UPF0001 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; L42023; AAC21768.1; -; Genomic_DNA. DR PIR; B64142; B64142. DR RefSeq; NP_438263.1; NC_000907.1. DR RefSeq; WP_005693829.1; NC_000907.1. DR ProteinModelPortal; P44506; -. DR SMR; P44506; 2-228. DR STRING; 71421.HI0090; -. DR EnsemblBacteria; AAC21768; AAC21768; HI_0090. DR GeneID; 950992; -. DR KEGG; hin:HI0090; -. DR PATRIC; 20188643; VBIHaeInf48452_0091. DR eggNOG; ENOG4105DFA; Bacteria. DR eggNOG; COG0325; LUCA. DR KO; K06997; -. DR OMA; HGSTMVR; -. DR OrthoDB; EOG6G7R84; -. DR PhylomeDB; P44506; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR Gene3D; 3.20.20.10; -; 1. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR029066; PLP-binding_barrel. DR InterPro; IPR011078; UPF0001. DR PANTHER; PTHR10146; PTHR10146; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR00044; TIGR00044; 1. DR PROSITE; PS01211; UPF0001; 1. PE 1: Evidence at protein level; KW Complete proteome; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 237 UPF0001 protein HI_0090. FT /FTId=PRO_0000163199. FT MOD_RES 35 35 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 237 AA; 26767 MW; 804FA860AFCFF7BD CRC64; MNIQHNLNLI QQKIETACKE ENRNQNTVKL LAVSKTKPIS AILSAYQAGQ TAFGENYVQE GVEKIQYFES QGINLEWHFI GPLQSNKTRL VAEHFDWMQT LDRAKIADRL NEQRPTNKAP LNVLIQINIS DEESKSGIQP EEMLTLAKHI ENLPHLCLRG LMAIPAPTDN IAEQENAFRK MLELFEQLKQ VLPNQQIDTL SMGMTDDMPS AIKCGSTMVR IGTAIFGARN YSTSQNK // ID Y092_HAEIN Reviewed; 419 AA. AC Q57493; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Uncharacterized transporter HI_0092; GN OrderedLocusNames=HI_0092; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter 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; L42023; AAC21770.1; -; Genomic_DNA. DR PIR; D64142; D64142. DR RefSeq; NP_438265.1; NC_000907.1. DR RefSeq; WP_005693828.1; NC_000907.1. DR ProteinModelPortal; Q57493; -. DR STRING; 71421.HI0092; -. DR TCDB; 2.A.8.1.9; the gluconate:h(+) symporter (gntp) family. DR DNASU; 950987; -. DR EnsemblBacteria; AAC21770; AAC21770; HI_0092. DR GeneID; 950987; -. DR KEGG; hin:HI0092; -. DR PATRIC; 20188647; VBIHaeInf48452_0093. DR eggNOG; ENOG4107QQ0; Bacteria. DR eggNOG; COG2610; LUCA. DR KO; K03299; -. DR OMA; VDAMYIL; -. DR OrthoDB; EOG6VHZCW; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IBA:GO_Central. DR InterPro; IPR003474; Glcn_transporter. DR Pfam; PF02447; GntP_permease; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 419 Uncharacterized transporter HI_0092. FT /FTId=PRO_0000077884. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 174 194 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. FT TRANSMEM 242 262 Helical. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 349 369 Helical. {ECO:0000255}. FT TRANSMEM 396 416 Helical. {ECO:0000255}. SQ SEQUENCE 419 AA; 42781 MW; 6DCA54BB0A55FF73 CRC64; MTTVSAIGAL VALIVAIFLI LKKVSPAYGM LVGALVGGLI GGADLSQTVS LMIGGAQGIT TAVMRILAAG VLAGVLIESG AANSITETIT NKLGETRALL ALALATMILT AVGVFVDVAV ITVSPIALAL SRRSDLSKAA ILLAMIGGGK AGNIMSPNPN AIAAADTFHL PLTSVMMAGI IPALFGLILT YFLAKRLINK GSKVTDKEVI VLETQNLPSF LTALVAPLVA ILLLALRPLF DIKVDPLIAL PLGGLIGAFC MGKLRNINSY AINGLSKMTP VAIMLLGTGA LAGIIANSGL KEVLIQGLEH SGLPSYILAP ISGVLMSLAT ASTTAGTAVA SNVFSSTLLE LGVSSLAGAA MIHAGATVFD HMPHGSFFHA TGGSVNMDIK ERLKLIPYES AVGLMMTIVS TLIFGVFKF // ID Y094_HAEIN Reviewed; 106 AA. AC P43939; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_0094; GN OrderedLocusNames=HI_0094; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21779.1; -; Genomic_DNA. DR PIR; B64001; B64001. DR RefSeq; NP_438268.2; NC_000907.1. DR RefSeq; WP_005693826.1; NC_000907.1. DR STRING; 71421.HI0094; -. DR EnsemblBacteria; AAC21779; AAC21779; HI_0094. DR GeneID; 950995; -. DR KEGG; hin:HI0094; -. DR PATRIC; 20188651; VBIHaeInf48452_0095. DR eggNOG; COG0451; LUCA. DR OMA; HGETSIC; -. DR OrthoDB; EOG693GQC; -. DR PhylomeDB; P43939; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003474; Glcn_transporter. DR Pfam; PF02447; GntP_permease; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 106 Uncharacterized protein HI_0094. FT /FTId=PRO_0000077885. FT TRANSMEM 78 98 Helical. {ECO:0000255}. SQ SEQUENCE 106 AA; 11735 MW; 672EC13E1F59E3E4 CRC64; MSELLINDYT RKGFVDGLCL RLPTICIRPG KPNKATSSFV SSIIREPLHG ETSICPVAEK MAFSFIKFLG KKKEEWALAI TGYVVSIPIV LPILIIFIKA ILDLGK // ID Y1008_HAEIN Reviewed; 112 AA. AC Q57134; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Uncharacterized protein HI_1008; DE Flags: Precursor; GN OrderedLocusNames=HI_1008; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 22-26. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Contains 2 HhH domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22669.1; -; Genomic_DNA. DR PIR; I64107; I64107. DR RefSeq; NP_439169.1; NC_000907.1. DR RefSeq; WP_010869106.1; NC_000907.1. DR ProteinModelPortal; Q57134; -. DR STRING; 71421.HI1008; -. DR TCDB; 3.A.11.2.2; the bacterial competence-related dna transformation transporter (dna-t) family. DR DNASU; 950002; -. DR EnsemblBacteria; AAC22669; AAC22669; HI_1008. DR GeneID; 950002; -. DR KEGG; hin:HI1008; -. DR PATRIC; 20190679; VBIHaeInf48452_1052. DR eggNOG; ENOG41083P1; Bacteria. DR eggNOG; COG1555; LUCA. DR KO; K02237; -. DR OMA; FAEEKAT; -. DR OrthoDB; EOG6GFGQQ; -. DR PhylomeDB; Q57134; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR010994; RuvA_2-like. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00426; TIGR00426; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Repeat; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 112 Uncharacterized protein HI_1008. FT /FTId=PRO_0000013794. FT DOMAIN 49 79 HhH 1. FT DOMAIN 80 109 HhH 2. SQ SEQUENCE 112 AA; 11975 MW; A102635387205DC0 CRC64; MKTLFTSVVL CGALVVSSSF AEEKATXQTA QSVVTTQAEA QVAPAVVSDK LNINTATASE IQKSLTGIGA KKAEAIVQYR EKHGNFXNAE QLLEVQGIGK ATLEKNRDRI IF // ID Y1030_HAEIN Reviewed; 161 AA. AC P44994; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Putative TRAP transporter small permease protein HI_1030; GN OrderedLocusNames=HI_1030; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAP transporter small permease 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; L42023; AAC22690.1; -; Genomic_DNA. DR PIR; B64165; B64165. DR RefSeq; NP_439190.1; NC_000907.1. DR RefSeq; WP_005693364.1; NC_000907.1. DR STRING; 71421.HI1030; -. DR EnsemblBacteria; AAC22690; AAC22690; HI_1030. DR GeneID; 950014; -. DR KEGG; hin:HI1030; -. DR PATRIC; 20190723; VBIHaeInf48452_1074. DR eggNOG; ENOG4105XDZ; Bacteria. DR eggNOG; COG3090; LUCA. DR OMA; MLFCCYL; -. DR OrthoDB; EOG6VXF99; -. DR PhylomeDB; P44994; -. DR Proteomes; UP000000579; 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; IPR007387; DctQ_transporter. DR Pfam; PF04290; DctQ; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 161 Putative TRAP transporter small permease FT protein HI_1030. FT /FTId=PRO_0000169596. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. SQ SEQUENCE 161 AA; 18070 MW; 15652FB24CF14A64 CRC64; MMRSLAHFIN KALEILCISI LALMSILVFL NVVLRYGFNS GISITEEISR YLFIWLAFLG AVLAFNENQH VSVTVLVNKL PPFGQAILKF ITDMMMLICC YLIIEGSWIQ FQLNLNNFAP ISGLPQGLTY FASVIAGILV SAILITRLIS TIFFIFRGEV K // ID Y1036_HAEIN Reviewed; 181 AA. AC P44097; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein HI_1036; GN OrderedLocusNames=HI_1036; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the YggT family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22696.1; 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; L42023; AAC22696.1; ALT_INIT; Genomic_DNA. DR PIR; G64018; G64018. DR RefSeq; NP_439196.2; NC_000907.1. DR RefSeq; WP_010869110.1; NC_000907.1. DR STRING; 71421.HI1036; -. DR EnsemblBacteria; AAC22696; AAC22696; HI_1036. DR GeneID; 950018; -. DR KEGG; hin:HI1036; -. DR PATRIC; 20190735; VBIHaeInf48452_1080. DR eggNOG; ENOG4108VIA; Bacteria. DR eggNOG; COG0762; LUCA. DR KO; K02221; -. DR OMA; MIDFSPM; -. DR OrthoDB; EOG69WFPS; -. DR PhylomeDB; P44097; -. DR Proteomes; UP000000579; 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; IPR003425; CCB3/YggT. DR Pfam; PF02325; YGGT; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 181 Uncharacterized protein HI_1036. FT /FTId=PRO_0000169378. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. SQ SEQUENCE 181 AA; 20201 MW; 3F086A77EA972232 CRC64; MELSQTALFI GSIINLNALV LILRAWLQFA RVDYYNPVST FAVKMTDPVL KPLRKIAPTV KNIDTSALLL IFIIGMLKGI IYFGLSVNVL LVLGVLTVLK SIGLAIFYVL FIGAVLSWFN RGNNSISYAF YQLSEPLLKP IRRLLPTLGM IDFSPMVVMF ILLFLNNFML DLLGGLWIIA G // ID Y1063_HAEIN Reviewed; 70 AA. AC P44107; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein HI_1063; GN OrderedLocusNames=HI_1063; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22723.1; -; Genomic_DNA. DR PIR; H64019; H64019. DR STRING; 71421.HI1063; -. DR EnsemblBacteria; AAC22723; AAC22723; HI_1063. DR PATRIC; 20190789; VBIHaeInf48452_1107. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020098; Unchr_HI1063_Tfrase-like. DR ProDom; PD055757; Unchr_HI1063_Tfrase-like; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 70 Uncharacterized protein HI_1063. FT /FTId=PRO_0000077999. SQ SEQUENCE 70 AA; 8285 MW; 7AF2631BF4DFFF2C CRC64; MERKEYKVFK SGLNFLEGIA NWIGIKNPQL TQTEDLFSNE SDKNDFGLQK RIDEKYRKDD DPAIDIRPKH // ID Y1064_HAEIN Reviewed; 485 AA. AC P71367; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 89. DE RecName: Full=Putative phosphoethanolamine transferase HI_1064; DE EC=2.7.-.-; GN OrderedLocusNames=HI_1064; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase 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; L42023; AAC22718.1; -; Genomic_DNA. DR PIR; F64165; F64165. DR ProteinModelPortal; P71367; -. DR STRING; 71421.HI1064; -. DR EnsemblBacteria; AAC22718; AAC22718; HI_1064. DR PATRIC; 20190791; VBIHaeInf48452_1108. DR eggNOG; ENOG4108I6E; Bacteria. DR eggNOG; COG2194; LUCA. DR OMA; RTFSMIY; -. DR OrthoDB; EOG6WDSC7; -. DR Proteomes; UP000000579; 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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 485 Putative phosphoethanolamine transferase FT HI_1064. FT /FTId=PRO_0000209154. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. SQ SEQUENCE 485 AA; 55401 MW; 3C0D8285C64D5F55 CRC64; MKKLNMEILS ERWIIATFSF QGRQYNTKKT SQILPALFAV ICAAFAGYFI LIGSGMFTEP SVALILLATI TILLLSSSKK SFYFILLPLT LLHAFYTPTG LNFGPPSYQY IASLFATDIL ETKEFLLQIP VSSYLIAFAI PILIFLQYKS AVKFGIKFYR NKTFIALATL LFAYNMPLAE PLKETVSSTL KIVDEVQKLK QISQSDNWGK STLENSRYDD YVIVLGESAR KDYHHAYGYP IENTPFMSNA KGTLIDGFRS AGTNTVASLR LMLTFPDKEK WEPNYSLSLV DLIKSAGIKT YWLSNHGMIG KFDTPVSSLA SKSDETFFLK KGGSFNSTNF SDFDLLPKFA QVLENSVQGK RFIVLHIYGS HPMACDRIED YPKIFDDKDL NPRYGYLNCY VSSIKKTDEF LKRVYDQLEE NVKKNHRTFS MIYFSDHGLC HQQDEKTIYF CSIKTVSAES TIIFRYSKFH QMIWNAKNIR CLNQV // ID Y112B_HAEIN Reviewed; 371 AA. AC O86233; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 17-FEB-2016, entry version 74. DE RecName: Full=Uncharacterized membrane protein HI_1126.1; GN OrderedLocusNames=HI_1126.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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 CstA 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; L42023; AAC22781.1; -; Genomic_DNA. DR EnsemblBacteria; AAC22781; AAC22781; HI_1126.1. DR OMA; ATYICHA; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0031669; P:cellular response to nutrient levels; IBA:GO_Central. DR GO; GO:0009267; P:cellular response to starvation; IEA:InterPro. DR InterPro; IPR003706; CstA_N. DR Pfam; PF02554; CstA; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 371 Uncharacterized membrane protein FT HI_1126.1. FT /FTId=PRO_0000190051. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 282 302 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. SQ SEQUENCE 371 AA; 40565 MW; 14E050AF57B87B58 CRC64; MRSLPMLWFF FCVTVLIIGY FIYGKIIEKI FVINPKRQTP AYQVNDGVDY MPMSKTKIWL IQLLNIAGTG PIFGPILGAL YGPVAMLWIV IGCIFAGAVH DYFCGMLSIR HGGATMPYLA GKFLGRPVKV FINTLALVLL LLVGVVFVAS PAQLMGTITM DVFGVSQGAL VLGDAEAVHH SVEAGGIKVW GMDKATVVAV WTAIIFAYYI LATLLPVDKI IGRIYPLFGA LLLFMSVGMV YGLVVSHFSA TDPIEFFRTI NADGEGLTWA KFTQNFQVKG DVPIWPLLFL TISCGALSGF HATQTPLMAR CTENESEGRF IFYGAMITEG VIALVWCMVG LAFYENPQAL QDAISAGCSM LKLCMIVRYI S // ID Y1146_HAEIN Reviewed; 285 AA. AC P45071; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Nucleotide-binding protein HI_1146 {ECO:0000255|HAMAP-Rule:MF_00636}; GN OrderedLocusNames=HI_1146; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Displays ATPase and GTPase activities. CC {ECO:0000255|HAMAP-Rule:MF_00636}. CC -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP- CC Rule:MF_00636}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22801.1; 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; L42023; AAC22801.1; ALT_INIT; Genomic_DNA. DR PIR; G64167; G64167. DR RefSeq; NP_439304.2; NC_000907.1. DR RefSeq; WP_010869138.1; NC_000907.1. DR ProteinModelPortal; P45071; -. DR STRING; 71421.HI1146; -. DR PRIDE; P45071; -. DR EnsemblBacteria; AAC22801; AAC22801; HI_1146. DR GeneID; 950109; -. DR KEGG; hin:HI1146; -. DR PATRIC; 20190967; VBIHaeInf48452_1196. DR eggNOG; ENOG4105C21; Bacteria. DR eggNOG; COG1660; LUCA. DR KO; K06958; -. DR OMA; VSFGYKY; -. DR OrthoDB; EOG6WHNW8; -. DR PhylomeDB; P45071; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00636; RapZ_like; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005337; RapZ-like. DR Pfam; PF03668; ATP_bind_2; 1. DR PIRSF; PIRSF005052; P-loopkin; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 285 Nucleotide-binding protein HI_1146. FT /FTId=PRO_0000107716. FT NP_BIND 8 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00636}. FT NP_BIND 56 59 GTP. {ECO:0000255|HAMAP-Rule:MF_00636}. SQ SEQUENCE 285 AA; 32564 MW; 5D27CCCB77FFDA56 CRC64; MEIIIISGRS GAGKSVALRA LEDAGYYCVD NIPLDLLPQL TDILSQSQSS VAISLDIRNI PNSAHSLKQT LSTLQKHHQI KIIFLEADRA TLIRRYSDSR RLHPLSLKDL SLEAAIDEEY RYLEPLIQHA NLILDTTHLS THSLAERLRE FLRGNSEKEL KIIVESFGFK YGIPLDADYV FDVRFLPNPH WDPTLRPMTG LEAPVAEFLN SHTEVNEFIY LTRHYIDTWL PMLEKNNRSY LTIAIGCTGG KHRSVYIAQQ LGEYFQAKGK TVKIQHKSLE RNKKI // ID Y120_HAEIN Reviewed; 168 AA. AC P43947; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0120; GN OrderedLocusNames=HI_0120; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21801.1; -; Genomic_DNA. DR PIR; A64002; A64002. DR RefSeq; NP_438292.1; NC_000907.1. DR RefSeq; WP_005653606.1; NC_000907.1. DR STRING; 71421.HI0120; -. DR EnsemblBacteria; AAC21801; AAC21801; HI_0120. DR GeneID; 951028; -. DR KEGG; hin:HI0120; -. DR PATRIC; 20188725; VBIHaeInf48452_0124. DR eggNOG; COG5413; LUCA. DR OMA; LSIQKWR; -. DR OrthoDB; EOG6MWNBH; -. DR Proteomes; UP000000579; 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; IPR019275; DUF2301. DR Pfam; PF10063; DUF2301; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 168 Uncharacterized protein HI_0120. FT /FTId=PRO_0000077892. FT TRANSMEM 15 33 Helical. {ECO:0000255}. FT TRANSMEM 41 57 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. SQ SEQUENCE 168 AA; 19159 MW; 27519DC2F8687A8D CRC64; MADPHIKSPM DFLDYLTVII YRTGFVIAAL AVLTVSWYPD LSLTFILIAA TCCASSLHIY LKSFRLLFQF ATWIGLLFYI NHYPALALGG ALLTLGGLCF KEYFCFRVPL LNLQPIFVAC LWFSWVLNNL IALRIFSIIS GVLLLVLAIQ KWRMPLHFDI GDKTKYQI // ID XYLA_HAEIN Reviewed; 439 AA. AC P44398; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OrderedLocusNames=HI_1112; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: D-xylopyranose = D-xylulose. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22766.1; -; Genomic_DNA. DR PIR; D64183; ISHIX. DR RefSeq; NP_439269.1; NC_000907.1. DR RefSeq; WP_005651773.1; NC_000907.1. DR ProteinModelPortal; P44398; -. DR SMR; P44398; 3-439. DR STRING; 71421.HI1112; -. DR EnsemblBacteria; AAC22766; AAC22766; HI_1112. DR GeneID; 950068; -. DR KEGG; hin:HI1112; -. DR PATRIC; 20190897; VBIHaeInf48452_1161. DR eggNOG; ENOG4105C93; Bacteria. DR eggNOG; COG2115; LUCA. DR KO; K01805; -. DR OMA; HTFQHEL; -. DR OrthoDB; EOG62NX4R; -. DR PhylomeDB; P44398; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009045; F:xylose isomerase activity; IBA:GO_Central. DR GO; GO:0042843; P:D-xylose catabolic process; IBA:GO_Central. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.150; -; 1. DR HAMAP; MF_00455; Xylose_isom_A; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013452; Xylose_isom_bac. DR InterPro; IPR001998; Xylose_isomerase. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; SSF51658; 1. DR TIGRFAMs; TIGR02630; xylose_isom_A; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Magnesium; Metal-binding; Pentose shunt; Reference proteome; KW Xylose metabolism. FT CHAIN 1 439 Xylose isomerase. FT /FTId=PRO_0000195779. FT ACT_SITE 101 101 {ECO:0000250}. FT ACT_SITE 104 104 {ECO:0000250}. FT METAL 232 232 Magnesium 1. {ECO:0000250}. FT METAL 268 268 Magnesium 1. {ECO:0000250}. FT METAL 268 268 Magnesium 2. {ECO:0000250}. FT METAL 271 271 Magnesium 2. {ECO:0000250}. FT METAL 296 296 Magnesium 1. {ECO:0000250}. FT METAL 307 307 Magnesium 2. {ECO:0000250}. FT METAL 309 309 Magnesium 2. {ECO:0000250}. FT METAL 339 339 Magnesium 1. {ECO:0000250}. SQ SEQUENCE 439 AA; 49896 MW; 24CD3CE4736A3EA6 CRC64; MTTYFDKIEK ISFEGEKSTN PFAFKHYDAN QVILGKTMAE HLRLAVCYWH TFCWNGNDMF GLGSLERSWQ KNSNLLAGAE QKADIAFEFL NKLGVPYYCF HDVDIAPEGN SVREYVQNFH HIVDILERKQ VETGVKLLWG TANCFTNPRY MSGAATNPNP EVFAWAATQV FNAMNATQRL GGENYVLWGG REGYETLLNT DLKREREQIG RFMQMVVEHK HKIGFKGTLL IEPKPQEPTK HQYDYDVATV YGFLKQFGLE KEIKVNIEAN HATLAGHTFQ HEIATACALD IFGSIDANRG DPQLGWDTDQ FPNSVEENTL VMYEILKHGG FTTGGFNFDA KIRRQSIDPY DLFYAHIGAI DVLALSLKRA AKMLQEETLQ KIVNERYAGW NSELGQHILQ GKTSLETLAQ LVQQKDLAPK PVSGQQEYLE NLVNQVIYS // ID Y042_HAEIN Reviewed; 224 AA. AC P43930; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized RNA pseudouridine synthase HI_0042; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase; DE AltName: Full=RNA-uridine isomerase; GN OrderedLocusNames=HI_0042; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine. CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA 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; L42023; AAC21720.1; -; Genomic_DNA. DR PIR; B64000; B64000. DR RefSeq; NP_438215.1; NC_000907.1. DR RefSeq; WP_005693879.1; NC_000907.1. DR ProteinModelPortal; P43930; -. DR STRING; 71421.HI0042; -. DR EnsemblBacteria; AAC21720; AAC21720; HI_0042. DR GeneID; 950939; -. DR KEGG; hin:HI0042; -. DR PATRIC; 20188535; VBIHaeInf48452_0042. DR eggNOG; ENOG4108W1A; Bacteria. DR eggNOG; COG0564; LUCA. DR KO; K06177; -. DR OMA; VENDCRR; -. DR OrthoDB; EOG6P070X; -. DR PhylomeDB; P43930; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR006508; PsdUridine_synth_RluA-like. DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR01621; RluA-like; 1. DR PROSITE; PS01129; PSI_RLU; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 224 Uncharacterized RNA pseudouridine FT synthase HI_0042. FT /FTId=PRO_0000162726. FT ACT_SITE 52 52 {ECO:0000250}. SQ SEQUENCE 224 AA; 25526 MW; 1EE581956D0E41BD CRC64; MEIEVVYQHS DFIIINKSEG ISVHKDQEEQ GLTELVAKQL NVPKVWLVHR LDKVTSGLLI LALNAESAAE FSRLFSEHKI HKTYLALSNQ KPKKKQGLII GDMKKAREGA WKLCQTKDNP AITRFESVSC EPNLRLFILK PQTGKTHQLR VAMKSLGSPI LGDGLYGKNT EKIDRTYLHA TQLEFDYLNN FISVTCLPSQ GQFWIKPTVF EQIQVYLTKP FLSK // ID Y073_HAEIN Reviewed; 114 AA. AC P43933; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=Uncharacterized protein HI_0073; GN OrderedLocusNames=HI_0073; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21758.1; -; Genomic_DNA. DR PIR; E64000; E64000. DR RefSeq; NP_438246.1; NC_000907.1. DR RefSeq; WP_005693849.1; NC_000907.1. DR PDB; 1NO5; X-ray; 1.80 A; A/B=1-114. DR PDBsum; 1NO5; -. DR ProteinModelPortal; P43933; -. DR SMR; P43933; 4-105. DR STRING; 71421.HI0073; -. DR EnsemblBacteria; AAC21758; AAC21758; HI_0073. DR GeneID; 950966; -. DR KEGG; hin:HI0073; -. DR PATRIC; 20188601; VBIHaeInf48452_0074. DR eggNOG; ENOG41060A7; Bacteria. DR eggNOG; COG1708; LUCA. DR KO; K07076; -. DR OMA; WHAISPE; -. DR OrthoDB; EOG6P071R; -. DR EvolutionaryTrace; P43933; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein HI_0073. FT /FTId=PRO_0000077881. FT HELIX 11 24 {ECO:0000244|PDB:1NO5}. FT STRAND 28 33 {ECO:0000244|PDB:1NO5}. FT HELIX 34 36 {ECO:0000244|PDB:1NO5}. FT TURN 37 39 {ECO:0000244|PDB:1NO5}. FT STRAND 47 52 {ECO:0000244|PDB:1NO5}. FT HELIX 59 71 {ECO:0000244|PDB:1NO5}. FT STRAND 78 82 {ECO:0000244|PDB:1NO5}. FT HELIX 83 85 {ECO:0000244|PDB:1NO5}. FT HELIX 88 96 {ECO:0000244|PDB:1NO5}. FT STRAND 99 102 {ECO:0000244|PDB:1NO5}. SQ SEQUENCE 114 AA; 13179 MW; B1367D6644F61DF6 CRC64; MTSFAQLDIK SEELAIVKTI LQQLVPDYTV WAFGSRVKGK AKKYSDLDLA IISEEPLDFL ARDRLKEAFS ESDLPWRVDL LDWATTSEDF REIIRKVYVV IQEKEKTVEK PTAL // ID Y074_HAEIN Reviewed; 146 AA. AC P43934; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Uncharacterized protein HI_0074; GN OrderedLocusNames=HI_0074; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21759.1; -; Genomic_DNA. DR PIR; F64000; F64000. DR RefSeq; NP_438247.1; NC_000907.1. DR RefSeq; WP_005693848.1; NC_000907.1. DR PDB; 1JOG; X-ray; 2.40 A; A/B/C/D=1-146. DR PDBsum; 1JOG; -. DR ProteinModelPortal; P43934; -. DR SMR; P43934; 7-142. DR STRING; 71421.HI0074; -. DR EnsemblBacteria; AAC21759; AAC21759; HI_0074. DR GeneID; 950972; -. DR KEGG; hin:HI0074; -. DR PATRIC; 20188603; VBIHaeInf48452_0075. DR eggNOG; ENOG41062MS; Bacteria. DR eggNOG; ENOG4112BTD; LUCA. DR OMA; VYAQIDD; -. DR OrthoDB; EOG62RSFM; -. DR EvolutionaryTrace; P43934; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010235; NucleotidylTrfase-bd_HI0074. DR Pfam; PF08780; NTase_sub_bind; 1. DR TIGRFAMs; TIGR01987; HI0074; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 146 Uncharacterized protein HI_0074. FT /FTId=PRO_0000077882. FT HELIX 8 26 {ECO:0000244|PDB:1JOG}. FT HELIX 28 31 {ECO:0000244|PDB:1JOG}. FT HELIX 36 68 {ECO:0000244|PDB:1JOG}. FT HELIX 80 89 {ECO:0000244|PDB:1JOG}. FT HELIX 96 106 {ECO:0000244|PDB:1JOG}. FT HELIX 107 111 {ECO:0000244|PDB:1JOG}. FT HELIX 115 123 {ECO:0000244|PDB:1JOG}. FT HELIX 125 140 {ECO:0000244|PDB:1JOG}. SQ SEQUENCE 146 AA; 17128 MW; 1DF7C7C199701999 CRC64; MMTDKLNLNV LDAAFYSLEQ TVVQISDRNW FDMQPSIVQD TLIAGAIQKF EFVYELSLKM MKRQLQQDAI NTDDIGAYGF KDILREALRF GLIGDMSKWV AYRDMRNITS HTYDQEKAMA VYAQIDDFLI ESSFLLEQLR QRNQYD // ID Y082_HAEIN Reviewed; 88 AA. AC P43937; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_0082; DE Flags: Precursor; GN OrderedLocusNames=HI_0082; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21761.1; -; Genomic_DNA. DR PIR; I64000; I64000. DR RefSeq; NP_438255.1; NC_000907.1. DR RefSeq; WP_005652512.1; NC_000907.1. DR ProteinModelPortal; P43937; -. DR STRING; 71421.HI0082; -. DR EnsemblBacteria; AAC21761; AAC21761; HI_0082. DR GeneID; 950979; -. DR KEGG; hin:HI0082; -. DR PATRIC; 20188619; VBIHaeInf48452_0083. DR OrthoDB; EOG600DMX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro. DR Gene3D; 1.10.540.10; -; 1. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR SUPFAM; SSF56645; SSF56645; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 88 Uncharacterized protein HI_0082. FT /FTId=PRO_0000013948. SQ SEQUENCE 88 AA; 9732 MW; FC9C47F289905C06 CRC64; MGLTLKEHAE VCMALAESSA SAGLCYMMSN VAVNCLNLFG SYQLKQKIFS DIVQNKTFAA LAYSELGTGT HFYSSFYINM AWNLVKIM // ID Y100_HAEIN Reviewed; 131 AA. AC P43941; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-SEP-2015, entry version 51. DE RecName: Full=Uncharacterized protein HI_0100; GN OrderedLocusNames=HI_0100; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21781.1; -; Genomic_DNA. DR PIR; D64001; D64001. DR EnsemblBacteria; AAC21781; AAC21781; HI_0100. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR InterPro; IPR003709; Pept_M15B. DR Pfam; PF02557; VanY; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 131 Uncharacterized protein HI_0100. FT /FTId=PRO_0000077888. SQ SEQUENCE 131 AA; 15062 MW; ED8756405581724B CRC64; MSGDFTLVCI TAASRHHWGT EVDIFDPDLL PRGQSLQLEP WEYEKGGYFF ELSEFLAENL PHFDFALPFM NMQSNKKVGR EPWHISYLPL AELASQQFSP EILPQAWKGE NILGADCLIS HLEQIFSEYI V // ID Y1015_HAEIN Reviewed; 488 AA. AC P71364; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Uncharacterized permease HI_1015; GN OrderedLocusNames=HI_1015; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GntP permease 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; L42023; AAC22676.1; -; Genomic_DNA. DR PIR; D64108; D64108. DR RefSeq; NP_439176.1; NC_000907.1. DR RefSeq; WP_005693351.1; NC_000907.1. DR STRING; 71421.HI1015; -. DR EnsemblBacteria; AAC22676; AAC22676; HI_1015. DR GeneID; 950013; -. DR KEGG; hin:HI1015; -. DR PATRIC; 20190693; VBIHaeInf48452_1059. DR eggNOG; ENOG4105C6Z; Bacteria. DR eggNOG; COG2610; LUCA. DR OMA; PVILGCW; -. DR OrthoDB; EOG6B8XPC; -. DR PhylomeDB; P71364; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015128; F:gluconate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR InterPro; IPR003474; Glcn_transporter. DR Pfam; PF02447; GntP_permease; 1. DR PIRSF; PIRSF002746; Gluconate_transporter; 1. DR TIGRFAMs; TIGR00791; gntP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 488 Uncharacterized permease HI_1015. FT /FTId=PRO_0000061945. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 106 126 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 347 367 Helical. {ECO:0000255}. FT TRANSMEM 368 388 Helical. {ECO:0000255}. FT TRANSMEM 438 458 Helical. {ECO:0000255}. FT TRANSMEM 461 481 Helical. {ECO:0000255}. SQ SEQUENCE 488 AA; 51718 MW; F5CD520C0993669A CRC64; MFGLPIPIIG LLIAVFVLVF LVLRTRVHAF IAMLIAASIA GLVGGMSADE TLNSITKGFG GTLGSIGIVI GLGVMMGSVL EVSGAAEKMA YSFIKMLGQK KEEWALAITG YVVSIPIFVD SAFVILYPVA KALAKNGKRS LLTLGVALAG GLAVTHHTVP PTPGPLGVAG LFGVDIGAML LTGMCMAFLP VVGIVLYAKW LDKKYPNFNQ EVFTEEELKQ KYDSYIESRE KKELPSLGLS LLPIVLPIVL IFIKAVVHLF VKDVPEALTS IPYQIVSFLG HPVIVLALSV LISVYTLLPK ADKNTTALHL EEGVKTAGII LLVTGAGGAL GAVLRDSGAG KQLAEQIANL PISPILIPFI VSTLVRFIQG SGTVAMITAA SISSPILAQI PGVNMLLAAQ AATMGSLFFG YFNDSLFWVV NRMMGINDVK KQMVVWSVPT TIAWGIGGIS VILANLIFGN DGSVFDLLFP VVVLASILFY IKLQNKNL // ID Y1048_HAEIN Reviewed; 369 AA. AC P44103; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1048; DE Flags: Precursor; GN OrderedLocusNames=HI_1048; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22710.1; -; Genomic_DNA. DR PIR; D64019; D64019. DR RefSeq; NP_439207.1; NC_000907.1. DR RefSeq; WP_010869115.1; NC_000907.1. DR ProteinModelPortal; P44103; -. DR STRING; 71421.HI1048; -. DR DNASU; 949536; -. DR EnsemblBacteria; AAC22710; AAC22710; HI_1048. DR GeneID; 949536; -. DR KEGG; hin:HI1048; -. DR PATRIC; 20190761; VBIHaeInf48452_1093. DR eggNOG; ENOG4108KS2; Bacteria. DR eggNOG; COG1305; LUCA. DR OMA; IVNNMER; -. DR OrthoDB; EOG6GTZFG; -. DR PhylomeDB; P44103; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.90.260.10; -; 1. DR InterPro; IPR002931; Transglutaminase-like. DR Pfam; PF01841; Transglut_core; 1. DR SMART; SM00460; TGc; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 369 Uncharacterized protein HI_1048. FT /FTId=PRO_0000013963. SQ SEQUENCE 369 AA; 41146 MW; E8378DFDA368002F CRC64; MKKLIAVAVL SACGSLAHAN TNIPNYNTDA HLYEFTQTYD LVVPKGSQGQ TNLWVPLPFN GEYQQVKSIH FEGNYMNAYV TENNKYGAKT LFATWNKDAQ KRDLKVMMVI ETKDREPMVK GALENYTPPK DIQYSVDVQE YLKATPHIKT DGIVKEFPDK ILGKETNPLK KAELIHHWFV KNMERDNSVL GCGDGDVEKI LTTGVLKGKC TDINSVFVAL ARAAGIPARE IFGIRLGAAE KMGKYSKGAF GSANEQGIAN VSGGQHCRAE FYLAGFGWVP VDSADVAKMR LAEKKSVEDK DTQAVAKYLF GNWEANWVGF NHARDFDLYP QPELAPINNF GYPYAEVGGD PLNSFDPKEF KYDYVSKKL // ID Y1128_HAEIN Reviewed; 58 AA. AC P44115; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_1128; GN OrderedLocusNames=HI_1128; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22783.1; -; Genomic_DNA. DR PIR; G64020; G64020. DR EnsemblBacteria; AAC22783; AAC22783; HI_1128. DR Proteomes; UP000000579; 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 58 Uncharacterized protein HI_1128. FT /FTId=PRO_0000078007. FT TRANSMEM 24 44 Helical. {ECO:0000255}. SQ SEQUENCE 58 AA; 6710 MW; A52CCC611D281B76 CRC64; MVYHNSMCTY LFYNKIGFGL DYQLSVYLGL ATTIVCIVLF FTMLKPLGTR DEEAYINN // ID Y1218_HAEIN Reviewed; 532 AA. AC Q57251; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative L-lactate permease; GN OrderedLocusNames=HI_1218; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May play a role in L-lactate transport. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the lactate permease 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; L42023; AAC22871.1; -; Genomic_DNA. DR PIR; H64110; H64110. DR RefSeq; NP_439374.1; NC_000907.1. DR RefSeq; WP_010869155.1; NC_000907.1. DR STRING; 71421.HI1218; -. DR TCDB; 2.A.14.2.1; the lactate permease (lctp) family. DR EnsemblBacteria; AAC22871; AAC22871; HI_1218. DR GeneID; 950748; -. DR KEGG; hin:HI1218; -. DR PATRIC; 20191115; VBIHaeInf48452_1270. DR eggNOG; ENOG4105DAA; Bacteria. DR eggNOG; COG1620; LUCA. DR KO; K03303; -. DR OMA; AMMNDAT; -. DR OrthoDB; EOG6Q8J3Z; -. DR PhylomeDB; Q57251; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003804; Lactate_perm. DR PANTHER; PTHR30003; PTHR30003; 1. DR Pfam; PF02652; Lactate_perm; 1. DR TIGRFAMs; TIGR00795; lctP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 532 Putative L-lactate permease. FT /FTId=PRO_0000210382. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. FT TRANSMEM 234 254 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. FT TRANSMEM 346 366 Helical. {ECO:0000255}. FT TRANSMEM 387 407 Helical. {ECO:0000255}. FT TRANSMEM 420 440 Helical. {ECO:0000255}. FT TRANSMEM 462 482 Helical. {ECO:0000255}. FT TRANSMEM 508 528 Helical. {ECO:0000255}. SQ SEQUENCE 532 AA; 56885 MW; F3C1DF47E54217FB CRC64; MLSFILSIFP IVLLIYLMVK RNALPSYVAL PWVATLVMGV HLLHFNTDIV TISANVVSAI IAVQTPITVI FGAILFNRFS EISGATNIMR KWLGNINPNP VAQLMIIGWA FAFMIEGASG FGTPAAIAAP ILVGLGFHPL KVAMLALIMN SVPVSFGAVG TPTWFGFGAL KLSEDMILEI GSITAFIHSI AALIIPLLAL RILVNWDDIR KNIVFIYISV LGCVVPYFLI AQVNYEFPSL VGGAIGLFIS VWAANRNIGL AKVTNTLDNN AVSAGEVVKA LFPTGLLIAF LIVTRIHQLP FKAMMNDATI WFSTTLGSLG LFEISKGLIF SLKNIFGSNV SSSYKLLYVP ALIPFVITVL IAIPFFKISS SNVKQILVSS LQQSKNPFIA LIGALVMVNL MLVGGEHSMV KIIGRTFAEI SGSNWTIFSS FLGAIGSFFS GSNTVSNLTF GSVQLSTAET TGISVALVLA LQSVGGAMGN MVCINNIVAV SSVLNISNQE GTIIKKTIIP MIIYGIIAAL GALFLVPLFY NL // ID Y122B_HAEIN Reviewed; 231 AA. AC O86235; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized protein HI_1225.1; GN OrderedLocusNames=HI_1225.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DnaA family. HdA 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; L42023; AAC22879.1; -; Genomic_DNA. DR RefSeq; NP_439382.1; NC_000907.1. DR RefSeq; WP_005694288.1; NC_000907.1. DR ProteinModelPortal; O86235; -. DR STRING; 71421.HI1225.1; -. DR EnsemblBacteria; AAC22879; AAC22879; HI_1225.1. DR GeneID; 950792; -. DR KEGG; hin:HI1225.1; -. DR PATRIC; 20191131; VBIHaeInf48452_1278. DR eggNOG; ENOG4108KZ1; Bacteria. DR eggNOG; COG0593; LUCA. DR KO; K10763; -. DR OMA; YELVCLD; -. DR OrthoDB; EOG6038W4; -. DR PhylomeDB; O86235; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR020591; Chromosome_initiator_DnaA-like. DR InterPro; IPR013317; DnaA. DR InterPro; IPR017788; Hda. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00308; Bac_DnaA; 1. DR PRINTS; PR00051; DNAA. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03420; DnaA_homol_Hda; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 231 Uncharacterized protein HI_1225.1. FT /FTId=PRO_0000114324. SQ SEQUENCE 231 AA; 26366 MW; 9567B4E6B389BBB0 CRC64; MNKQLPLPIH QIDDATLENF YGDNNLLLLD SLRKNSSDLK QPFFYIWGDK GSGKTHLLRA FSNEYLINQR TAIYVPLSKS QYFSTAVLEN LEQQELVCLD DLQSVIGNDE WELAIFDLFN RIKASGKTLL LISADKSPSA LSVKLPDLNS RLTWGEIYQL NSLTDEQKIK VLQLAAYQRG FQLSDETANF LITRLARDMH TLFEALDLLD KASLQAQRNL TIPFVKKILN L // ID Y1248_HAEIN Reviewed; 322 AA. AC P44136; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Putative nickel/cobalt efflux system HI_1248; GN OrderedLocusNames=HI_1248; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Efflux system for nickel and cobalt. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) 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; L42023; AAC22907.1; -; Genomic_DNA. DR PIR; A64023; A64023. DR RefSeq; NP_439404.1; NC_000907.1. DR RefSeq; WP_005694309.1; NC_000907.1. DR STRING; 71421.HI1248; -. DR EnsemblBacteria; AAC22907; AAC22907; HI_1248. DR GeneID; 950186; -. DR KEGG; hin:HI1248; -. DR PATRIC; 20191177; VBIHaeInf48452_1300. DR eggNOG; ENOG4105D7X; Bacteria. DR eggNOG; COG2215; LUCA. DR OMA; SIGARPC; -. DR OrthoDB; EOG6NWBNJ; -. DR PhylomeDB; P44136; -. DR Proteomes; UP000000579; 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:0015099; F:nickel cation transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW. DR InterPro; IPR011541; Ni/Co_transpt_high_affinity. DR Pfam; PF03824; NicO; 2. PE 3: Inferred from homology; KW Cell membrane; Cobalt; Cobalt transport; Complete proteome; KW Ion transport; Membrane; Nickel; Nickel transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 322 Putative nickel/cobalt efflux system FT HI_1248. FT /FTId=PRO_0000194014. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 294 314 Helical. {ECO:0000255}. SQ SEQUENCE 322 AA; 35669 MW; EC1248D2F25A1F47 CRC64; MKKYKTGLVL LVIALALLVY FSPWFFLHIA SWQKEFNQLI SENLHQIQNN SIKAGTTLIF ASFVYGVLHA LGPGHGKFII ASYLSTHESQ LKQSTILSLL SSLMQGIVAI TATTLLVVVL NLSSRYFKLS QLWLERTALL LLVFLGCYWI WQGLRAYRKK AKLAIKSLNP LPLHEKSAVK NNRTFQPNTC SCGHQHLPSP TQTAQATNLK SQFLVILTIG MRPCSGAIFV LFLAYMLDLY SWGILAVLAM SFGTGLMLSA FAGIVRYARN TAIHLGHWYS SKNTKGKSES IVKLIAGGIM LFFALSLLYG TTISTGGSKI LF // ID Y1249_HAEIN Reviewed; 206 AA. AC P44137; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_1249; DE Flags: Precursor; GN OrderedLocusNames=HI_1249; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22908.1; -; Genomic_DNA. DR PIR; B64023; B64023. DR RefSeq; NP_439405.1; NC_000907.1. DR RefSeq; WP_005694310.1; NC_000907.1. DR STRING; 71421.HI1249; -. DR DNASU; 950126; -. DR EnsemblBacteria; AAC22908; AAC22908; HI_1249. DR GeneID; 950126; -. DR KEGG; hin:HI1249; -. DR PATRIC; 20191179; VBIHaeInf48452_1301. DR eggNOG; ENOG41065CD; Bacteria. DR eggNOG; COG3683; LUCA. DR OMA; HNGQKVK; -. DR OrthoDB; EOG6J48KP; -. DR PhylomeDB; P44137; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010412; DUF1007. DR InterPro; IPR016537; UCP008159_ABC. DR Pfam; PF06226; DUF1007; 1. DR PIRSF; PIRSF008159; UCP008159_ABC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 206 Uncharacterized protein HI_1249. FT /FTId=PRO_0000013968. SQ SEQUENCE 206 AA; 23440 MW; 45D9DCA6DB9E3E01 CRC64; MKTYSLLLGL FISFGVLAHP HAFIDIQTTP IIENNQLTGF SMKWTLDEPS SSAVIYDMKQ ARTKAEKQKL LDDVMGNIVS EHYFSYLYDA QNNKIKYSPR PKNYGINVQG LQLQYYFDVP LAHPQKLEKN TFSLQTYDPT YYVAMTYASK SAVDFSALSK NCQGKLIEPN VDEKIQAYAS SLDKSQKNED DSLGVMFAQK IIIQCE // ID Y1278_HAEIN Reviewed; 220 AA. AC Q57431; O05050; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Putative NAD(P)H nitroreductase; DE EC=1.-.-.-; GN OrderedLocusNames=HI_1278; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the nitroreductase 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; L42023; AAC22926.1; -; Genomic_DNA. DR PIR; B64114; B64114. DR RefSeq; NP_439431.1; NC_000907.1. DR RefSeq; WP_005694521.1; NC_000907.1. DR ProteinModelPortal; Q57431; -. DR STRING; 71421.HI1278; -. DR EnsemblBacteria; AAC22926; AAC22926; HI_1278. DR GeneID; 950210; -. DR KEGG; hin:HI1278; -. DR PATRIC; 20191235; VBIHaeInf48452_1329. DR eggNOG; ENOG4108RCM; Bacteria. DR eggNOG; COG0778; LUCA. DR OMA; CLAEEGL; -. DR OrthoDB; EOG65QWJJ; -. DR PhylomeDB; Q57431; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 1: Evidence at protein level; KW Complete proteome; Flavoprotein; FMN; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 220 Putative NAD(P)H nitroreductase. FT /FTId=PRO_0000072715. FT NP_BIND 155 160 NAD or NADP. {ECO:0000250}. SQ SEQUENCE 220 AA; 25189 MW; AB0D804601BC975E CRC64; MTQLTREQVL ELFHQRSSTR YYDPTKKISD EDFECILECG RLSPSSVGSE PWKFLVIQNK TLREKMKPFS WGMINQLDNC SHLVVILAKK NARYDSPFFV DVMARKGLNA EQQQAALTKY KALQEEDMKL LENDRTLFDW CSKQTYIALA NMLTGASALG IDSCPIEGFH YDKMNECLAE EGLFDPQEYA VSVAATFGYR SRDIAKKSRK GLDEVVKWVG // ID Y1297_HAEIN Reviewed; 140 AA. AC P45145; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=UPF0299 membrane protein HI_1297 {ECO:0000255|HAMAP-Rule:MF_01144}; GN OrderedLocusNames=HI_1297; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01144}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01144}. CC -!- SIMILARITY: Belongs to the UPF0299 family. {ECO:0000255|HAMAP- CC Rule:MF_01144}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22943.1; -; Genomic_DNA. DR PIR; C64170; C64170. DR RefSeq; NP_439448.1; NC_000907.1. DR RefSeq; WP_005694471.1; NC_000907.1. DR STRING; 71421.HI1297; -. DR EnsemblBacteria; AAC22943; AAC22943; HI_1297. DR GeneID; 950233; -. DR KEGG; hin:HI1297; -. DR PATRIC; 20191275; VBIHaeInf48452_1348. DR eggNOG; ENOG4105VAW; Bacteria. DR eggNOG; COG1380; LUCA. DR KO; K06518; -. DR OMA; GLMQHFD; -. DR OrthoDB; EOG65N1HV; -. DR PhylomeDB; P45145; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_01144; UPF0299; 1. DR InterPro; IPR005538; LrgA/CidA. DR InterPro; IPR022957; Uncharacterised_UPF0299. DR Pfam; PF03788; LrgA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 140 UPF0299 membrane protein HI_1297. FT /FTId=PRO_0000072809. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01144}. FT TRANSMEM 33 52 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01144}. FT TRANSMEM 60 80 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01144}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01144}. SQ SEQUENCE 140 AA; 15959 MW; A1DD839852316F3E CRC64; MIKKLFLLVR SLVILSIMLY LGNLIAYYIP SGVPGSIWGL LLLFLGLTTR VIHLNWIYLG ASLLIRFMAV LFVPVSVGII KYSDLLIEQI NILLVPNIVS TCVTLLVIGF LGHYLYQMQS FTHKRKKVIK RRENQVKQAN // ID Y1298_HAEIN Reviewed; 231 AA. AC P45146; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Uncharacterized protein HI_1298; GN OrderedLocusNames=HI_1298; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the YohK (E.coli)/YwbG (IPA-22R) CC (B.subtilis) 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; L42023; AAC22944.1; -; Genomic_DNA. DR PIR; D64170; D64170. DR RefSeq; NP_439449.1; NC_000907.1. DR RefSeq; WP_005694470.1; NC_000907.1. DR STRING; 71421.HI1298; -. DR EnsemblBacteria; AAC22944; AAC22944; HI_1298. DR GeneID; 950227; -. DR KEGG; hin:HI1298; -. DR PATRIC; 20191277; VBIHaeInf48452_1349. DR eggNOG; ENOG41067MG; Bacteria. DR eggNOG; COG1346; LUCA. DR OMA; QMHQIRA; -. DR OrthoDB; EOG6NPMDR; -. DR PhylomeDB; P45146; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR InterPro; IPR005261; CHP00659. DR InterPro; IPR007300; CidB/LrgB. DR Pfam; PF04172; LrgB; 1. DR TIGRFAMs; TIGR00659; TIGR00659; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 231 Uncharacterized protein HI_1298. FT /FTId=PRO_0000169142. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. SQ SEQUENCE 231 AA; 24886 MW; 3B9A6EA8CA27F188 CRC64; MQQYIIYLYT FLTIFGFWLA LQISKRWKSM IFNTFVLTVL ILAAILVIGK IPYDDYMAGN APINNLLGLS IVALALPLYE QLRQIARQWK IILSTVVIAS FLAMLSGGLL ALLLGSTPEM VATVLPKSIT MPIAMEVSRH LGGIPAVTAV GVVVAGLQGS IFGYLVLKKL GVKHQEAIGL SVGSVSHALG TVSCMETNPT AGSYSSISLV LCGIISSILA PFVFKLIYFF V // ID Y1317_HAEIN Reviewed; 271 AA. AC P44160; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Putative glucose-6-phosphate 1-epimerase; DE EC=5.1.3.15; DE AltName: Full=Putative D-hexose-6-phosphate mutarotase; GN OrderedLocusNames=HI_1317; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Alpha-D-glucose 6-phosphate = beta-D-glucose CC 6-phosphate. CC -!- SIMILARITY: Belongs to the Glucose-6-phosphate 1-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; L42023; AAC22962.1; -; Genomic_DNA. DR PIR; G64025; G64025. DR RefSeq; NP_439468.1; NC_000907.1. DR RefSeq; WP_010869181.1; NC_000907.1. DR ProteinModelPortal; P44160; -. DR STRING; 71421.HI1317; -. DR DrugBank; DB03754; Tris. DR EnsemblBacteria; AAC22962; AAC22962; HI_1317. DR GeneID; 950209; -. DR KEGG; hin:HI1317; -. DR PATRIC; 20191317; VBIHaeInf48452_1369. DR eggNOG; ENOG4105DSB; Bacteria. DR eggNOG; COG0676; LUCA. DR KO; K01792; -. DR OMA; TICFSNT; -. DR OrthoDB; EOG6M0T7Z; -. DR PhylomeDB; P44160; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_SF_dom. DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. DR Pfam; PF01263; Aldose_epim; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 271 Putative glucose-6-phosphate 1-epimerase. FT /FTId=PRO_0000213037. FT ACT_SITE 151 151 {ECO:0000250}. FT ACT_SITE 249 249 {ECO:0000250}. FT BINDING 71 71 Substrate. {ECO:0000250}. FT BINDING 93 93 Substrate. {ECO:0000250}. SQ SEQUENCE 271 AA; 30802 MW; 1B6FB70991EFF9FB CRC64; MKTTLLKTLT PELHLVQHND IPVPSLKTCG WNTKNFPCKG HSLSVGXPQN AKQDVLWLSE VEPFKNGNAI RGGVPICYPW FGGVKQPAHG TARIRLWQLS HYYISVHKVR LEFELFSDLN IIEAKVSMVF TDKCHLTFTH YGEESAQAAL HTYFNIGDIN QVEVQGLPET CFNSLNQQQE NVPSPRHISE NVDCIYSAEN MQNQILDKSF NRTIALHHHN ASQFVLWNPW HKKTSGMSET GYQKMLCLET ARIHHLLEFG ESLSVEISLK G // ID Y134_HAEIN Reviewed; 391 AA. AC P43952; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 73. DE RecName: Full=Uncharacterized protein HI_0134; GN OrderedLocusNames=HI_0134; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21811.1; -; Genomic_DNA. DR PIR; F64002; F64002. DR RefSeq; NP_438303.1; NC_000907.1. DR RefSeq; WP_005694421.1; NC_000907.1. DR STRING; 71421.HI0134; -. DR EnsemblBacteria; AAC21811; AAC21811; HI_0134. DR GeneID; 951034; -. DR KEGG; hin:HI0134; -. DR PATRIC; 20188755; VBIHaeInf48452_0136. DR OMA; NGENHIR; -. DR OrthoDB; EOG6CGC9G; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032712; AsmA_C. DR Pfam; PF13502; AsmA_2; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 391 Uncharacterized protein HI_0134. FT /FTId=PRO_0000077893. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 391 AA; 44575 MW; DA52577A8B962848 CRC64; MKKFALIVGI VALAIFSFLY IQLYRVQSAI NEQLAQQNIA VQSINLSLFS PALSLENIKT TQFSAQKIEA KFSFLPLLYG NAALHSLNIQ QLKLTQNTQN PANVSIEISP FSLKQLLSKK VILNGENHIR IEFNKPIYGK TKTFHFSFHK ANLDFSTSES TPLQFVDASL NNQPIGYIET HTAHQQIVTY IKPQCDNDCL AVLKYQQIDN QSAVNFSGKY FPVQRLFALL NLPEMLSGHA DFDLDFSFSS SSLIQGKLNF LAQNGEILGV NLLDMVAQYF PINYNNDLLQ NKELNTRFEQ FYLQLFLQQN QLIAEKIELK TPALLGQGKG IIDLNRMECN VDINLNSTDQ RYQNLTLPIN FFGNCNSPQY KINFTKKFRH QLIDAIKEKL R // ID Y1376_HAEIN Reviewed; 291 AA. AC P44170; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein HI_1376; GN OrderedLocusNames=HI_1376; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 EamA 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; L42023; AAC23030.1; -; Genomic_DNA. DR PIR; I64026; I64026. DR RefSeq; NP_439528.1; NC_000907.1. DR RefSeq; WP_005693980.1; NC_000907.1. DR STRING; 71421.HI1376; -. DR EnsemblBacteria; AAC23030; AAC23030; HI_1376. DR GeneID; 950804; -. DR KEGG; hin:HI1376; -. DR PATRIC; 20191441; VBIHaeInf48452_1431. DR eggNOG; ENOG4108TZV; Bacteria. DR eggNOG; ENOG4111H5E; LUCA. DR OMA; FNYITAI; -. DR OrthoDB; EOG6BW4ZJ; -. DR Proteomes; UP000000579; 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 1 291 Uncharacterized protein HI_1376. FT /FTId=PRO_0000078033. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 270 290 Helical. {ECO:0000255}. FT DOMAIN 107 138 EamA. SQ SEQUENCE 291 AA; 31916 MW; F7BA4E681B6490F7 CRC64; MHNLIFAILC SVAVSVLLKI ARKKNIIIEQ AIAFNYITAI TFSYFLLKPD FKGLEFTDYI AQSENSPIFL ALGLLLPSVF IIMSKAVEFA GIVRSDAAQR LSLFLPILAA FLIFHETLSQ SKIIGVVLAF IGLFCLLTKP TQGQSAVNFK GVLGLIGVWF GYGIIDILFK QVAKSGGAFP ATLFISFSLA ACVMFIYLFL KRVQWTSSSV IGGIVLGVLN FFNILFYIKA HQSFAGNPTL VFAGMNIGVI CLGTITGALV FKERISKLNW LGIIFSLSAI FCLYYLDKII A // ID Y1399_HAEIN Reviewed; 202 AA. AC P44175; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 64. DE RecName: Full=Uncharacterized protein HI_1399; GN OrderedLocusNames=HI_1399; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23051.1; -; Genomic_DNA. DR PIR; E64027; E64027. DR RefSeq; NP_439552.1; NC_000907.1. DR RefSeq; WP_005656697.1; NC_000907.1. DR STRING; 71421.HI1399; -. DR EnsemblBacteria; AAC23051; AAC23051; HI_1399. DR GeneID; 950317; -. DR KEGG; hin:HI1399; -. DR PATRIC; 20191497; VBIHaeInf48452_1459. DR eggNOG; ENOG4105RHG; Bacteria. DR eggNOG; ENOG4111WAP; LUCA. DR OMA; GQFWYRA; -. DR OrthoDB; EOG69KTVT; -. DR PhylomeDB; P44175; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro. DR InterPro; IPR016087; Chalcone_isomerase. DR Pfam; PF16036; Chalcone_3; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 202 Uncharacterized protein HI_1399. FT /FTId=PRO_0000078039. SQ SEQUENCE 202 AA; 23238 MW; D55017DAB9D191C4 CRC64; MKMKSLFVAM ITFFSAAPFA HWQPIGNAEY TWGPFHVYTI GLFSETGTYQ ENERPLMLSF KYEKPIEGKN FAITLIKEIE TLKLNDGDTQ SWLKEMQATF PDFSPNDILN YIALPDRGYF VLNDTVLEHD FDAKFNQAFI GIWLAPNSTF VKLQPQLLGK TKSNHEATEF YLKPEIESFD EQDSTPELPP NYLLDSQKKS QG // ID Y1415_HAEIN Reviewed; 200 AA. AC P44187; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_1415; GN OrderedLocusNames=HI_1415; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage D29 and phage L5 gp10. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23066.1; -; Genomic_DNA. DR PIR; H64028; H64028. DR RefSeq; NP_439566.1; NC_000907.1. DR RefSeq; WP_005693948.1; NC_000907.1. DR ProteinModelPortal; P44187; -. DR STRING; 71421.HI1415; -. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR EnsemblBacteria; AAC23066; AAC23066; HI_1415. DR GeneID; 950713; -. DR KEGG; hin:HI1415; -. DR PATRIC; 20191527; VBIHaeInf48452_1474. DR eggNOG; ENOG4105NVB; Bacteria. DR eggNOG; COG3179; LUCA. DR KO; K03791; -. DR OMA; EVTFNKI; -. DR OrthoDB; EOG6RVFXW; -. DR PhylomeDB; P44187; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004568; F:chitinase activity; IEA:InterPro. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR InterPro; IPR023346; Lysozyme-like_dom. DR Pfam; PF00182; Glyco_hydro_19; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 200 Uncharacterized protein HI_1415. FT /FTId=PRO_0000078052. SQ SEQUENCE 200 AA; 22895 MW; 42199FDDA4859FBB CRC64; MTMMISEVTF NKIFPHAVKG VYQAISAQIE KAGCVNKMQQ AMFLAQCGHE SGGFIRFKEN LNYSWLGLSQ TFRKYFPDPL TAKKYERKPE LIANRIYANR LGNGDEKSGD GWKYRGRGLI QITGKDNYAA FRKWLGRDIE PEDVAGNLDL SVKTAVWYWK CYELAELNSV EKVTRRINGG LNGIDERCKL YRALMVTDND // ID Y1430_HAEIN Reviewed; 252 AA. AC P45200; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Probable NADP-dependent dehydrogenase HI_1430; DE EC=1.1.1.-; GN OrderedLocusNames=HI_1430; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23077.1; -; Genomic_DNA. DR PIR; H64122; H64122. DR RefSeq; NP_439579.1; NC_000907.1. DR RefSeq; WP_005693935.1; NC_000907.1. DR ProteinModelPortal; P45200; -. DR STRING; 71421.HI1430; -. DR PRIDE; P45200; -. DR EnsemblBacteria; AAC23077; AAC23077; HI_1430. DR GeneID; 950332; -. DR KEGG; hin:HI1430; -. DR PATRIC; 20191555; VBIHaeInf48452_1487. DR eggNOG; ENOG4105EMU; Bacteria. DR eggNOG; COG4221; LUCA. DR KO; K00540; -. DR OMA; DWENMID; -. DR OrthoDB; EOG6N3CR8; -. DR PhylomeDB; P45200; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 2. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 252 Probable NADP-dependent dehydrogenase FT HI_1430. FT /FTId=PRO_0000054831. FT NP_BIND 7 31 NADP. {ECO:0000250}. FT ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 137 137 Substrate. {ECO:0000250}. SQ SEQUENCE 252 AA; 27398 MW; 227FB2E8CE7D9A98 CRC64; MKTTTALVTG ATAGFGLAIC KKLIEAGYKV IGTGRRADRL AEIHSQLGNN FLPLAFDIRD EQATINALNT LPEGWQAVDL LVNNAGLALG LEPAHKADLQ DWYQMIDTNI KGLVTITRLV LPNMVARNYG QIINLSSIAG TYPYAGSNVY GGTKAFVTQF SLNLRADLAG TKIRVSNVEP GLCGGTEFSN VRFHGDDERA AKVYENVQSV QPEDIANIVL WLHQQPEHVN INRIEVMPTA QSFAGMSVSK EK // ID Y143A_HAEIN Reviewed; 52 AA. AC P56507; O86238; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=UPF0181 protein HI_1434.2 {ECO:0000255|HAMAP-Rule:MF_00507}; GN OrderedLocusNames=HI_1434.2; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RX PubMed=9588799; DOI=10.1002/elps.1150190413; RA Rudd K.E., Humphery-Smith I., Wasinger V.C., Bairoch A.; RT "Low molecular weight proteins: a challenge for post-genomic RT research."; RL Electrophoresis 19:536-544(1998). CC -!- SIMILARITY: Belongs to the UPF0181 family. {ECO:0000255|HAMAP- CC Rule:MF_00507}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23083.1; 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; L42023; AAC23083.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_439585.2; NC_000907.1. DR STRING; 71421.HI1434.2; -. DR EnsemblBacteria; AAC23083; AAC23083; HI_1434.2. DR GeneID; 949916; -. DR KEGG; hin:HI1434.2; -. DR PATRIC; 20191567; VBIHaeInf48452_1493. DR eggNOG; COG3140; LUCA. DR KO; K09917; -. DR OMA; REQNKNT; -. DR OrthoDB; EOG68H8FF; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00507; UPF0181; 1. DR InterPro; IPR005371; UPF0181. DR Pfam; PF03701; UPF0181; 1. DR ProDom; PD026807; UPF0181; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 52 UPF0181 protein HI_1434.2. FT /FTId=PRO_0000216196. SQ SEQUENCE 52 AA; 5903 MW; FF8E364E185FB262 CRC64; MFDINLTHEQ QQKAVEQIQE LMAQGISSGE AIQIVAKALR EIHKNDKKTP EN // ID Y1472_HAEIN Reviewed; 351 AA. AC P44206; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Uncharacterized protein HI_1472; DE Flags: Precursor; GN OrderedLocusNames=HI_1472; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23120.1; -; Genomic_DNA. DR PIR; I64030; I64030. DR RefSeq; NP_439623.1; NC_000907.1. DR RefSeq; WP_005693488.1; NC_000907.1. DR PDB; 3PSA; X-ray; 1.70 A; A=22-347. DR PDB; 3PSH; X-ray; 1.50 A; A=22-347. DR PDBsum; 3PSA; -. DR PDBsum; 3PSH; -. DR ProteinModelPortal; P44206; -. DR DIP; DIP-58992N; -. DR STRING; 71421.HI1472; -. DR EnsemblBacteria; AAC23120; AAC23120; HI_1472. DR GeneID; 950575; -. DR KEGG; hin:HI1472; -. DR PATRIC; 20191659; VBIHaeInf48452_1539. DR eggNOG; ENOG4105S10; Bacteria. DR eggNOG; COG0614; LUCA. DR KO; K02016; -. DR OMA; SLPTHNI; -. DR OrthoDB; EOG6XSZRN; -. DR PhylomeDB; P44206; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 351 Uncharacterized protein HI_1472. FT /FTId=PRO_0000013972. FT DOMAIN 41 322 Fe/B12 periplasmic-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00344}. FT STRAND 23 26 {ECO:0000244|PDB:3PSH}. FT STRAND 32 35 {ECO:0000244|PDB:3PSH}. FT STRAND 42 45 {ECO:0000244|PDB:3PSH}. FT HELIX 47 55 {ECO:0000244|PDB:3PSH}. FT HELIX 59 61 {ECO:0000244|PDB:3PSH}. FT STRAND 62 65 {ECO:0000244|PDB:3PSH}. FT HELIX 69 73 {ECO:0000244|PDB:3PSH}. FT HELIX 77 79 {ECO:0000244|PDB:3PSH}. FT HELIX 82 86 {ECO:0000244|PDB:3PSH}. FT HELIX 98 103 {ECO:0000244|PDB:3PSH}. FT STRAND 107 112 {ECO:0000244|PDB:3PSH}. FT HELIX 117 124 {ECO:0000244|PDB:3PSH}. FT TURN 125 127 {ECO:0000244|PDB:3PSH}. FT STRAND 130 133 {ECO:0000244|PDB:3PSH}. FT HELIX 140 142 {ECO:0000244|PDB:3PSH}. FT HELIX 153 172 {ECO:0000244|PDB:3PSH}. FT HELIX 175 186 {ECO:0000244|PDB:3PSH}. FT HELIX 189 196 {ECO:0000244|PDB:3PSH}. FT TURN 201 203 {ECO:0000244|PDB:3PSH}. FT STRAND 204 209 {ECO:0000244|PDB:3PSH}. FT TURN 212 214 {ECO:0000244|PDB:3PSH}. FT STRAND 215 217 {ECO:0000244|PDB:3PSH}. FT STRAND 219 221 {ECO:0000244|PDB:3PSH}. FT HELIX 222 229 {ECO:0000244|PDB:3PSH}. FT STRAND 232 234 {ECO:0000244|PDB:3PSH}. FT TURN 235 239 {ECO:0000244|PDB:3PSH}. FT STRAND 241 245 {ECO:0000244|PDB:3PSH}. FT HELIX 248 254 {ECO:0000244|PDB:3PSH}. FT STRAND 257 261 {ECO:0000244|PDB:3PSH}. FT HELIX 268 273 {ECO:0000244|PDB:3PSH}. FT HELIX 276 278 {ECO:0000244|PDB:3PSH}. FT HELIX 282 285 {ECO:0000244|PDB:3PSH}. FT STRAND 289 291 {ECO:0000244|PDB:3PSH}. FT HELIX 304 308 {ECO:0000244|PDB:3PSH}. FT HELIX 310 318 {ECO:0000244|PDB:3PSH}. FT HELIX 320 322 {ECO:0000244|PDB:3PSH}. FT HELIX 328 339 {ECO:0000244|PDB:3PSH}. FT STRAND 340 342 {ECO:0000244|PDB:3PSH}. SQ SEQUENCE 351 AA; 39205 MW; 166842B3F4D2BBED CRC64; MKLKSLLIAC LLSSLSFSAL ADRIITDQLD RKVTIPDHIN RAVVLQHQTL NIAVQLDATK QIVGVLSNWK KQLGKNYVRL APELENMAMP GDLNSVNIES LLALKPDVVF VTNYAPSEMI KQISDVNIPV VAISLRTGEV GEKGKLNPTL TDEDKAYNDG LKQGIELIAE VFEKKQQGDE LVKAAFANRK LLADRLGDVS ADKRVRTYMA NPDLGTYGSG KYTGLMMEHA GAYNVAAATI KGFKQVSLEN VLEWNPAVIL VQDRYPDVVP QILNDQGWAN IQALKDKKVF LMPEYAKAWG YPMPEALALG EVWLAKALYP QRFQDVDLDK MVNDYYQKFY RTSYKPDNAA R // ID Y1476_HAEIN Reviewed; 239 AA. AC P44207; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1476; GN OrderedLocusNames=HI_1476; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23123.1; -; Genomic_DNA. DR PIR; A64031; A64031. DR RefSeq; NP_439627.1; NC_000907.1. DR RefSeq; WP_005693492.1; NC_000907.1. DR ProteinModelPortal; P44207; -. DR STRING; 71421.HI1476; -. DR DNASU; 950582; -. DR EnsemblBacteria; AAC23123; AAC23123; HI_1476. DR GeneID; 950582; -. DR KEGG; hin:HI1476; -. DR PATRIC; 20191669; VBIHaeInf48452_1544. DR eggNOG; ENOG4105M7P; Bacteria. DR eggNOG; COG2932; LUCA. DR OMA; TTISAYQ; -. DR OrthoDB; EOG6TBHDR; -. DR PhylomeDB; P44207; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF01381; HTH_3; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 239 Uncharacterized HTH-type transcriptional FT regulator HI_1476. FT /FTId=PRO_0000149771. FT DOMAIN 13 66 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 24 43 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 239 AA; 26668 MW; 6E63CECCC5A92FA6 CRC64; MQYQNQDNFP ERIEYLVDKL NGPSEFARKT GVTLSTITRW RKGEADPSRS NLVKIAEVTG VSIEWLATGK IKEEKTTEEK PAGSLVSRAF ERMQAMLEEG VSMIDSYSSI NVSAGFGSFN EGITQPDGQE PYSDELLTSL GVKADNCAVF WANGNSMLPT INNYDQMLVD LSRKEIQGDR IYLVQNGESV WVKRVKMEWD GISLISDNKE EYPPISITGE NAQNLQIIGQ VVHIGHSLI // ID Y020_HAEIN Reviewed; 479 AA. AC Q57048; O05004; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Uncharacterized transporter HI_0020; GN OrderedLocusNames=HI_0020; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) CC family. DIT1 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; L42023; AAC21698.1; -; Genomic_DNA. DR PIR; B64043; B64043. DR RefSeq; NP_438193.1; NC_000907.1. DR RefSeq; WP_005652640.1; NC_000907.1. DR STRING; 71421.HI0020; -. DR EnsemblBacteria; AAC21698; AAC21698; HI_0020. DR GeneID; 950917; -. DR KEGG; hin:HI0020; -. DR PATRIC; 20188491; VBIHaeInf48452_0020. DR eggNOG; ENOG4107QPK; Bacteria. DR eggNOG; COG0471; LUCA. DR KO; K03319; -. DR OMA; WHLFALF; -. DR OrthoDB; EOG6WT8FN; -. DR PhylomeDB; Q57048; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR InterPro; IPR030676; CitT-rel. DR InterPro; IPR001898; Na/sul_symport. DR Pfam; PF00939; Na_sulph_symp; 1. DR PIRSF; PIRSF002457; DASS; 1. DR TIGRFAMs; TIGR00785; dass; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 479 Uncharacterized transporter HI_0020. FT /FTId=PRO_0000172524. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 447 467 Helical. {ECO:0000255}. SQ SEQUENCE 479 AA; 51354 MW; 2C99285F1798E2C4 CRC64; MALSKNTKLV ILMAIPLITF LLPAPDGLSL IAWRLLGVYI ATIVGLVLKP YGEPVILLAA IAVSGVIIGN TEGAKELVKV GNMLDGYKSG TTWLIFTAFT LSSAFVITGL GKRIAYHMIG AMGSTTLRLG YVTMFLDLLL SPATPSNTAR SGGIIFPIIN SVVVALGSDP EKSPKKAGRY LMMNVYMVVK TTSYIFLTAM APNALALSLM APILGFETTW IKWFLAASVP GLLCLFLIPL ICYWVSPPEL KKVDNKAIAK KGLEELGPMS FREKALSVLF VIALFGWIFS NSLHINATIV AIIVMVLCIV LSIVTWDDIL KSKGAWNTLV WYGGIIGMSG LLEKSGFFKW LANTLSTILQ FEGHGMMALI VILTLSVSVR YLFASGGAYV AAMVPVFATV GHVTGAPTEL LALGLVFANS YGGSVTHYGG GPGPIAFGAG YNDIKSWWIT GAIIAFGSLI IHLTIGMAWW KLLMSLGWL // ID Y043_HAEIN Reviewed; 354 AA. AC P43931; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=UPF0283 membrane protein HI_0043 {ECO:0000255|HAMAP-Rule:MF_01085}; GN OrderedLocusNames=HI_0043; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01085}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01085}. CC -!- SIMILARITY: Belongs to the UPF0283 family. {ECO:0000255|HAMAP- CC Rule:MF_01085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21721.1; -; Genomic_DNA. DR PIR; C64000; C64000. DR RefSeq; NP_438216.1; NC_000907.1. DR RefSeq; WP_010868921.1; NC_000907.1. DR STRING; 71421.HI0043; -. DR EnsemblBacteria; AAC21721; AAC21721; HI_0043. DR GeneID; 950940; -. DR KEGG; hin:HI0043; -. DR PATRIC; 20188537; VBIHaeInf48452_0043. DR eggNOG; ENOG4106K28; Bacteria. DR eggNOG; COG3768; LUCA. DR KO; K08990; -. DR OMA; EAYSAQE; -. DR OrthoDB; EOG64FKC8; -. DR PhylomeDB; P43931; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_01085; UPF0283; 1. DR InterPro; IPR021147; DUF697. DR InterPro; IPR006507; UPF0283. DR Pfam; PF05128; DUF697; 1. DR TIGRFAMs; TIGR01620; hyp_HI0043; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 354 UPF0283 membrane protein HI_0043. FT /FTId=PRO_0000214176. FT TRANSMEM 57 77 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01085}. FT TRANSMEM 87 107 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01085}. FT TRANSMEM 211 231 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01085}. SQ SEQUENCE 354 AA; 40436 MW; 2155995D9B62FF92 CRC64; MEKQIFEHSV NVEEEHYQPK QEFHNMEAKL DEALDGELLD AQLEQALKPK SSFRKTLLKF TALLFGLATV AQSVQWIWDS YQKHQWIYLA FALVSLIIIL LGIKEIICEW RRLVRLKKRE QWQQQSQQIW LESAVKNGDV FSVHNAEKSK ILCLDIAKSL GLENDSPTVI QWQHQLNEAY SAQEIAHLFS RHVLSSFDAQ AKKLISKMAA ESAVIVAISP LAVVDMFFIA WRNLRLMNKI AEIYGIELGY FPRIRLLRMV LVNIAFAGAT EVAQDIGMDW LSQDVTAKLS TRIAQGIGVG LLTARLGVKA MELCRPLAFQ LNEKPKLSHI QQELLSSVKD IVLGKNKIYK KEQI // ID Y048_HAEIN Reviewed; 285 AA. AC P44481; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 98. DE RecName: Full=Uncharacterized oxidoreductase HI_0048; DE EC=1.-.-.-; GN OrderedLocusNames=HI_0048; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21726.1; -; Genomic_DNA. DR PIR; B64045; B64045. DR RefSeq; NP_438221.1; NC_000907.1. DR RefSeq; WP_005693873.1; NC_000907.1. DR ProteinModelPortal; P44481; -. DR STRING; 71421.HI0048; -. DR EnsemblBacteria; AAC21726; AAC21726; HI_0048. DR GeneID; 950942; -. DR KEGG; hin:HI0048; -. DR PATRIC; 20188549; VBIHaeInf48452_0048. DR eggNOG; ENOG4105DMW; Bacteria. DR eggNOG; COG1028; LUCA. DR OMA; YTKANIA; -. DR OrthoDB; EOG6N3CR8; -. DR PhylomeDB; P44481; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR24322; PTHR24322; 3. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 285 Uncharacterized oxidoreductase HI_0048. FT /FTId=PRO_0000054841. FT ACT_SITE 181 181 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10001}. FT BINDING 168 168 Substrate. {ECO:0000250}. SQ SEQUENCE 285 AA; 30906 MW; 54440C3CD90595FC CRC64; MEFTMNIAAN HNLENKLIII TGAGGVLCSF LAKQLAYTKA NIALLDLNFE AADKVAKEIN QSGGKAKAYK TNVLELENIK EVRNQIETDF GTCDILINGA GGNNPKATTD NEFHQFDLNE TTRTFFDLDK SGIEFVFNLN YLGSLLPTQV FAKDMLGKQG ANIINISSMN AFTPLTKIPA YSGAKAAISN FTQWLAVYFS KVGIRCNAIA PGFLVSNQNL ALLFDTEGKP TDRANKILTN TPMGRFGESE ELLGALLFLI DENYSAFVNG VVLPVDGGFS AYSGV // ID Y050_HAEIN Reviewed; 401 AA. AC P44483; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Putative TRAP transporter large permease protein HI_0050; GN OrderedLocusNames=HI_0050; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAP transporter large permease 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; L42023; AAC21728.1; -; Genomic_DNA. DR PIR; C64141; C64141. DR RefSeq; NP_438223.1; NC_000907.1. DR STRING; 71421.HI0050m; -. DR EnsemblBacteria; AAC21728; AAC21728; HI_0050. DR GeneID; 950948; -. DR KEGG; hin:HI0050m; -. DR PATRIC; 20188553; VBIHaeInf48452_0050. DR eggNOG; ENOG4105CG6; Bacteria. DR eggNOG; COG1593; LUCA. DR OMA; IMDALAF; -. DR OrthoDB; EOG63C0QK; -. DR Proteomes; UP000000579; 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; IPR010656; DctM. DR InterPro; IPR004681; TRAP_transpt_permease. DR Pfam; PF06808; DctM; 1. DR PIRSF; PIRSF006066; HI0050; 1. DR TIGRFAMs; TIGR00786; dctM; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 401 Putative TRAP transporter large permease FT protein HI_0050. FT /FTId=PRO_0000169600. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. FT TRANSMEM 253 273 Helical. {ECO:0000255}. FT TRANSMEM 290 310 Helical. {ECO:0000255}. FT TRANSMEM 330 350 Helical. {ECO:0000255}. FT TRANSMEM 353 373 Helical. {ECO:0000255}. FT TRANSMEM 375 395 Helical. {ECO:0000255}. SQ SEQUENCE 401 AA; 42991 MW; 862855BAEBBE95CB CRC64; MLLSASIMLY HLDMFDTQLI TENFVMGTNN FPLMAIPFFM LTGEIMKHGG ISERIINFAT SMVGHIKGGL GYVAIISGLI FAGLSGSAVA DTAALGAILI PMMISKKYDG ARSTGLICAA GIISVVIPPS IPMIIYGITA GASITKLFMG GTVPGLLMVV GLWVTWKILY RNNDTSLERK QTGKERWVAF KKAFWPLLLP IIIIVGLRGG IFTPTEAGVV AAIYAGIVSI AYKGLTFSKL KDVFIGTIKT TSMVMFVAAS AMISAFAITV AQIPTELVQT IKGLTDSPTI LMFIIMLFLL LVGCVMDLIP AVLIFVPVLL PVLRAYNIDI AYFGIMMVIN LSIGLITPPV GTVLYVGSGI SKLGIGALSK GIAPFLFVYA IIMMLIVFFP EIVIVPMNWL S // ID Y051_HAEIN Reviewed; 165 AA. AC P44484; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative TRAP transporter small permease protein HI_0051; GN OrderedLocusNames=HI_0051; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAP transporter small permease 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; L42023; AAC21729.1; -; Genomic_DNA. DR PIR; D64141; D64141. DR RefSeq; NP_438224.1; NC_000907.1. DR RefSeq; WP_010868925.1; NC_000907.1. DR STRING; 71421.HI0051; -. DR EnsemblBacteria; AAC21729; AAC21729; HI_0051. DR GeneID; 950946; -. DR KEGG; hin:HI0051; -. DR PATRIC; 20188555; VBIHaeInf48452_0051. DR eggNOG; ENOG4105XDZ; Bacteria. DR eggNOG; COG3090; LUCA. DR OMA; MPATEIS; -. DR OrthoDB; EOG6VXF99; -. DR PhylomeDB; P44484; -. DR Proteomes; UP000000579; 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; IPR007387; DctQ_transporter. DR Pfam; PF04290; DctQ; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 165 Putative TRAP transporter small permease FT protein HI_0051. FT /FTId=PRO_0000169597. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. SQ SEQUENCE 165 AA; 18580 MW; CEC9D4AFBB6A2647 CRC64; MGDKEGACFM KIAKYLDKAL EYLSILALVI MISLVFFNSV LRYFFDSGIA FSEEFSRICF VYMISFGIIL VAKDKAHLTV DIIIPALPEQ YRKIVLIVAN ICVLIAMIFI AYGALQLMSL TYTQQMPATG ISSSFLYLAA VISAVSYFFI VMFSMIKDYK ESSDK // ID Y081_HAEIN Reviewed; 262 AA. AC P44500; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Uncharacterized metal-dependent hydrolase HI_0081 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=HI_0081; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21756.1; -; Genomic_DNA. DR PIR; A64142; A64142. DR RefSeq; NP_438254.1; NC_000907.1. DR RefSeq; WP_005693839.1; NC_000907.1. DR ProteinModelPortal; P44500; -. DR STRING; 71421.HI0081; -. DR EnsemblBacteria; AAC21756; AAC21756; HI_0081. DR GeneID; 950980; -. DR KEGG; hin:HI0081; -. DR PATRIC; 20188617; VBIHaeInf48452_0082. DR eggNOG; ENOG4105EYA; Bacteria. DR eggNOG; COG0084; LUCA. DR KO; K03424; -. DR OMA; GAATWPQ; -. DR OrthoDB; EOG66QM1C; -. DR PhylomeDB; P44500; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004536; F:deoxyribonuclease activity; IBA:GO_Central. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central. DR InterPro; IPR018228; DNase_TatD-rel_CS. 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 PROSITE; PS01137; TATD_1; 1. DR PROSITE; PS01090; TATD_2; 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 HI_0081. FT /FTId=PRO_0000202000. 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 98 98 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 98 98 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 138 138 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 162 162 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 212 212 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 262 AA; 29789 MW; 382D860E063DF852 CRC64; MHFFDTHTHL NYLQQFTGEP LSQLIDNAKQ ADVQKILVVA VKEADFKTIQ NMTALFPDNL CYGLGLHPLY IQEHAENDLI LLEQALKNRD TNCTAVAEIG LERAIPDLLT DELWAKQCHF FESQLYLAKQ FNLPVNIHSR KTHDQIFTFL KRIPLSKLGV VHGFSGSYDQ AKRFVDLGYK IGVGGTITYE RANKTRQAIA KLPLDALVLE TDSPDMPVFG FQGQPNRPER IVESFKALCT LRNEPAELIK KLTWENACQI FS // ID Y093_HAEIN Reviewed; 368 AA. AC P44509; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0093; GN OrderedLocusNames=HI_0093; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the CdaR 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; L42023; AAC21771.1; -; Genomic_DNA. DR PIR; E64142; E64142. DR RefSeq; NP_438266.1; NC_000907.1. DR RefSeq; WP_005693827.1; NC_000907.1. DR STRING; 71421.HI0093; -. DR DNASU; 950994; -. DR EnsemblBacteria; AAC21771; AAC21771; HI_0093. DR GeneID; 950994; -. DR KEGG; hin:HI0093; -. DR PATRIC; 20188649; VBIHaeInf48452_0094. DR eggNOG; ENOG4107VHA; Bacteria. DR eggNOG; COG3835; LUCA. DR KO; K02647; -. DR OMA; WHRRYKE; -. DR OrthoDB; EOG6B3623; -. DR PhylomeDB; P44509; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR008599; Diacid_rec. DR InterPro; IPR025736; PucR_C-HTH_dom. DR Pfam; PF05651; Diacid_rec; 1. DR Pfam; PF13556; HTH_30; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 368 Uncharacterized protein HI_0093. FT /FTId=PRO_0000165946. SQ SEQUENCE 368 AA; 42251 MW; C77F1C9EF043B89A CRC64; MQLDKYTAKK IVKRAMKIIH HSVNVMDHDG VIIASGNSTR LNQRHTGAVL ALRENRVVEI DQALAQKWNF EAQPGINLPI HYLGKNIGVV GISGEPTQVK QYAELVKMTA ELIVEQQALL EQESWHRRYK EEFILQLLHC NLNWKEMEQQ AKFFSFDLNK SRVVVLIKLL NPALDNLQNL INYLEQSEFA QDVAILSLDQ VVVLKTWQNS TVLSAQMKTL LPADYSKQDY KIAVGACLNL PLFEQLPLSF QSAQSTLSYG LKHHPRKGIY VFDEHRLPVL LAGLSHSWQG NELIKPLSPL FSEENAILYK TLQQYFLSNC DLYLTAEKLF VHPNTLRYRL NKIEQITGLF FNKIDDKLTL YLGTLLEH // ID Y095_HAEIN Reviewed; 251 AA. AC Q57060; O05007; 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=Uncharacterized protein HI_0095; GN OrderedLocusNames=HI_0095; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21772.1; -; Genomic_DNA. DR PIR; B64048; B64048. DR RefSeq; NP_438269.1; NC_000907.1. DR RefSeq; WP_005693825.1; NC_000907.1. DR ProteinModelPortal; Q57060; -. DR DNASU; 950997; -. DR EnsemblBacteria; AAC21772; AAC21772; HI_0095. DR GeneID; 950997; -. DR KEGG; hin:HI0095; -. DR PATRIC; 20188655; VBIHaeInf48452_0097. DR eggNOG; ENOG4105DVA; Bacteria. DR eggNOG; ENOG410XQBS; LUCA. DR OMA; RAIKVNA; -. DR OrthoDB; EOG613079; -. DR PhylomeDB; Q57060; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 251 Uncharacterized protein HI_0095. FT /FTId=PRO_0000077886. SQ SEQUENCE 251 AA; 28051 MW; 75C3891A55D485B6 CRC64; MAKDEVGHNF LARLGKTRLR PGGKKATDWL IANGGFSQDK KVLEVACNMG TTAIGLAKQF GCHIEGVDLD ENALAKAQAN IEANGLQEKI HVQRANAMKL PFEDESFDIV INEAMLTMLP VEAKKKAIAE YFRVLKPNGL LLTHDVMLVG NDHQTILENM RKAINVTVTP LTKDGWKGIF QESGFRNVDT FSGEMTLLSP KGMIYDEGIF GTLKIIRNAM KAENREQFKR MFKTFNDPEH KLHFIAVCSQ K // ID Y1011_HAEIN Reviewed; 413 AA. AC P44093; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Uncharacterized protein HI_1011; GN OrderedLocusNames=HI_1011; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YgbK. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22672.1; -; Genomic_DNA. DR PIR; C64018; C64018. DR RefSeq; NP_439172.1; NC_000907.1. DR RefSeq; WP_005693348.1; NC_000907.1. DR PDB; 1YZY; X-ray; 2.10 A; A/B=1-413. DR PDBsum; 1YZY; -. DR ProteinModelPortal; P44093; -. DR SMR; P44093; 2-413. DR STRING; 71421.HI1011; -. DR DNASU; 950004; -. DR EnsemblBacteria; AAC22672; AAC22672; HI_1011. DR GeneID; 950004; -. DR KEGG; hin:HI1011; -. DR PATRIC; 20190685; VBIHaeInf48452_1055. DR eggNOG; ENOG4105G63; Bacteria. DR eggNOG; COG3395; LUCA. DR OMA; IDPGVPW; -. DR OrthoDB; EOG64XXHR; -. DR PhylomeDB; P44093; -. DR BioCyc; RETL1328306-WGS:GSTH-4805-MONOMER; -. DR EvolutionaryTrace; P44093; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010737; DUF1537. DR InterPro; IPR031475; DUF1537_C. DR Pfam; PF17042; DUF1357_C; 1. DR Pfam; PF07005; DUF1537; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 413 Uncharacterized protein HI_1011. FT /FTId=PRO_0000169314. FT STRAND 3 8 {ECO:0000244|PDB:1YZY}. FT HELIX 9 20 {ECO:0000244|PDB:1YZY}. FT TURN 21 23 {ECO:0000244|PDB:1YZY}. FT STRAND 26 31 {ECO:0000244|PDB:1YZY}. FT STRAND 42 47 {ECO:0000244|PDB:1YZY}. FT STRAND 51 53 {ECO:0000244|PDB:1YZY}. FT HELIX 55 71 {ECO:0000244|PDB:1YZY}. FT STRAND 76 80 {ECO:0000244|PDB:1YZY}. FT HELIX 93 104 {ECO:0000244|PDB:1YZY}. FT STRAND 109 111 {ECO:0000244|PDB:1YZY}. FT HELIX 116 118 {ECO:0000244|PDB:1YZY}. FT STRAND 120 123 {ECO:0000244|PDB:1YZY}. FT STRAND 126 129 {ECO:0000244|PDB:1YZY}. FT HELIX 134 136 {ECO:0000244|PDB:1YZY}. FT HELIX 138 141 {ECO:0000244|PDB:1YZY}. FT STRAND 143 145 {ECO:0000244|PDB:1YZY}. FT HELIX 152 159 {ECO:0000244|PDB:1YZY}. FT STRAND 164 167 {ECO:0000244|PDB:1YZY}. FT HELIX 169 172 {ECO:0000244|PDB:1YZY}. FT HELIX 176 188 {ECO:0000244|PDB:1YZY}. FT STRAND 192 196 {ECO:0000244|PDB:1YZY}. FT STRAND 198 200 {ECO:0000244|PDB:1YZY}. FT HELIX 202 210 {ECO:0000244|PDB:1YZY}. FT TURN 211 213 {ECO:0000244|PDB:1YZY}. FT STRAND 215 220 {ECO:0000244|PDB:1YZY}. FT HELIX 221 232 {ECO:0000244|PDB:1YZY}. FT HELIX 237 239 {ECO:0000244|PDB:1YZY}. FT STRAND 248 252 {ECO:0000244|PDB:1YZY}. FT HELIX 257 266 {ECO:0000244|PDB:1YZY}. FT TURN 267 269 {ECO:0000244|PDB:1YZY}. FT STRAND 272 274 {ECO:0000244|PDB:1YZY}. FT HELIX 277 282 {ECO:0000244|PDB:1YZY}. FT HELIX 286 295 {ECO:0000244|PDB:1YZY}. FT TURN 296 299 {ECO:0000244|PDB:1YZY}. FT STRAND 300 302 {ECO:0000244|PDB:1YZY}. FT STRAND 305 307 {ECO:0000244|PDB:1YZY}. FT HELIX 312 319 {ECO:0000244|PDB:1YZY}. FT HELIX 324 345 {ECO:0000244|PDB:1YZY}. FT STRAND 349 354 {ECO:0000244|PDB:1YZY}. FT HELIX 355 365 {ECO:0000244|PDB:1YZY}. FT STRAND 369 377 {ECO:0000244|PDB:1YZY}. FT STRAND 380 389 {ECO:0000244|PDB:1YZY}. FT STRAND 391 395 {ECO:0000244|PDB:1YZY}. FT HELIX 404 410 {ECO:0000244|PDB:1YZY}. SQ SEQUENCE 413 AA; 44787 MW; 0639C8DA33D6A6D5 CRC64; MLGVIADDFT GASDIASFLV ENGLSTVQMN GVPTQSLNSK VDAIVISLKS RSNPVNEAIE QSLRAYQWLK ENGCTQFYFK YCSTFDSTAK GNIGPVTDAL LDELNEDFTV ITPALPVNGR TIFNGYLFVG DVLLSESGMK NHPITPMVDA NLMRLMDAQA KGKTGLVAYA DVIKGASRVQ ECFAELKAQG YRYAVVDAVD NSQLEVLAEA VADFKLVTGG SGLGAYMAAR LSGGKKGTNA FTPTKGKTVV LSGSCSVMTN KQVEKYREKA PHFQLDVEQA IHNENYIEQL YQWVIANLDS EFAPMVYATV PPDALKAIQH QFGVDQASHA IENTFAKLAA KLKQYGVTNF ITAGGETSSI VVQELGFTGF HIGKQIAPGV PWLKAVEEDI FLALKSGNFG KEDFFEYAQG MFL // ID Y1079_HAEIN Reviewed; 210 AA. AC P45023; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 98. DE RecName: Full=Probable amino-acid ABC transporter permease protein HI_0179; GN OrderedLocusNames=HI_1079; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system for an amino acid. Probably responsible for the CC translocation of the substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. HisMQ 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; L42023; AAC22735.1; -; Genomic_DNA. DR RefSeq; NP_439236.1; NC_000907.1. DR ProteinModelPortal; P45023; -. DR STRING; 71421.HI1079m; -. DR EnsemblBacteria; AAC22735; AAC22735; HI_1079. DR GeneID; 949554; -. DR KEGG; hin:HI1079m; -. DR PATRIC; 20190823; VBIHaeInf48452_1124. DR eggNOG; ENOG4105E5Q; Bacteria. DR eggNOG; COG0765; LUCA. DR KO; K10009; -. DR OMA; GQWNAAY; -. DR OrthoDB; EOG6MM1R5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0033229; F:cysteine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:1903712; P:cysteine transmembrane transport; IBA:GOC. DR GO; GO:0015811; P:L-cystine transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 210 Probable amino-acid ABC transporter FT permease protein HI_0179. FT /FTId=PRO_0000060280. FT TRANSMEM 10 30 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 57 77 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 79 99 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 177 197 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 6 199 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 210 AA; 23393 MW; 662C7C590DC4FDCD CRC64; MLEAAILYTL PLAVISFFCG LLIAVIVAVI RTLPSPNLPL KLLQALCRVY ISIIRGTPML VQIFIIFYGL PEVGITLEPF PTAIIAFSIN IGAYAAETVR ASIIAIPKGQ WEASYAIGMN YRQAFIRTIM PQALRISVPS LSNTFISTVK DTSLASLVLV TELFRVAQNI TAANYEFILI YSEAALIYWI FCFVLSFLQD RLEIRLSRHL // ID Y1171_HAEIN Reviewed; 193 AA. AC P44339; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Putative anthranilate synthase component II; DE EC=4.1.3.27; DE AltName: Full=Glutamine amido-transferase; GN OrderedLocusNames=HI_1171; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Tetramer of two components I and two components II. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22824.1; -; Genomic_DNA. DR PIR; G64187; G64187. DR RefSeq; NP_439329.1; NC_000907.1. DR RefSeq; WP_005694270.1; NC_000907.1. DR ProteinModelPortal; P44339; -. DR STRING; 71421.HI1171; -. DR EnsemblBacteria; AAC22824; AAC22824; HI_1171. DR GeneID; 950129; -. DR KEGG; hin:HI1171; -. DR PATRIC; 20191021; VBIHaeInf48452_1223. DR eggNOG; ENOG4105DDQ; Bacteria. DR eggNOG; COG0512; LUCA. DR KO; K01664; -. DR OMA; FNIGLYH; -. DR OrthoDB; EOG6M9F11; -. DR PhylomeDB; P44339; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glutamine amidotransferase; Lyase; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 193 Putative anthranilate synthase component FT II. FT /FTId=PRO_0000056879. FT DOMAIN 2 193 Glutamine amidotransferase type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 78 78 {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 168 168 {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 170 170 {ECO:0000255|PROSITE-ProRule:PRU00605}. SQ SEQUENCE 193 AA; 22300 MW; 2C6468C440E56999 CRC64; MKLLIINNHD SFTFNLVDLI RKLNVPYDVL NVEDLKENTA ENYSHILISP GPDIPRAYPQ LFSMLEKYYQ QKSILGVCLG HQTLCEFFGG TLYNLENVRH GQKRTLKVRS NSPLFFDLPT EFNIGLYHSW GVQEEDFPDC LEITALCDED VVMAMQHKSL PIYSVQFHPE SYMSDFGEKI LRNWLAIPPT TNP // ID Y1198_HAEIN Reviewed; 207 AA. AC P45103; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized protein HI_1198; GN OrderedLocusNames=HI_1198; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}. 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; L42023; AAC22852.1; -; Genomic_DNA. DR PIR; I64168; I64168. DR RefSeq; NP_439354.1; NC_000907.1. DR RefSeq; WP_005667400.1; NC_000907.1. DR ProteinModelPortal; P45103; -. DR SMR; P45103; 1-207. DR STRING; 71421.HI1198; -. DR EnsemblBacteria; AAC22852; AAC22852; HI_1198. DR GeneID; 950741; -. DR KEGG; hin:HI1198; -. DR PATRIC; 20191075; VBIHaeInf48452_1250. DR eggNOG; ENOG4107RTD; Bacteria. DR eggNOG; COG0009; LUCA. DR OMA; HPKKKTV; -. DR OrthoDB; EOG6C5RT4; -. DR PhylomeDB; P45103; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00057; TIGR00057; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 207 Uncharacterized protein HI_1198. FT /FTId=PRO_0000202017. FT DOMAIN 14 201 YrdC-like. {ECO:0000255|PROSITE- FT ProRule:PRU00518}. SQ SEQUENCE 207 AA; 23092 MW; 644D9AA82ACDC514 CRC64; MSQFFYIHPE NPQARLINQA VEILQKGGVI VYPTDSGYAL GCMMGDKHAM DRIVAIRKLP EGHNFTLVCS DLSELSTYAR VNNTAYRLIK NNTPGRYTFI LTATKELPRR LMTSKRKTIG LRVPDNKIAL DLLSALGEPI LSCSLMLPNE EHTTQSDPEE IRDRLEHQVD LIIHGGYLGQ EPTTVVDLTE ESPVILREGS GSTAPFI // ID Y1225_HAEIN Reviewed; 106 AA. AC P45116; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_1225; GN OrderedLocusNames=HI_1225; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the SUI1 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; L42023; AAC22878.1; -; Genomic_DNA. DR PIR; C64111; C64111. DR RefSeq; NP_439381.1; NC_000907.1. DR RefSeq; WP_005663537.1; NC_000907.1. DR ProteinModelPortal; P45116; -. DR SMR; P45116; 26-106. DR STRING; 71421.HI1225; -. DR EnsemblBacteria; AAC22878; AAC22878; HI_1225. DR GeneID; 950401; -. DR KEGG; hin:HI1225; -. DR PATRIC; 20191129; VBIHaeInf48452_1277. DR eggNOG; ENOG4108ZJT; Bacteria. DR eggNOG; COG0023; LUCA. DR KO; K03113; -. DR OMA; EIQGDNR; -. DR OrthoDB; EOG6HMXKK; -. DR PhylomeDB; P45116; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR Gene3D; 3.30.780.10; -; 1. DR InterPro; IPR005872; SUI1_arc_bac. DR InterPro; IPR001950; TIF_SUI1. DR Pfam; PF01253; SUI1; 1. DR PIRSF; PIRSF037511; Transl_init_SUI1_pro; 1. DR SUPFAM; SSF55159; SSF55159; 1. DR TIGRFAMs; TIGR01158; SUI1_rel; 1. DR PROSITE; PS50296; SUI1; 1. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Reference proteome; KW Translation regulation. FT CHAIN 1 106 Uncharacterized protein HI_1225. FT /FTId=PRO_0000130598. SQ SEQUENCE 106 AA; 11326 MW; F03757E1CB68DB76 CRC64; MSDSVLVYST DVGRIKEEKA SVVRPKGDGV VRIQKQTSGR KGAGVSVITG LDLSDEELKK LAAELKKRCG CGGAVKNGII EIQGEKRDLL KQLLEQKGFK VKLSGG // ID Y1265_HAEIN Reviewed; 587 AA. AC P44144; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_1265; GN OrderedLocusNames=HI_1265; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 YcaO domain. {ECO:0000255|PROSITE- CC ProRule:PRU00999}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22918.2; -; Genomic_DNA. DR PIR; I64023; I64023. DR RefSeq; NP_439420.1; NC_000907.1. DR RefSeq; WP_010869168.1; NC_000907.1. DR STRING; 71421.HI1265; -. DR EnsemblBacteria; AAC22918; AAC22918; HI_1265. DR GeneID; 950187; -. DR KEGG; hin:HI1265; -. DR PATRIC; 20191211; VBIHaeInf48452_1317. DR eggNOG; ENOG4105DDY; Bacteria. DR eggNOG; COG1944; LUCA. DR KO; K09136; -. DR OMA; EFVEWDF; -. DR OrthoDB; EOG60KN12; -. DR PhylomeDB; P44144; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003776; YcaO-like_dom. DR Pfam; PF02624; YcaO; 1. DR TIGRFAMs; TIGR00702; TIGR00702; 1. DR PROSITE; PS51664; YCAO; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 587 Uncharacterized protein HI_1265. FT /FTId=PRO_0000144977. FT DOMAIN 61 426 YcaO. {ECO:0000255|PROSITE- FT ProRule:PRU00999}. SQ SEQUENCE 587 AA; 66529 MW; 0551446E74D8B57F CRC64; MTEQTFILGK DAALEDSIAK FQQKLTALGF NIEEASWLNP VPNVWSVHIR DKDCPQCFSN GKGASKKAAL ASALGEYFER LSTNYFFADF YLGQEIANSD FVHYPNEKWF PIEDDALLPN GILDDYLLDY FBPNAELTPE LLVDLQSGNY DRGIVAMPYV RQSDEQTVYI PQSIIANLYV SNGMSAGNTK FEARVQGLSE VFERYVKNKI IAEAISLPEI PKSVMDRYPS IQASIAKLEE EGFPIYAFDA SLGGKYPVIC VVLLNPNNGT CFSSFGAHPN FQVALERTVT ELLQGRSLKD LDVFSPPSFN NDDVAEHANL ETHFIDSSGL ISWDLLKETP DYEFADWDFS GTTQEEYNNL MAIFRADEKE VYVMDYNHLD VYACRIIVPG MSDIYPADDL IYANNNMGMD WREILLDLPN WHHDAETYQE LLEELDGQDI DDATRVREFI GIVAPKNSGW TTLRVGELKS MLHLALGELE QALDWANWTL NMNSSVFTTE PVNYYRTLIS IIELHLDQNR DPAQYRAVFE KMYGKDAVKQ AWAAVSEGGN PFYNLPASDE NLKNFKEHQA LLGAYGKLQK AKKENWK // ID Y1327_HAEIN Reviewed; 45 AA. AC P44163; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAY-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_1327; GN OrderedLocusNames=HI_1327; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22981.1; -; Genomic_DNA. DR PIR; A64026; A64026. DR RefSeq; NP_439478.1; NC_000907.1. DR RefSeq; WP_005694447.1; NC_000907.1. DR STRING; 71421.HI1327; -. DR EnsemblBacteria; AAC22981; AAC22981; HI_1327. DR GeneID; 950255; -. DR KEGG; hin:HI1327; -. DR PATRIC; 20191337; VBIHaeInf48452_1379. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 45 Uncharacterized protein HI_1327. FT /FTId=PRO_0000078026. FT TRANSMEM 5 25 Helical. {ECO:0000255}. SQ SEQUENCE 45 AA; 4276 MW; C2D668F0C6D26586 CRC64; MMKKIFFIFA LSGILAACTV GGGVSAGGGS NGVGLGVGIG SGIRF // ID Y1349_HAEIN Reviewed; 160 AA. AC P45173; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein HI_1349; GN OrderedLocusNames=HI_1349; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the Dps 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; L42023; AAC22996.1; -; Genomic_DNA. DR PIR; C64171; C64171. DR RefSeq; NP_439500.1; NC_000907.1. DR RefSeq; WP_005650692.1; NC_000907.1. DR ProteinModelPortal; P45173; -. DR STRING; 71421.HI1349; -. DR EnsemblBacteria; AAC22996; AAC22996; HI_1349. DR GeneID; 950182; -. DR KEGG; hin:HI1349; -. DR PATRIC; 20191383; VBIHaeInf48452_1402. DR eggNOG; ENOG4108RMU; Bacteria. DR eggNOG; COG0783; LUCA. DR KO; K04047; -. DR OMA; PLHAYSD; -. DR OrthoDB; EOG6Z9B6G; -. DR PhylomeDB; P45173; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IEA:InterPro. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR002177; DPS_DNA-bd. DR InterPro; IPR023188; DPS_DNA-bd_CS. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR008331; Ferritin_DPS_dom. DR Pfam; PF00210; Ferritin; 1. DR PIRSF; PIRSF005900; Dps; 1. DR PRINTS; PR01346; HELNAPAPROT. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS00818; DPS_1; 1. DR PROSITE; PS00819; DPS_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 160 Uncharacterized protein HI_1349. FT /FTId=PRO_0000201669. SQ SEQUENCE 160 AA; 18168 MW; 7C084FF468D9E7F1 CRC64; MSKTSIGLDK VQSAELADKL NELLATYQVF YTNVRGYHWN IKGVNFFALH AKFEEIYTNL VARVDEVAER ILTLGYTPNN AYSQYLKISR IKEDIAVSEA QECLSGTLQG LKTLLDQQRE ILAFANNAND EGTASQMSDY IKEQEKLVWM FQAACQTCHN // ID Y1390_HAEIN Reviewed; 21 AA. AC P45194; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_1390; GN OrderedLocusNames=HI_1390; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23037.1; -; Genomic_DNA. DR PIR; F64121; F64121. DR EnsemblBacteria; AAC23037; AAC23037; HI_1390. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019812; Hydgase_assmbl_chp_CS. DR PROSITE; PS01097; HUPF_HYPC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 21 Uncharacterized protein HI_1390. FT /FTId=PRO_0000078036. SQ SEQUENCE 21 AA; 2387 MW; 2A63C08B47C2ED3B CRC64; MCLGVPIKLS KLMKILFNLP Q // ID Y1405_HAEIN Reviewed; 366 AA. AC P44180; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_1405; GN OrderedLocusNames=HI_1405; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23055.1; -; Genomic_DNA. DR PIR; A64028; A64028. DR RefSeq; NP_439557.1; NC_000907.1. DR RefSeq; WP_005693957.1; NC_000907.1. DR STRING; 71421.HI1405; -. DR EnsemblBacteria; AAC23055; AAC23055; HI_1405. DR GeneID; 950333; -. DR KEGG; hin:HI1405; -. DR PATRIC; 20191509; VBIHaeInf48452_1465. DR eggNOG; ENOG41090AG; Bacteria. DR eggNOG; COG3566; LUCA. DR KO; K09960; -. DR OMA; DEDKTIM; -. DR OrthoDB; EOG63C0V1; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR016913; UCP029215. DR Pfam; PF09979; DUF2213; 1. DR PIRSF; PIRSF029215; UCP029215; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 366 Uncharacterized protein HI_1405. FT /FTId=PRO_0000078043. SQ SEQUENCE 366 AA; 40122 MW; 68040800B631AEC0 CRC64; MKFTDKTTQA DTQRTITKDG FLVVPATISK VGVFDYLATE LGLKEDGIKK VARTEKSLFS DETIKSFENA TLTVGHLKDG VNAKNWKQLS VGVVRNVKRV GDELTAEAWI YDEQAIKTVQ EHGVEQLSCG YDCDIKPSTV QDADFEMSPM IGNHVAIVAK GRCGGSVKLA DEDKTIMGKT AKILDAFLGA FGIKLSDEQK KQIEDEEKSG SEEGKEPKGE QPTKPKEKKS EPENKKEDDV EKEELEKSLK AKDEEIQQLK DAQAKRDAEV KQAAVLADAK TAFKEVNFAD NATVREIQES AVVAQGIFTK DEAAKLSDEE ISGAYQTAKV VVAKLADERK SLGNILLGDA EPKAAPKIDF NKTYNS // ID Y1410_HAEIN Reviewed; 394 AA. AC P44184; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1410; GN OrderedLocusNames=HI_1410; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23058.1; -; Genomic_DNA. DR PIR; E64028; E64028. DR RefSeq; NP_439561.1; NC_000907.1. DR RefSeq; WP_010869206.1; NC_000907.1. DR STRING; 71421.HI1410; -. DR EnsemblBacteria; AAC23058; AAC23058; HI_1410. DR GeneID; 950727; -. DR KEGG; hin:HI1410; -. DR PATRIC; 20191517; VBIHaeInf48452_1469. DR eggNOG; ENOG4108N0N; Bacteria. DR eggNOG; COG1783; LUCA. DR KO; K06909; -. DR OMA; RAVKYGD; -. DR OrthoDB; EOG62RS86; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006323; P:DNA packaging; IEA:InterPro. DR InterPro; IPR006437; Phage_terminase_lsu. DR Pfam; PF04466; Terminase_3; 1. DR TIGRFAMs; TIGR01547; phage_term_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 394 Uncharacterized protein HI_1410. FT /FTId=PRO_0000078047. SQ SEQUENCE 394 AA; 44782 MW; D4217986BAB6C772 CRC64; MFREIQKSIS DSVIQMLADQ IEMLSLQAFF DVQKTQIIGQ NGSRFTFAGL KTNITSIKSM TGIDVVWVEE GENVSKESWD ILIPTIREDG SQIIVSFNPK NILDDTYQRF VIHPPERCKS VLVNWQDNPY FPKELMEDME QMRERDYELY RHVYEGEPVA DSDLAIIKPV WIEYAVDAHL KLGFTAKGMK KVGFDVADEG ADSNANAFVH GSVVLDIEVW KNGDVIDSAN RTNQSAVKFK ADLIIFDSIG VGAGVKAHFK RLPKSLQVEG FNAGGAVAYP EREYIKGKKN QDMFSNIKAQ SWWALRDRFY KTYRAVKYGD VYPDDELISL SSKIKELEYL KAELSRPRVD YDNNGRVKVE SKKDMKKRGI PSPNMADALV MCYAPTKPKS LLDL // ID Y1427_HAEIN Reviewed; 278 AA. AC P44196; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_1427; DE Flags: Precursor; GN OrderedLocusNames=HI_1427; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23074.1; -; Genomic_DNA. DR PIR; H64029; H64029. DR RefSeq; NP_439576.1; NC_000907.1. DR RefSeq; WP_005693940.1; NC_000907.1. DR STRING; 71421.HI1427; -. DR EnsemblBacteria; AAC23074; AAC23074; HI_1427. DR GeneID; 950330; -. DR KEGG; hin:HI1427; -. DR PATRIC; 20191549; VBIHaeInf48452_1484. DR eggNOG; COG5266; LUCA. DR OMA; CEQTQMF; -. DR OrthoDB; EOG622PN0; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019613; DUF4198. DR Pfam; PF10670; DUF4198; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 278 Uncharacterized protein HI_1427. FT /FTId=PRO_0000013970. SQ SEQUENCE 278 AA; 30836 MW; D52962EF64839CA0 CRC64; MKKTLITSLL VLSGIAQAHE VWVQAPTKLA SGSVLKAELA YGDYPYVEKI PEARLKIFAP MEIIHQNGEK QTLIQKGENY QYQSEKALSD GSYWVTATYK PTFWSQNAEG WKMDNLKGLE NPTYCEQTQM FGKSLVTVGK KPLNAEMAMT RVGLPLEIVP LRDPSKAKSG EPFPVQIFYQ DQPLAGETVI ATADTIIVKD LEASTGHREP QGFSGKTDSQ GRVNIIPLID GIWKIKVIHK TPFADQQICQ QSASYSTLIL PVGKGLAKLP PKPEHHHH // ID Y1457_HAEIN Reviewed; 178 AA. AC Q57201; O05063; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_1457; DE Flags: Precursor; GN OrderedLocusNames=HI_1457; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the opacity porin 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; L42023; AAC23104.1; -; Genomic_DNA. DR PIR; F64124; F64124. DR RefSeq; NP_439608.1; NC_000907.1. DR RefSeq; WP_005693912.1; NC_000907.1. DR ProteinModelPortal; Q57201; -. DR STRING; 71421.HI1457; -. DR EnsemblBacteria; AAC23104; AAC23104; HI_1457. DR GeneID; 950146; -. DR KEGG; hin:HI1457; -. DR PATRIC; 20191617; VBIHaeInf48452_1518. DR eggNOG; COG3637; LUCA. DR OMA; FTQRISV; -. DR OrthoDB; EOG6T4RXN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0015288; F:porin activity; IEA:InterPro. DR Gene3D; 2.40.160.20; -; 1. DR InterPro; IPR006315; OM_autotransptr_brl. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 1. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 178 Uncharacterized protein HI_1457. FT /FTId=PRO_0000013971. SQ SEQUENCE 178 AA; 19470 MW; 15CAC5C44FF49AFF CRC64; MKKLLIVTML FTLALSAQAQ WYVQGDLGAS KIDITHVNSS NSPSFTQRIS VGYAFDKNFR LAVDYTNYGK VTANYADVVD VSLKGKSLGL TGFYDFDLAD FKPYVGVRVS TNGADVTANA RYYRIEAFAT ETRIGIGALA GVQYKLTDNV ALNTNIEYNR LASNVSDVGV KAGLRFSF // ID Y1498_HAEIN Reviewed; 139 AA. AC P44222; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1498; GN OrderedLocusNames=HI_1498; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC23148.1; -; Genomic_DNA. DR PIR; G64032; G64032. DR RefSeq; NP_439647.1; NC_000907.1. DR RefSeq; WP_005693517.1; NC_000907.1. DR STRING; 71421.HI1498; -. DR EnsemblBacteria; AAC23148; AAC23148; HI_1498. DR GeneID; 950364; -. DR KEGG; hin:HI1498; -. DR PATRIC; 20191715; VBIHaeInf48452_1567. DR OMA; KMDSKYA; -. DR OrthoDB; EOG6XQ3RK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR020269; Phage_Mu_Gp25. DR Pfam; PF10805; DUF2730; 1. DR ProDom; PD283729; Uncharacterised_HI1498_bac; 1. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 139 Uncharacterized protein HI_1498. FT /FTId=PRO_0000078078. FT TRANSMEM 43 59 Helical. {ECO:0000255}. SQ SEQUENCE 139 AA; 15625 MW; EAEDE7EADA58AA7F CRC64; MWLAHSHYTL ACESIRSPLC KLPARLGGRT MISEFWEFVR SNFGVISTLI AIFIGAFWLK LDSKYAKKHD LSQLADIARS HDNRLATLES KVENLPTAVD VERLKTLLTD VKGDTKATSR QVDAMSHQVG LLLEAKLKE // ID Y1562_HAEIN Reviewed; 52 AA. AC P44254; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_1562; GN OrderedLocusNames=HI_1562; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23220.1; -; Genomic_DNA. DR PIR; C64036; C64036. DR STRING; 71421.HI1562; -. DR EnsemblBacteria; AAC23220; AAC23220; HI_1562. DR PATRIC; 20191849; VBIHaeInf48452_1633. DR OrthoDB; EOG6HJ27Z; -. DR Proteomes; UP000000579; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 52 Uncharacterized protein HI_1562. FT /FTId=PRO_0000078086. SQ SEQUENCE 52 AA; 6035 MW; 459726C0AD4CC18E CRC64; MLSKDPKVLI KLGELEKDKS KAKKYFGDAC DLRSQEGCDK YRELNQKQDT NK // ID Y1577_HAEIN Reviewed; 72 AA. AC Q57070; P96345; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 07-JAN-2015, entry version 52. DE RecName: Full=Uncharacterized protein HI_1577; GN OrderedLocusNames=HI_1577; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23226.1; -; Genomic_DNA. DR PIR; G64130; G64130. DR EnsemblBacteria; AAC23226; AAC23226; HI_1577. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 72 Uncharacterized protein HI_1577. FT /FTId=PRO_0000078092. SQ SEQUENCE 72 AA; 8370 MW; D00DAB69A8E96660 CRC64; MRESRLSQYK QNKLIEIFLA SVTALATAKL VNINKLQLIT FIVYHCLSLK AAYIWKCLKV KFKRMKAILV VL // ID Y1578_HAEIN Reviewed; 323 AA. AC Q57287; O05077; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Uncharacterized glycosyltransferase HI_1578; DE EC=2.4.-.-; GN OrderedLocusNames=HI_1578; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC23227.1; -; Genomic_DNA. DR PIR; H64130; H64130. DR RefSeq; NP_439724.1; NC_000907.1. DR RefSeq; WP_005693601.1; NC_000907.1. DR ProteinModelPortal; Q57287; -. DR STRING; 71421.HI1578; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC23227; AAC23227; HI_1578. DR GeneID; 950438; -. DR KEGG; hin:HI1578; -. DR PATRIC; 20191887; VBIHaeInf48452_1651. DR eggNOG; ENOG4107S6X; Bacteria. DR eggNOG; ENOG410ZVME; LUCA. DR OMA; KSGMGEY; -. DR OrthoDB; EOG6M0T47; -. DR PhylomeDB; Q57287; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 323 Uncharacterized glycosyltransferase FT HI_1578. FT /FTId=PRO_0000059240. SQ SEQUENCE 323 AA; 37681 MW; 7CBC2681039AB5B4 CRC64; MENCPLVSVI VCAYNAEQYI DESISSIINQ TYENLEIIVI NDGSTDLTLS HLEEISKLDK RIKIISNKYN LGFINSLNIG LGCFSGKYFA RMDADDIAKP SWIEKIVTYL EKNDHITAMG SYLEIIVEKE CGIIGSQYKT GDIWKNPLLH NDICEAMLFY NPIHNNTMIM RANVYREHKL IFNKDYPYAE DYKFWSEVSR LGCLANYPEA LVKYRLHGNQ TSSVYNHEQN ETAKKIKREN ITYYLNKIGI DIKVINSVSL LEIYHVDKSN KVLKSILYEM YMSLDKYTIT SLLHFIKYHL ELFDLKQNLK IIKKFIRKIN VIF // ID Y1600_HAEIN Reviewed; 307 AA. AC P44268; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 17-FEB-2016, entry version 80. DE RecName: Full=UPF0276 protein HI_1600; GN OrderedLocusNames=HI_1600; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0276 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23259.1; 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; L42023; AAC23259.1; ALT_INIT; Genomic_DNA. DR PIR; H64037; H64037. DR RefSeq; NP_439742.1; NC_000907.1. DR RefSeq; WP_005693615.1; NC_000907.1. DR ProteinModelPortal; P44268; -. DR SMR; P44268; 4-305. DR STRING; 71421.HI1600; -. DR DNASU; 950455; -. DR EnsemblBacteria; AAC23259; AAC23259; HI_1600. DR GeneID; 950455; -. DR KEGG; hin:HI1600; -. DR PATRIC; 20191931; VBIHaeInf48452_1673. DR eggNOG; ENOG4105E18; Bacteria. DR eggNOG; COG3220; LUCA. DR KO; K09930; -. DR OMA; IYSEHLS; -. DR OrthoDB; EOG6X9MK9; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.20.20.150; -; 2. DR HAMAP; MF_00697; UPF0276; 1. DR InterPro; IPR007801; UPF0276. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF05114; DUF692; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 307 UPF0276 protein HI_1600. FT /FTId=PRO_0000192696. SQ SEQUENCE 307 AA; 34801 MW; 00BE993F86ACCB5A CRC64; MKLQGAGLGY RRNLAEDFLQ LPSNNAIQFI EVAPENWSKM GGMARYQFDQ AAERFPLAVH GLSLSLGGQA PLDRELLRNT KALINQYNSS FFSEHLSYCE CEGHLYDLLP MPFTEEAVKH VAQRIRDVQD FLGLQISLEN TSYYLHSPTS TMNEVEFLNA IAQEADCGIH LDVNNIYVNG VNHGLLDPYI FLDQVDVKRV NYIHIAGHDE EHSAAQVVEN SANESFNKVK GAYRHLPELL IDTHGEAVKG TVWDLLEYAY QRLPTIPPTL LERDFNFPPF AELYAEVEHI AQLQQKYAHT EVMSYAA // ID Y1601_HAEIN Reviewed; 95 AA. AC P44269; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_1601; DE Flags: Precursor; GN OrderedLocusNames=HI_1601; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23260.1; -; Genomic_DNA. DR PIR; I64037; I64037. DR RefSeq; NP_439743.1; NC_000907.1. DR RefSeq; WP_005691265.1; NC_000907.1. DR STRING; 71421.HI1601; -. DR EnsemblBacteria; AAC23260; AAC23260; HI_1601. DR GeneID; 950456; -. DR KEGG; hin:HI1601; -. DR PATRIC; 20191933; VBIHaeInf48452_1674. DR eggNOG; ENOG41078SB; Bacteria. DR eggNOG; COG3767; LUCA. DR OMA; KSAQGSC; -. DR OrthoDB; EOG69KV19; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 Or 21. {ECO:0000255}. FT CHAIN 25 95 Uncharacterized protein HI_1601. FT /FTId=PRO_0000013974. SQ SEQUENCE 95 AA; 9235 MW; 68DE056A29ECC598 CRC64; MKKLATLTAL AGALTMAVAT AAQAESKSSS TDNTATPCVG DKCVKTKAAE GKCGEGKCGA DKAKSAEGKC GEGKCGADKA KSAEGKCGEG KCGSK // ID Y1666_HAEIN Reviewed; 127 AA. AC P44284; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized protein HI_1666; GN OrderedLocusNames=HI_1666; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YcbK. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23311.1; -; Genomic_DNA. DR PIR; F64039; F64039. DR STRING; 71421.HI1666; -. DR DNASU; 950486; -. DR EnsemblBacteria; AAC23311; AAC23311; HI_1666. DR PATRIC; 20192081; VBIHaeInf48452_1744. DR eggNOG; COG3108; LUCA. DR OMA; MADINLS; -. DR OrthoDB; EOG6D5G60; -. DR PhylomeDB; P44284; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.30.1380.10; -; 1. DR InterPro; IPR010275; DUF882. DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom. DR Pfam; PF05951; Peptidase_M15_2; 1. DR SUPFAM; SSF55166; SSF55166; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 127 Uncharacterized protein HI_1666. FT /FTId=PRO_0000168777. FT TRANSMEM 11 32 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 14494 MW; 872425EC84002E63 CRC64; MNYVDQNKRK WLSLGGIALG ISILPNSVLA MVSTPKPRIL TFRNINTGER LSGEFSLAKG FSPAMLKKLD YLMRDKRTNQ VHKMDPNLFQ KFYNIQTNLG LRNAEIEVIC GYRSASTNAM RRRQSRA // ID Y1690_HAEIN Reviewed; 457 AA. AC P45320; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized sodium-dependent transporter HI_1690; GN OrderedLocusNames=HI_1690; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Putative sodium-dependent transporter. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) 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; L42023; AAC23336.1; -; Genomic_DNA. DR PIR; H64136; H64136. DR RefSeq; NP_439832.1; NC_000907.1. DR RefSeq; WP_005694179.1; NC_000907.1. DR ProteinModelPortal; P45320; -. DR STRING; 71421.HI1690; -. DR EnsemblBacteria; AAC23336; AAC23336; HI_1690. DR GeneID; 950500; -. DR KEGG; hin:HI1690; -. DR PATRIC; 20192131; VBIHaeInf48452_1769. DR eggNOG; ENOG4105C8J; Bacteria. DR eggNOG; COG0733; LUCA. DR KO; K03308; -. DR OMA; TLTIWHT; -. DR OrthoDB; EOG6PGK51; -. DR PhylomeDB; P45320; -. DR Proteomes; UP000000579; 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:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro. DR InterPro; IPR000175; Na/ntran_symport. DR PANTHER; PTHR11616; PTHR11616; 1. DR Pfam; PF00209; SNF; 2. DR PRINTS; PR00176; NANEUSMPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 457 Uncharacterized sodium-dependent FT transporter HI_1690. FT /FTId=PRO_0000214819. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 294 314 Helical. {ECO:0000255}. FT TRANSMEM 316 336 Helical. {ECO:0000255}. FT TRANSMEM 355 375 Helical. {ECO:0000255}. FT TRANSMEM 396 416 Helical. {ECO:0000255}. FT TRANSMEM 433 453 Helical. {ECO:0000255}. SQ SEQUENCE 457 AA; 50756 MW; 00C1897F3A3E112A CRC64; MTTNNKQRQT WSSRLTYVMT VAGATVGFGA TWRFPYLVGE NGGGAYVLLF CIAMIVIGIP MILVENVIGR RLRVNSIDAF GDKILDKGKG ISKYWKILGY MGLLGAFGIM AYYMVLGGWV ISYIISLISG TLDISTPITK DIAKNFYDLH IGNSPYEIIF YTLLFVIVNY IILAKGIIGG IERSVKYLMP LLFIFLIGMV IRNVTLPGAM EGITFYLKPD FSKITPQLFI FVLGQVFFAL SLGFGVLITL SSYLNKEENL IHTAVITGFT NTIIAVLAGF MIFPSLFTFG IEPNAGPTLV FQSLPIVFSH LWAGKFFAII FFGLLLIAAL TTSITIYEVI ITALQEKLRM CRGKAIVLTL SGIFLLGNIP AILGDNLWKN VTIFGKSIFD FYDYASGNIL FMLTALGCAI FVGFVLKDEA KKELSSTKYS TFIKIWFNYV KFVVPLIILV IFISNLF // ID Y1706_HAEIN Reviewed; 669 AA. AC P45335; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Uncharacterized transporter HI_1706; GN OrderedLocusNames=HI_1706; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) 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; L42023; AAC23352.1; -; Genomic_DNA. DR PIR; D64137; D64137. DR RefSeq; NP_439848.2; NC_000907.1. DR ProteinModelPortal; P45335; -. DR STRING; 71421.HI1706; -. DR EnsemblBacteria; AAC23352; AAC23352; HI_1706. DR GeneID; 950523; -. DR KEGG; hin:HI1706; -. DR PATRIC; 20192163; VBIHaeInf48452_1785. DR eggNOG; ENOG4105C94; Bacteria. DR eggNOG; COG1292; LUCA. DR KO; K02168; -. DR OMA; DDWLKIN; -. DR OrthoDB; EOG6D8B89; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015077; F:monovalent inorganic cation transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015672; P:monovalent inorganic cation transport; IBA:GOC. DR GO; GO:0071705; P:nitrogen compound transport; IBA:GO_Central. DR InterPro; IPR018093; BCCT_CS. DR InterPro; IPR000060; BCCT_transptr. DR Pfam; PF02028; BCCT; 1. DR TIGRFAMs; TIGR00842; bcct; 1. DR PROSITE; PS01303; BCCT; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 669 Uncharacterized transporter HI_1706. FT /FTId=PRO_0000201496. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 345 365 Helical. {ECO:0000255}. FT TRANSMEM 397 417 Helical. {ECO:0000255}. FT TRANSMEM 444 464 Helical. {ECO:0000255}. FT TRANSMEM 470 490 Helical. {ECO:0000255}. SQ SEQUENCE 669 AA; 75021 MW; 0AEEE803BB5C733F CRC64; MTKRTSFNPL VIGVTLFFIL LLMAMIFIAP EQTQALLNQA KSGIFANFSW FYVLTFSVFL GFLLILSVSS LGNIKLGQDE EEPEFSFLSW LAMLFAAGMG VGLMFFGVAE PLTHYLSDIT AGSAEHKQQE ALLHTLFHWG IHAWAVYGTI ALALAYFGFR YKLPLALRSC FYPLLKDRIN GKIGDAIDVM ALLATLFGII TTLGFGSSQL GAGLEQIGWI SQNSFALQVG VIVVVMCLAV FSAISGVGKG VKILSEINLT LAFCLLLFVL ISGPTLYLLS AFSDNIGNYF SNLVQLSFKT YAYEQEHTSW FSGWTVLYWA WWCSWAPFVG LFIARISKGR TIREFIFGVL VIPSLFGILW FTVFGNTAVW LNDGIAAGGL GEFISSPEIL LFKFLNYLPL PTITGFVSLL VILLFFITSA DSGIYVLNNI ASRDKSLASP AWQAIMWGTL MSVVAIVLMQ SGGLANLQTM TLIVALPFAL LMLVMCFSLW KGLIADKKYF STKVNPTSIF WSGDKWKSHL EQMMNQTQEK DILRFLKNTA LPAMRELRQE LTGKYNLSVE INTLFEQEEP ALELVIHKES MRDFMYGIKS VGREVSEQLI NDENLPHIQH SATYEPYTYF FDGRVGYDVQ YMDQDELIAD MLKQYERYLS LLDDVGQELM AHEQTELAE // ID Y1724_HAEIN Reviewed; 117 AA. AC P44297; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 79. DE RecName: Full=UPF0231 protein HI_1724; GN OrderedLocusNames=HI_1724; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0231 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23370.1; 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; L42023; AAC23370.1; ALT_INIT; Genomic_DNA. DR PIR; A64041; A64041. DR RefSeq; NP_439865.2; NC_000907.1. DR RefSeq; WP_010869281.1; NC_000907.1. DR STRING; 71421.HI1724; -. DR EnsemblBacteria; AAC23370; AAC23370; HI_1724. DR GeneID; 950875; -. DR KEGG; hin:HI1724; -. DR PATRIC; 20192201; VBIHaeInf48452_1803. DR eggNOG; ENOG4108ZIG; Bacteria. DR eggNOG; COG3112; LUCA. DR KO; K09910; -. DR OMA; HEYTLLM; -. DR OrthoDB; EOG6ZD6BC; -. DR PhylomeDB; P44297; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_01053; UPF0231; 1. DR InterPro; IPR008249; UPF0231. DR Pfam; PF06062; UPF0231; 1. DR PIRSF; PIRSF006287; UCP006287; 1. DR ProDom; PD020773; UCP006287; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 117 UPF0231 protein HI_1724. FT /FTId=PRO_0000214650. SQ SEQUENCE 117 AA; 13487 MW; 0ECAE500D5F62CC7 CRC64; MDFQFTHYQG NVSVKCSMEH IALANWFNTE VRSNSDKILT ALSTAKSLIE NQEKVLIGTE YTLFLNADEV MVRANNLAIE SDEILEQDFH YYDEESLAFC GTQDFIHFLQ SYVDFIA // ID Y1731_HAEIN Reviewed; 213 AA. AC P44299; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Uncharacterized protein HI_1731; GN OrderedLocusNames=HI_1731; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YbgJ. {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YcsJ and yeast urea amidolyase (DUR1,2). 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; L42023; AAC23377.1; -; Genomic_DNA. DR PIR; C64041; C64041. DR RefSeq; NP_439872.1; NC_000907.1. DR RefSeq; WP_005694217.1; NC_000907.1. DR ProteinModelPortal; P44299; -. DR STRING; 71421.HI1731; -. DR EnsemblBacteria; AAC23377; AAC23377; HI_1731. DR GeneID; 950880; -. DR KEGG; hin:HI1731; -. DR PATRIC; 20192215; VBIHaeInf48452_1810. DR eggNOG; ENOG4105P4J; Bacteria. DR eggNOG; COG2049; LUCA. DR OMA; QPGFAYM; -. DR OrthoDB; EOG6VTK1C; -. DR PhylomeDB; P44299; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.40.100.10; -; 1. DR Gene3D; 3.30.1360.40; -; 1. DR InterPro; IPR024946; Arg_repress_C-like. DR InterPro; IPR003833; CT_C_D. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR010016; KipI_fam. DR Pfam; PF02682; AHS1; 1. DR SMART; SM00796; AHS1; 1. DR SUPFAM; SSF50891; SSF50891; 1. DR TIGRFAMs; TIGR00370; TIGR00370; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 213 Uncharacterized protein HI_1731. FT /FTId=PRO_0000168708. SQ SEQUENCE 213 AA; 23641 MW; 1A2360FC83F2D77E CRC64; MNIVPISESA VVCSLPPPAS IQQQRQLWAF ARQLQSEQDI VEVVLGMNNL TVFTDFFVDF KPLVQRLEQL WAELKVSDFQ GRHIEIPVIY GGERGQDLSD VAKFHQTTPE RIIQMHSEPI YTVYMIGFQA GFPYLGGLPE NLHTPRRATP RTVVPAGSVG IGGAQTGIYP FSSPGGWQLI GYTKQALFDK NQAQPTLLQA GDTVKFIVEG IEL // ID Y1736_HAEIN Reviewed; 77 AA. AC P44300; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein HI_1736; GN OrderedLocusNames=HI_1736; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23384.1; -; Genomic_DNA. DR PIR; D64041; D64041. DR RefSeq; NP_439878.1; NC_000907.1. DR RefSeq; WP_005632089.1; NC_000907.1. DR STRING; 71421.HI1736; -. DR EnsemblBacteria; AAC23384; AAC23384; HI_1736. DR GeneID; 950544; -. DR KEGG; hin:HI1736; -. DR PATRIC; 20192229; VBIHaeInf48452_1817. DR eggNOG; ENOG4106CC8; Bacteria. DR eggNOG; ENOG410XWA9; LUCA. DR OMA; ISLMMKD; -. DR OrthoDB; EOG6PGKBK; -. DR PhylomeDB; P44300; -. DR Proteomes; UP000000579; 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; IPR020137; Uncharacterised_HI1736. DR InterPro; IPR019629; Uncharacterised_HI1736/YgjV. DR Pfam; PF10688; Imp-YgjV; 1. DR ProDom; PD058023; Uncharacterised_HI1736; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 77 Uncharacterized protein HI_1736. FT /FTId=PRO_0000078111. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 35 55 Helical. {ECO:0000255}. SQ SEQUENCE 77 AA; 8881 MW; 566BC460DA0E93F3 CRC64; MDFNFIEFLG YMATFFVAAS FLFKSIVHLR IVNSIGAILF VIYSLIITAY PVALLNAFLV VVNIYQLWRL KQENLSK // ID Y175_HAEIN Reviewed; 244 AA. AC P44552; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Laccase domain protein HI_0175; GN OrderedLocusNames=HI_0175; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the LACC1 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; L42023; AAC21844.1; -; Genomic_DNA. DR PIR; E64144; E64144. DR RefSeq; NP_438343.1; NC_000907.1. DR RefSeq; WP_005694112.1; NC_000907.1. DR ProteinModelPortal; P44552; -. DR SMR; P44552; 4-243. DR STRING; 71421.HI0175; -. DR EnsemblBacteria; AAC21844; AAC21844; HI_0175. DR GeneID; 951085; -. DR KEGG; hin:HI0175; -. DR PATRIC; 20188845; VBIHaeInf48452_0179. DR eggNOG; ENOG4105DBW; Bacteria. DR eggNOG; COG1496; LUCA. DR KO; K05810; -. DR OMA; VVMTADC; -. DR OrthoDB; EOG60GRZN; -. DR PhylomeDB; P44552; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.60.140.10; -; 1. DR InterPro; IPR003730; Cu_polyphenol_OxRdtase_Laccase. DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat. DR Pfam; PF02578; Cu-oxidase_4; 1. DR SUPFAM; SSF64438; SSF64438; 1. DR TIGRFAMs; TIGR00726; TIGR00726; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 244 Laccase domain protein HI_0175. FT /FTId=PRO_0000163164. SQ SEQUENCE 244 AA; 27138 MW; B840AA696571F8E2 CRC64; MQAINPNWNV PKNIHAFTTT REGGVSLAPY LSFNLGDHVG DNKSAVKTNR TLLVEKFGLP QTPIFLTQTH STRVIQLPYS GQNLEADAVY TNVPNQVCVV MTADCLPVLF TTTSGNEVAA THAGWRGLCD GVLEETVKYF QAKPEDIIAW FGPAIGPKAF QVGIDVVEKF VVVDEKAKLA FQPDAIEEGK YLSNLYQIAT QRLNNLGITQ IYGGNHCTFN EKEKFFSYRR DNQTGRMASV IWFE // ID WECA_HAEIN Reviewed; 355 AA. AC P45341; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030}; DE EC=2.7.8.33 {ECO:0000255|HAMAP-Rule:MF_02030}; DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030}; DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030}; GN Name=wecA {ECO:0000255|HAMAP-Rule:MF_02030}; Synonyms=rfe; GN OrderedLocusNames=HI_1716; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety CC from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate CC (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP- CC C55). {ECO:0000255|HAMAP-Rule:MF_02030}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + CC ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D- CC glucosaminyl-diphospho-ditrans,octacis-undecaprenol. CC {ECO:0000255|HAMAP-Rule:MF_02030}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_02030}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_02030}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02030}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23361.1; -; Genomic_DNA. DR PIR; A64138; A64138. DR RefSeq; NP_439858.1; NC_000907.1. DR RefSeq; WP_005694200.1; NC_000907.1. DR STRING; 71421.HI1716; -. DR EnsemblBacteria; AAC23361; AAC23361; HI_1716. DR GeneID; 950539; -. DR KEGG; hin:HI1716; -. DR PATRIC; 20192185; VBIHaeInf48452_1795. DR eggNOG; ENOG4105ESV; Bacteria. DR eggNOG; COG0472; LUCA. DR KO; K02851; -. DR OMA; LPHNFQP; -. DR OrthoDB; EOG60GRWX; -. DR PhylomeDB; P45341; -. DR UniPathway; UPA00281; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; ISS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; ISS:UniProtKB. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; ISS:UniProtKB. DR GO; GO:0071555; P:cell wall organization; ISS:UniProtKB. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_02030; WecA_Gammaproteo; 1. DR InterPro; IPR012750; ECA_WecA-rel. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR TIGRFAMs; TIGR02380; ECA_wecA; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Magnesium; KW Manganese; Membrane; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 355 Undecaprenyl-phosphate alpha-N- FT acetylglucosaminyl 1-phosphate FT transferase. FT /FTId=PRO_0000108948. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 63 83 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 123 143 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 182 202 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 208 228 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 237 257 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. FT TRANSMEM 315 335 Helical. {ECO:0000255|HAMAP- FT Rule:MF_02030}. SQ SEQUENCE 355 AA; 40070 MW; 32A331505420AA08 CRC64; MLSIFVTFLG AFLTLIVMRP LANWIGLVDK PNYRKRHQGT IPLIGGASLF VGNLCYYLME WDQLRLPYLY LFSIFVLLAI GILDDRFDIS PFLRAGIQAI LAILMIDLGN IYLDHLGQIL GPFQLTLGSI GLIITVFATI AIINAFNMID GIDGLLGGLS CVSFAAIGIL MYRDGQMDMA HWSFALIVSI LPYLMLNLGI PFGPKYKVFM GDAGSTLIGF TIIWILLLST QGKGHPMNPV TALWIIAIPL IDMVAIIYRR VRKGKSPFRP DRLHVHHLMV RAGLTSRQAF LLITFVSAVC ATIGILGEVY YVNEWAMFVG FFILFFLYVY SITHAWRITR WVRRMKRRAK RLKKA // ID XERC_HAEIN Reviewed; 295 AA. AC P44818; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 107. DE RecName: Full=Tyrosine recombinase XerC; GN Name=xerC; OrderedLocusNames=HI_0676; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP CHARACTERIZATION, FUNCTION, AND MUTAGENESIS OF TYR-272. RX PubMed=10048034; DOI=10.1046/j.1365-2958.1999.01231.x; RA Neilson L., Blakely G., Sherratt D.J.; RT "Site-specific recombination at dif by Haemophilus influenzae XerC."; RL Mol. Microbiol. 31:915-926(1999). CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by CC catalyzing the cutting and rejoining of the recombining DNA CC molecules. The XerC-XerD complex is essential to convert dimers of CC the bacterial chromosome into monomers to permit their segregation CC at cell division. It also contributes to the segregational CC stability of plasmids. {ECO:0000269|PubMed:10048034}. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC 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; L42023; AAC22336.1; -; Genomic_DNA. DR PIR; F64085; F64085. DR RefSeq; NP_438836.1; NC_000907.1. DR RefSeq; WP_005692390.1; NC_000907.1. DR ProteinModelPortal; P44818; -. DR STRING; 71421.HI0676; -. DR EnsemblBacteria; AAC22336; AAC22336; HI_0676. DR GeneID; 950745; -. DR KEGG; hin:HI0676; -. DR PATRIC; 20189969; VBIHaeInf48452_0706. DR eggNOG; ENOG4108IYS; Bacteria. DR eggNOG; COG4973; LUCA. DR KO; K03733; -. DR OMA; ERQVSPH; -. DR OrthoDB; EOG6PZXFP; -. DR PhylomeDB; P44818; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009037; F:tyrosine-based site-specific recombinase 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:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR HAMAP; MF_01808; Recomb_XerC_XerD; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR010998; Integrase_Lambda-type_N. DR InterPro; IPR023109; Integrase_recombinase_N. DR InterPro; IPR004107; Integrase_SAM-like_N. DR InterPro; IPR011931; Recomb_XerC. DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD. DR Pfam; PF02899; Phage_int_SAM_1; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF47823; SSF47823; 1. DR SUPFAM; SSF56349; SSF56349; 1. DR TIGRFAMs; TIGR02224; recomb_XerC; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; DNA integration; DNA recombination; DNA-binding; KW Reference proteome. FT CHAIN 1 295 Tyrosine recombinase XerC. FT /FTId=PRO_0000095298. FT ACT_SITE 145 145 {ECO:0000250}. FT ACT_SITE 169 169 {ECO:0000250}. FT ACT_SITE 237 237 {ECO:0000250}. FT ACT_SITE 240 240 {ECO:0000250}. FT ACT_SITE 263 263 {ECO:0000250}. FT ACT_SITE 272 272 O-(3'-phospho-DNA)-tyrosine intermediate. FT MUTAGEN 272 272 Y->F: Abolishes DNA cleavage activity. FT {ECO:0000269|PubMed:10048034}. SQ SEQUENCE 295 AA; 33935 MW; CF59B475F0DA25AE CRC64; MLTALNRYWD YLRIERQMSP HTITNYQHQL DATIKILAQQ DIHSWTQVTP SVVRFILAES KKQGLKEKSL ALRLSALRRF LSFLVQQGEL KVNPATGISA PKQGRHLPKN MDGEQVQQLL ANDSKEPIDI RDRAILELMY SSGLRLSELQ GLDLNSINTR VREVRVIGKG NKERVVPFGR YASHAIQEWL KVRALFNPKD EALFVSQLGN RISHRAIQKR LETWGIRQGL NSHLNPHKLR HSFATHMLEA SSDLRAVQEL LGHSNLSTTQ IYTHLNFQHL AEVYDQAHPR AKRKK // ID XERD_HAEIN Reviewed; 297 AA. AC P44630; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 111. DE RecName: Full=Tyrosine recombinase XerD {ECO:0000255|HAMAP-Rule:MF_01807}; GN Name=xerD {ECO:0000255|HAMAP-Rule:MF_01807}; Synonyms=xprB; GN OrderedLocusNames=HI_0309; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by CC catalyzing the cutting and rejoining of the recombining DNA CC molecules. The XerC-XerD complex is essential to convert dimers of CC the bacterial chromosome into monomers to permit their segregation CC at cell division. It also contributes to the segregational CC stability of plasmids. {ECO:0000255|HAMAP-Rule:MF_01807}. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP- CC Rule:MF_01807}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01807}. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01807}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21974.1; -; Genomic_DNA. DR PIR; A64061; A64061. DR RefSeq; NP_438476.1; NC_000907.1. DR RefSeq; WP_005694355.1; NC_000907.1. DR ProteinModelPortal; P44630; -. DR SMR; P44630; 2-291. DR STRING; 71421.HI0309; -. DR EnsemblBacteria; AAC21974; AAC21974; HI_0309. DR GeneID; 949437; -. DR KEGG; hin:HI0309; -. DR PATRIC; 20189159; VBIHaeInf48452_0326. DR eggNOG; ENOG4105C13; Bacteria. DR eggNOG; COG4974; LUCA. DR KO; K04763; -. DR OMA; QMMLGHE; -. DR OrthoDB; EOG6PZXFP; -. DR PhylomeDB; P44630; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009037; F:tyrosine-based site-specific recombinase 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:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR HAMAP; MF_01807; Recomb_XerD; 1. DR HAMAP; MF_01808; Recomb_XerC_XerD; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR InterPro; IPR004107; Integrase_SAM-like_N. DR InterPro; IPR011932; Recomb_XerD. DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD. DR Pfam; PF02899; Phage_int_SAM_1; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. DR TIGRFAMs; TIGR02225; recomb_XerD; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Chromosome partition; Complete proteome; KW Cytoplasm; DNA integration; DNA recombination; DNA-binding; KW Reference proteome. FT CHAIN 1 297 Tyrosine recombinase XerD. FT /FTId=PRO_0000095390. FT ACT_SITE 147 147 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 171 171 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 243 243 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 246 246 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 269 269 {ECO:0000255|HAMAP-Rule:MF_01807}. FT ACT_SITE 278 278 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01807}. SQ SEQUENCE 297 AA; 34120 MW; A57706FA343CA82A CRC64; MKNLALIDLF LNEYWIEKGL SENTVQSYRL DLTALCDWLD KNDLSLETLD AVDLQGFLGE RLEKGYKATS TARMLSAMRK LFQYLYREKY RVDDPSAVLS SPKLPSRLPK YLTEQQVSDL LNTPNVEVPL ELRDKAMLEL LYATGLRVTE LVSLTIENMS VQQGVVRVIG KGNKERIVPM GEEAAYWVRQ FMLYGRPVLL NGQSSDVVFP SQRAQQMTRQ TFWHRVKHYA ILADIDADAL SPHVLRHAFA THLVNHGADL RVVQMLLGHT DLSTTQIYTH VAKERLKRLH ERFHPRG // ID XYLF_HAEIN Reviewed; 332 AA. AC P45047; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=D-xylose-binding periplasmic protein; DE Flags: Precursor; GN Name=xylF; OrderedLocusNames=HI_1111; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the high-affinity D-xylose membrane CC transport system. Binds with high affinity to xylose (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 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; L42023; AAC22765.1; -; Genomic_DNA. DR PIR; C64183; C64183. DR RefSeq; NP_439268.1; NC_000907.1. DR RefSeq; WP_005693436.1; NC_000907.1. DR ProteinModelPortal; P45047; -. DR STRING; 71421.HI1111; -. DR EnsemblBacteria; AAC22765; AAC22765; HI_1111. DR GeneID; 950082; -. DR KEGG; hin:HI1111; -. DR PATRIC; 20190895; VBIHaeInf48452_1160. DR eggNOG; ENOG4105DFW; Bacteria. DR eggNOG; COG4213; LUCA. DR KO; K10543; -. DR OMA; QQWVPEW; -. DR OrthoDB; EOG6SJJGT; -. DR PhylomeDB; P45047; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0048029; F:monosaccharide binding; IEA:InterPro. DR GO; GO:0015753; P:D-xylose transport; IEA:InterPro. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR InterPro; IPR013456; XylF. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR TIGRFAMs; TIGR02634; xylF; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Signal; KW Sugar transport; Transport. FT SIGNAL 1 23 {ECO:0000250}. FT CHAIN 24 332 D-xylose-binding periplasmic protein. FT /FTId=PRO_0000031739. SQ SEQUENCE 332 AA; 35901 MW; D5241F25CC0C3D34 CRC64; MKIKSALLTL VGALTVFSSS AHSKDLKIGL SIDDLRLERW QKDRDIFVNK AESMGAKVFV QSANGDDSAQ ISQIENMINK NIDVLVIIPH NGEVLSNVIS EAKKEGIKVL AYDRLINNAD LDFYVSFDNE KVGELQAKSI VAVKPEGNYF LMGGSPVDNN AKLFRKGQMK VLDPLIASGK IKVVGDQWVD SWLAEKALQI MENALTANKN NVDAVVASND ATAGGAIQAL SAQGLSGKVA ISGQDADLAA IKRIVNGSQT MTVYKPITKL ADKAAEIAVE LGKNEKIEAN AELNNGLKNV PAYLLDPIAV DKRNINETVI KDGFHTKESI YH // ID Y045_HAEIN Reviewed; 184 AA. AC P44478; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_0045; DE Flags: Precursor; GN OrderedLocusNames=HI_0045; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: To E.coli YtfJ. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21723.1; -; Genomic_DNA. DR PIR; B64141; B64141. DR RefSeq; NP_438218.1; NC_000907.1. DR RefSeq; WP_010868922.1; NC_000907.1. DR STRING; 71421.HI0045; -. DR EnsemblBacteria; AAC21723; AAC21723; HI_0045. DR GeneID; 950943; -. DR KEGG; hin:HI0045; -. DR PATRIC; 20188543; VBIHaeInf48452_0045. DR eggNOG; ENOG4108UUE; Bacteria. DR eggNOG; COG3054; LUCA. DR KO; K07109; -. DR OMA; QFSYKNW; -. DR OrthoDB; EOG6B628X; -. DR PhylomeDB; P44478; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR InterPro; IPR006513; CHP01626_YtfJ. DR Pfam; PF09695; YtfJ_HI0045; 1. DR TIGRFAMs; TIGR01626; ytfJ_HI0045; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 184 Uncharacterized protein HI_0045. FT /FTId=PRO_0000013945. SQ SEQUENCE 184 AA; 19869 MW; 3A658DB7217450A9 CRC64; MKKQILALVC GVIFSSSTWA HNLQLEQSLP SVKVSEYGEI VLSGKDTVFQ PWGSAELAGK VRVVHHLAGR TAAKEXNQSM IDVIKASHFN PVKYQTTTII NADDAIVGTG MFVKNGAKKG KQENPHSQVV LDDKSAVKNA WGLNSKDSAI IVLDKTGKVK FVKEGKLSDS DIQTVISLVN GLTK // ID Y053_HAEIN Reviewed; 342 AA. AC Q57517; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 108. DE RecName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein HI_0053; DE EC=1.-.-.-; GN OrderedLocusNames=HI_0053; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21731.1; -; Genomic_DNA. DR PIR; F64141; F64141. DR RefSeq; NP_438226.1; NC_000907.1. DR RefSeq; WP_010868926.1; NC_000907.1. DR ProteinModelPortal; Q57517; -. DR STRING; 71421.HI0053; -. DR EnsemblBacteria; AAC21731; AAC21731; HI_0053. DR GeneID; 950952; -. DR KEGG; hin:HI0053; -. DR PATRIC; 20188559; VBIHaeInf48452_0053. DR eggNOG; ENOG4105CPQ; Bacteria. DR eggNOG; COG1063; LUCA. DR OMA; DRICTHQ; -. DR OrthoDB; EOG6ZWJCC; -. DR PhylomeDB; Q57517; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11695; PTHR11695; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Oxidoreductase; Reference proteome; KW Zinc. FT CHAIN 1 342 Uncharacterized zinc-type alcohol FT dehydrogenase-like protein HI_0053. FT /FTId=PRO_0000160896. FT METAL 41 41 Zinc 1; catalytic. {ECO:0000250}. FT METAL 63 63 Zinc 1; catalytic. {ECO:0000250}. FT METAL 94 94 Zinc 2. {ECO:0000250}. FT METAL 97 97 Zinc 2. {ECO:0000250}. FT METAL 100 100 Zinc 2. {ECO:0000250}. FT METAL 108 108 Zinc 2. {ECO:0000250}. FT METAL 149 149 Zinc 1; catalytic. {ECO:0000250}. SQ SEQUENCE 342 AA; 37429 MW; 100B07F9194E6954 CRC64; MKERIKAICL EKPNNVVVKE VPYPEKSDND VLIQVESMGI CGSDIGAYRG TNPLVTYPRI LGHEIVGRVI ESGIGMSDGV RVGDRVIVDP YVCCGQCYPC SIGRTNCCES LKVIGVHIDG GMQEVIRHPA HLLTKVPDNL PIHQLPLAEP LTIALHALHR TTLKSGEHIV IIGAGAIGLM AALAAVQYGA IPILVDILEQ RLEYAKSLGI EHIVNPHKED DIKRIKEITS GRMAEVVMEA SGANISIKNT LHYASFAGRI ALTGWPKTET PLPTNLITFK ELNIYGSRTS KGEFEEALDM LATNKINASH IITKCIKFEE IPSFISDLSD HPENYLKINA VF // ID Y056_HAEIN Reviewed; 237 AA. AC P43932; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=UPF0053 protein HI_0056; GN OrderedLocusNames=HI_0056; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21734.1; -; Genomic_DNA. DR PIR; D64000; D64000. DR RefSeq; NP_438229.1; NC_000907.1. DR RefSeq; WP_005693866.1; NC_000907.1. DR STRING; 71421.HI0056; -. DR EnsemblBacteria; AAC21734; AAC21734; HI_0056. DR GeneID; 950954; -. DR KEGG; hin:HI0056; -. DR PATRIC; 20188565; VBIHaeInf48452_0056. DR eggNOG; ENOG4105EE5; Bacteria. DR eggNOG; COG0861; LUCA. DR OMA; VHSFFGA; -. DR OrthoDB; EOG6F297P; -. DR PhylomeDB; P43932; -. DR Proteomes; UP000000579; 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; IPR005496; Integral_membrane_TerC. DR Pfam; PF03741; TerC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 237 UPF0053 protein HI_0056. FT /FTId=PRO_0000088369. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. SQ SEQUENCE 237 AA; 26231 MW; C70DDAC70C7C1DB4 CRC64; MFEWIADPEA WISLVTLAAL EIVLGIDNII FINILVGRLP ERQRQSGRIL GLALAMLTRI LLLMSLAWIM KLTAPLFTVF NQEISGRDLI LLIGGLFLII KSSGEIKEAI NHQEHHESES KNKVSYLGVL IQIAVLDIVF SLDSVITAVG MASHLPVMIL AIMIAVGVMM FAAKPIGDFV DTHPTLKILA LAFLVLVGIS LIAESLDIHI PKGYIYFAMG FSVVVEMINI RMRRLMK // ID Y096_HAEIN Reviewed; 191 AA. AC P43940; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_0096; GN OrderedLocusNames=HI_0096; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21780.1; -; Genomic_DNA. DR PIR; C64001; C64001. DR RefSeq; NP_438270.1; NC_000907.1. DR RefSeq; WP_005693822.1; NC_000907.1. DR STRING; 71421.HI0096; -. DR EnsemblBacteria; AAC21780; AAC21780; HI_0096. DR GeneID; 951000; -. DR KEGG; hin:HI0096; -. DR PATRIC; 20188659; VBIHaeInf48452_0099. DR OrthoDB; EOG63FW4Z; -. DR Proteomes; UP000000579; 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 1 191 Uncharacterized protein HI_0096. FT /FTId=PRO_0000077887. FT TRANSMEM 59 78 Helical. {ECO:0000255}. SQ SEQUENCE 191 AA; 21910 MW; FA7921A62A03B9A3 CRC64; MDLADSQITQ GNEIIQSMGL TNVRLLEYFI YQVGSFTIQS LTQHIEENKE FANITENELY SAVLSLVILG YVYVYLTTYP IYSFEDNKTY IPKSFTQYVK TLVEGANQYI GAGNMYNGDV EDLNKLHLYI MSQMEKPTTK AELKSALQGY LIQNEYQDMN NNDKLIDETY DCTELFNALF DVLTRLGISS L // ID Y1005_HAEIN Reviewed; 519 AA. AC P44974; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 98. DE RecName: Full=Putative phosphoethanolamine transferase HI_1005; DE EC=2.7.-.-; GN OrderedLocusNames=HI_1005; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase 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; L42023; AAC22666.1; -; Genomic_DNA. DR PIR; I64163; I64163. DR RefSeq; NP_439166.1; NC_000907.1. DR RefSeq; WP_005693345.1; NC_000907.1. DR ProteinModelPortal; P44974; -. DR STRING; 71421.HI1005; -. DR EnsemblBacteria; AAC22666; AAC22666; HI_1005. DR GeneID; 949997; -. DR KEGG; hin:HI1005; -. DR PATRIC; 20190671; VBIHaeInf48452_1048. DR eggNOG; ENOG4108I6E; Bacteria. DR eggNOG; COG2194; LUCA. DR OMA; RWGKMET; -. DR OrthoDB; EOG6H1PW4; -. DR PhylomeDB; P44974; -. DR Proteomes; UP000000579; 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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 519 Putative phosphoethanolamine transferase FT HI_1005. FT /FTId=PRO_0000209153. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. SQ SEQUENCE 519 AA; 60431 MW; 24F18370E82C032A CRC64; MMFGKKIIHS KTIWFYFLLF LFSIFTNMGL GNVLSENIPV SDYAILFVIT AISFYFTPWL GRILITVLFL SALFYCSAGF FYGIPSLGII ASVYETNINE TLEYYTTIPF WIFLFQASYF ILFVALMKLS FHVKQQAFKW LNTAVISLLL VFSYNQFSDW NYGYKFRFYP VLFYSEFDRM NDLYLEQRDF LNQSANAPSQ WDIQSFMPKY KNYILIIGES MRKDYMSLYG FPLKTTPFLE RVKGTVFENY YSAAPNTQPS LQLTLYRAEK GETVYTDNII SLAKKAGVKT YWISNQGKIG EFDTIASRIG QSADETIFMK PLGYNSKKVY DDEMLPVLDK ALKENISNSK LIVIHLIGSH PAFCERLPYE VKNYFINQSM SCYLESIKYT DQFLEKLNSQ LVAQNEPYSV IYFSDHGLAH YEDSNGLSLH PNNLYKQDYE IPFIMFSSDS QKVEKIKTPQ SAFNFVYGFA DWMGIKEKHL QGVDFFHPEK QEIKVFDWNN VVNVKELADD PAKLPETVQ // ID Y1043_HAEIN Reviewed; 166 AA. AC P44101; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Uncharacterized protein HI_1043; GN OrderedLocusNames=HI_1043; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22702.1; -; Genomic_DNA. DR PIR; B64019; B64019. DR RefSeq; NP_439202.1; NC_000907.1. DR RefSeq; WP_010869114.1; NC_000907.1. DR ProteinModelPortal; P44101; -. DR STRING; 71421.HI1043; -. DR EnsemblBacteria; AAC22702; AAC22702; HI_1043. DR GeneID; 950023; -. DR KEGG; hin:HI1043; -. DR PATRIC; 20190751; VBIHaeInf48452_1088. DR eggNOG; ENOG4105N1P; Bacteria. DR eggNOG; COG1145; LUCA. DR OMA; NGCGECK; -. DR OrthoDB; EOG60SCM3; -. DR PhylomeDB; P44101; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004496; NapF. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF12838; Fer4_7; 1. DR TIGRFAMs; TIGR00402; napF; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1 166 Uncharacterized protein HI_1043. FT /FTId=PRO_0000159307. FT DOMAIN 44 73 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 75 104 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 139 166 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 53 53 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 56 56 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 59 59 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 63 63 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 84 84 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 87 87 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 90 90 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 94 94 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 166 AA; 18144 MW; D5BC129C5D432CC2 CRC64; MKNEAYYQAY LSHHHISRRG LLRHVFPATK STIEKTQSRP PFSAREDLFS AVCNGCGECA SACPNGLIQL KQQQATLEID YAPCDLCGKC AEVCPTNALH PNFPGDTLLR PQFSSACLIL QNQTCPDCQT ACPLQAISST LEIDNERCNG CGECKITCFV AAITLK // ID Y1073_HAEIN Reviewed; 124 AA. AC P45019; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=UPF0382 membrane protein HI_1073; GN OrderedLocusNames=HI_1073; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0382 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; L42023; AAC22729.1; -; Genomic_DNA. DR PIR; H64165; H64165. DR RefSeq; NP_439229.1; NC_000907.1. DR RefSeq; WP_005693396.1; NC_000907.1. DR STRING; 71421.HI1073; -. DR DNASU; 950051; -. DR EnsemblBacteria; AAC22729; AAC22729; HI_1073. DR GeneID; 950051; -. DR KEGG; hin:HI1073; -. DR PATRIC; 20190805; VBIHaeInf48452_1115. DR eggNOG; ENOG4105M08; Bacteria. DR eggNOG; COG2363; LUCA. DR OMA; ARYQMYH; -. DR OrthoDB; EOG661HB8; -. DR PhylomeDB; P45019; -. DR Proteomes; UP000000579; 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; IPR006696; DUF423. DR Pfam; PF04241; DUF423; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 124 UPF0382 membrane protein HI_1073. FT /FTId=PRO_0000169333. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. SQ SEQUENCE 124 AA; 13450 MW; B71D3E4ABCE0FA13 CRC64; MKNKYLTLVA LSGFFCVALG AFAAHGLSHI LEAKALSWID TGLEYQMFHT IAVLAVALSA LRDNKFARLS MSSWLIGILL FSGSLYALAF EASNVIVWIT PIGGTLFLIG WISLAYGSFK SKSL // ID Y1098_HAEIN Reviewed; 44 AA. AC P44111; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_1098; GN OrderedLocusNames=HI_1098; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22754.1; -; Genomic_DNA. DR PIR; C64020; C64020. DR EnsemblBacteria; AAC22754; AAC22754; HI_1098. DR PATRIC; 20190863; VBIHaeInf48452_1144. DR OrthoDB; EOG6ZWJN0; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 44 Uncharacterized protein HI_1098. FT /FTId=PRO_0000078002. SQ SEQUENCE 44 AA; 5028 MW; 2FCA574BCAFB7176 CRC64; MPVYSITDKD LSKRIQLKEN KTLKEKTANY VSEGRAVLTD VICK // ID Y1107_HAEIN Reviewed; 468 AA. AC Q57007; P96339; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 99. DE RecName: Full=Uncharacterized Na(+)/H(+) antiporter HI_1107; GN OrderedLocusNames=HI_1107; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter 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; L42023; AAC22762.1; -; Genomic_DNA. DR PIR; I64182; I64182. DR RefSeq; NP_439264.1; NC_000907.1. DR RefSeq; WP_010869131.1; NC_000907.1. DR STRING; 71421.HI1107; -. DR EnsemblBacteria; AAC22762; AAC22762; HI_1107. DR GeneID; 950734; -. DR KEGG; hin:HI1107; -. DR PATRIC; 20190885; VBIHaeInf48452_1155. DR eggNOG; ENOG4105DFD; Bacteria. DR eggNOG; COG1757; LUCA. DR KO; K03315; -. DR OMA; TCGAYMA; -. DR OrthoDB; EOG61GG5F; -. DR PhylomeDB; Q57007; -. DR Proteomes; UP000000579; 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:UniProtKB-KW. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR004770; Na/H_antiport_NhaC. DR InterPro; IPR018461; Na/H_Antiport_NhaC-like_C. DR Pfam; PF03553; Na_H_antiporter; 1. DR TIGRFAMs; TIGR00931; antiport_nhaC; 1. PE 3: Inferred from homology; KW Antiport; Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 468 Uncharacterized Na(+)/H(+) antiporter FT HI_1107. FT /FTId=PRO_0000052418. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. FT TRANSMEM 260 280 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. FT TRANSMEM 414 434 Helical. {ECO:0000255}. FT TRANSMEM 443 463 Helical. {ECO:0000255}. SQ SEQUENCE 468 AA; 49890 MW; 4213BC32C7F13F27 CRC64; MKTTHRTRMP TTLEAFSPII VMLLLLGLGY ALFDLPAEPL MIISTVFAGF LVFKLGHCYL DILDAISEKI AKTMPALLIL ITVGLLIGTW ISGGTIPMMI YYGLKAISPE YLYVTALFLT AIVSICTGTS WGSAGTVGVA FMGVAIGLDA NLAATAGAVV AGAYFGDKLS PLSDTTNIAS AAAGVDLYEH IAHLLYTTLP SFILSATVYV VYGLNYDFSN VATPEKVNTM IHELEQVYHF NFLLLIPVAI VLWGSITKKP TIPVMLLSAF IAIINAILIQ KFSLSDVINS AVNGFDTSMI HHTSVSSDLS RLLNRGGMNS MMGTLLICFC ALSFAGVLQL SGALTVIIQK LLTFVHSTLS LIITTILCGL TMIGVTCNGQ ISILIPGEML KNAYVEKGLH PKNLSRTAED SATIIEPILP WTAAGAYMAG TLGVATLSYL PWAILCWSGI IFAIIYGASG IGIAKLKK // ID Y1154_HAEIN Reviewed; 440 AA. AC P45079; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized symporter HI_1154; GN OrderedLocusNames=HI_1154; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter CC (TC 2.A.23) 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; L42023; AAC22809.1; -; Genomic_DNA. DR PIR; D64186; D64186. DR RefSeq; NP_439312.1; NC_000907.1. DR RefSeq; WP_005693469.1; NC_000907.1. DR ProteinModelPortal; P45079; -. DR STRING; 71421.HI1154; -. DR EnsemblBacteria; AAC22809; AAC22809; HI_1154. DR GeneID; 950771; -. DR KEGG; hin:HI1154; -. DR PATRIC; 20190985; VBIHaeInf48452_1205. DR eggNOG; ENOG4107R6U; Bacteria. DR eggNOG; COG1823; LUCA. DR KO; K06956; -. DR OMA; HLAYGTH; -. DR OrthoDB; EOG6HQSKK; -. DR PhylomeDB; P45079; -. DR Proteomes; UP000000579; 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:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR Gene3D; 1.10.3860.10; -; 1. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR PANTHER; PTHR11958; PTHR11958; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; SSF118215; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 440 Uncharacterized symporter HI_1154. FT /FTId=PRO_0000202122. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TRANSMEM 343 363 Helical. {ECO:0000255}. FT TRANSMEM 366 386 Helical. {ECO:0000255}. FT TRANSMEM 389 409 Helical. {ECO:0000255}. SQ SEQUENCE 440 AA; 46492 MW; F9298839559FD06A CRC64; MLLVNLAIFI AFLLLLAQLY RKTEKLGQTV FIGLLLGLLF GAVLQSAFEK PLLDKTLDWI NVVSNGYVRL LQMIVMPLVF VSILSAIARI NQTRSLGKVS VGVLSTLLIT TAISAAIGIA MVHLFDVSAA GLIVGDRELA AQGKVLDKAG QVSNLTVPAM LVSFIPKNPF ADLTGANPTS IISVVIFSAL LGVAALSLGK EDQALGERIA QGVETLNKLV MRLVRFVIRL TPYGVFALMI KMAATSKWAD IVNLGNFIVA SYAAIALMFV VHGILLFFVK VNPVDYYKKV LPTLSFAFTS RSSAATIPLN IETQTAKLGN NNVIANFAAT FGATIGQNGC GGIYPAMLAV MVAPMVGIDP FSFSYILTLI FVVAISSFGI AGVGGGATFA AIVVLSTLGL PLELIGLLIS IEPIIDMGRT ALNVNGAMVA GTITDRLLNK // ID Y1205_HAEIN Reviewed; 147 AA. AC P44127; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=UPF0208 membrane protein HI_1205 {ECO:0000255|HAMAP-Rule:MF_01101}; GN OrderedLocusNames=HI_1205; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01101}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01101}. CC -!- SIMILARITY: Belongs to the UPF0208 family. {ECO:0000255|HAMAP- CC Rule:MF_01101}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22859.1; -; Genomic_DNA. DR PIR; A64022; A64022. DR RefSeq; NP_439361.1; NC_000907.1. DR RefSeq; WP_005694240.1; NC_000907.1. DR STRING; 71421.HI1205; -. DR EnsemblBacteria; AAC22859; AAC22859; HI_1205. DR GeneID; 950166; -. DR KEGG; hin:HI1205; -. DR PATRIC; 20191089; VBIHaeInf48452_1257. DR eggNOG; ENOG4105PQ6; Bacteria. DR eggNOG; COG3092; LUCA. DR KO; K09899; -. DR OMA; WPVRKEL; -. DR OrthoDB; EOG6KQ6FX; -. DR PhylomeDB; P44127; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_01101; UPF0208; 1. DR InterPro; IPR007334; UPF0208. DR Pfam; PF04217; DUF412; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 147 UPF0208 membrane protein HI_1205. FT /FTId=PRO_0000080814. FT TRANSMEM 38 58 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01101}. FT TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01101}. SQ SEQUENCE 147 AA; 17270 MW; E0A599F97B4CFB6F CRC64; MAFFSIFKQG QIYLNTWPLE AKLGIIFPEN RIMKATSFAQ KFMPFVAVFA ILWQQFYAKN DLMAFSIAIL TALFALLIPF QGLYWLGKRA NTPLENQSAV WFYDICERLK QLHEPLPFVQ EKPTYQHLAE VLKKAQSKLE RAFWQEI // ID Y1215_HAEIN Reviewed; 235 AA. AC P44128; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1215; DE Flags: Precursor; GN OrderedLocusNames=HI_1215; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22868.1; -; Genomic_DNA. DR PIR; B64022; B64022. DR RefSeq; NP_439371.2; NC_000907.1. DR ProteinModelPortal; P44128; -. DR STRING; 71421.HI1215; -. DR EnsemblBacteria; AAC22868; AAC22868; HI_1215. DR GeneID; 950165; -. DR KEGG; hin:HI1215; -. DR PATRIC; 20191109; VBIHaeInf48452_1267. DR eggNOG; COG0526; LUCA. DR KO; K03673; -. DR OMA; FFDYDCR; -. DR OrthoDB; EOG6PKFBC; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR012336; Thioredoxin-like_fold. DR SUPFAM; SSF52833; SSF52833; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 235 Uncharacterized protein HI_1215. FT /FTId=PRO_0000013966. SQ SEQUENCE 235 AA; 27235 MW; 11D3EADD65ABE003 CRC64; MSDRMKLKGL LAFCLLFLSS FVLAEVNQKE FSVQNSPHLP SRDTIYFEDG RDYFSYKEPI EQASRTDKKI RIQFFFDYDC RVCSSAQDIL ELYSQIRTYK VALEQYPIAT ADNQFSARIF YTLQALSAGE LSNVLLFETS EKSRYTELST SNKIQQWAEE QGLDKQLFIQ TENSQSVKEQ IQNAIELTEE YGVFTYPYVV IGGKYVLTAS TLYNDDYSVA VLDFLVNKIE QEQKQ // ID Y1235_HAEIN Reviewed; 155 AA. AC P44131; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_1235; DE Flags: Precursor; GN OrderedLocusNames=HI_1235; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22891.1; -; Genomic_DNA. DR PIR; E64022; E64022. DR STRING; 71421.HI1235; -. DR EnsemblBacteria; AAC22891; AAC22891; HI_1235. DR PATRIC; 20191149; VBIHaeInf48452_1287. DR OrthoDB; EOG6CGC8W; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010352; DUF945. DR Pfam; PF06097; DUF945; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 155 Uncharacterized protein HI_1235. FT /FTId=PRO_0000013967. SQ SEQUENCE 155 AA; 17229 MW; 8B81433095157132 CRC64; MPLSKTLVQK LQQAGMAIAN NQPQIKFTPL SISDEKGKVA LDLNIALVPN PKFDLMHSGL YKQFKDFSIN FDVNKETAIS LLSKFVPENQ KQDLVYRMDE LIAEGEANGI IVNTDKTVTL TLALENNDLK LNGKPIPEEQ LKVVLFILVM GGFGR // ID Y1273_HAEIN Reviewed; 268 AA. AC P44150; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Uncharacterized protein HI_1273; GN OrderedLocusNames=HI_1273; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22921.1; -; Genomic_DNA. DR PIR; F64024; F64024. DR RefSeq; NP_439426.1; NC_000907.1. DR RefSeq; WP_005694515.1; NC_000907.1. DR ProteinModelPortal; P44150; -. DR STRING; 71421.HI1273; -. DR EnsemblBacteria; AAC22921; AAC22921; HI_1273. DR GeneID; 950164; -. DR KEGG; hin:HI1273; -. DR PATRIC; 20191225; VBIHaeInf48452_1324. DR eggNOG; ENOG4108BSC; Bacteria. DR eggNOG; COG0500; LUCA. DR OMA; REDIGFP; -. DR OrthoDB; EOG661H8R; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 268 Uncharacterized protein HI_1273. FT /FTId=PRO_0000078020. SQ SEQUENCE 268 AA; 30511 MW; E5B28DA7AADC4D0B CRC64; MTIYDINFAE LYQQHLIACN HYNLPPIKWD KKAVKMAENL VGKPSAYNQQ LLQAMNVQTD EAVLDIGCGP GTFAVPLAQQ GSTVYALDYS NGMLDCLAQF KQKFGLHHLT TFHKSWADNW DDVPQADVVL ASRSTLVDDL DDMIEKLCAK AKKRVFLTSV TQRHFLDEGV FEAIGREDIG FPTYIYLLNR LYQKGIQANL NFIETESGCF QGESYEDLLA SVEFSLGELS EKEKQGLKAF YDRKQANNEP ISHGQKKWAL IWWNVDRI // ID Y1280_HAEIN Reviewed; 91 AA. AC P44151; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_1280; GN OrderedLocusNames=HI_1280; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 integrase catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU00457}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22928.1; -; Genomic_DNA. DR PIR; G64024; G64024. DR ProteinModelPortal; P44151; -. DR EnsemblBacteria; AAC22928; AAC22928; HI_1280. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 91 Uncharacterized protein HI_1280. FT /FTId=PRO_0000078021. FT DOMAIN 1 91 Integrase catalytic. FT {ECO:0000255|PROSITE-ProRule:PRU00457}. SQ SEQUENCE 91 AA; 10671 MW; 6A159C7A97590A81 CRC64; MLTFWHWKWL GIKNTEFKCV KGKLYLSPIK DLFNNEIIAY DLVRSPNSEQ ITQMMKQAVA RLAGAKPILH SDQGWQYQMI GYQNILRENG I // ID Y1296_HAEIN Reviewed; 178 AA. AC Q57519; O05055; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized endonuclease HI_1296; DE EC=3.1.-.-; DE Flags: Precursor; GN OrderedLocusNames=HI_1296; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the thermonuclease family. CC {ECO:0000255|PROSITE-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; L42023; AAC22942.1; -; Genomic_DNA. DR PIR; A64115; A64115. DR RefSeq; NP_439447.2; NC_000907.1. DR ProteinModelPortal; Q57519; -. DR STRING; 71421.HI1296; -. DR EnsemblBacteria; AAC22942; AAC22942; HI_1296. DR GeneID; 950236; -. DR KEGG; hin:HI1296; -. DR PATRIC; 20191273; VBIHaeInf48452_1347. DR eggNOG; ENOG4105KK6; Bacteria. DR eggNOG; COG1525; LUCA. DR OMA; SACSREK; -. DR OrthoDB; EOG632D5H; -. DR Proteomes; UP000000579; Chromosome. 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 Pfam; PF00565; SNase; 1. DR SMART; SM00318; SNc; 1. DR SUPFAM; SSF50199; SSF50199; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01123; TNASE_1; 1. DR PROSITE; PS01284; TNASE_2; 1. DR PROSITE; PS50830; TNASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 178 Uncharacterized endonuclease HI_1296. FT /FTId=PRO_0000034397. FT ACT_SITE 52 52 {ECO:0000250}. FT ACT_SITE 60 60 {ECO:0000250}. FT ACT_SITE 94 94 {ECO:0000250}. SQ SEQUENCE 178 AA; 20441 MW; 4169580DDFB6B340 CRC64; MINRKILLTS LLLIFTVLSA CSREKNTCRV VKISDGDTLT CLTKGNKSIK VRLAEIDAPE KSQAFGQKSK KTLSDLVYQK NVRLARKGKD RYQRTLAVVY YQKQNINLEM VKQGMAWAYK QYSHDPIYLQ AQENAQAKGI GLWADNNPIE PSQWRRQEKI NMAFDYQTFP SSISLFPT // ID Y1326_HAEIN Reviewed; 242 AA. AC P44162; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1326; GN OrderedLocusNames=HI_1326; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22980.1; -; Genomic_DNA. DR PIR; I64025; I64025. DR RefSeq; NP_439477.1; NC_000907.1. DR RefSeq; WP_005662421.1; NC_000907.1. DR STRING; 71421.HI1326; -. DR EnsemblBacteria; AAC22980; AAC22980; HI_1326. DR GeneID; 950251; -. DR KEGG; hin:HI1326; -. DR PATRIC; 20191335; VBIHaeInf48452_1378. DR eggNOG; ENOG4105XTM; Bacteria. DR eggNOG; ENOG4111X9I; LUCA. DR OMA; YWLKQPE; -. DR OrthoDB; EOG65N19S; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR011009; Kinase-like_dom. DR SUPFAM; SSF56112; SSF56112; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 242 Uncharacterized protein HI_1326. FT /FTId=PRO_0000078025. SQ SEQUENCE 242 AA; 29169 MW; 04C90A3241FC60FA CRC64; MMVNDDFQEY VKQLVTKHRD ERIYPFQYEG KKYWLKQPEK LKGIWLLLKP HPKKSFKNEL YTLLKLAEQN APVPKVSYYS DHFFVLENVG LTVSQWLCNK NIDEQQKFLI IYDACLALID LHAKNLVHGR PAIRDITWDK GKVTFLDFES RSNSRNQNWV VIRDMLFFFD SLCREEDISD TFIQKVALYY QTHCEAKNWQ NMIVFLQRFS WVYYLLLPFK PIAKTDLISI YRLFEIFLIK KK // ID Y1329_HAEIN Reviewed; 103 AA. AC Q57255; P96342; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 07-JAN-2015, entry version 54. DE RecName: Full=Uncharacterized protein HI_1329; GN OrderedLocusNames=HI_1329; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22974.1; -; Genomic_DNA. DR PIR; I64116; I64116. DR EnsemblBacteria; AAC22974; AAC22974; HI_1329. DR OMA; NEMQGLY; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 103 Uncharacterized protein HI_1329. FT /FTId=PRO_0000078028. SQ SEQUENCE 103 AA; 11610 MW; 2DE87E6832E8B602 CRC64; MRKSRLSQHK QNKLIELFVA GVTARTASKL VNVNKNTATI TFIDYAYSFI KQAHIWKCLK AKLKPMKAIS AVLEKANVVA VLQGKSQYSG FSNEMQGLYR RCS // ID Y1339_HAEIN Reviewed; 129 AA. AC P71378; O86240; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1339/HI_1462.1; GN OrderedLocusNames=HI_1339; GN and GN OrderedLocusNames=HI_1462.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the LEA type 1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23114.1; 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; L42023; AAC22992.1; -; Genomic_DNA. DR EMBL; L42023; AAC23114.1; ALT_INIT; Genomic_DNA. DR PIR; F64117; F64117. DR RefSeq; NP_439490.1; NC_000907.1. DR RefSeq; NP_439612.2; NC_000907.1. DR RefSeq; WP_005694656.1; NC_000907.1. DR STRING; 71421.HI1462.1; -. DR EnsemblBacteria; AAC22992; AAC22992; HI_1339. DR EnsemblBacteria; AAC23114; AAC23114; HI_1462.1. DR GeneID; 950572; -. DR GeneID; 950818; -. DR KEGG; hin:HI1339; -. DR KEGG; hin:HI1462.1; -. DR PATRIC; 20191361; VBIHaeInf48452_1391. DR eggNOG; ENOG4106DNW; Bacteria. DR eggNOG; ENOG410XVRI; LUCA. DR OrthoDB; EOG67430P; -. DR Proteomes; UP000000579; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein FT HI_1339/HI_1462.1. FT /FTId=PRO_0000078029. SQ SEQUENCE 129 AA; 13779 MW; 7B15E06D554702A7 CRC64; MEKIMKKLTL ALVLGSALVV TGCFDKQEAK QKVEDTKQTV ASVASETKDA AANTMTEVKE KAQQLSTDVK NKVAEKVEDA KEVIKSATEA ASEKVGEMKE AASEKASEMK EAVSEKATQA VDAVKEATK // ID Y1340_HAEIN Reviewed; 441 AA. AC P44165; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_1340; GN OrderedLocusNames=HI_1340; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) 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; L42023; AAC22986.1; -; Genomic_DNA. DR PIR; C64026; C64026. DR RefSeq; NP_439491.1; NC_000907.1. DR RefSeq; WP_010869184.1; NC_000907.1. DR ProteinModelPortal; P44165; -. DR SMR; P44165; 19-200. DR STRING; 71421.HI1340; -. DR EnsemblBacteria; AAC22986; AAC22986; HI_1340. DR GeneID; 950814; -. DR KEGG; hin:HI1340; -. DR PATRIC; 20191363; VBIHaeInf48452_1392. DR eggNOG; COG0780; LUCA. DR eggNOG; COG1538; LUCA. DR eggNOG; COG2904; LUCA. DR OMA; WGTDQAQ; -. DR OrthoDB; EOG6V7BHC; -. DR PhylomeDB; P44165; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR InterPro; IPR029139; QueF_N. DR Pfam; PF02321; OEP; 1. DR Pfam; PF14819; QueF_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 441 Uncharacterized protein HI_1340. FT /FTId=PRO_0000078030. SQ SEQUENCE 441 AA; 49790 MW; D06BB069EC6FF9A7 CRC64; MNYQDNSLKS LKLGQKTEYA SQYDRTLLQP VPRALNRDGL GITQNQPFTI GADIWTAYEI SWLNEKGLPQ VAIADIYLDY QSQNLIESKS FKLYLNSFNQ SKFTDFNAVQ QTMQRDLSEC AQGDVKVRLN PVAVYDAQKI NHLQGDCIDE QDIEITSYEF NANWLKDCVS NEIVEEKLVS HLLKSNCLIT NQPDWGTDQA QQAILTARNN KLNFETQRKT AEQTLRNLLN LKPNEALNIT FPHIMNVKTA GVNLNVPVSV IANRPDVKAA QFRLSSAFKN AKATQKSWFP EVNLGASLSS TASTVGTALH NPVAAGTVGI SLPFLNWNTV KWNVKISEAD YETARLNYEQ RITTALNNVD TNYFAFTQAQ STLSNLQQTH SYNQRITQYY RNRYNAGVSE LREWLVAANT EKSSQLAILN AKYQVLQSEN AVYSSMAGYY L // ID Y1395_HAEIN Reviewed; 140 AA. AC P44173; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_1395; GN OrderedLocusNames=HI_1395; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23049.1; -; Genomic_DNA. DR PIR; C64027; C64027. DR ProteinModelPortal; P44173; -. DR STRING; 71421.HI1395; -. DR EnsemblBacteria; AAC23049; AAC23049; HI_1395. DR PATRIC; 20191489; VBIHaeInf48452_1455. DR eggNOG; COG4185; LUCA. DR OMA; MQNKAIF; -. DR OrthoDB; EOG6MH5CK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IEA:InterPro. DR InterPro; IPR010488; Zeta_toxin_domain. DR Pfam; PF06414; Zeta_toxin; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein HI_1395. FT /FTId=PRO_0000078037. SQ SEQUENCE 140 AA; 15866 MW; 10BED95440C651DD CRC64; MVRKKLWVMQ NKAIFYCGTN GSGKSTLRSF NQDAVQIVID SDHIAMQINP QNPRLADIDA GRKAIGLFHF AIKQHIGFPM ESTLSGNSII QRMKTAKENG FYVHLNYIGI NRVEINLARI KARVKSGGHF IAEDIVKYRY // ID Y1396_HAEIN Reviewed; 56 AA. AC P44174; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 50. DE RecName: Full=Uncharacterized protein HI_1396; GN OrderedLocusNames=HI_1396; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23050.1; -; Genomic_DNA. DR PIR; D64027; D64027. DR EnsemblBacteria; AAC23050; AAC23050; HI_1396. DR OMA; HEVVIFQ; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 56 Uncharacterized protein HI_1396. FT /FTId=PRO_0000078038. SQ SEQUENCE 56 AA; 6637 MW; 85927C4DF93E9EEF CRC64; MTEREKIIQQ QKQLKALFSV WMKEKMNHEV VIFQKTDGKI VEHYPDGSEK IVGYAK // ID Y1411_HAEIN Reviewed; 171 AA. AC Q57374; O05060; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_1411; GN OrderedLocusNames=HI_1411; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23059.1; -; Genomic_DNA. DR PIR; C64122; C64122. DR RefSeq; NP_439562.1; NC_000907.1. DR RefSeq; WP_005693952.1; NC_000907.1. DR ProteinModelPortal; Q57374; -. DR STRING; 71421.HI1411; -. DR EnsemblBacteria; AAC23059; AAC23059; HI_1411. DR GeneID; 950482; -. DR KEGG; hin:HI1411; -. DR PATRIC; 20191519; VBIHaeInf48452_1470. DR eggNOG; ENOG41061CV; Bacteria. DR eggNOG; ENOG4112CQ0; LUCA. DR OMA; HLGMFAN; -. DR OrthoDB; EOG6R5C7V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006323; P:DNA packaging; IEA:InterPro. DR InterPro; IPR005335; Terminase_ssu. DR Pfam; PF03592; Terminase_2; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 171 Uncharacterized protein HI_1411. FT /FTId=PRO_0000078048. SQ SEQUENCE 171 AA; 18966 MW; 7605DFA4FB473C93 CRC64; MSDVKGKSTS GRGLTPKQEK FCQLYIELGN ASEAYRQSYD CSKMTTEVIN VKASELLNKN GKITVRVEEL RQAHQQRHNL TLDNIIADLQ EYRDICMGRK PLTITTVVKN AQEGTAQSVN TECFVFEPTG ANKALELLGK HLGMFTNKVD VTTDGKPLPT VINVTFSDEP A // ID Y1418_HAEIN Reviewed; 201 AA. AC P44189; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_1418; GN OrderedLocusNames=HI_1418; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 Bro-N domain. {ECO:0000255|PROSITE- CC ProRule:PRU01086, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23068.1; -; Genomic_DNA. DR PIR; A64029; A64029. DR RefSeq; NP_439568.2; NC_000907.1. DR STRING; 71421.HI1418; -. DR EnsemblBacteria; AAC23068; AAC23068; HI_1418. DR GeneID; 950323; -. DR KEGG; hin:HI1418; -. DR PATRIC; 20191531; VBIHaeInf48452_1476. DR eggNOG; ENOG4105WXW; Bacteria. DR eggNOG; COG3617; LUCA. DR OMA; EMTFINE; -. DR OrthoDB; EOG644ZVD; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003497; BRO_N_domain. DR InterPro; IPR018876; Phage_P22_antirepressor_C. DR Pfam; PF02498; Bro-N; 1. DR Pfam; PF10548; P22_AR_C; 1. DR SMART; SM01040; Bro-N; 1. DR PROSITE; PS51750; BRO_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 201 Uncharacterized protein HI_1418. FT /FTId=PRO_0000078053. FT DOMAIN 15 122 Bro-N. {ECO:0000255|PROSITE- FT ProRule:PRU01086}. SQ SEQUENCE 201 AA; 23567 MW; 87964F8E43B4327B CRC64; MGKLSILSKR KYTMKNQIQF STFNFKDLPV RVILDPKGEF WFCGTDVCHI LGYTNSRKAL QDHCKQGGVT KRYTPTKSAD QEMTFINEPN LYRLIIKSRK PEAEPFEAWV FEEVLPQIRK TGKYQLQPQQ LALPEPEKKF SFEFTEYELQ QLVWLWFAFM RGIVTFQHIE KAFKALGSNM SGDIYGQAYE YLSVYAQQTK S // ID Y1436_HAEIN Reviewed; 106 AA. AC Q57152; O05061; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_1436; GN OrderedLocusNames=HI_1436; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To the N-terminal of E.carotovora exoenzyme regulation CC regulon ORF1. The C-terminal part is colinear with YqcB. CC {ECO:0000305}. CC -!- SIMILARITY: To E.coli YqcC. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23085.1; -; Genomic_DNA. DR PIR; I64171; I64171. DR RefSeq; NP_439587.1; NC_000907.1. DR RefSeq; WP_010869213.1; NC_000907.1. DR ProteinModelPortal; Q57152; -. DR STRING; 71421.HI1436; -. DR EnsemblBacteria; AAC23085; AAC23085; HI_1436. DR GeneID; 950784; -. DR KEGG; hin:HI1436; -. DR PATRIC; 20191573; VBIHaeInf48452_1496. DR eggNOG; ENOG4105WP7; Bacteria. DR eggNOG; COG3098; LUCA. DR OMA; MNTENQV; -. DR OrthoDB; EOG6QCDD7; -. DR PhylomeDB; Q57152; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.20.1440.40; -; 1. DR InterPro; IPR007384; UCP006257. DR InterPro; IPR023376; YqcC-like_dom. DR Pfam; PF04287; DUF446; 1. DR PIRSF; PIRSF006257; UCP006257; 1. DR SUPFAM; SSF158452; SSF158452; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 106 Uncharacterized protein HI_1436. FT /FTId=PRO_0000169327. SQ SEQUENCE 106 AA; 12274 MW; 0955920EBD63228C CRC64; MRNQTKQHLE QLQITMQQLN LWQTMPPAAE AFLSEEPFSI DTMSAEEWLQ WVFIPRMQAL LESGSALPNK IAISPYIEEA MKEFNELQQL LTPLVALEEL XNNNEC // ID Y1446_HAEIN Reviewed; 88 AA. AC P44198; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 2. DT 13-APR-2016, entry version 88. DE RecName: Full=YcgL domain-containing protein HI_1446 {ECO:0000255|HAMAP-Rule:MF_01866}; GN OrderedLocusNames=HI_1446; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 YcgL domain. {ECO:0000255|HAMAP- CC Rule:MF_01866}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23096.1; 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; L42023; AAC23096.1; ALT_INIT; Genomic_DNA. DR PIR; A64030; A64030. DR RefSeq; NP_439598.1; NC_000907.1. DR RefSeq; WP_005693919.1; NC_000907.1. DR ProteinModelPortal; P44198; -. DR STRING; 71421.HI1446; -. DR EnsemblBacteria; AAC23096; AAC23096; HI_1446. DR GeneID; 950564; -. DR KEGG; hin:HI1446; -. DR PATRIC; 20191597; VBIHaeInf48452_1508. DR eggNOG; COG3100; LUCA. DR KO; K09902; -. DR OMA; CAIYKSK; -. DR OrthoDB; EOG61CM3Q; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_01866; UPF0745; 1. DR InterPro; IPR027354; YcgL_dom. DR Pfam; PF05166; YcgL; 1. DR ProDom; PD030374; YcgL_domain; 1. DR PROSITE; PS51648; YCGL; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 88 YcgL domain-containing protein HI_1446. FT /FTId=PRO_0000168857. FT DOMAIN 1 85 YcgL. {ECO:0000255|HAMAP-Rule:MF_01866}. SQ SEQUENCE 88 AA; 10086 MW; FABC22B9EE5B06D0 CRC64; MLCAIYKSKK KLGSYLYVAN REDFSSVPSV LLEHFGKPEL VMMFNLLGRK ALHNVDCNEV LETIKRQGFY LQIAKQDDGL FNSLSEIK // ID Y1454_HAEIN Reviewed; 213 AA. AC P44202; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative cytochrome c-type biogenesis protein HI_1454; GN OrderedLocusNames=HI_1454; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be involved in cytochrome c synthesis. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DsbD 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; L42023; AAC23102.1; -; Genomic_DNA. DR PIR; E64030; E64030. DR RefSeq; NP_439605.1; NC_000907.1. DR RefSeq; WP_005628783.1; NC_000907.1. DR STRING; 71421.HI1454; -. DR EnsemblBacteria; AAC23102; AAC23102; HI_1454. DR GeneID; 950340; -. DR KEGG; hin:HI1454; -. DR PATRIC; 20191611; VBIHaeInf48452_1515. DR eggNOG; ENOG4107QIV; Bacteria. DR eggNOG; COG0785; LUCA. DR KO; K06196; -. DR OMA; FRFSFLY; -. DR OrthoDB; EOG64BQ62; -. DR PhylomeDB; P44202; -. DR Proteomes; UP000000579; 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:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom. DR Pfam; PF02683; DsbD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytochrome c-type biogenesis; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 213 Putative cytochrome c-type biogenesis FT protein HI_1454. FT /FTId=PRO_0000201625. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. SQ SEQUENCE 213 AA; 22789 MW; A4EA5D138DC27305 CRC64; MLDQQLLIGT VFLAGLASFL SPCIFPIIPI YFGILSKGGK KVLNTFLFIL GLSLTFVSLG FSFGFLGNIL FSNTTRIIAG VIVIILGIHQ LGIFKIGLLE RTKLVEIKTS GKSTALEAFV LGLTFSLGWT PCIGPILASV LALSGDEGSA LYGASMMFVY VLGLATPFVL FSFFSDSLLK RAKGLNKHLD KFKIGGGILI IVMGILLITN NFS // ID Y1459_HAEIN Reviewed; 194 AA. AC P45215; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Probable RNA polymerase sigma factor HI_1459; GN OrderedLocusNames=HI_1459; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF 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; L42023; AAC23107.1; -; Genomic_DNA. DR PIR; G64124; G64124. DR RefSeq; NP_439610.2; NC_000907.1. DR ProteinModelPortal; P45215; -. DR STRING; 71421.HI1459; -. DR EnsemblBacteria; AAC23107; AAC23107; HI_1459. DR GeneID; 950350; -. DR KEGG; hin:HI1459; -. DR PATRIC; 20191625; VBIHaeInf48452_1522. DR eggNOG; ENOG4108WQI; Bacteria. DR eggNOG; COG1595; LUCA. DR KO; K03088; -. DR OMA; PEEMMEQ; -. DR OrthoDB; EOG6F299N; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014289; RNA_pol_sigma-24-rel. DR InterPro; IPR014284; RNA_pol_sigma-70_dom. DR InterPro; IPR000838; RNA_pol_sigma70_ECF_CS. DR InterPro; IPR007627; RNA_pol_sigma70_r2. DR InterPro; IPR013249; RNA_pol_sigma70_r4_t2. DR InterPro; IPR013325; RNA_pol_sigma_r2. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04542; Sigma70_r2; 1. DR Pfam; PF08281; Sigma70_r4_2; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR SUPFAM; SSF88946; SSF88946; 1. DR TIGRFAMs; TIGR02943; Sig70_famx1; 1. DR TIGRFAMs; TIGR02937; sigma70-ECF; 1. DR PROSITE; PS01063; SIGMA70_ECF; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Sigma factor; KW Transcription; Transcription regulation. FT CHAIN 1 194 Probable RNA polymerase sigma factor FT HI_1459. FT /FTId=PRO_0000094020. FT DNA_BIND 161 180 H-T-H motif. {ECO:0000250}. FT MOTIF 45 58 Polymerase core binding. SQ SEQUENCE 194 AA; 22843 MW; 9E55F57235B43CE1 CRC64; MSFISYISFK GIKMNVISDL ELQQIRTQML TFAQLQVNQA DLAEDLVQEA FLSAFKNLAN FKRQSAFKTW IFAILKNKII DYLRQKGRFV LESELEDENT NNSFFDEKGH WKPEYHPSEL QGEEETVYSD EFWLIFETCL NCLPAKQAKI FMMREFLELS SEEICQETHL TSSNLHTTLY RARLQLQNCL SKKL // ID Y1474_HAEIN Reviewed; 199 AA. AC Q57213; O05067; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1474; GN OrderedLocusNames=HI_1474; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23122.1; -; Genomic_DNA. DR PIR; I64125; I64125. DR RefSeq; NP_439625.1; NC_000907.1. DR RefSeq; WP_005645090.1; NC_000907.1. DR ProteinModelPortal; Q57213; -. DR STRING; 71421.HI1474; -. DR EnsemblBacteria; AAC23122; AAC23122; HI_1474. DR GeneID; 950574; -. DR KEGG; hin:HI1474; -. DR PATRIC; 20191663; VBIHaeInf48452_1541. DR eggNOG; ENOG4108VEN; Bacteria. DR eggNOG; ENOG4111MPA; LUCA. DR KO; K02017; -. DR OMA; WIAASKT; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; Q57213; -. DR Proteomes; UP000000579; 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 1 199 Uncharacterized ABC transporter ATP- FT binding protein HI_1474. FT /FTId=PRO_0000093208. FT DOMAIN 2 199 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 29 36 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 199 AA; 22737 MW; E3F1EC2BDFA4B1DC CRC64; MLIVQNLQTN ILKSISFSIE KSECLSVVGE SGSGKTTLLN AIAGYIDYSG SILWNNQVLE NNPPWKRNFR YLNQRLYLFP HKTVRGNLIL ANPSASDAEQ QILLSELKID HLINRYPHQL SGGEQQRVAL ARALIYRPDL LLLDEPFSSL DWSSRKDIWK VLKNLIQTNE ITTILVTHEP KEAEYFSGKQ IQLYQGQLI // ID Y1475_HAEIN Reviewed; 119 AA. AC Q57380; O05068; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Putative uncharacterized protein HI_1475; GN OrderedLocusNames=HI_1475; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23128.1; -; Genomic_DNA. DR PIR; A64126; A64126. DR RefSeq; NP_439626.1; NC_000907.1. DR RefSeq; WP_010869220.1; NC_000907.1. DR ProteinModelPortal; Q57380; -. DR STRING; 71421.HI1475; -. DR EnsemblBacteria; AAC23128; AAC23128; HI_1475. DR GeneID; 950353; -. DR KEGG; hin:HI1475; -. DR PATRIC; 20191665; VBIHaeInf48452_1542. DR eggNOG; COG0555; LUCA. DR KO; K02018; -. DR OMA; LELSPFK; -. DR OrthoDB; EOG66XBDW; -. DR PhylomeDB; Q57380; -. DR Proteomes; UP000000579; 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 5: Uncertain; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 119 Putative uncharacterized protein HI_1475. FT /FTId=PRO_0000060282. FT TRANSMEM 51 73 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 91 111 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 1 112 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 119 AA; 13272 MW; 8C3860C51340B6AA CRC64; MVFNMRSTRG IFSSFESGYR FASYTLELSP FKTLIKIEIP MCWKPLVCAS VLAWSRAIGE FGATLMLAGA TRFKTETLPM AVYLNISSGD FEIAIGASLW LLFISSCLLL VLRMINRAV // ID Y1485_HAEIN Reviewed; 73 AA. AC P44212; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Putative uncharacterized protein HI_1485 in Mu-like prophage FluMu region; GN OrderedLocusNames=HI_1485; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23140.1; -; Genomic_DNA. DR PIR; F64031; F64031. DR RefSeq; NP_439635.1; NC_000907.1. DR RefSeq; WP_005693504.1; NC_000907.1. DR STRING; 71421.HI1485; -. DR EnsemblBacteria; AAC23140; AAC23140; HI_1485. DR GeneID; 950356; -. DR KEGG; hin:HI1485; -. DR PATRIC; 20191687; VBIHaeInf48452_1553. DR OMA; KEWAIRR; -. DR OrthoDB; EOG6C2WNT; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020107; Uncharacterised_HI1485. DR ProDom; PD056718; Uncharacterised_HI1485; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 73 Putative uncharacterized protein HI_1485 FT in Mu-like prophage FluMu region. FT /FTId=PRO_0000078069. SQ SEQUENCE 73 AA; 8834 MW; AC20D81B670923FD CRC64; MKTKRPHAKS VENFNRYRFY AEKAAKEEQA GNYEEAETHW DLAMLSASPE NKEWAIRRRD FCQRMHQRPF EGE // ID Y1525_HAEIN Reviewed; 245 AA. AC P71391; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Putative binding protein HI_1525; DE Flags: Precursor; GN OrderedLocusNames=HI_1525; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Probably involved in the binding-dependent system. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein ModA 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; L42023; AAC23171.1; -; Genomic_DNA. DR PIR; B64127; B64127. DR RefSeq; NP_439674.1; NC_000907.1. DR RefSeq; WP_005693547.1; NC_000907.1. DR ProteinModelPortal; P71391; -. DR STRING; 71421.HI1525; -. DR EnsemblBacteria; AAC23171; AAC23171; HI_1525. DR GeneID; 950823; -. DR KEGG; hin:HI1525; -. DR PATRIC; 20191775; VBIHaeInf48452_1596. DR eggNOG; ENOG4107XNE; Bacteria. DR eggNOG; COG0725; LUCA. DR KO; K02020; -. DR OMA; GDIFMPG; -. DR OrthoDB; EOG680X4N; -. DR PhylomeDB; P71391; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015412; F:molybdate transmembrane-transporting ATPase activity; IEA:InterPro. DR InterPro; IPR005950; Mo_ABC_perip-bd. DR PIRSF; PIRSF004846; ModA; 1. DR TIGRFAMs; TIGR01256; modA; 1. PE 1: Evidence at protein level; KW Complete proteome; Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 245 Putative binding protein HI_1525. FT /FTId=PRO_0000031832. SQ SEQUENCE 245 AA; 26765 MW; AB9CA49238C5B8A5 CRC64; MKKLVAVTSM ILTTFSVQAA DLYLYAGAGL KEPVEKIIHQ YEQETGNKVT VEYGGSGQIL ARYNTVKSGD LFLAGSEDYV TKLQKTNDVN NIGTIVLHVP VMAIRKDKIS GIDSFKALAE SSLRLGIGDS KAMALGKGAE KMFELSGYQK QLNDKIVVKA ATVKQLMLYL LNGDVDAAVV GRSGAWKVRD KVELLPSPKG TPEEKVTIGL LFSSKYPKEA QQLFDFFKSP QGVKYFTDEG FLPAK // ID Y152_HAEIN Reviewed; 235 AA. AC P43954; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 81. DE RecName: Full=Putative 4'-phosphopantetheinyl transferase HI_0152; DE EC=2.7.8.-; GN OrderedLocusNames=HI_0152; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May transfer the 4'-phosphopantetheine moiety from CC coenzyme A (CoA) to a serine residue of a carrier protein domain. CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. CC Gsp/Sfp/HetI/AcpT 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; L42023; AAC21831.1; -; Genomic_DNA. DR PIR; H64002; H64002. DR RefSeq; NP_438322.1; NC_000907.1. DR RefSeq; WP_005694435.1; NC_000907.1. DR ProteinModelPortal; P43954; -. DR STRING; 71421.HI0152; -. DR DNASU; 951063; -. DR EnsemblBacteria; AAC21831; AAC21831; HI_0152. DR GeneID; 951063; -. DR KEGG; hin:HI0152; -. DR PATRIC; 20188797; VBIHaeInf48452_0155. DR eggNOG; COG2091; LUCA. DR KO; K06133; -. DR OMA; SWCLREA; -. DR OrthoDB; EOG6JX7GV; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central. DR GO; GO:0018070; P:peptidyl-serine phosphopantetheinylation; IBA:GO_Central. DR Gene3D; 3.90.470.20; -; 2. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_SF. DR Pfam; PF01648; ACPS; 1. DR SUPFAM; SSF56214; SSF56214; 2. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1 235 Putative 4'-phosphopantetheinyl FT transferase HI_0152. FT /FTId=PRO_0000206085. FT METAL 112 112 Magnesium. {ECO:0000250}. FT METAL 114 114 Magnesium. {ECO:0000250}. FT METAL 155 155 Magnesium. {ECO:0000250}. SQ SEQUENCE 235 AA; 27808 MW; CC9B6219BBA561DE CRC64; MTTYIAYGNI NQPFSLESLP DELIPENLYQ IETDSSRVFQ RHQCRRLAHL LLFQLLKIAG KSTALLSQIH RTESGRPYFL DERIDFNISH SGDWVAVILD IRNEEKSAVG IDIEFPKIRN FTALMEHIAP KEEIDWFHHQ QDSLNAFYRC WCLREAVLKS QGFGIVKLSN VRHFPEQQKI FSDYCPQGQL WFTDELPIYL AAFVNHQEKL PHFYEWNRES LQIKELEKYV LYEVN // ID Y1558_HAEIN Reviewed; 267 AA. AC P45252; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 77. DE RecName: Full=UPF0162 protein HI_1558; GN OrderedLocusNames=HI_1558; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0162 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; L42023; AAC23207.1; -; Genomic_DNA. DR PIR; E64172; E64172. DR RefSeq; NP_439707.1; NC_000907.1. DR RefSeq; WP_005654786.1; NC_000907.1. DR STRING; 71421.HI1558; -. DR EnsemblBacteria; AAC23207; AAC23207; HI_1558. DR GeneID; 950418; -. DR KEGG; hin:HI1558; -. DR PATRIC; 20191841; VBIHaeInf48452_1629. DR eggNOG; ENOG41063JG; Bacteria. DR eggNOG; COG2912; LUCA. DR OMA; DGEMWLI; -. DR OrthoDB; EOG6P334F; -. DR PhylomeDB; P45252; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR032698; SirB1_N. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF13371; TPR_9; 1. DR Pfam; PF13369; Transglut_core2; 1. DR SUPFAM; SSF48452; SSF48452; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 267 UPF0162 protein HI_1558. FT /FTId=PRO_0000202384. SQ SEQUENCE 267 AA; 31232 MW; F210A3A19E681E0F CRC64; MKYYRRALYD KFVHFYLVIS DDGSSEAQLR GKMGGLVRKA RKKISPDWPK EEQIHQLLQL FYGDWGFHCD PEDYFYARNL YLPYVFEHRQ GMPVTLGAMV FYLAEALDLP IYPVNFPTQL ILRAEVRDEV AFIDPWDGTY ISQEKLQQLY EGAFGFGAKI QPEELDRADL SLLYSRFEQL AKNALIREEH NDMAYHYIKN LMITDAENPY HIRDRGLVLA QMGAYPSALK DLEFFVEHCP KDPTAAFIRT QLLELKGEIN KDTFPLH // ID Y1603_HAEIN Reviewed; 226 AA. AC P44271; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 82. DE RecName: Full=UPF0111 protein HI_1603; GN OrderedLocusNames=HI_1603; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0111 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23247.1; -; Genomic_DNA. DR PIR; B64038; B64038. DR RefSeq; NP_439745.1; NC_000907.1. DR RefSeq; WP_005647270.1; NC_000907.1. DR ProteinModelPortal; P44271; -. DR SMR; P44271; 13-225. DR STRING; 71421.HI1603; -. DR EnsemblBacteria; AAC23247; AAC23247; HI_1603. DR GeneID; 950838; -. DR KEGG; hin:HI1603; -. DR PATRIC; 20191937; VBIHaeInf48452_1676. DR eggNOG; ENOG4107IX6; Bacteria. DR eggNOG; COG1392; LUCA. DR KO; K07220; -. DR OMA; WVGDLAD; -. DR OrthoDB; EOG6QVRHT; -. DR PhylomeDB; P44271; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR002727; DUF47. DR InterPro; IPR018445; Put_Phosphate_transp_reg. DR Pfam; PF01865; PhoU_div; 1. DR TIGRFAMs; TIGR00153; TIGR00153; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 226 UPF0111 protein HI_1603. FT /FTId=PRO_0000154909. SQ SEQUENCE 226 AA; 26483 MW; B4ECE15DE005C903 CRC64; MAMNNILGLF AHSPLKPLQK HSEKVTECSD LLIPFFQTTF SKNWEQAEEK RLEISQCERE ADSLKREIRL KLPRGLFLPI DRTDLLELVT QQDKLANYAK DIAGRMIGRQ FGIPEEMQEE FLHYVKRSLD AIHQAHRVIE EMDKLLETGF KGRELKLVND MIQELDSIED DTDQMQIKLR KMLYTIESRY NPIDVMFLYK IIEWVGVLAD QAQRVGSRIE LMLARS // ID Y1632_HAEIN Reviewed; 121 AA. AC Q57525; O05078; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Putative inactive aspartokinase 3 HI_1632; GN OrderedLocusNames=HI_1632; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. This protein lacks CC the central 330 residues found in AKIII, including a number of CC amino acids known to be important for function in E.coli. 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; L42023; AAC23284.1; -; Genomic_DNA. DR PIR; F64133; F64133. DR RefSeq; NP_439774.1; NC_000907.1. DR RefSeq; WP_005693641.1; NC_000907.1. DR ProteinModelPortal; Q57525; -. DR SMR; Q57525; 6-63. DR STRING; 71421.HI1632; -. DR DNASU; 950850; -. DR EnsemblBacteria; AAC23284; AAC23284; HI_1632. DR GeneID; 950850; -. DR KEGG; hin:HI1632; -. DR PATRIC; 20192007; VBIHaeInf48452_1707. DR eggNOG; COG0527; LUCA. DR OMA; DAMTACA; -. DR OrthoDB; EOG6M0T34; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004072; F:aspartate kinase activity; IEA:InterPro. DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR018042; Aspartate_kinase_CS. DR Pfam; PF00696; AA_kinase; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Putative inactive aspartokinase 3 FT HI_1632. FT /FTId=PRO_0000066691. SQ SEQUENCE 121 AA; 12951 MW; 628E132F6FF5B79D CRC64; MPYLSVAKFG GTSVANHDAM TACAKIVIAD PNTRVVVLSA SAGVTNLLVA LANGVKATER EKLIGNDLHI TSGVAKRIFD TVQSYNVRMI SYGASTNNVC MLVQSEHSDE IVRSLHKSLF E // ID Y1643_HAEIN Reviewed; 338 AA. AC P45290; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=UPF0324 membrane protein HI_1643; GN OrderedLocusNames=HI_1643; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0324 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; L42023; AAC23290.1; -; Genomic_DNA. DR PIR; E64173; E64173. DR RefSeq; NP_439785.1; NC_000907.1. DR RefSeq; WP_005693652.1; NC_000907.1. DR STRING; 71421.HI1643; -. DR EnsemblBacteria; AAC23290; AAC23290; HI_1643. DR GeneID; 950484; -. DR KEGG; hin:HI1643; -. DR PATRIC; 20192031; VBIHaeInf48452_1719. DR eggNOG; ENOG4105HMI; Bacteria. DR eggNOG; COG2855; LUCA. DR KO; K19239; -. DR OMA; FTIFVVY; -. DR OrthoDB; EOG65QWM8; -. DR PhylomeDB; P45290; -. DR Proteomes; UP000000579; 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; IPR004630; UPF0324_bac. DR InterPro; IPR018383; UPF0324_pro. DR PANTHER; PTHR30106; PTHR30106; 1. DR Pfam; PF03601; Cons_hypoth698; 1. DR TIGRFAMs; TIGR00698; TIGR00698; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 338 UPF0324 membrane protein HI_1643. FT /FTId=PRO_0000157420. FT TRANSMEM 5 23 Helical. {ECO:0000255}. FT TRANSMEM 33 55 Helical. {ECO:0000255}. FT TRANSMEM 62 84 Helical. {ECO:0000255}. FT TRANSMEM 94 116 Helical. {ECO:0000255}. FT TRANSMEM 123 145 Helical. {ECO:0000255}. FT TRANSMEM 155 177 Helical. {ECO:0000255}. FT TRANSMEM 222 239 Helical. {ECO:0000255}. FT TRANSMEM 254 273 Helical. {ECO:0000255}. FT TRANSMEM 280 302 Helical. {ECO:0000255}. FT TRANSMEM 312 334 Helical. {ECO:0000255}. SQ SEQUENCE 338 AA; 36721 MW; 2507CDC3AB251E89 CRC64; MNTRPFYFGL IFIAIIAVLA NYLGSTDFSH HYHISALIIA ILLGMAIGNT IYPQFSSQVE KGVLFAKGTL LRAGIVLYGF RLTFGDIADV GLNAVVTDAI MLISTFFLTA LLGIRYLKMD KQLVYLTGAG CSICGAAAVM AAEPVTKAES HKVSVAIAVV VIFGTLSIFT YPFFYTWSQH LINAHQFGIY VGSSVHEVAQ VYAIGGNIDP IVANTAVITK MLRVMMLAPF LFMLSWLLTR SDGISENTSH KITIPWFAVL FIGVAIFNSF DLLPKELVKL FVEIDSFLLI SAMAALGLTT QASAIKKAGL KPLVLGVLIY LWLVIGGFLV NYGISKLI // ID Y1651_HAEIN Reviewed; 92 AA. AC P44282; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein HI_1651; GN OrderedLocusNames=HI_1651; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23304.1; -; Genomic_DNA. DR PIR; D64039; D64039. DR RefSeq; NP_439793.1; NC_000907.1. DR RefSeq; WP_005694377.1; NC_000907.1. DR STRING; 71421.HI1651; -. DR EnsemblBacteria; AAC23304; AAC23304; HI_1651. DR GeneID; 950855; -. DR KEGG; hin:HI1651; -. DR PATRIC; 20192047; VBIHaeInf48452_1727. DR eggNOG; COG2198; LUCA. DR OMA; IIEMNDN; -. DR OrthoDB; EOG6K9QK9; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR Gene3D; 1.20.120.160; -; 1. DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom. DR SUPFAM; SSF47226; SSF47226; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 92 Uncharacterized protein HI_1651. FT /FTId=PRO_0000078104. SQ SEQUENCE 92 AA; 10748 MW; 846A8F5355CC8FA7 CRC64; MDGILRKLIS IKDLHHCLQK FFVDERESII EMNDNKLSEQ FDLALIETHG KSKILKNLSL FKQTMSNYLT QLSKDNMKET ENTVHKIKRV AA // ID Y1695_HAEIN Reviewed; 267 AA. AC Q48215; O05081; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized glycosyltransferase HI_1695; DE EC=2.4.-.-; GN OrderedLocusNames=HI_1695; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; M94855; AAA24983.1; -; Genomic_DNA. DR EMBL; L42023; AAC23341.1; -; Genomic_DNA. DR PIR; C64175; C64175. DR RefSeq; NP_439837.2; NC_000907.1. DR ProteinModelPortal; Q48215; -. DR STRING; 71421.HI1695; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC23341; AAC23341; HI_1695. DR GeneID; 950753; -. DR KEGG; hin:HI1695; -. DR PATRIC; 20192141; VBIHaeInf48452_1774. DR eggNOG; ENOG4108RYC; Bacteria. DR eggNOG; COG0463; LUCA. DR OMA; DYYLWIK; -. DR OrthoDB; EOG6T4S25; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 267 Uncharacterized glycosyltransferase FT HI_1695. FT /FTId=PRO_0000059233. FT CONFLICT 26 26 V -> G (in Ref. 1; AAA24983). FT {ECO:0000305}. FT CONFLICT 46 46 D -> E (in Ref. 1; AAA24983). FT {ECO:0000305}. FT CONFLICT 49 49 F -> S (in Ref. 1; AAA24983). FT {ECO:0000305}. SQ SEQUENCE 267 AA; 30770 MW; A2F1A0532737D8C3 CRC64; MKFSVLMSLY IKENPQFLRE CFESLVAQTR QADEIVLVFD GVVTPDLEFV VTEFETKLPL KLVKLPQNRG LGKALNEGLL HCDYDWVFRM DTDDICVPDR FEKQVAFIEQ HPESIIFGGQ IAEFGKNVND IVAYRNVPTS AQEIIKFTQK RCPFNHMTVA YQKSAVINCG GYEDLQEDYY LWIKLVAQGL YMANLPDILV YARVGNGMVS RRRGVNQAKA EWRLFKLKYR LGIQGLLSGL FTFALRFGSR LLPTSLLKKL YQTFLRK // ID Y1698_HAEIN Reviewed; 353 AA. AC O05083; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized glycosyltransferase HI_1698; DE EC=2.4.-.-; GN OrderedLocusNames=HI_1698; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 4 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; L42023; AAC23344.1; -; Genomic_DNA. DR PIR; F64175; F64175. DR RefSeq; NP_439840.1; NC_000907.1. DR RefSeq; WP_005694187.1; NC_000907.1. DR ProteinModelPortal; O05083; -. DR STRING; 71421.HI1698; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAC23344; AAC23344; HI_1698. DR GeneID; 950521; -. DR KEGG; hin:HI1698; -. DR PATRIC; 20192147; VBIHaeInf48452_1777. DR eggNOG; ENOG4105CG5; Bacteria. DR eggNOG; COG0438; LUCA. DR OMA; HILWEHY; -. DR OrthoDB; EOG68DD33; -. DR PhylomeDB; O05083; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Membrane; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 353 Uncharacterized glycosyltransferase FT HI_1698. FT /FTId=PRO_0000080317. FT TRANSMEM 267 287 Helical. {ECO:0000255}. SQ SEQUENCE 353 AA; 40005 MW; 27260B90A1DFB398 CRC64; MKKIGFFIMN IGSAGGTERV SINVANALAK QGYDVSFISI GGNKPFFQVD EKINIYAMNK LPYSLKKDYF SITKKLRELV KELQLDTLIV VDGAIMLFSA LALVNLNIKH ILWEHYSFNF TGNRLVRTLG KYLAVTTCDK IVTLTEAEKT LWQEKFKTNN IISIANPNTL LPKNKLAKLE NKTILSVGHL FSYKGFDYLL KVWQVLAKKY PDWNLKIVGS GEEEENLKNL AKALDIEDSV NFIPRTNDVS FYYESSSIYC LPSQTEGLPL VVIEAMAFGL PIVAFNCSPG VKQLVEHKEN GFLCEQNNIE EMVKGLDLLI NNPELYLQMS DKSRLMSEDY GIEKIIEEWK GIL // ID Y1701_HAEIN Reviewed; 247 AA. AC P44292; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Uncharacterized protein HI_1701; GN OrderedLocusNames=HI_1701; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23347.1; -; Genomic_DNA. DR PIR; E64040; E64040. DR RefSeq; NP_439843.1; NC_000907.1. DR RefSeq; WP_005694191.1; NC_000907.1. DR ProteinModelPortal; P44292; -. DR STRING; 71421.HI1701; -. DR EnsemblBacteria; AAC23347; AAC23347; HI_1701. DR GeneID; 949784; -. DR KEGG; hin:HI1701; -. DR PATRIC; 20192153; VBIHaeInf48452_1780. DR eggNOG; ENOG41080C8; Bacteria. DR eggNOG; COG1434; LUCA. DR OMA; WLGYWKE; -. DR OrthoDB; EOG69WFMM; -. DR PhylomeDB; P44292; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR003848; DUF218. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02698; DUF218; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 247 Uncharacterized protein HI_1701. FT /FTId=PRO_0000078106. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. SQ SEQUENCE 247 AA; 27612 MW; 8242407AB6F8D739 CRC64; MLELGKLLTA LIAPPLNTFV LLIIAAIIYC VHFKKLAKFI AIISFTWLYI MSAPFTGLLL TNNDDSPALT LDEYKQAQAI VILGGGSYQT KELYAETASG APQLERLRYA AFLQKETGLP ILTTGYSLIG ISEGDLMAKE LNQFFNVPTQ WIENKARNTE ENASFTKNIL IKDHIQKIIL VTNQWHMKRA KYLFEKQGFD VLPAAAASYG SKGNLSAKSF IPDLGALNSN MVLLKEWIGY WKAHYVE // ID Y195A_HAEIN Reviewed; 1111 AA. AC Q57362; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=Uncharacterized MscS family protein HI_0195.1; DE Flags: Precursor; GN OrderedLocusNames=HI_0195.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) 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; L42023; AAC21864.1; -; Genomic_DNA. DR RefSeq; NP_438364.1; NC_000907.1. DR RefSeq; WP_010868954.1; NC_000907.1. DR ProteinModelPortal; Q57362; -. DR STRING; 71421.HI0195.1; -. DR PRIDE; Q57362; -. DR EnsemblBacteria; AAC21864; AAC21864; HI_0195.1. DR GeneID; 951104; -. DR KEGG; hin:HI0195.1; -. DR PATRIC; 20188887; VBIHaeInf48452_0200. DR eggNOG; ENOG4105EGS; Bacteria. DR eggNOG; COG3264; LUCA. DR KO; K05802; -. DR OMA; LHTPKAI; -. DR OrthoDB; EOG6J1DC5; -. DR PhylomeDB; Q57362; -. DR Proteomes; UP000000579; 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:0009992; P:cellular water homeostasis; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR011066; MscC_channel_C. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR006686; MscS_channel_CS. DR InterPro; IPR011014; MscS_channel_TM-2. DR InterPro; IPR025692; MscS_IM_dom1. DR InterPro; IPR024393; MscS_porin. DR Pfam; PF00924; MS_channel; 1. DR Pfam; PF12795; MscS_porin; 1. DR Pfam; PF12794; MscS_TM; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82689; SSF82689; 1. DR SUPFAM; SSF82861; SSF82861; 1. DR PROSITE; PS01246; UPF0003; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 31 {ECO:0000255}. FT CHAIN 32 1111 Uncharacterized MscS family protein FT HI_0195.1. FT /FTId=PRO_0000036181. FT TRANSMEM 490 510 Helical. {ECO:0000255}. FT TRANSMEM 538 558 Helical. {ECO:0000255}. FT TRANSMEM 572 592 Helical. {ECO:0000255}. FT TRANSMEM 620 640 Helical. {ECO:0000255}. FT TRANSMEM 644 664 Helical. {ECO:0000255}. FT TRANSMEM 694 714 Helical. {ECO:0000255}. FT TRANSMEM 797 817 Helical. {ECO:0000255}. FT TRANSMEM 840 860 Helical. {ECO:0000255}. FT TRANSMEM 885 905 Helical. {ECO:0000255}. FT TRANSMEM 922 942 Helical. {ECO:0000255}. FT TRANSMEM 1003 1023 Helical. {ECO:0000255}. SQ SEQUENCE 1111 AA; 126826 MW; 15DF8F9F7E4E701C CRC64; MIRKLMKIPP FFTALFASAM FTLSVSQGVL AANSTNVLPT EQSLKADLAN AQKMSEGEAK NRLLAELQTS IDLLQQIQAQ QKINDALQTT LSHSESEIRK NNAEIQALKK QQETATSTDD NAQSQDYLQN SLTKLNDQLQ DTQNALSTAN AQLAGQSSIS ERAQAALTEN VVRTQQINQQ LANNDIGSTL RKQYQIDLQL IDLKNSYNQN LLKNNDQLSL LYQSRYNLLN LRLQVQQQNI IAIQEVINQK NLQQSQNQVE QAQQQQKTVQ NDYIQKELDR NAQLGQYLLQ QTEKANSLTQ DELRMRNILD SLTQTQRTID EQISALQGTL VLSRIIQQQK QKLPTNLNIQ GLSKQIADLR VHIFDITQKR NELYDLDNYI NKVESEDGKQ FTEAERTQVK TLLTERRKMT SDLIKSLNNQ LNLAISLELT QLQITQISDQ IQSKLEQQSF WVKSNNPINL DWVKMLPRAL IEQFNGMLKK LGFPTNYDNL PYLLMYFLGL FIVGGAIFKF KNRIKQQLNK INREIHRLDT DSQWSTPLAL LLTAFLTLSS TLWFLAVCQM IGFFFFKNPE EFWHWSFSMA GYWWFFTFWI SLFRPNGIFV NHFESSKENA QRFRGVIQRI IVVVVLLLNT SVFSNVTDAG LANDVLGQIN TIAALIFCAA IIAPRFNRVL RSYEPETNKH HWLIRIVQIG FRLIPVGLIV LIVLGYYYTA LNLIEHFIHS YIAWCVWWLV RNTIYRGITV SSRRLAHRRL AEKRRQKALE NNYENISSDD VVAVGEPEES LALNDVRSQL LRFVDLFIWT ALLGIFYYVW SDLVTVVSYL REITLWQQTT TTDAGTVMES ITLFNLLVAL VIVGITYVLV RNISGILEVL IFSRVNLSQG TPYTITTLLT YIFIAIGGAW AFATLGMSWS KLQWLFAALS VGLGFGMQEI FANFVSGIIL LFERPIRVGD VVTINEVSGT VAKIRIRAIT LIDFDRKEVI VPNKSFVTGQ VTNWALSNTM TRLVISVGVA YGSDLTLVRQ LLLQAADEQP TILRDPKPSA YFLTFGASTL DHELRVYVEQ VGDRTSTTDA LNRRINELFA EHNIDIAFNQ LDVFIKNNDT GEEIPFVDVK K // ID Y1010_HAEIN Reviewed; 301 AA. AC P44979; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=Uncharacterized oxidoreductase HI_1010; DE EC=1.1.-.-; GN OrderedLocusNames=HI_1010; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the 3-hydroxyisobutyrate dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22671.1; -; Genomic_DNA. DR PIR; B64164; B64164. DR RefSeq; NP_439171.1; NC_000907.1. DR RefSeq; WP_005665973.1; NC_000907.1. DR ProteinModelPortal; P44979; -. DR STRING; 71421.HI1010; -. DR EnsemblBacteria; AAC22671; AAC22671; HI_1010. DR GeneID; 950607; -. DR KEGG; hin:HI1010; -. DR PATRIC; 20190683; VBIHaeInf48452_1054. DR eggNOG; ENOG4105ZXK; Bacteria. DR eggNOG; COG2084; LUCA. DR KO; K08319; -. DR OMA; AVIKIFP; -. DR OrthoDB; EOG6XDH0X; -. DR PhylomeDB; P44979; -. DR BioCyc; RETL1328306-WGS:GSTH-4807-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR015815; HIBADH-related. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR029154; NADP-bd. DR Pfam; PF14833; NAD_binding_11; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000103; HIBADH; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 301 Uncharacterized oxidoreductase HI_1010. FT /FTId=PRO_0000173063. FT NP_BIND 9 23 NAD. {ECO:0000250}. FT ACT_SITE 177 177 {ECO:0000250}. FT BINDING 101 101 NAD. {ECO:0000250}. FT BINDING 245 245 NAD. {ECO:0000250}. SQ SEQUENCE 301 AA; 31035 MW; 7C615A25B0947D18 CRC64; MENQNYSVAV IGLGSMGMGA AVSCINAGLT TYGIDLNPVA LEKLKAAGAK AVAANGYDFA HELDAVVILV VNAAQANAVL FGENGIAKKL KAGTAVMVSS TMAAQDAQII SQKLTELGLI MLDAPVSGGA AKALKGEMTV MASGSKQAFE LLQPVLDATA AKVYNIGEEI GLGATVKIVH QLLAGVHIAA GAEAMALASK AGIPLDVMYD VVTNAAGNSW MFENRMKHVV EGDYTPLSMV DIFVKDLGLV NDTAKSLHFP LHLASTAYSM FTEASNAGYG KEDDSAVIKI FSGVSLPKKG A // ID Y1014_HAEIN Reviewed; 315 AA. AC P44094; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_1014; GN OrderedLocusNames=HI_1014; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22675.1; -; Genomic_DNA. DR PIR; D64018; D64018. DR RefSeq; NP_439175.1; NC_000907.1. DR RefSeq; WP_005693350.1; NC_000907.1. DR ProteinModelPortal; P44094; -. DR STRING; 71421.HI1014; -. DR EnsemblBacteria; AAC22675; AAC22675; HI_1014. DR GeneID; 950006; -. DR KEGG; hin:HI1014; -. DR PATRIC; 20190691; VBIHaeInf48452_1058. DR eggNOG; ENOG4105EXW; Bacteria. DR eggNOG; COG0451; LUCA. DR OMA; RWDTTRA; -. DR OrthoDB; EOG693GQC; -. DR PhylomeDB; P44094; -. DR BioCyc; RETL1328306-WGS:GSTH-4338-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 315 Uncharacterized protein HI_1014. FT /FTId=PRO_0000077991. SQ SEQUENCE 315 AA; 35145 MW; 51595A24A5B54823 CRC64; MKVVITGGQG FLGQRLAKTL LAQNNVHIDD LILIDVVKPI APNNDPRVRC YEMNLRYPTG LDELITEETD AIFHLAAIVS SHAEQDPDLG YETNFLATRN ILEICRKNNP KVRFIFSSSL AIFGGELPET ILDSTAFTPQ STYGTQKAMC ELLINDYSRK GFVDGIVVRL PTICIRPGKP NKAASSFVSS IMREPLHGED AVCPVSEELR LWLSSPNTVV ANFIHALQLP SLPLRSWHTI NLPGFSVTVK QMLSDLTQVK GEAILEHIKF EFDESINNIV ASWPSRIDNT QALALGFKVD SNFQNVIQQF IEYDM // ID Y1051_HAEIN Reviewed; 614 AA. AC Q57180; O05043; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 112. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1051; GN OrderedLocusNames=HI_1051; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22709.1; -; Genomic_DNA. DR PIR; A64180; A64180. DR RefSeq; NP_439210.1; NC_000907.1. DR RefSeq; WP_005686318.1; NC_000907.1. DR ProteinModelPortal; Q57180; -. DR STRING; 71421.HI1051; -. DR EnsemblBacteria; AAC22709; AAC22709; HI_1051. DR GeneID; 950028; -. DR KEGG; hin:HI1051; -. DR PATRIC; 20190767; VBIHaeInf48452_1096. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K18893; -. DR OMA; IKFEHVD; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; Q57180; -. DR BioCyc; RETL1328306-WGS:GSTH-2033-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-3084-MONOMER; -. DR Proteomes; UP000000579; 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:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Membrane; KW Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 614 Uncharacterized ABC transporter ATP- FT binding protein HI_1051. FT /FTId=PRO_0000093203. FT TRANSMEM 41 61 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 87 107 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 157 177 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 178 198 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 43 330 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 364 603 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 397 404 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 614 AA; 68399 MW; 306BBA9646921EA0 CRC64; MFNKIFSWFE NRLNPYPESN PTTPKKGLFR FIWSSITGMK GWIFLLAILT VGTGVMEAVL FQFMGTLVDW LGTFTPERLW QEKSHLLIGM AALLLISIVW GFLASAVHLQ TLQGVFPMRL RWNFHRLMLG QSLSFYQDEF AGRVSAKVMQ TALAVRDTVL TLANMFVYVL VYFITSGVVL VALDSWFLLP FITWIILFGL ILRTLIPKLS KTAQRQADAR SLMTGRITDA YSNIATVKLF SHGSREATYA KRSMQDFMVT VHAQMRLATS LDTLTYATNI LLTLSTAILG IILWKNGQVG VGAIATATAM ALRVNGLSRW IMWESARLFE NIGTVNDGMN TLTKPHTIVD KPQASPLQVK QGEIKFNDIT FAYDPTKPLL NHFNLTIKPG EKVGLIGRSG AGKSTIVNLL LRFYEAQQGE ITIDGQNVLN VQQESLRRQI GLVTQDTSLL HRSVRDNIIY GRPNATDEEM VLAAERAEAA DFIPFLSDSQ GRKGYDAHVG ERGVKLSGGQ RQRIAIARVM LKDAPILLLD EATSALDSEV EVAIQESLDK MMENKTVIAI AHRLSTIAAM DRLIVLDKGQ IVEQGTHAEL LELNGLYAKL WNHQSGGFLS ESAE // ID Y1052_HAEIN Reviewed; 298 AA. AC P45008; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1052; GN OrderedLocusNames=HI_1052; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH araC/xylS-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00593}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22711.1; -; Genomic_DNA. DR PIR; B64180; B64180. DR RefSeq; NP_439211.1; NC_000907.1. DR RefSeq; WP_005665936.1; NC_000907.1. DR ProteinModelPortal; P45008; -. DR STRING; 71421.HI1052; -. DR DNASU; 950029; -. DR EnsemblBacteria; AAC22711; AAC22711; HI_1052. DR GeneID; 950029; -. DR KEGG; hin:HI1052; -. DR PATRIC; 20190769; VBIHaeInf48452_1097. DR eggNOG; ENOG4105E7U; Bacteria. DR eggNOG; ENOG4111N2I; LUCA. DR KO; K18991; -. DR OMA; EATFHIV; -. DR OrthoDB; EOG690MBW; -. DR PhylomeDB; P45008; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR Gene3D; 2.60.120.280; -; 1. DR InterPro; IPR003313; AraC-bd. DR InterPro; IPR032783; AraC_lig. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR InterPro; IPR018062; HTH_AraC-typ_CS. DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type. DR Pfam; PF12852; Cupin_6; 1. DR Pfam; PF12833; HTH_18; 1. DR PRINTS; PR00032; HTHARAC. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 2. DR SUPFAM; SSF51215; SSF51215; 1. DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 298 Uncharacterized HTH-type transcriptional FT regulator HI_1052. FT /FTId=PRO_0000194619. FT DNA_BIND 213 232 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00593}. SQ SEQUENCE 298 AA; 34291 MW; 287C984ABA078BF4 CRC64; MDYLDKLTHL AQVRGEINIR CEFQGEWQIS HQEKDAGKGI FHLIEQGECW LTLNEKQFHL KEGDVFFLPQ NQPHSMHYSA NKRADIPTKK SHQGLFELHQ IGRGTPDLKM FCGNFYYQQD ALLTASMPEY LHINLCDTPI HPLVQLFLQE AQKNDAGTKS VVDALSNVLL IYILRHAIQQ NLIEQGILFA LQDKRLNTAL IAILQQPQND WHIEQLAELA TMSRANFIRI FQQHIGMSPG RFLTKVRLQS AAFLLKQSQQ SVLAIALEVG YQSEAHFCKV FKNYYQLSPS QYRKSVSL // ID Y1074_HAEIN Reviewed; 150 AA. AC P44110; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=UPF0756 membrane protein HI_1074 {ECO:0000255|HAMAP-Rule:MF_01874}; GN OrderedLocusNames=HI_1074; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01874}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01874}. CC -!- SIMILARITY: Belongs to the UPF0756 family. {ECO:0000255|HAMAP- CC Rule:MF_01874}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22730.1; -; Genomic_DNA. DR PIR; B64020; B64020. DR RefSeq; NP_439230.1; NC_000907.1. DR RefSeq; WP_005693397.1; NC_000907.1. DR STRING; 71421.HI1074; -. DR EnsemblBacteria; AAC22730; AAC22730; HI_1074. DR GeneID; 950048; -. DR KEGG; hin:HI1074; -. DR PATRIC; 20190807; VBIHaeInf48452_1116. DR eggNOG; ENOG4108VMM; Bacteria. DR eggNOG; COG2707; LUCA. DR OMA; SKGINWG; -. DR OrthoDB; EOG67DPST; -. DR PhylomeDB; P44110; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01874; UPF0756; 1. DR InterPro; IPR007382; UPF0756_TM. DR Pfam; PF04284; DUF441; 1. DR ProDom; PD021096; DUF441_TM; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 150 UPF0756 membrane protein HI_1074. FT /FTId=PRO_0000169022. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 52 72 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 81 101 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 123 143 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. SQ SEQUENCE 150 AA; 15479 MW; B0C6440A7FA95B9F CRC64; MTLQLNTIAL LLVILLILGV LSNNSTITIS AAVLLIMQQT FLSSHIPLLE KYGVKIGIII LTIGVLSPLV SGKIQLPDLS GFLSWKMALS ISVGVLVAWL AGKGVPLMGE QPILVTGLLI GTIIGVAFLG GIPVGPLIAA GILALLLGKI // ID Y1078_HAEIN Reviewed; 257 AA. AC P45022; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Probable amino-acid ABC transporter ATP-binding protein HI_1078; GN OrderedLocusNames=HI_1078; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system for an amino acid. Probably responsible for energy coupling CC to the transport system. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22734.1; -; Genomic_DNA. DR PIR; G64181; G64181. DR RefSeq; NP_439235.2; NC_000907.1. DR ProteinModelPortal; P45022; -. DR SMR; P45022; 1-245. DR STRING; 71421.HI1078; -. DR EnsemblBacteria; AAC22734; AAC22734; HI_1078. DR GeneID; 950054; -. DR KEGG; hin:HI1078; -. DR PATRIC; 20190821; VBIHaeInf48452_1123. DR eggNOG; ENOG4105CDA; Bacteria. DR eggNOG; COG1126; LUCA. DR KO; K10010; -. DR OMA; ELANNGM; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015424; F:amino acid-transporting ATPase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR030679; ABC_ATPase_HisP-typ. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW Amino-acid transport; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 257 Probable amino-acid ABC transporter ATP- FT binding protein HI_1078. FT /FTId=PRO_0000093204. FT DOMAIN 4 244 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 257 AA; 28895 MW; C54633598117C0D7 CRC64; MSMLKVSNIQ KNFNGNHVLK GIDFEINKGE VVAILGPSGS GKTTFLRCLN LLERPEQGIL EFTDGSLKID FSQKISKADE LKLRRRSSMV FQQYNLFPHR SALENVMEGM VVVQKQDKAQ AREKALSLLE KVGLKNKADL FPSQLSGGQQ QRVGIARALA VKPDIILLDE PTSALDPELV GEVLQTLKML AQEGWTMIIV THEMQFAKDV ADRVILMADG HIVEQNTADK FFTCPQHERT KQFLLQAKIP LELDYYI // ID Y1099_HAEIN Reviewed; 102 AA. AC P44112; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_1099; GN OrderedLocusNames=HI_1099; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22755.1; -; Genomic_DNA. DR PIR; D64020; D64020. DR RefSeq; NP_439256.1; NC_000907.1. DR RefSeq; WP_005693422.1; NC_000907.1. DR EnsemblBacteria; AAC22755; AAC22755; HI_1099. DR GeneID; 950069; -. DR KEGG; hin:HI1099; -. DR PATRIC; 20190865; VBIHaeInf48452_1145. DR OMA; VESAQMD; -. DR OrthoDB; EOG6FBX1M; -. DR Proteomes; UP000000579; 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 HI_1099. FT /FTId=PRO_0000078003. FT TRANSMEM 7 23 Helical. {ECO:0000255}. SQ SEQUENCE 102 AA; 11601 MW; 63FF8D8FC466E782 CRC64; MYLMRKIVFV SCVILGLAAC SSQPEQIGGG VYDMKTVQEY NARVISGNTV TQTQKDKITQ QIDTSLKLNQ SDNKVKTRTR RVLPVLPVTP SVGYHYNYHY FR // ID Y1126_HAEIN Reviewed; 76 AA. AC P44114; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_1126; GN OrderedLocusNames=HI_1126; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22780.1; -; Genomic_DNA. DR PIR; F64020; F64020. DR EnsemblBacteria; AAC22780; AAC22780; HI_1126. DR OMA; CRRKISE; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR018886; UPF0547. DR Pfam; PF10571; UPF0547; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 76 Uncharacterized protein HI_1126. FT /FTId=PRO_0000078005. FT TRANSMEM 53 70 Helical. {ECO:0000255}. SQ SEQUENCE 76 AA; 9084 MW; 7801594E36BACF47 CRC64; MSLTRCPECR KKISENAENC PNCGFSFKQK DLEMYKQRLE ARRLHNEEVN RKSTKLHIIW FCIFAIFIAV TSWMVN // ID Y1127_HAEIN Reviewed; 138 AA. AC O86234; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 17-FEB-2016, entry version 66. DE RecName: Full=Uncharacterized protein HI_1127; GN OrderedLocusNames=HI_1127; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC22782.1; -; Genomic_DNA. DR EnsemblBacteria; AAC22782; AAC22782; HI_1127. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0031669; P:cellular response to nutrient levels; IBA:GO_Central. DR InterPro; IPR025299; CstA_C. DR Pfam; PF13722; CstA_5TM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 138 Uncharacterized protein HI_1127. FT /FTId=PRO_0000078006. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. SQ SEQUENCE 138 AA; 15599 MW; 8833E1195A6184EC CRC64; MLHAKVVYDS SLHFLGFIGG IFAILGVIVL PITSGDTAFR AARLQIAEIF NVDQRSLPKR LLIAVPLFVL GYFISTIDFS VLWRYFTWAN QMTAMVMLWT AAGYLYRYHK FHWVASLPAW FITTVCALIC STTKLVSA // ID Y112_HAEIN Reviewed; 98 AA. AC P71339; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_0112; GN OrderedLocusNames=HI_0112; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the IS150/IS1296 orfA 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; L42023; AAC21791.1; -; Genomic_DNA. DR PIR; A64143; A64143. DR RefSeq; NP_438286.1; NC_000907.1. DR RefSeq; WP_005672023.1; NC_000907.1. DR STRING; 71421.HI0112; -. DR EnsemblBacteria; AAC21791; AAC21791; HI_0112. DR GeneID; 951016; -. DR KEGG; hin:HI0112; -. DR PATRIC; 20188693; VBIHaeInf48452_0116. DR eggNOG; COG2963; LUCA. DR KO; K07483; -. DR OMA; KARYFYL; -. DR OrthoDB; EOG64NB0S; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR SUPFAM; SSF46689; SSF46689; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein HI_0112. FT /FTId=PRO_0000077890. SQ SEQUENCE 98 AA; 11900 MW; E08384A9AD4DF38F CRC64; MIKARYFYLY KLIVRCRFFI AKYNTLFKQQ VIEFYIQNGK NYSLISKHFQ LDSRTLRHWI NQFNHSRING LAVLGKTRNY SLKFKLNVIQ TVKNGQFL // ID Y1151_HAEIN Reviewed; 178 AA. AC P45076; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=UPF0307 protein HI_1151; GN OrderedLocusNames=HI_1151; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0307 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; L42023; AAC22806.1; -; Genomic_DNA. DR PIR; C64168; C64168. DR RefSeq; NP_439309.1; NC_000907.1. DR RefSeq; WP_005651852.1; NC_000907.1. DR ProteinModelPortal; P45076; -. DR STRING; 71421.HI1151; -. DR EnsemblBacteria; AAC22806; AAC22806; HI_1151. DR GeneID; 949961; -. DR KEGG; hin:HI1151; -. DR PATRIC; 20190977; VBIHaeInf48452_1201. DR eggNOG; ENOG4105N42; Bacteria. DR eggNOG; COG3028; LUCA. DR KO; K09889; -. DR OMA; QKAPWEE; -. DR OrthoDB; EOG6RJV5H; -. DR PhylomeDB; P45076; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.10.60.30; -; 2. DR HAMAP; MF_00765; UPF0307; 1. DR InterPro; IPR023153; PSPTO4464-like_domain. DR InterPro; IPR006839; Ribosome-assoc_YjgA. DR Pfam; PF04751; DUF615; 1. DR PIRSF; PIRSF016183; UCP016183; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 178 UPF0307 protein HI_1151. FT /FTId=PRO_0000208217. FT COMPBIAS 3 7 Arg/Lys-rich (basic). FT COMPBIAS 11 19 Asp/Glu-rich (acidic). SQ SEQUENCE 178 AA; 21034 MW; A5184A96133A7CF7 CRC64; MAKRKKKEVF DWEDEDQEEI IWVSKSEIKR DAEDLKQLGE KIVNLTKANL AKIPLDESLL DAIELAQRLQ KEARRRQLQY IGKLFRGIDV EPIREALDKI ENKHNQQQAM LHKIEKVRDE LVEKGDVALT DLLNDYPNGD RQQLRNLIRS AQKELEQNKP SKAYREIYQM LKVLMLED // ID Y1162_HAEIN Reviewed; 157 AA. AC P44116; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Uncharacterized protein HI_1162; GN OrderedLocusNames=HI_1162; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli YcjD and H.influenzae HI_0925. 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; L42023; AAC22817.1; -; Genomic_DNA. DR PIR; H64020; H64020. DR RefSeq; NP_439320.1; NC_000907.1. DR RefSeq; WP_010869141.1; NC_000907.1. DR ProteinModelPortal; P44116; -. DR STRING; 71421.HI1162; -. DR EnsemblBacteria; AAC22817; AAC22817; HI_1162. DR GeneID; 950122; -. DR KEGG; hin:HI1162; -. DR PATRIC; 20191003; VBIHaeInf48452_1214. DR eggNOG; ENOG4105WDY; Bacteria. DR eggNOG; COG2852; LUCA. DR OMA; TIGPYFA; -. DR OrthoDB; EOG6PKFM9; -. DR PhylomeDB; P44116; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF04480; DUF559; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 157 Uncharacterized protein HI_1162. FT /FTId=PRO_0000168892. SQ SEQUENCE 157 AA; 18542 MW; 723D6BBA4EB72BCE CRC64; MITCLPLLAG EGARRKGDIG MRNKNKRLAQ YATELRRNMT DAEYALWYHL RNKLFCGIRF NRQVIIGHYI VDFCSRKLKL VIELDGIQHV EQEQYDLERT KFLTAQGYKV IRFWNDEVLK NIDNVLEAIY VEIEHLSPPH FGSSPHKWVE PRLEVLK // ID Y1244_HAEIN Reviewed; 206 AA. AC P44134; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1244; GN OrderedLocusNames=HI_1244; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22899.1; -; Genomic_DNA. DR PIR; H64022; H64022. DR RefSeq; NP_439400.1; NC_000907.1. DR RefSeq; WP_005694305.1; NC_000907.1. DR ProteinModelPortal; P44134; -. DR STRING; 71421.HI1244; -. DR DNASU; 950183; -. DR EnsemblBacteria; AAC22899; AAC22899; HI_1244. DR GeneID; 950183; -. DR KEGG; hin:HI1244; -. DR PATRIC; 20191167; VBIHaeInf48452_1296. DR eggNOG; ENOG4105TWJ; Bacteria. DR eggNOG; COG3955; LUCA. DR OMA; YHSEQEA; -. DR OrthoDB; EOG6JMMZ4; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR015037; DUF1919. DR Pfam; PF08942; DUF1919; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 206 Uncharacterized protein HI_1244. FT /FTId=PRO_0000078012. SQ SEQUENCE 206 AA; 24637 MW; 61E4F24CD43320F0 CRC64; MNPFQKIKSA VNKRQRFFIN RTLQRKLTNQ GMTVISANCV GAFILHDLHQ PFNSPFVNLY LSPQDFLRYL QNIDFYLTQP LTFVQTEKSY PVGKLADLEI HFMHYHSEQE ANEKWQLRTS RMKLDNLFIM MTDRDGVTEK DIQLFDQLPF KNKVIFTHKP YPAFKSAYYI KGFEKQNQVG DIFEFSGWNG KKYYDQFDYV KWFNHA // ID Y1257_HAEIN Reviewed; 57 AA. AC P44143; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 52. DE RecName: Full=Uncharacterized protein HI_1257; GN OrderedLocusNames=HI_1257; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22912.1; -; Genomic_DNA. DR PIR; H64023; H64023. DR EnsemblBacteria; AAC22912; AAC22912; HI_1257. DR OMA; RVLMKNE; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Uncharacterized protein HI_1257. FT /FTId=PRO_0000078017. SQ SEQUENCE 57 AA; 6549 MW; C62B2970ADCDE27D CRC64; MTEQAAKPKG WFKRALEKYD NFIKEWGLDQ PNCSCVPMSA TEDENGNLKK KESSLKK // ID Y1314_HAEIN Reviewed; 161 AA. AC Q57223; O05058; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Probable endopeptidase HI_1314; DE EC=3.4.-.-; DE Flags: Precursor; GN OrderedLocusNames=HI_1314; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 peptidase C40 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; L42023; AAC22960.1; -; Genomic_DNA. DR PIR; H64170; H64170. DR RefSeq; NP_439465.1; NC_000907.1. DR RefSeq; WP_010869179.1; NC_000907.1. DR ProteinModelPortal; Q57223; -. DR SMR; Q57223; 48-161. DR STRING; 71421.HI1314; -. DR MEROPS; C40.A01; -. DR EnsemblBacteria; AAC22960; AAC22960; HI_1314. DR GeneID; 949594; -. DR KEGG; hin:HI1314; -. DR PATRIC; 20191311; VBIHaeInf48452_1366. DR eggNOG; ENOG4108QBX; Bacteria. DR eggNOG; COG0791; LUCA. DR KO; K13695; -. DR OMA; KFWQIRR; -. DR OrthoDB; EOG60CWQW; -. DR PhylomeDB; Q57223; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.1720.10; -; 1. DR InterPro; IPR000064; NLP_P60_dom. DR Pfam; PF00877; NLPC_P60; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Lipoprotein; Membrane; KW Palmitate; Protease; Reference proteome; Signal; Thiol protease. FT SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 19 161 Probable endopeptidase HI_1314. FT /FTId=PRO_0000019769. FT ACT_SITE 69 69 Nucleophile. {ECO:0000250}. FT ACT_SITE 122 122 Proton acceptor. {ECO:0000250}. FT LIPID 19 19 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 161 AA; 18388 MW; 7B9C17C50EFCA960 CRC64; MKVYKSFLIA TASLFLFACS SFQNDDYAMN YKGQIGEPIM AIAMLSEQQH EWAGTPYVLG GVSRRGVDCS GFVQKTFFDR FNLRLPRSTV EQANYGKHVR KEDIQTGDLI FFKTGRGPNG YHVGIYVKED KFLHASTRGG VVYSSMNNPY WSKAFWQVRR I // ID Y1343_HAEIN Reviewed; 238 AA. AC P71379; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative csd-like protein HI_1343; GN OrderedLocusNames=HI_1343; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. Csd subfamily. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. This protein seems CC to be a truncated duplicated copy of csd/HI_1295. It is encoded at CC the border of a duplicated DNA segment and is therefore probably CC non-functional. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22994.1; -; Genomic_DNA. DR PIR; G64117; G64117. DR RefSeq; NP_439493.1; NC_000907.1. DR RefSeq; WP_005694016.1; NC_000907.1. DR ProteinModelPortal; P71379; -. DR STRING; 71421.HI1343; -. DR EnsemblBacteria; AAC22994; AAC22994; HI_1343. DR GeneID; 949643; -. DR KEGG; hin:HI1343; -. DR PATRIC; 20191367; VBIHaeInf48452_1394. DR eggNOG; COG0520; LUCA. DR OMA; TERSWEI; -. DR OrthoDB; EOG68DD0M; -. DR PhylomeDB; P71379; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Pfam; PF00266; Aminotran_5; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 5: Uncertain; KW Complete proteome; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 238 Putative csd-like protein HI_1343. FT /FTId=PRO_0000150340. FT MOD_RES 146 146 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 238 AA; 26720 MW; 36F977896AA3C5C8 CRC64; MRVAILRITE RSWEINTMLP WKSSKKFSNH SIASTSKWLV HQVANFVTWH ETAKKCGAKI RVLPILDNWL IDENVLISTL SEKTKLVALN FVSNVTGTEQ PIKRLIQLIR KHSHALVLVD AAQAISHIKI DLQDLDADFL AFSAHKIYGP NGLGVLTGKL TALSQLQPLF FGGKMVERVS NNRITFAELP YRLEAGTPNI AGVIGFNAVL DWLQKWDFTA AEQHAISLAE SVKVRRNF // ID Y1386_HAEIN Reviewed; 148 AA. AC P44171; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein HI_1386; GN OrderedLocusNames=HI_1386; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23042.1; -; Genomic_DNA. DR PIR; A64027; A64027. DR RefSeq; NP_439538.1; NC_000907.1. DR RefSeq; WP_010869199.1; NC_000907.1. DR STRING; 71421.HI1386; -. DR EnsemblBacteria; AAC23042; AAC23042; HI_1386. DR GeneID; 950299; -. DR KEGG; hin:HI1386; -. DR PATRIC; 20191465; VBIHaeInf48452_1443. DR OrthoDB; EOG6TR0G6; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 148 Uncharacterized protein HI_1386. FT /FTId=PRO_0000078034. SQ SEQUENCE 148 AA; 17004 MW; F9D35B6728DFB9CF CRC64; MYLLMAIFSG IKPNLYWNTK SDIFVDVKIE DIQQQLHFTF NEVNGHIDTN CYAVPREIAQ KTSYSWNTSL IGDRSFLSAL KSLGLIGQTS GKYTVKYRAD FNKLIAVRRV FPQLSLSDED NNNISAKILE VINQQNIEYY GGRPWAKE // ID Y138A_HAEIN Reviewed; 128 AA. AC O86237; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_1388.1; GN OrderedLocusNames=HI_1388.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23043.1; -; Genomic_DNA. DR RefSeq; NP_439541.1; NC_000907.1. DR RefSeq; WP_005666933.1; NC_000907.1. DR PDB; 1MWW; X-ray; 2.08 A; A/B/C=1-128. DR PDBsum; 1MWW; -. DR ProteinModelPortal; O86237; -. DR SMR; O86237; 1-120. DR STRING; 71421.HI1388.1; -. DR EnsemblBacteria; AAC23043; AAC23043; HI_1388.1. DR GeneID; 950703; -. DR KEGG; hin:HI1388.1; -. DR PATRIC; 20191471; VBIHaeInf48452_1446. DR eggNOG; ENOG4108V5Q; Bacteria. DR eggNOG; ENOG4111J38; LUCA. DR OMA; TVIEINM; -. DR OrthoDB; EOG6QZMS4; -. DR EvolutionaryTrace; O86237; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:InterPro. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. DR InterPro; IPR004370; 4-oxalocrotonate_tautomerase. DR InterPro; IPR014347; Tautomerase/MIF_sf. DR Pfam; PF14552; Tautomerase_2; 1. DR SUPFAM; SSF55331; SSF55331; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein HI_1388.1. FT /FTId=PRO_0000078035. FT STRAND 2 7 {ECO:0000244|PDB:1MWW}. FT HELIX 8 30 {ECO:0000244|PDB:1MWW}. FT STRAND 39 44 {ECO:0000244|PDB:1MWW}. FT HELIX 46 48 {ECO:0000244|PDB:1MWW}. FT STRAND 60 68 {ECO:0000244|PDB:1MWW}. FT HELIX 72 90 {ECO:0000244|PDB:1MWW}. FT HELIX 94 96 {ECO:0000244|PDB:1MWW}. FT STRAND 97 104 {ECO:0000244|PDB:1MWW}. FT HELIX 106 108 {ECO:0000244|PDB:1MWW}. FT STRAND 109 111 {ECO:0000244|PDB:1MWW}. FT TURN 116 118 {ECO:0000244|PDB:1MWW}. SQ SEQUENCE 128 AA; 14961 MW; 00CBEED384195003 CRC64; MITVFGLKSK LAPRREKLAE VIYNSLHLGL DIPKGKHAIR FLCLEKEDFY YPFDRSDDYT VIEINLMAGR MEGTKKRLIK MLFSELEYKL GIRAHDVEIT IKEQPAHCWG FRGMTGDEAR DLDYDIYV // ID Y1413_HAEIN Reviewed; 93 AA. AC P44185; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_1413; GN OrderedLocusNames=HI_1413; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23064.1; -; Genomic_DNA. DR PIR; F64028; F64028. DR RefSeq; NP_439564.1; NC_000907.1. DR RefSeq; WP_005693951.1; NC_000907.1. DR STRING; 71421.HI1413; -. DR EnsemblBacteria; AAC23064; AAC23064; HI_1413. DR GeneID; 949414; -. DR KEGG; hin:HI1413; -. DR PATRIC; 20191523; VBIHaeInf48452_1472. DR OMA; CTKKITT; -. DR OrthoDB; EOG693GSR; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein HI_1413. FT /FTId=PRO_0000078050. FT TRANSMEM 11 27 Helical. {ECO:0000255}. SQ SEQUENCE 93 AA; 10360 MW; 5671A2539EB04FF8 CRC64; MLNQLKQSLR LNLVLTLVCL SLFLTACTNK ITTKPEYIYP PQAYTAPCVK TAFTGETYGD VVIQLVKVTA ERDKCASQVD HLNKWINQAK GGK // ID Y1416_HAEIN Reviewed; 118 AA. AC P44188; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_1416; DE Flags: Precursor; GN OrderedLocusNames=HI_1416; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23067.1; -; Genomic_DNA. DR PIR; I64028; I64028. DR RefSeq; NP_439567.1; NC_000907.1. DR RefSeq; WP_005650535.1; NC_000907.1. DR STRING; 71421.HI1416; -. DR TCDB; 1.E.2.1.3; the holin s (holin) family. DR EnsemblBacteria; AAC23067; AAC23067; HI_1416. DR GeneID; 950758; -. DR KEGG; hin:HI1416; -. DR PATRIC; 20191529; VBIHaeInf48452_1475. DR OMA; LDGSICG; -. DR OrthoDB; EOG6N94BD; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006481; Phage_lambda_GpS_holin. DR Pfam; PF05106; Phage_holin_3_1; 1. DR TIGRFAMs; TIGR01594; holin_lambda; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 118 Uncharacterized protein HI_1416. FT /FTId=PRO_0000013969. SQ SEQUENCE 118 AA; 13516 MW; 96CE5D469DF8E2EB CRC64; MPIKEPDVWA LIWSWLQTNL SSSSAQSAFW ALFISLLRFG FMRKKPAIRY VLIDAAMCAS IAGVAVPICT HLFGHTEYSS FLGTMIGFVG TEKIREFLFK FINRRIEKDD NDDFRSDI // ID Y1419_HAEIN Reviewed; 99 AA. AC P44190; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 75. DE RecName: Full=Uncharacterized protein HI_1419; GN OrderedLocusNames=HI_1419; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23069.1; -; Genomic_DNA. DR PIR; B64029; B64029. DR RefSeq; NP_439569.1; NC_000907.1. DR RefSeq; WP_005693946.1; NC_000907.1. DR STRING; 71421.HI1419; -. DR EnsemblBacteria; AAC23069; AAC23069; HI_1419. DR GeneID; 949900; -. DR KEGG; hin:HI1419; -. DR PATRIC; 20191533; VBIHaeInf48452_1477. DR eggNOG; ENOG4105VUH; Bacteria. DR eggNOG; COG3657; LUCA. DR OMA; IEIRQTE; -. DR OrthoDB; EOG696C09; -. DR PhylomeDB; P44190; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR014056; Addiction_killer_pred. DR InterPro; IPR009241; HigB-like. DR Pfam; PF05973; Gp49; 1. DR PIRSF; PIRSF028744; Addict_mod_HI1419; 1. DR TIGRFAMs; TIGR02683; upstrm_HI1419; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 99 Uncharacterized protein HI_1419. FT /FTId=PRO_0000078054. SQ SEQUENCE 99 AA; 11169 MW; 44BBB9DE216119BC CRC64; MTIQIKTTLT FDSWLSKLKN LRAKAKINAR IKRLQFGNFG DIKSVNDGIF ELRIDEGQGY RVYLKNQNGV LVILLCGGDK STQDKDIKQA KLLAQELGL // ID Y1423_HAEIN Reviewed; 94 AA. AC P44194; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 29-APR-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_1423; GN OrderedLocusNames=HI_1423; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23073.1; -; Genomic_DNA. DR PIR; F64029; F64029. DR RefSeq; NP_439572.1; NC_000907.1. DR RefSeq; WP_005693943.1; NC_000907.1. DR STRING; 71421.HI1423; -. DR EnsemblBacteria; AAC23073; AAC23073; HI_1423. DR GeneID; 950324; -. DR KEGG; hin:HI1423; -. DR PATRIC; 20191541; VBIHaeInf48452_1481. DR OMA; MLNILAN; -. DR OrthoDB; EOG6RZB7B; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 94 Uncharacterized protein HI_1423. FT /FTId=PRO_0000078058. SQ SEQUENCE 94 AA; 10657 MW; 5E9BC6CA282C0973 CRC64; MESIKLSQKA EEEIVNAARM AALSNLTEKS QNLITLEDIA IYFGRHYQTV AKIISKLPNF PKPVTPVTVD QQNSRPRYIA GEVVRWGRIN AKPY // ID Y143B_HAEIN Reviewed; 54 AA. AC O86239; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 45. DE RecName: Full=Uncharacterized protein HI_1436.2; GN OrderedLocusNames=HI_1436.2; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23091.1; -; Genomic_DNA. DR EnsemblBacteria; AAC23091; AAC23091; HI_1436.2. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 54 Uncharacterized protein HI_1436.2. FT /FTId=PRO_0000078059. SQ SEQUENCE 54 AA; 6250 MW; E65C8D73AE9CF431 CRC64; MELSFIHGKN CLPLYCILLE LLKNYFKLGP VDFSLSLRKI LATLNPQEIP KLFI // ID Y143_HAEIN Reviewed; 288 AA. AC P44540; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0143; GN OrderedLocusNames=HI_0143; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 HTH rpiR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00390}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21815.1; -; Genomic_DNA. DR RefSeq; NP_438312.1; NC_000907.1. DR RefSeq; WP_010868944.1; NC_000907.1. DR ProteinModelPortal; P44540; -. DR STRING; 71421.HI0143; -. DR EnsemblBacteria; AAC21815; AAC21815; HI_0143. DR GeneID; 951052; -. DR KEGG; hin:HI0143; -. DR PATRIC; 20188777; VBIHaeInf48452_0145. DR eggNOG; ENOG4105QEK; Bacteria. DR eggNOG; COG1737; LUCA. DR OMA; LRPAAMS; -. DR OrthoDB; EOG6HMXHM; -. DR PhylomeDB; P44540; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR000281; HTH_RpiR. DR InterPro; IPR001347; SIS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01418; HTH_6; 1. DR Pfam; PF01380; SIS; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS51071; HTH_RPIR; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 288 Uncharacterized HTH-type transcriptional FT regulator HI_0143. FT /FTId=PRO_0000068627. FT DOMAIN 5 81 HTH rpiR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00390}. FT DOMAIN 129 269 SIS. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT DNA_BIND 41 60 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00390}. SQ SEQUENCE 288 AA; 31465 MW; FBC951EAFE6FB4A4 CRC64; MAKSGNVLNK IGSLYQSLTK SEKKIADTIL RSPDLVSQCS LSEIAKHLQV GEATLVRFCR TIGFKGFSEF KLELSIELAT KDNQDESILE TEIMPSDDSL TIAQKLQTAV ANVMEETINL LDLKQLEEVV KVLKKARRIF LFGVGSSGVT AEDAKNKLMR IGFQVDASGN NHFMYMQAAL LTSSDVAIGL SHSGYSAETA HTIKIAKQNG ATTVALTHSL RSPVTEYADY VLVNGNKQGK LQGDSIGTKI AQLFVLDLIY ALLVQGEEDI AAQTKQKTLN VILEQRIK // ID Y1458_HAEIN Reviewed; 80 AA. AC P44204; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_1458; GN OrderedLocusNames=HI_1458; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23113.1; -; Genomic_DNA. DR PIR; G64030; G64030. DR EnsemblBacteria; AAC23113; AAC23113; HI_1458. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 80 Uncharacterized protein HI_1458. FT /FTId=PRO_0000078061. SQ SEQUENCE 80 AA; 9400 MW; E43DD2FC77114CDD CRC64; MQIAQIFNMN LSELVDENRG IIFLLNENGN NTSTNYYGNN DSLIIEIEKL KLTLFHKNEL LEQKEKELET LRKMISLLEK // ID Y1469_HAEIN Reviewed; 115 AA. AC P44205; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 58. DE RecName: Full=Uncharacterized protein HI_1469; GN OrderedLocusNames=HI_1469; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23127.1; -; Genomic_DNA. DR PIR; H64030; H64030. DR ProteinModelPortal; P44205; -. DR STRING; 71421.HI1469; -. DR EnsemblBacteria; AAC23127; AAC23127; HI_1469. DR PATRIC; 20191653; VBIHaeInf48452_1536. DR eggNOG; COG0725; LUCA. DR OrthoDB; EOG680X4N; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 115 Uncharacterized protein HI_1469. FT /FTId=PRO_0000078064. SQ SEQUENCE 115 AA; 13064 MW; D02DE8B68AAD9430 CRC64; MESITVFSAG SFCYALQELS DIFRQIHHIE IKAFCGPAGI LRQQIEQGNR GDIFISANPG NVLQLADSKK IYQKLTIAFN QLALTTLNLE HFRHKSIFEL LFDRSFLGVK NVSKY // ID Y1492_HAEIN Reviewed; 168 AA. AC P44217; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_1492; DE Flags: Precursor; GN OrderedLocusNames=HI_1492; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23144.1; -; Genomic_DNA. DR PIR; B64032; B64032. DR RefSeq; NP_439641.1; NC_000907.1. DR RefSeq; WP_005693510.1; NC_000907.1. DR STRING; 71421.HI1492; -. DR EnsemblBacteria; AAC23144; AAC23144; HI_1492. DR GeneID; 950359; -. DR KEGG; hin:HI1492; -. DR PATRIC; 20191701; VBIHaeInf48452_1560. DR eggNOG; ENOG4106ID6; Bacteria. DR eggNOG; ENOG410Y637; LUCA. DR OMA; KSKYGMT; -. DR OrthoDB; EOG60SCMK; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 Or 19. {ECO:0000255}. FT CHAIN 22 168 Uncharacterized protein HI_1492. FT /FTId=PRO_0000013973. SQ SEQUENCE 168 AA; 19213 MW; B512E5E6F3571D42 CRC64; MKLLKALAVL SLATISSHSF AVDGFQNVKF GASKTEVRNA YQKCQWQKDE YDLFCPNFTL GAIKDTGAYF YFIDDKFERI AINIPNVNID GIGQALSEKY TLSSQPTQRE LANPKPNNVY DFGFDKDTIL IRYTYDNDMT EEIFLIYTTP DFNNKLQTKD AQSVKDQL // ID Y1494_HAEIN Reviewed; 116 AA. AC O05071; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_1494; GN OrderedLocusNames=HI_1494; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To phage T3 and T7 N-acetylmuramoyl-L-alanine CC amidases. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23136.1; -; Genomic_DNA. DR PIR; G64126; G64126. DR ProteinModelPortal; O05071; -. DR STRING; 71421.HI1494; -. DR EnsemblBacteria; AAC23136; AAC23136; HI_1494. DR PATRIC; 20191705; VBIHaeInf48452_1562. DR eggNOG; COG3023; LUCA. DR OMA; AESIGIC; -. DR OrthoDB; EOG63RGXX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 3.40.80.10; -; 1. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR015510; PGRP. DR PANTHER; PTHR11022; PTHR11022; 1. DR Pfam; PF01510; Amidase_2; 1. DR SUPFAM; SSF55846; SSF55846; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 116 Uncharacterized protein HI_1494. FT /FTId=PRO_0000078075. SQ SEQUENCE 116 AA; 12770 MW; CED90DDA9C9951EE CRC64; MDGSVGTGRQ VGEIGAHVKG HNQNSVGICL VGGITASGKN HGEYTEAQWQ SLYKLLQELE AEHPKALICG HRDLSPDLNG DGVITPKEWL KDCPCFDVWS WLDSEQVVNL DHLYKE // ID Y1495_HAEIN Reviewed; 86 AA. AC P44219; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_1495; GN OrderedLocusNames=HI_1495; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23146.1; -; Genomic_DNA. DR PIR; D64032; D64032. DR RefSeq; NP_439644.1; NC_000907.1. DR RefSeq; WP_005693512.1; NC_000907.1. DR STRING; 71421.HI1495; -. DR EnsemblBacteria; AAC23146; AAC23146; HI_1495. DR GeneID; 950744; -. DR KEGG; hin:HI1495; -. DR PATRIC; 20191707; VBIHaeInf48452_1563. DR OMA; ELFMTFA; -. DR OrthoDB; EOG6NSGNM; -. DR Proteomes; UP000000579; 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; IPR020300; DUF2644. DR Pfam; PF10841; DUF2644; 1. DR ProDom; PD062017; Uncharacterised_HI1495; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 86 Uncharacterized protein HI_1495. FT /FTId=PRO_0000078076. FT TRANSMEM 20 38 Helical. {ECO:0000255}. FT TRANSMEM 47 63 Helical. {ECO:0000255}. SQ SEQUENCE 86 AA; 9464 MW; F773C45283F06EBF CRC64; MGFSELFTNA DGRLSTTASI QFWGFVAATG VLLYSVYLDK PYVPEMFSTF LFACVGTAAT KGVANALSQR REQGKEQGRE QGREQE // ID Y1560_HAEIN Reviewed; 156 AA. AC P44253; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein HI_1560; GN OrderedLocusNames=HI_1560; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23211.1; -; Genomic_DNA. DR PIR; B64036; B64036. DR RefSeq; NP_439709.1; NC_000907.1. DR RefSeq; WP_005693589.1; NC_000907.1. DR STRING; 71421.HI1560; -. DR EnsemblBacteria; AAC23211; AAC23211; HI_1560. DR GeneID; 950420; -. DR KEGG; hin:HI1560; -. DR PATRIC; 20191845; VBIHaeInf48452_1631. DR eggNOG; COG1714; LUCA. DR OMA; ASRFKRW; -. DR OrthoDB; EOG6VXFB9; -. DR Proteomes; UP000000579; 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 1 156 Uncharacterized protein HI_1560. FT /FTId=PRO_0000078085. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. SQ SEQUENCE 156 AA; 17582 MW; C1DCCFC975A208C9 CRC64; MSFLTLKGNK MIIENQKDAE FSSAFKPSQL AQASRFKRWL ASMINGLVLW VMAGLGFALG DFAGVVGMIV YAGFQLYFMK TYGQTMAKRW LGLRVFNYHT NQPVEFGKYI GREIIDILLA WTSFLLIISG IVALVRDDRR SLTDLVAGTI VLKDEK // ID Y1572_HAEIN Reviewed; 366 AA. AC P46495; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 78. DE RecName: Full=Putative integrase/recombinase HI_1572; GN OrderedLocusNames=HI_1572; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Erroneous termination; Positions=106; Note=Translated as Arg.; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P46495; -. DR OMA; PRMLMRY; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome; DNA integration; DNA recombination; KW Reference proteome; Viral genome integration; KW Virus entry into host cell. FT CHAIN 1 366 Putative integrase/recombinase HI_1572. FT /FTId=PRO_0000197538. SQ SEQUENCE 366 AA; 42415 MW; 3A6D5ED685116590 CRC64; MATIIKNGKR WHAQVRKFGV SKSAIFLTQA DAKKWAEMLE KQLESGKYNE IPDITLDELI DKYLKEVTVT KRGKREERIR LLRLSRTPLA AISLQEIGKA HFREWRNQRL KEVSPTTVLR ERSSLSALMA KTIEWDFITE NPLKYLEKPK APAPRTRRYN EHEIERLIFV SGYDVEHIEP PKTLQNCTGA AFLFAIETAM RAGEIASLTW NNINFEKRTT FLPITKNGHS RTVPLSVKAI EILQHLTSVK TESDPRVFQM EARQLDHNFR KLKKMEGLEN ANLHFHDTRR ERLAEKVDVM VLAKISGHRD LSILQNTYYA PDMAEGYKTK AGYDLTPTKG LSQRNFFFFN ENFIVFTTNP PIVIKL // ID Y1581_HAEIN Reviewed; 191 AA. AC P44262; P44261; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_1581/HI_1582; GN OrderedLocusNames=HI_1581/HI_1582; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YecM. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23229.1; Type=Frameshift; Positions=137; 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; L42023; AAC23230.1; ALT_FRAME; Genomic_DNA. DR EMBL; L42023; AAC23229.1; ALT_FRAME; Genomic_DNA. DR PIR; A64037; A64037. DR PIR; B64037; B64037. DR ProteinModelPortal; P44262; -. DR STRING; 71421.HI1582; -. DR EnsemblBacteria; AAC23229; AAC23229; HI_1581. DR EnsemblBacteria; AAC23230; AAC23230; HI_1582. DR PATRIC; 20191895; VBIHaeInf48452_1655. DR eggNOG; ENOG4105NBI; Bacteria. DR eggNOG; COG3102; LUCA. DR OrthoDB; EOG696BWM; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.10.180.10; -; 1. DR InterPro; IPR010393; DUF991. DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase. DR Pfam; PF06185; YecM; 1. DR SUPFAM; SSF54593; SSF54593; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 191 Uncharacterized protein HI_1581/HI_1582. FT /FTId=PRO_0000169080. SQ SEQUENCE 191 AA; 22252 MW; B1FEF0AD446B9261 CRC64; MTNLQENLTA LSADLAIFER KIQHLAKEMT IDLSHYEIDH LALRVNSEQS AKNWLILLLK CGRILSDNIV NGRKIYLIEL EKPVKFANQF VDIIELPLPK NKKYPIEGWE HIEIVMPFLP KESINEWINR VNMYFLXLTQ LTIKVSEPKV DGERLPNPSI AVSFTDKTVN HTCIKVHPYS IKKYLRFSKN E // ID Y1604_HAEIN Reviewed; 420 AA. AC P45268; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Putative phosphate permease HI_1604; GN OrderedLocusNames=HI_1604; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Potential transporter for phosphate. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) CC (TC 2.A.20) 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; L42023; AAC23248.1; -; Genomic_DNA. DR PIR; A64132; A64132. DR RefSeq; NP_439746.1; NC_000907.1. DR RefSeq; WP_010869255.1; NC_000907.1. DR STRING; 71421.HI1604; -. DR EnsemblBacteria; AAC23248; AAC23248; HI_1604. DR GeneID; 950410; -. DR KEGG; hin:HI1604; -. DR PATRIC; 20191939; VBIHaeInf48452_1677. DR eggNOG; ENOG4105CJ3; Bacteria. DR eggNOG; COG0306; LUCA. DR KO; K03306; -. DR OMA; SGTHTII; -. DR OrthoDB; EOG6NWBS7; -. DR PhylomeDB; P45268; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PTHR11101; 1. DR Pfam; PF01384; PHO4; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Phosphate transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 420 Putative phosphate permease HI_1604. FT /FTId=PRO_0000080798. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 300 320 Helical. {ECO:0000255}. FT TRANSMEM 343 363 Helical. {ECO:0000255}. FT TRANSMEM 370 390 Helical. {ECO:0000255}. FT TRANSMEM 393 413 Helical. {ECO:0000255}. SQ SEQUENCE 420 AA; 44026 MW; 89651207F01D3810 CRC64; MEIISQYGSW LVWITAVFGF FMAFGIGAND VSNSMGTSVG SGTITAKQAI IIALIFESAG AYLAGGEVTQ TIKSGVIEPI QFVDTPDILA LGMLSTLFAS GAWLFIATKM GWPVSGTHTI IGAIIGFACI TIGPSSVDWS KIGSIVGSWF VTPVIAGILA YAIFASTQKL IFDTEQPLKN AQKYGPYYMG ITVFVLCIVT MKKGLKHVGL NLSNSETLII SLAISLIGMF FFHFYFKSKI FTQSANKGTF GAVEKVFSIL MLLTACAMAF AHGSNDVANA IGPLSAVVSI VNEGGKIVSG GALTWWILPL GALGIAVGLI TMGQKVMATV GSGITDLTPS RGFAAQFATA MTVVVASGTG LPISTTQTLV GAILGIGFAR GIAALNLTVI RNIISSWIVT LPAGAFFAII IFYVLRTIFN // ID Y1621_HAEIN Reviewed; 206 AA. AC P44274; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Putative metal transport protein HI_1621; GN OrderedLocusNames=HI_1621; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May be involved in metal transport. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiM 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; L42023; AAC23267.1; -; Genomic_DNA. DR PIR; E64038; E64038. DR RefSeq; NP_439763.1; NC_000907.1. DR RefSeq; WP_005693633.1; NC_000907.1. DR STRING; 71421.HI1621; -. DR EnsemblBacteria; AAC23267; AAC23267; HI_1621. DR GeneID; 950848; -. DR KEGG; hin:HI1621; -. DR PATRIC; 20191977; VBIHaeInf48452_1696. DR eggNOG; ENOG4107XQ1; Bacteria. DR eggNOG; COG0310; LUCA. DR KO; K02007; -. DR OMA; VLFQYGG; -. DR OrthoDB; EOG6DC6KD; -. DR PhylomeDB; P44274; -. DR Proteomes; UP000000579; 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:0000041; P:transition metal ion transport; IEA:InterPro. DR InterPro; IPR002751; CbiM_fam. DR Pfam; PF01891; CbiM; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 206 Putative metal transport protein HI_1621. FT /FTId=PRO_0000078100. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255}. SQ SEQUENCE 206 AA; 21704 MW; 7631D942110F8E32 CRC64; MHLSEGVLHT PILLAGAVLA VAGIAVGLRR LESERLPLTA LFAAAFFVAG TIHVPVGIGS VHLILNGMAG LFLGWAVFPA FLIALLLQVI FFSFGGFAVL GVNLCVMATP AVIAHYLFRS RLQPQMALKD RLLVGIGAGV IGVGGAGALA SFVLMLDGGK SYLNLVWLLL VSHIPVFILD SIISVGVITL LGKMYPEVMN RTENFS // ID Y1627_HAEIN Reviewed; 116 AA. AC P71394; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-JAN-2016, entry version 90. DE RecName: Full=RutC family protein HI_1627; GN OrderedLocusNames=HI_1627; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the RutC 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; L42023; AAC23274.1; -; Genomic_DNA. DR PIR; C64173; C64173. DR RefSeq; NP_439769.1; NC_000907.1. DR RefSeq; WP_005693637.1; NC_000907.1. DR ProteinModelPortal; P71394; -. DR STRING; 71421.HI1627; -. DR EnsemblBacteria; AAC23274; AAC23274; HI_1627. DR GeneID; 950462; -. DR KEGG; hin:HI1627; -. DR PATRIC; 20191989; VBIHaeInf48452_1702. DR eggNOG; ENOG4105M4H; Bacteria. DR eggNOG; COG0251; LUCA. DR OMA; SEMAVHN; -. DR OrthoDB; EOG6QVRPF; -. DR PhylomeDB; P71394; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.1330.40; -; 1. DR InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like. DR InterPro; IPR019897; RidA_CS. DR InterPro; IPR006175; YjgF/YER057c/UK114. DR PANTHER; PTHR11803; PTHR11803; 1. DR Pfam; PF01042; Ribonuc_L-PSP; 1. DR SUPFAM; SSF55298; SSF55298; 1. DR PROSITE; PS01094; UPF0076; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 116 RutC family protein HI_1627. FT /FTId=PRO_0000170335. SQ SEQUENCE 116 AA; 13001 MW; 817C0EEA8C8A87C2 CRC64; MTIQRILPSA RLSEVSIHNN LAYFAGQVPE LTIEQNAYEQ TKEVLGLIDK LLAKIGSNKS NILTAQIFLA DMKDYAQLNQ AWDEWVDHVS PPSRATVEAK LADPHWKVEI VIIATC // ID Y1631_HAEIN Reviewed; 190 AA. AC P44279; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_1631; DE Flags: Precursor; GN OrderedLocusNames=HI_1631; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23283.1; -; Genomic_DNA. DR PIR; A64039; A64039. DR RefSeq; NP_439773.1; NC_000907.1. DR RefSeq; WP_005693640.1; NC_000907.1. DR STRING; 71421.HI1631; -. DR EnsemblBacteria; AAC23283; AAC23283; HI_1631. DR GeneID; 950845; -. DR KEGG; hin:HI1631; -. DR PATRIC; 20191997; VBIHaeInf48452_1706. DR eggNOG; ENOG41064N2; Bacteria. DR eggNOG; ENOG41127MS; LUCA. DR OMA; KREACRK; -. DR OrthoDB; EOG6DJZ54; -. DR PhylomeDB; P44279; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR024402; DUF2726. DR Pfam; PF10881; DUF2726; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 190 Uncharacterized protein HI_1631. FT /FTId=PRO_0000013977. SQ SEQUENCE 190 AA; 22314 MW; E4E3A8C7957EC908 CRC64; MEFSLQYITI FIFVILFLIG LFSSKSRSTR RNEKKSRLYL STENKINIVN KNDHLDVVIL SKYKRKALMN KSEYQLFLRL EKLLSKGYQE FRLFTQVSMG EFLESIDKEA HFAINSKRVD FLIVDKNGYA VIVIEYQGQG HYQDNAAKRD AVKREACRKA GVIFLEFQPN YGKAELEFVG ENLKRYLIKN // ID Y1710_HAEIN Reviewed; 46 AA. AC P44294; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_1710; GN OrderedLocusNames=HI_1710; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23363.1; -; Genomic_DNA. DR PIR; G64040; G64040. DR STRING; 71421.HI1710; -. DR EnsemblBacteria; AAC23363; AAC23363; HI_1710. DR PATRIC; 20192171; VBIHaeInf48452_1789. DR OrthoDB; EOG6130B2; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 46 Uncharacterized protein HI_1710. FT /FTId=PRO_0000078107. SQ SEQUENCE 46 AA; 4839 MW; 2741D4993BBD8FE4 CRC64; MKGQLNLRSE TTALSLKQGE VAFITAGAAY EVEGLIEGYA VVAKLP // ID Y1717_HAEIN Reviewed; 32 AA. AC P44295; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_1717; GN OrderedLocusNames=HI_1717; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23364.1; -; Genomic_DNA. DR PIR; H64040; H64040. DR EnsemblBacteria; AAC23364; AAC23364; HI_1717. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 32 Uncharacterized protein HI_1717. FT /FTId=PRO_0000078108. SQ SEQUENCE 32 AA; 3666 MW; 4A117C0B1EB768C2 CRC64; MLGEGASKVE LQQLRTEHDS LKVQIRKDQK SI // ID Y210_HAEIN Reviewed; 35 AA. AC P43964; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_0210; GN OrderedLocusNames=HI_0210; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21885.1; -; Genomic_DNA. DR PIR; I64003; I64003. DR EnsemblBacteria; AAC21885; AAC21885; HI_0210. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 35 Uncharacterized protein HI_0210. FT /FTId=PRO_0000077896. SQ SEQUENCE 35 AA; 4448 MW; 3D4B3E86D9462393 CRC64; MNYFIMDKTF LEQEILLPQF IIQNIERWFK THNFV // ID Y213A_HAEIN Reviewed; 63 AA. AC O86221; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_0213.1; GN OrderedLocusNames=HI_0213.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC21886.1; -; Genomic_DNA. DR PIR; A59452; D64055. DR EnsemblBacteria; AAC21886; AAC21886; HI_0213.1. DR Proteomes; UP000000579; 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 63 Uncharacterized protein HI_0213.1. FT /FTId=PRO_0000077897. FT TRANSMEM 3 23 Helical. {ECO:0000255}. SQ SEQUENCE 63 AA; 7437 MW; 4264AAB0C49E5E2C CRC64; MKIIYIILGF LSLAIGIIGI FPSSFAYHAF FITYFIFLHK RFKTLRTMVF RHKYLSKTSQ VLS // ID XYLR_HAEIN Reviewed; 387 AA. AC P45043; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Xylose operon regulatory protein; GN Name=xylR; OrderedLocusNames=HI_1106; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Regulatory protein for the xylBAFGHR operon. CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH araC/xylS-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00593}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22761.1; -; Genomic_DNA. DR PIR; H64182; H64182. DR RefSeq; NP_439263.1; NC_000907.1. DR RefSeq; WP_010869130.1; NC_000907.1. DR ProteinModelPortal; P45043; -. DR STRING; 71421.HI1106; -. DR EnsemblBacteria; AAC22761; AAC22761; HI_1106. DR GeneID; 949767; -. DR KEGG; hin:HI1106; -. DR PATRIC; 20190883; VBIHaeInf48452_1154. DR eggNOG; ENOG4105T16; Bacteria. DR eggNOG; COG1609; LUCA. DR eggNOG; COG2207; LUCA. DR KO; K02529; -. DR OMA; DFRCRLA; -. DR OrthoDB; EOG6JHRGK; -. DR PhylomeDB; P45043; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.60; -; 2. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR018060; HTH_AraC. DR InterPro; IPR018062; HTH_AraC-typ_CS. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type. DR Pfam; PF12833; HTH_18; 1. DR PRINTS; PR00032; HTHARAC. DR SMART; SM00342; HTH_ARAC; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF53822; SSF53822; 1. DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 387 Xylose operon regulatory protein. FT /FTId=PRO_0000194600. FT DNA_BIND 304 323 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00593}. SQ SEQUENCE 387 AA; 44932 MW; 4601673E413828CA CRC64; MTEQYYKIAL LFNANKVYDR QVVEGIGQYI QASQCMWDIF VEDEFIYHTD TINQLSIDGI IADFDDPKTV ELLQHTLIPT IAVGGSYKQA DFYPHFPYIA TDNMALVEMA LSHLQEKGLS QFAFYGLQVN THKHWSIERR DAFVELMEKN HYPIYLYEGV QVHAQNWLEE QQKLIVWLKS LPSHTGIIAV TDARARHLLQ ACEYSKIAVP EELCVVGIDN EELIQYLSRM SLSSVEQGTR EIGYQAAKLL HKLLNGQKVS HTPILIPPIT VHSRNSTDYR SLTDPLVIQA MHYIRHRACH RIKVGQVLDH LETSRSNLEQ RFKNEMNKTI HQVIHEEKIS RAKNLLQQTD ISIKEITEIC GYPSIQYFYS VFKKEFEMTP KEFRLNC // ID Y077_HAEIN Reviewed; 288 AA. AC P43935; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_0077; GN OrderedLocusNames=HI_0077; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21760.1; -; Genomic_DNA. DR PIR; G64000; G64000. DR RefSeq; NP_438250.1; NC_000907.1. DR RefSeq; WP_005693845.1; NC_000907.1. DR STRING; 71421.HI0077; -. DR EnsemblBacteria; AAC21760; AAC21760; HI_0077. DR GeneID; 950975; -. DR KEGG; hin:HI0077; -. DR PATRIC; 20188609; VBIHaeInf48452_0078. DR eggNOG; ENOG4105ED9; Bacteria. DR eggNOG; COG2833; LUCA. DR OMA; WRFAGMP; -. DR OrthoDB; EOG6GR36Q; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007402; DUF455. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR011197; UCP012318. DR Pfam; PF04305; DUF455; 1. DR PIRSF; PIRSF012318; UCP012318; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 288 Uncharacterized protein HI_0077. FT /FTId=PRO_0000077883. SQ SEQUENCE 288 AA; 33033 MW; 9D97F4D85326003C CRC64; MTALITQFWQ QVETALKTAN PQEKCRLVND LYDNLLPQIQ LIKLEDFPEI VPQDNIAAFP EKPLLVAPKD VPKRSFATEE GYAATLHAIA HIEFNAINLG LDAAWRFGRN AQEELGEGLA FVKDWLRVAR EESTHFSLVN EHLKTLGYQY GDFEAHAGLW EMAQATAHDI WERMALVPRV LEARGLDATP VLQEKIAQRK DFAAVNILDI ILRDEIGHVY IGNHWYHALS KKRGLDAMKC FTELLHKYRI VIFKGVINTD ARIQAGFTQH ELDWIYEVEQ TLKSYIKK // ID Y1016_HAEIN Reviewed; 142 AA. AC P44095; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 78. DE RecName: Full=Uncharacterized protein HI_1016; GN OrderedLocusNames=HI_1016; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22681.1; -; Genomic_DNA. DR PIR; E64018; E64018. DR RefSeq; NP_439177.1; NC_000907.1. DR RefSeq; WP_005693352.1; NC_000907.1. DR ProteinModelPortal; P44095; -. DR STRING; 71421.HI1016; -. DR EnsemblBacteria; AAC22681; AAC22681; HI_1016. DR GeneID; 949991; -. DR KEGG; hin:HI1016; -. DR PATRIC; 20190695; VBIHaeInf48452_1060. DR eggNOG; COG1878; LUCA. DR OrthoDB; EOG6KMB57; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004061; F:arylformamidase activity; IBA:GO_Central. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central. DR InterPro; IPR007325; KFase. DR Pfam; PF04199; Cyclase; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 142 Uncharacterized protein HI_1016. FT /FTId=PRO_0000077992. FT TRANSMEM 75 91 Helical. {ECO:0000255}. SQ SEQUENCE 142 AA; 15926 MW; 4126515CC2B8E6FB CRC64; MIRCTDINEI TPFSSFISKI PNHCGTHMDA SRHFVKDGLS INELPIGYFC HKDVVLLEVP KGEAEGITKE DLEPYAAILA QVSFAFLCTG FEKYRTENPL IYQNEGPYIA TSAGKYLSDN YPNLKGVGIW FPCTWFAVFS CT // ID Y1029_HAEIN Reviewed; 425 AA. AC P44993; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative TRAP transporter large permease protein HI_1029; GN OrderedLocusNames=HI_1029; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAP transporter large permease 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; L42023; AAC22689.1; -; Genomic_DNA. DR PIR; A64165; A64165. DR RefSeq; NP_439189.1; NC_000907.1. DR RefSeq; WP_005647842.1; NC_000907.1. DR STRING; 71421.HI1029; -. DR EnsemblBacteria; AAC22689; AAC22689; HI_1029. DR GeneID; 949652; -. DR KEGG; hin:HI1029; -. DR PATRIC; 20190721; VBIHaeInf48452_1073. DR eggNOG; ENOG4105CG6; Bacteria. DR eggNOG; COG1593; LUCA. DR OMA; YPMSYSA; -. DR OrthoDB; EOG690MB5; -. DR PhylomeDB; P44993; -. DR Proteomes; UP000000579; 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; IPR010656; DctM. DR InterPro; IPR004681; TRAP_transpt_permease. DR Pfam; PF06808; DctM; 1. DR PIRSF; PIRSF006066; HI0050; 1. DR TIGRFAMs; TIGR00786; dctM; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 425 Putative TRAP transporter large permease FT protein HI_1029. FT /FTId=PRO_0000169599. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 312 332 Helical. {ECO:0000255}. FT TRANSMEM 334 354 Helical. {ECO:0000255}. FT TRANSMEM 355 375 Helical. {ECO:0000255}. FT TRANSMEM 399 419 Helical. {ECO:0000255}. SQ SEQUENCE 425 AA; 45468 MW; AC50AD3F206411AC CRC64; MTVIIFLSVL LGTIILGVPV AFALLICGIA LMLHLDFFNA QILAQQLVSG ADSFSLMAIP FFILAGEIMN EGGLSKRIID LPMKLVGHKR GGLGFVAILS AMIMASLSGS AVADTAAVAA MLLPMMKTTG YPIHRSAGLI GTAGIIAPII PPSIPFIVFG VASGVSITKL FLAGIFPGVI MGCCLAILWR WQAKRLNLMT FSKATKQDLC FSFKNSVWAL MLPVIIIGGF RSGIFTPTEA GVVATFYALI VSLFIYHELP LKHLPKVLLA AAKTTAVVMF LVASANVTGY LITVAELPTM LTILLEPLIE NPTILLLVIM LAVFVIGMVM DLTPTVLILT PVLMPLVEEA GIDPVYFGVL FILNTSIGLI TPPVGNVLNV ITGVSKLPFD QAAKGIMPYL GMMIMLLLTF IFIPELILMP LQWIQ // ID Y1050_HAEIN Reviewed; 92 AA. AC P71365; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_1050; GN OrderedLocusNames=HI_1050; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HMA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22708.1; -; Genomic_DNA. DR PIR; I64109; I64109. DR RefSeq; NP_439209.1; NC_000907.1. DR RefSeq; WP_005662887.1; NC_000907.1. DR ProteinModelPortal; P71365; -. DR STRING; 71421.HI1050; -. DR TCDB; 1.A.72.1.3; the mer superfamily. DR EnsemblBacteria; AAC22708; AAC22708; HI_1050. DR GeneID; 950027; -. DR KEGG; hin:HI1050; -. DR PATRIC; 20190765; VBIHaeInf48452_1095. DR eggNOG; ENOG410681U; Bacteria. DR eggNOG; ENOG410XUQ1; LUCA. DR KO; K08364; -. DR OMA; FYIKEMT; -. DR OrthoDB; EOG6742RM; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR006121; HMA_dom. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 92 Uncharacterized protein HI_1050. FT /FTId=PRO_0000077996. FT DOMAIN 25 90 HMA. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. FT METAL 35 35 {ECO:0000255|PROSITE-ProRule:PRU00280}. FT METAL 38 38 {ECO:0000255|PROSITE-ProRule:PRU00280}. SQ SEQUENCE 92 AA; 10249 MW; 71E01078206445DD CRC64; MKKLCTALLL SLFAISFAHA NETKQIVLKV KEMNCQLCAY LVNKELRNIN GVISTKASIK DGLVTVVEDP NVTNQQLFDA IHKLKYTAEV VN // ID Y108_HAEIN Reviewed; 297 AA. AC P44520; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein HI_0108; GN OrderedLocusNames=HI_0108; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YjjP. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21786.1; -; Genomic_DNA. DR PIR; I64142; I64142. DR RefSeq; NP_438282.1; NC_000907.1. DR RefSeq; WP_005693811.1; NC_000907.1. DR STRING; 71421.HI0108; -. DR EnsemblBacteria; AAC21786; AAC21786; HI_0108. DR GeneID; 951010; -. DR KEGG; hin:HI0108; -. DR PATRIC; 20188685; VBIHaeInf48452_0112. DR eggNOG; ENOG4107XM3; Bacteria. DR eggNOG; COG2966; LUCA. DR eggNOG; COG3610; LUCA. DR OMA; HLSSGDW; -. DR OrthoDB; EOG66QM3D; -. DR PhylomeDB; P44520; -. DR Proteomes; UP000000579; 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; IPR010619; ThrE. DR InterPro; IPR024528; ThrE_2. DR Pfam; PF06738; ThrE; 1. DR Pfam; PF12821; ThrE_2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 297 Uncharacterized protein HI_0108. FT /FTId=PRO_0000169813. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 270 290 Helical. {ECO:0000255}. SQ SEQUENCE 297 AA; 32821 MW; 156C86891CB27B9E CRC64; MEHEYQRAVT RVCVQTALLL LQHGAESTVV VQMAQRLGVA LGVESVECAL TANAVVLTTL SDNHCITTAR KNTDKGINMQ MVTDVQRIVI AVEHHLYELE IAQRKLDQLK PLKYNRWLVV FMIGLSCAAF AHLSSGDWII CGITIFMLKL LYDMLFAAIP AVGFALVFNV PPKALKYCAI LAALGHVTRT LLLHINMPIV FATFFATCVI GFLGVHLSHR YLAHPKAFTV AAIIPMIPGV HAYKAMISMV QIHHFGFSDA LFEQMISSFI NTSFILGAIV FGLALPGLLF YRQKPVV // ID Y109_HAEIN Reviewed; 113 AA. AC P43943; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_0109; DE Flags: Precursor; GN OrderedLocusNames=HI_0109; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21790.1; -; Genomic_DNA. DR PIR; F64001; F64001. DR RefSeq; NP_438283.1; NC_000907.1. DR RefSeq; WP_005693810.1; NC_000907.1. DR ProteinModelPortal; P43943; -. DR EnsemblBacteria; AAC21790; AAC21790; HI_0109. DR GeneID; 951013; -. DR KEGG; hin:HI0109; -. DR PATRIC; 20188687; VBIHaeInf48452_0113. DR eggNOG; COG3765; LUCA. DR OMA; SAYHEFT; -. DR OrthoDB; EOG690MH9; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 38 {ECO:0000255}. FT CHAIN 39 113 Uncharacterized protein HI_0109. FT /FTId=PRO_0000013950. SQ SEQUENCE 113 AA; 13379 MW; D9CFF33BA44F92E7 CRC64; MVKIERKATD SAYHEFTKIL TSSAQLMAFL NQSDFVKARA KVENETVQQI ASHFKFSQEN NLNQLILSSF DREEVDQLFV EYIRYVNNQV RQTLNNELIT KWKSLFEKRK ITD // ID Y114_HAEIN Reviewed; 38 AA. AC P43944; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_0114; GN OrderedLocusNames=HI_0114; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21792.1; -; Genomic_DNA. DR PIR; G64001; G64001. DR EnsemblBacteria; AAC21792; AAC21792; HI_0114. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 38 Uncharacterized protein HI_0114. FT /FTId=PRO_0000077891. SQ SEQUENCE 38 AA; 4407 MW; 285A7A76A1E3FF83 CRC64; MRTTGYIVWG ILIGKKGKLE EMCIDFVVKL DAKLYLNF // ID Y1161_HAEIN Reviewed; 138 AA. AC P45083; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 102. DE RecName: Full=Putative esterase HI_1161; DE EC=3.1.2.-; GN OrderedLocusNames=HI_1161; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RG Northeast structural genomics consortium (NESG); RT "X-ray structure of YB61_HAEIN northeast structural genomics RT consortium target IR63."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- SIMILARITY: Belongs to the thioesterase PaaI 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; L42023; AAC22816.1; -; Genomic_DNA. DR PIR; A64187; A64187. DR RefSeq; NP_439319.1; NC_000907.1. DR RefSeq; WP_005693476.1; NC_000907.1. DR PDB; 1SC0; X-ray; 1.70 A; A/B=1-138. DR PDB; 2B6E; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-138. DR PDB; 3LZ7; X-ray; 2.19 A; A/B/C/D=1-138. DR PDBsum; 1SC0; -. DR PDBsum; 2B6E; -. DR PDBsum; 3LZ7; -. DR ProteinModelPortal; P45083; -. DR SMR; P45083; 1-138. DR STRING; 71421.HI1161; -. DR EnsemblBacteria; AAC22816; AAC22816; HI_1161. DR GeneID; 950121; -. DR KEGG; hin:HI1161; -. DR PATRIC; 20191001; VBIHaeInf48452_1213. DR eggNOG; ENOG4105KA0; Bacteria. DR eggNOG; COG2050; LUCA. DR OMA; TQVWQID; -. DR OrthoDB; EOG6PGKBS; -. DR PhylomeDB; P45083; -. DR EvolutionaryTrace; P45083; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR003736; PAAI_dom. DR InterPro; IPR006683; Thioestr_dom. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR00369; unchar_dom_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 138 Putative esterase HI_1161. FT /FTId=PRO_0000156682. FT HELIX 9 15 {ECO:0000244|PDB:1SC0}. FT HELIX 20 23 {ECO:0000244|PDB:1SC0}. FT STRAND 27 31 {ECO:0000244|PDB:1SC0}. FT STRAND 36 41 {ECO:0000244|PDB:1SC0}. FT TURN 44 46 {ECO:0000244|PDB:1SC0}. FT STRAND 51 53 {ECO:0000244|PDB:1SC0}. FT HELIX 55 72 {ECO:0000244|PDB:1SC0}. FT STRAND 79 89 {ECO:0000244|PDB:1SC0}. FT STRAND 95 107 {ECO:0000244|PDB:1SC0}. FT STRAND 109 119 {ECO:0000244|PDB:1SC0}. FT STRAND 125 136 {ECO:0000244|PDB:1SC0}. SQ SEQUENCE 138 AA; 15051 MW; 983FF31EDBF357D7 CRC64; MLWKKTFTLE NLNQLCSNSA VSHLGIEISA FGEDWIEATM PVDHRTMQPF GVLHGGVSVA LAETIGSLAG SLCLEEGKTV VGLDINANHL RPVRSGKVTA RATPINLGRN IQVWQIDIRT EENKLCCVSR LTLSVINL // ID Y1176_HAEIN Reviewed; 73 AA. AC P44120; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=Uncharacterized protein HI_1176; GN OrderedLocusNames=HI_1176; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22835.1; -; Genomic_DNA. DR PIR; C64021; C64021. DR ProteinModelPortal; P44120; -. DR EnsemblBacteria; AAC22835; AAC22835; HI_1176. DR OMA; TLSRTIC; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 73 Uncharacterized protein HI_1176. FT /FTId=PRO_0000078009. SQ SEQUENCE 73 AA; 7700 MW; 844354527F3B54D8 CRC64; MEQLKTAANP NQAKIDNATK SYETAKNELV STWKGTAGSV SVGNKIRGIT HQITGVAAGT LSRTICCCSW SSL // ID Y1192_HAEIN Reviewed; 47 AA. AC P44125; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_1192; DE Flags: Precursor; GN OrderedLocusNames=HI_1192; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22847.1; -; Genomic_DNA. DR PIR; H64021; H64021. DR RefSeq; NP_439348.1; NC_000907.1. DR RefSeq; WP_005634891.1; NC_000907.1. DR STRING; 71421.HI1192; -. DR EnsemblBacteria; AAC22847; AAC22847; HI_1192. DR GeneID; 950139; -. DR KEGG; hin:HI1192; -. DR PATRIC; 20191063; VBIHaeInf48452_1244. DR OrthoDB; EOG64XXV4; -. DR Proteomes; UP000000579; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 19 47 Uncharacterized protein HI_1192. FT /FTId=PRO_0000013965. SQ SEQUENCE 47 AA; 5182 MW; DA524691333B91FE CRC64; MKKWLLIIAG ALIISACANK DVYFNGAEGS HSGVKFDKDS RQWGLNQ // ID Y1208_HAEIN Reviewed; 296 AA. AC P71373; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Epimerase family protein HI_1208; GN OrderedLocusNames=HI_1208; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. SDR39U1 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; L42023; AAC22862.1; -; Genomic_DNA. DR PIR; A64110; A64110. DR RefSeq; NP_439364.1; NC_000907.1. DR RefSeq; WP_005694236.1; NC_000907.1. DR ProteinModelPortal; P71373; -. DR STRING; 71421.HI1208; -. DR EnsemblBacteria; AAC22862; AAC22862; HI_1208. DR GeneID; 950157; -. DR KEGG; hin:HI1208; -. DR PATRIC; 20191095; VBIHaeInf48452_1260. DR eggNOG; ENOG4105ECP; Bacteria. DR eggNOG; COG1090; LUCA. DR KO; K07071; -. DR OMA; NVWNSRI; -. DR OrthoDB; EOG6NKR30; -. DR PhylomeDB; P71373; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013549; DUF1731. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR010099; SDR39U1. DR PANTHER; PTHR11092; PTHR11092; 1. DR Pfam; PF08338; DUF1731; 1. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01777; yfcH; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 296 Epimerase family protein HI_1208. FT /FTId=PRO_0000162405. SQ SEQUENCE 296 AA; 33372 MW; 7AF393B7669E6C60 CRC64; MNILLTGGTG LIGKALVERL CLRNEQVTIL TRSSSPHTLS KHKNIKFITA LSQLNSQEQF DAIINLAGEP IFHKVWSKNQ KSILRESRLS LTTQLVEFIN QYQQHPIFIS GSATGIYGDQ DEQKITETSK TAKTFTAQLC QDWENIAQQA NGRVCLIRTG MVFSTKGGAL AKILPFYKWG LGGKLGKGEQ YFPWIALEDM VNGILFLLDH SECRGAFNFA APKSIKQHKF NRTLAQLLKR PAFATIPKWL LHFILGERAN LLLESQNVVP EKLLNAGFQF QYADCENYLE DILKNK // ID Y1217_HAEIN Reviewed; 913 AA. AC P45114; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Probable TonB-dependent receptor HI_1217; DE Flags: Precursor; GN OrderedLocusNames=HI_1217; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Probable receptor, TonB-dependent. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor 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; L42023; AAC22870.1; -; Genomic_DNA. DR PIR; G64110; G64110. DR RefSeq; NP_439373.1; NC_000907.1. DR RefSeq; WP_005694229.1; NC_000907.1. DR ProteinModelPortal; P45114; -. DR STRING; 71421.HI1217; -. DR TCDB; 1.B.14.7.3; the outer membrane receptor (omr) family. DR EnsemblBacteria; AAC22870; AAC22870; HI_1217. DR GeneID; 950767; -. DR KEGG; hin:HI1217; -. DR PATRIC; 20191113; VBIHaeInf48452_1269. DR eggNOG; COG1629; LUCA. DR KO; K16087; -. DR OMA; GINDIVH; -. DR OrthoDB; EOG6T7N3H; -. DR PhylomeDB; P45114; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 2. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Membrane; Receptor; KW Reference proteome; Signal; TonB box; Transmembrane; KW Transmembrane beta strand. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 913 Probable TonB-dependent receptor HI_1217. FT /FTId=PRO_0000034793. FT MOTIF 896 913 TonB C-terminal box. SQ SEQUENCE 913 AA; 102768 MW; 01BEFDE6D6AEF617 CRC64; MKKAIKLNLI TLGLINTIGM TITQAQAEET LGQIDVVEKV ISNDKKPFTE AKAKSTRENV FKETQTIDQV IRSIPGAFTQ QDKGSGVVSV NIRGENGLGR VNTMVDGVTQ TFYSTALDSG QSGGSSQFGA AIDPNFIAGV DVNKSNFSGA SGINALAGSA NFRTLGVNDV ITDDKPFGII LKGMTGSNAT KSNFMTMAAG RKWLDNGGYV GVVYGYSQRE VSQDYRIGGG ERLASLGQDI LAKEKEAYFR NAGYILNPEG QWTPDLSKKH WSCNKPDYQK NGDCSYYRIG SAAKTRREIL QELLTNGKKP KDIEKLQKGN DGIEETDKSF ERNKDQYSVA PIEPGSLQSR SRSHLLKFEY GDDHQNLGAQ LRTLDNKIGS RKIENRNYQV NYNFNNNSYL DLNLMAAHNI GKTIYPKGGF FAGWQVADKL ITKNVANIVD INNSHTFLLP KEIDLKTTLG FNYFTNEYSK NRFPEELSLF YNDASHDQGL YSHSKRGRYS GTKSLLPQRS VILQPSGKQK FKTVYFDTAL SKGIYHLNYS VNFTHYAFNG EYVGYENTAG QQINEPILHK SGHKKAFNHS ATLSAELSDY FMPFFTYSRT HRMPNIQEMF FSQVSNAGVN TALKPEQSDT YQLGFNTYKK GLFTQDDVLG VKLVGYRSFI KNYIHNVYGV WWRDGMPTWA ESNGFKYTIA HQNYKPIVKK SGVELEINYD MGRFFANVSY AYQRTNQPTN YADASPRPNN ASQEDILKQG YGLSRVSMLP KDYGRLELGT RWFDQKLTLG LAARYYGKSK RATIEEEYIN GSRFKKNTLR RENYYAVKKT EDIKKQPIIL DLHVSYEPIK DLIIKAEVQN LLDKRYVDPL DAGNDAASQR YYSSLNNSIE CAQDSSACGG SDKTVLYNFA RGRTYILSLN YKF // ID Y1241_HAEIN Reviewed; 266 AA. AC P44133; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein HI_1241; GN OrderedLocusNames=HI_1241; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22898.1; -; Genomic_DNA. DR PIR; G64022; G64022. DR RefSeq; NP_439397.1; NC_000907.1. DR RefSeq; WP_005694301.1; NC_000907.1. DR STRING; 71421.HI1241; -. DR EnsemblBacteria; AAC22898; AAC22898; HI_1241. DR GeneID; 950179; -. DR KEGG; hin:HI1241; -. DR PATRIC; 20191161; VBIHaeInf48452_1293. DR OMA; SYLMIFT; -. DR OrthoDB; EOG63JR7C; -. DR Proteomes; UP000000579; 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 1 266 Uncharacterized protein HI_1241. FT /FTId=PRO_0000078011. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 184 204 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. FT TRANSMEM 246 266 Helical. {ECO:0000255}. SQ SEQUENCE 266 AA; 29651 MW; 5FF0D4C939402560 CRC64; MSEQSSKYIA ALLAVLSISM VLGIDLFIFS LQSEKQTMPH LGVGVLVAQL ISLLVFYRGE ICPGQRGRLI KVNMTFAIYW AVWLLISLLQ NNHTLTNVMS VCGLSVVYFI WKQPKTEKIR NSFLLMAALI AGLGCLSYLM IFTELPASDF AEYNPFAPIL SGVILANLVL VIARNRLQGF IALLPLAMII LLALNALAMF LFLLLNGMES AVNSESVFAY IIYFVCHFVI AAILILHSFQ KWTLSTNSLF ILLFIAVCLP LWMVFV // ID Y1251_HAEIN Reviewed; 107 AA. AC Q57089; O05048; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1251; GN OrderedLocusNames=HI_1251; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the VapA/VapI family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22901.1; -; Genomic_DNA. DR PIR; H64112; H64112. DR RefSeq; NP_439407.1; NC_000907.1. DR RefSeq; WP_005650217.1; NC_000907.1. DR ProteinModelPortal; Q57089; -. DR SMR; Q57089; 5-96. DR STRING; 71421.HI1251; -. DR EnsemblBacteria; AAC22901; AAC22901; HI_1251. DR GeneID; 950190; -. DR KEGG; hin:HI1251; -. DR PATRIC; 20191183; VBIHaeInf48452_1303. DR eggNOG; ENOG4105VDM; Bacteria. DR eggNOG; COG3093; LUCA. DR OMA; VNELCND; -. DR OrthoDB; EOG67DPQ2; -. DR PhylomeDB; Q57089; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR013430; Toxin_antidote_HigA. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR TIGRFAMs; TIGR02607; antidote_HigA; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 107 Uncharacterized HTH-type transcriptional FT regulator HI_1251. FT /FTId=PRO_0000149755. FT DOMAIN 13 68 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 24 43 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 107 AA; 12347 MW; 3BBCD65C7F14B798 CRC64; MMTRKPTSVG EILQEEFLEP LSLKISDLAQ ILDVHRNTAS NIVNNSSRIT LEMAVKLAKV FDTTPEFWLN LQTRIDLWDL EHNKRFQQSL ANVKPALHRH DTSTFAM // ID Y1253_HAEIN Reviewed; 127 AA. AC P44139; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_1253; GN OrderedLocusNames=HI_1253; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22903.1; -; Genomic_DNA. DR PIR; D64023; D64023. DR RefSeq; NP_439409.1; NC_000907.1. DR RefSeq; WP_005694312.1; NC_000907.1. DR STRING; 71421.HI1253; -. DR EnsemblBacteria; AAC22903; AAC22903; HI_1253. DR GeneID; 950692; -. DR KEGG; hin:HI1253; -. DR PATRIC; 20191187; VBIHaeInf48452_1305. DR eggNOG; COG3094; LUCA. DR OMA; MVDWRQY; -. DR OrthoDB; EOG65F8WK; -. DR Proteomes; UP000000579; 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; IPR007360; SirB. DR Pfam; PF04247; SirB; 1. DR PIRSF; PIRSF005610; SirB; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 127 Uncharacterized protein HI_1253. FT /FTId=PRO_0000078015. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 82 102 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 14576 MW; 023B5AA8DF9C6D8D CRC64; MNFDRTFLTF LGVIMLVHLH IFFAFLSLAL LVIRGAMQLN GKNWRSIKLL KILPHLSDTL LIVSGVVILY LFAFGIEWWL VAKFALLILY IVFAAKFFSK KVSQPKSIFF WLACVSFIGA MLIAYLK // ID Y125_HAEIN Reviewed; 438 AA. AC P44530; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative permease HI_0125; GN OrderedLocusNames=HI_0125; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the xanthine/uracil permease family. AzgA CC purine transporter (TC 2.A.1.40) 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; L42023; AAC21799.1; -; Genomic_DNA. DR PIR; C64143; C64143. DR RefSeq; NP_438297.1; NC_000907.1. DR RefSeq; WP_005694416.1; NC_000907.1. DR STRING; 71421.HI0125; -. DR EnsemblBacteria; AAC21799; AAC21799; HI_0125. DR GeneID; 951038; -. DR KEGG; hin:HI0125; -. DR PATRIC; 20188741; VBIHaeInf48452_0129. DR eggNOG; ENOG4105C7N; Bacteria. DR eggNOG; COG2252; LUCA. DR KO; K06901; -. DR OMA; FFNIREN; -. DR OrthoDB; EOG6DNT97; -. DR PhylomeDB; P44530; -. DR Proteomes; UP000000579; 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:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 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 1 438 Putative permease HI_0125. FT /FTId=PRO_0000169722. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TRANSMEM 326 346 Helical. {ECO:0000255}. FT TRANSMEM 347 367 Helical. {ECO:0000255}. FT TRANSMEM 386 406 Helical. {ECO:0000255}. FT TRANSMEM 418 438 Helical. {ECO:0000255}. FT NP_BIND 315 322 ATP. {ECO:0000255}. SQ SEQUENCE 438 AA; 45298 MW; CAA1801D1B33D473 CRC64; MPTLEKTFEL KQRGSTVRQE IIAGLTTFLA MVYSVIVVPN MLGAAGFPAE SVFIATCLVA GLGSILIGLW ANAPMAIGCA ISLTAFTAFS LVIGQKVAIP VALGAVFLMG VVFTLISTTG IRAWILRNLP SNIAHGAGIG IGLFLLLIAA NGVGLVVSNQ AGLPVKLGDF TSFPVMMSLI GLALIIGLEK MKIKGGILWV IIAITIVGLI FDPNVKFGGE IFKMPTFGEN SLFLQLDFMG ALQPAILPVV FALVMTAVFD ATGTIRAVAG QADLLDKDGQ IINGGKALTS DSISSLFSGL FGTAPAAVYI ESAAGTAAGG KTGITAIVVG VLFLLMLFFQ PLAFLVPGYA TAPALMYVGL LMLSNVSKLD FDDFVGAMSG LICAVFIVLT ANIVTGIMLG FAALVIGRIV SGDIKRLNVG TVIIAIVLVA FYAGGWAI // ID Y1266_HAEIN Reviewed; 128 AA. AC P44145; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_1266; GN OrderedLocusNames=HI_1266; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22919.1; -; Genomic_DNA. DR PIR; A64024; A64024. DR RefSeq; NP_439421.1; NC_000907.1. DR RefSeq; WP_005694510.1; NC_000907.1. DR STRING; 71421.HI1266; -. DR EnsemblBacteria; AAC22919; AAC22919; HI_1266. DR GeneID; 950198; -. DR KEGG; hin:HI1266; -. DR PATRIC; 20191213; VBIHaeInf48452_1318. DR eggNOG; ENOG4106ZKY; Bacteria. DR eggNOG; ENOG410YVW8; LUCA. DR OMA; YQAIYLI; -. DR OrthoDB; EOG6BPDHN; -. DR Proteomes; UP000000579; 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 1 128 Uncharacterized protein HI_1266. FT /FTId=PRO_0000078018. FT TRANSMEM 8 28 Helical. {ECO:0000255}. SQ SEQUENCE 128 AA; 15107 MW; C1D4AB277C88873C CRC64; MLQLVFRYQA IYLIFAGFTV FGLLLHFYSR KKKWIKINTQ FADLITHNRM PSYCNLDRLM MTFEHFSIQQ IAEQLNLSLP ILLNELSQAQ INITDSHRTL RENFPLNDEK IFAAITIALK VRFNPTLL // ID Y1315_HAEIN Reviewed; 105 AA. AC P71375; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative uncharacterized symporter HI_1315; GN OrderedLocusNames=HI_1315; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) CC (TC 2.A.21) family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. Similar to the N- CC terminal section of E.coli YidK, but does not seem to be complete CC and thus may not be functional as a transporter. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22969.1; -; Genomic_DNA. DR PIR; I64170; I64170. DR RefSeq; NP_439466.2; NC_000907.1. DR STRING; 71421.HI1315; -. DR EnsemblBacteria; AAC22969; AAC22969; HI_1315. DR GeneID; 950581; -. DR KEGG; hin:HI1315; -. DR PATRIC; 20191313; VBIHaeInf48452_1367. DR eggNOG; COG4146; LUCA. DR KO; K03307; -. DR OrthoDB; EOG6MSS23; -. DR Proteomes; UP000000579; 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:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR001734; Na/solute_symporter. DR PANTHER; PTHR11819; PTHR11819; 1. DR Pfam; PF00474; SSF; 1. DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1. PE 5: Uncertain; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 105 Putative uncharacterized symporter FT HI_1315. FT /FTId=PRO_0000105420. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. SQ SEQUENCE 105 AA; 11404 MW; BDFC1757EC6E4178 CRC64; MLVDMGEQYM LTTILSFLIV TTVVAYVSWL KTKGDDLKSS KGYFLAGRGL SGLVIGCSMV LTSLSTEQLI GVNAVSYKGN FSVIAWTVPT VIPLCFLALY IIGWL // ID Y1316_HAEIN Reviewed; 194 AA. AC P44159; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_1316; GN OrderedLocusNames=HI_1316; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22970.1; -; Genomic_DNA. DR PIR; F64025; F64025. DR RefSeq; NP_439467.2; NC_000907.1. DR ProteinModelPortal; P44159; -. DR STRING; 71421.HI1316; -. DR EnsemblBacteria; AAC22970; AAC22970; HI_1316. DR GeneID; 950238; -. DR KEGG; hin:HI1316; -. DR PATRIC; 20191315; VBIHaeInf48452_1368. DR eggNOG; COG3119; LUCA. DR OMA; IRNDPEE; -. DR OrthoDB; EOG6M3P91; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR032506; DUF4976. DR Pfam; PF16347; DUF4976; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 194 Uncharacterized protein HI_1316. FT /FTId=PRO_0000078024. SQ SEQUENCE 194 AA; 23604 MW; F86A85C85ECE6C24 CRC64; MPEPYYSMYR KEDVVLDKSF FTPLEGKPDH FRTISKMWGM WEASEDHWKE VITKFWGYIT LIEDDNLVYL HDLTSTVFDL ANQKVPESFE GQSVLPIMRQ HQDNQRKGVL GQLAGHFVYF EQRMWRRKDY KLVFNATDVC ELYNIRNDPE EMHNLFYDPQ YNRIKKEMLE EMRAEMKRLN DPLENWVYRI IDEI // ID Y1394_HAEIN Reviewed; 123 AA. AC P44172; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=UPF0267 protein HI_1394; GN OrderedLocusNames=HI_1394; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7959067; DOI=10.1016/0378-1119(94)90861-3; RA Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., RA Benner J.S., Wilson G.G.; RT "Cloning, analysis and expression of the HindIII R-M-encoding genes."; RL Gene 150:75-80(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0267 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; L15391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L42023; AAC23041.1; -; Genomic_DNA. DR PIR; B64027; B64027. DR RefSeq; NP_439548.1; NC_000907.1. DR RefSeq; WP_010869202.1; NC_000907.1. DR ProteinModelPortal; P44172; -. DR SMR; P44172; 1-100. DR STRING; 71421.HI1394; -. DR EnsemblBacteria; AAC23041; AAC23041; HI_1394. DR GeneID; 950304; -. DR KEGG; hin:HI1394; -. DR PATRIC; 20191485; VBIHaeInf48452_1453. DR eggNOG; ENOG4105N5Z; Bacteria. DR eggNOG; COG3097; LUCA. DR KO; K09900; -. DR OMA; HARQENM; -. DR OrthoDB; EOG60390Z; -. DR PhylomeDB; P44172; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00684; UPF0267; 1. DR InterPro; IPR007374; ASCH_domain. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR008314; UCP029143. DR Pfam; PF04266; ASCH; 1. DR PIRSF; PIRSF029143; UCP029143; 1. DR SMART; SM01022; ASCH; 1. DR SUPFAM; SSF88697; SSF88697; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 123 UPF0267 protein HI_1394. FT /FTId=PRO_0000214603. FT CONFLICT 69 69 P -> Q (in Ref. 1). {ECO:0000305}. SQ SEQUENCE 123 AA; 14517 MW; 9999AE76D7D074A7 CRC64; MQPNDITFYQ RFEADILAGH KTISIRDDSE SHFKAGDILR VGRFEDNQYF CNIEVLSVSP ITLDELTQPH AKQENMGLDE LKEVIRGIYP NEIIFWVIQF SLKEYFNEEK CVREIIITDR KFN // ID Y1414_HAEIN Reviewed; 91 AA. AC P44186; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAY-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_1414; GN OrderedLocusNames=HI_1414; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23065.1; -; Genomic_DNA. DR PIR; G64028; G64028. DR RefSeq; NP_439565.1; NC_000907.1. DR RefSeq; WP_005693950.1; NC_000907.1. DR STRING; 71421.HI1414; -. DR EnsemblBacteria; AAC23065; AAC23065; HI_1414. DR GeneID; 950322; -. DR KEGG; hin:HI1414; -. DR PATRIC; 20191525; VBIHaeInf48452_1473. DR OMA; CAHTRLP; -. DR OrthoDB; EOG6F81W2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR022538; DUF2570. DR Pfam; PF10828; DUF2570; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 91 Uncharacterized protein HI_1414. FT /FTId=PRO_0000078051. FT TRANSMEM 7 23 Helical. {ECO:0000255}. SQ SEQUENCE 91 AA; 10343 MW; 01172C1636DE070D CRC64; MTKYIYIALV GVVVVLFGAL RYQSSVIDEL EITTKQQEDT NKSLSLALQQ ERNDEIERIA TENAESVKTI IKTQPCAHTR LPQSVLDRLH E // ID Y1420_HAEIN Reviewed; 97 AA. AC P44191; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_1420; GN OrderedLocusNames=HI_1420; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23070.1; -; Genomic_DNA. DR PIR; C64029; C64029. DR RefSeq; NP_439570.1; NC_000907.1. DR RefSeq; WP_005643896.1; NC_000907.1. DR STRING; 71421.HI1420; -. DR EnsemblBacteria; AAC23070; AAC23070; HI_1420. DR GeneID; 950760; -. DR KEGG; hin:HI1420; -. DR PATRIC; 20191535; VBIHaeInf48452_1478. DR eggNOG; ENOG4105YES; Bacteria. DR eggNOG; COG3636; LUCA. DR OMA; NMSQIAR; -. DR OrthoDB; EOG64BQBM; -. DR PhylomeDB; P44191; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR014057; Addict_mod_HI1420. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR TIGRFAMs; TIGR02684; dnstrm_HI1420; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein HI_1420. FT /FTId=PRO_0000078055. SQ SEQUENCE 97 AA; 10889 MW; 79CBCBB44CEE3331 CRC64; MTEQLKDFDV AEHLTSEEEI QLYLNEILQE DNIELILSAL GDIARARNMS QIARDAGISR EGLYKALSGT GNPTFATVMK VMKALNLQFQ VQQSRFA // ID Y1424_HAEIN Reviewed; 304 AA. AC P45198; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative integrase/recombinase HI_1414; GN OrderedLocusNames=HI_1424; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the 'phage' integrase 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; L42023; AAC23061.1; -; Genomic_DNA. DR PIR; D64122; D64122. DR RefSeq; NP_439573.1; NC_000907.1. DR RefSeq; WP_005693942.1; NC_000907.1. DR ProteinModelPortal; P45198; -. DR STRING; 71421.HI1424; -. DR EnsemblBacteria; AAC23061; AAC23061; HI_1424. DR GeneID; 950326; -. DR KEGG; hin:HI1424; -. DR eggNOG; COG0582; LUCA. DR OMA; VIREMAM; -. DR OrthoDB; EOG61ZTF7; -. DR PhylomeDB; P45198; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome; DNA integration; DNA recombination; KW Reference proteome; Viral genome integration; KW Virus entry into host cell. FT CHAIN 1 304 Putative integrase/recombinase HI_1414. FT /FTId=PRO_0000197537. SQ SEQUENCE 304 AA; 34856 MW; 7FCF8168F7D3C398 CRC64; MHRLRQCNMK WGAEEEKKIE LQAQGLQPDT LFSDVIKRYL NKITPTKRGE KHEFNRLNRF LRHPVTDKYI SDVSRRDIED WIAERLESVK SESVRRELST IGHIFKIALE RWGYIQKSPM VGIQLPEKGK PRTQRVTEEN INAIVAISEY VDTLKTAKAR TAAAILFAVE TAMRAGKICS LSWGNVNFEK RTAFLPMTKN GTSRTVPLTK NAIAILERLK VEIGDAGLCF DIKSSVLDAT FRKLKKLAER EYLHFHDTRR EALTRLSKKV DVMTLAKISG HKDISILQNV YYAPDMAEVA ELLD // ID Y1453_HAEIN Reviewed; 156 AA. AC Q57127; O05062; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Uncharacterized protein HI_1453; DE Flags: Precursor; GN OrderedLocusNames=HI_1453; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin 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; L42023; AAC23101.1; -; Genomic_DNA. DR PIR; D64124; D64124. DR RefSeq; NP_439604.1; NC_000907.1. DR RefSeq; WP_005652758.1; NC_000907.1. DR ProteinModelPortal; Q57127; -. DR STRING; 71421.HI1453; -. DR EnsemblBacteria; AAC23101; AAC23101; HI_1453. DR GeneID; 950347; -. DR KEGG; hin:HI1453; -. DR PATRIC; 20191609; VBIHaeInf48452_1514. DR eggNOG; ENOG4105KJP; Bacteria. DR eggNOG; COG0526; LUCA. DR OMA; YIKMWAS; -. DR OrthoDB; EOG6GBMJ4; -. DR PhylomeDB; Q57127; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF00578; AhpC-TSA; 1. DR SUPFAM; SSF52833; SSF52833; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Redox-active center; KW Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 156 Uncharacterized protein HI_1453. FT /FTId=PRO_0000034281. FT DOMAIN 19 156 Thioredoxin. FT DISULFID 54 57 Redox-active. {ECO:0000250}. SQ SEQUENCE 156 AA; 17727 MW; 6A8730B0418060B9 CRC64; MKKLLSIFLM AFSLNAFAQT NLADVQLKDL NNQPVTLSQY KGKPVYVKMW ASWCPICLAG LAEIDDLSAE KDRNFEVITI VSPDHKGEKD TADFIEWYKG LEYKNITVLL DEKGEIIDKA RVRGYPFNLF LDSDLNLKKT VPGHLGAEQI RVFAEK // ID Y1456_HAEIN Reviewed; 168 AA. AC P44203; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_1456; GN OrderedLocusNames=HI_1456; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23106.1; -; Genomic_DNA. DR PIR; F64030; F64030. DR RefSeq; NP_439607.2; NC_000907.1. DR STRING; 71421.HI1456; -. DR EnsemblBacteria; AAC23106; AAC23106; HI_1456. DR GeneID; 950348; -. DR KEGG; hin:HI1456; -. DR PATRIC; 20191615; VBIHaeInf48452_1517. DR eggNOG; ENOG41090VV; Bacteria. DR eggNOG; ENOG4111P2T; LUCA. DR OMA; YFIRQYI; -. DR OrthoDB; EOG6C8N35; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR022548; DUF2846. DR InterPro; IPR016596; UCP012335. DR Pfam; PF11008; DUF2846; 1. DR PIRSF; PIRSF012335; UCP012335; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 168 Uncharacterized protein HI_1456. FT /FTId=PRO_0000078060. FT TRANSMEM 23 47 Helical. {ECO:0000255}. SQ SEQUENCE 168 AA; 18752 MW; 1A86077999148E9A CRC64; MFLMWALRLV YVLVSNGYFV KQLFARASII GVALLLSACA TVPMASVEES NTAKQFRSPE KGNSGLYIYR DSFIGKALKK DLYIDDKFIG ESAPDVFFYK TIKAGEHKIS TESEFSNSDL NIKTESGKNY FIRQYTKFGV FVGGANLEQV SEEEGKKAIS KLNMAVSH // ID Y1462_HAEIN Reviewed; 454 AA. AC P45217; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_1462; GN OrderedLocusNames=HI_1462; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) 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; L42023; AAC23108.1; -; Genomic_DNA. DR PIR; I64124; I64124. DR RefSeq; NP_439611.1; NC_000907.1. DR RefSeq; WP_010869219.1; NC_000907.1. DR ProteinModelPortal; P45217; -. DR STRING; 71421.HI1462; -. DR TCDB; 1.B.17.3.7; the outer membrane factor (omf) family. DR EnsemblBacteria; AAC23108; AAC23108; HI_1462. DR GeneID; 950787; -. DR KEGG; hin:HI1462; -. DR PATRIC; 20191633; VBIHaeInf48452_1526. DR eggNOG; ENOG4105ENJ; Bacteria. DR eggNOG; COG1538; LUCA. DR OMA; NSAISHK; -. DR OrthoDB; EOG6H4K4N; -. DR PhylomeDB; P45217; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR003423; OMP_efflux. DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT. DR Pfam; PF02321; OEP; 2. DR TIGRFAMs; TIGR01845; outer_NodT; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 454 Uncharacterized protein HI_1462. FT /FTId=PRO_0000078062. SQ SEQUENCE 454 AA; 50289 MW; 41C9869F388DA998 CRC64; MFKMKNITLA LLMSGALVGC ANIGDSYQAS LEDYKQYEEI TKQYNVKENW WSLYDDAQLN RVVGQALINN KDLAKAAVAV NRALYSANLV GANLVPAFNG STSSAAQRRV DISTNSAISH KGSLNVSYTL DLWQRLANTV DAAEWSHKAT AEDMESARLS LINSVVTTYY QIAYLNDAIS TTNETIKYYT DIGNIMQTRL VQGVADAASV DQAQQAILTA RNNKLNFETQ RKTAEQTLRN LLNLKPNEAL NITFPHIMNV KTAGVNLNVP VSVIANRPDV KAAQFRLSSA FKNAKATQKS WFPEVNLGAS LSSTASTVGT ALHNPVAAGT VGISLPFLNW NTVKWNVKIS EADYETARLN YEQRITTALN NVDTNYFAFT QAQSTLSNLQ QTHSYNQRIT QYYRNRYNAG VSELREWLVA ANTEKSSQLA ILNAKYQVLQ SENAVYSSMA GYYL // ID Y1466_HAEIN Reviewed; 181 AA. AC P45220; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein HI_1466; GN OrderedLocusNames=HI_1466; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23115.1; -; Genomic_DNA. DR PIR; C64125; C64125. DR ProteinModelPortal; P45220; -. DR EnsemblBacteria; AAC23115; AAC23115; HI_1466. DR OMA; KRGFGRN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR InterPro; IPR012910; Plug_dom. DR Pfam; PF07715; Plug; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 181 Uncharacterized protein HI_1466. FT /FTId=PRO_0000078063. SQ SEQUENCE 181 AA; 19549 MW; E27B59ACE2503F52 CRC64; MNFKLSLVYT ALFAGISVSA LAETRHKANT ETIEQINVQD TGIKQNGYQT TGTSVVSKAE VPVFDTPNTV NILSTKLLED RKPESLIDAL YNVSGVSQAN TLGGMFDAIQ KRGFGRNRDN SIMRNGLQAG PAKNFSATTE TVEVLKGPAS VLYGIQDPGG VELISLLKNH NKRHVMSLVE P // ID Y1471_HAEIN Reviewed; 337 AA. AC Q57130; O05065; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Probable ABC transporter permease protein HI_1471; GN OrderedLocusNames=HI_1471; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD 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; L42023; AAC23119.1; -; Genomic_DNA. DR PIR; G64125; G64125. DR RefSeq; NP_439622.1; NC_000907.1. DR RefSeq; WP_005693487.1; NC_000907.1. DR PDB; 2NQ2; X-ray; 2.40 A; A/B=1-337. DR PDBsum; 2NQ2; -. DR ProteinModelPortal; Q57130; -. DR SMR; Q57130; 6-330. DR DIP; DIP-58991N; -. DR STRING; 71421.HI1471; -. DR TCDB; 3.A.1.14.11; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC23119; AAC23119; HI_1471. DR GeneID; 950354; -. DR KEGG; hin:HI1471; -. DR PATRIC; 20191657; VBIHaeInf48452_1538. DR eggNOG; ENOG4105EHG; Bacteria. DR eggNOG; COG0609; LUCA. DR KO; K02015; -. DR OMA; WRVNLMS; -. DR OrthoDB; EOG61ZTDC; -. DR PhylomeDB; Q57130; -. DR EvolutionaryTrace; Q57130; -. DR Proteomes; UP000000579; 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 Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 337 Probable ABC transporter permease protein FT HI_1471. FT /FTId=PRO_0000060281. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TRANSMEM 307 327 Helical. {ECO:0000255}. FT HELIX 7 24 {ECO:0000244|PDB:2NQ2}. FT HELIX 53 60 {ECO:0000244|PDB:2NQ2}. FT HELIX 62 86 {ECO:0000244|PDB:2NQ2}. FT TURN 94 97 {ECO:0000244|PDB:2NQ2}. FT HELIX 99 112 {ECO:0000244|PDB:2NQ2}. FT HELIX 117 139 {ECO:0000244|PDB:2NQ2}. FT HELIX 147 170 {ECO:0000244|PDB:2NQ2}. FT TURN 174 176 {ECO:0000244|PDB:2NQ2}. FT HELIX 177 184 {ECO:0000244|PDB:2NQ2}. FT HELIX 194 213 {ECO:0000244|PDB:2NQ2}. FT TURN 214 216 {ECO:0000244|PDB:2NQ2}. FT HELIX 217 222 {ECO:0000244|PDB:2NQ2}. FT HELIX 225 230 {ECO:0000244|PDB:2NQ2}. FT HELIX 235 257 {ECO:0000244|PDB:2NQ2}. FT HELIX 266 275 {ECO:0000244|PDB:2NQ2}. FT HELIX 279 303 {ECO:0000244|PDB:2NQ2}. FT HELIX 311 328 {ECO:0000244|PDB:2NQ2}. SQ SEQUENCE 337 AA; 36531 MW; 83298CCBCF2DC1F5 CRC64; MQPDSYPKIL FGLTLLLVIT AVISLGIGRY SLSVPQIGQI LWAKATALEI DPVQQQVIFQ VRLPRILTAL CVGAGLALSG VVLQGIFRNP LVNPHIIGVT SGSAFGGTLA IFFGFSLYGL FTSTILFGFG TLALVFLFSF KFNQRSLLML ILIGMILSGL FSALVSLLQY ISDTEEKLPS IVFWLMGSFA TSNWEKLLFF FVPFLLCSSI LLSLSWRLNL LSLDEKEAKA LGVKMAPLRW LVIFLSGSLV ACQVAISGSI GWVGLIIPHL SRMLVGANHQ SLLPCTMLVG ATYMLLVDNV ARSLSDAEIP ISILTALIGA PLFGVLVYKL KRGGMNE // ID Y1523_HAEIN Reviewed; 296 AA. AC P44243; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_1523; GN OrderedLocusNames=HI_1523; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23180.1; -; Genomic_DNA. DR PIR; A64035; A64035. DR RefSeq; NP_439673.1; NC_000907.1. DR RefSeq; WP_005693546.1; NC_000907.1. DR ProteinModelPortal; P44243; -. DR STRING; 71421.HI1523; -. DR REBASE; 42132; M.HindVII. DR EnsemblBacteria; AAC23180; AAC23180; HI_1523. DR GeneID; 949672; -. DR KEGG; hin:HI1523; -. DR PATRIC; 20191771; VBIHaeInf48452_1594. DR eggNOG; ENOG4107H6E; Bacteria. DR eggNOG; ENOG410Y4Y9; LUCA. DR OMA; NDFDGYA; -. DR OrthoDB; EOG6K6VC6; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 296 Uncharacterized protein HI_1523. FT /FTId=PRO_0000078081. SQ SEQUENCE 296 AA; 34486 MW; 10FE0B74076D5A12 CRC64; MSEYLEYQNA IEGKTMANKK TFKQAPLPFI GQKRMFLKHV EIVLNKHIDG EGEGWTIVDV FGGSGLLSHT AKQLKPKATV IYNDFDGYAE RLNHIDDINR LRQIIFNCLH GIIPKNGRLS KEIKEEIINK INDFKGYKDL NCLASWLLFS GQQVGSVEAL FAKDFWNCVR QSDYPTAEGY LDGIEVISES FHKLIPRYQN QDKVLLLLDP PYLCTRQESY KQATYFDLID FLRLINLTKP PYIFFSSTKS EFIRYLNYMQ ESKTDNWRAF ENYKRIVVKA SASKDGIYED NMIYKF // ID Y1536_HAEIN Reviewed; 115 AA. AC P44247; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein HI_1536; GN OrderedLocusNames=HI_1536; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23186.1; -; Genomic_DNA. DR PIR; E64035; E64035. DR ProteinModelPortal; P44247; -. DR STRING; 71421.HI1536; -. DR EnsemblBacteria; AAC23186; AAC23186; HI_1536. DR PATRIC; 20191797; VBIHaeInf48452_1607. DR eggNOG; COG0665; LUCA. DR OrthoDB; EOG61P6QH; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 115 Uncharacterized protein HI_1536. FT /FTId=PRO_0000078083. SQ SEQUENCE 115 AA; 12779 MW; 8E230B0A35BA9BE2 CRC64; MDTSDNLARV GIRCSVRDLA PMVGNVPHFE QQQADYYNLF NLRRRKQPIQ SAANFQNLFL IAALGSRGLT SAPLLGETLA SIIYGEPLPI SEGILHNLSA NRAWVKKWLK GSKVE // ID Y1546_HAEIN Reviewed; 140 AA. AC P44249; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1546; GN OrderedLocusNames=HI_1546; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the peptidase S24 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; L42023; AAC23196.1; -; Genomic_DNA. DR PIR; G64035; G64035. DR RefSeq; NP_439695.1; NC_000907.1. DR RefSeq; WP_010869241.1; NC_000907.1. DR ProteinModelPortal; P44249; -. DR STRING; 71421.HI1546; -. DR EnsemblBacteria; AAC23196; AAC23196; HI_1546. DR GeneID; 950409; -. DR KEGG; hin:HI1546; -. DR PATRIC; 20191817; VBIHaeInf48452_1617. DR eggNOG; COG1974; LUCA. DR OrthoDB; EOG6C5RQ1; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF00717; Peptidase_S24; 1. DR SUPFAM; SSF51306; SSF51306; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein HI_1546. FT /FTId=PRO_0000170118. SQ SEQUENCE 140 AA; 16579 MW; 135075C621406545 CRC64; MNNQTLATQY EMDFSYNPLP FFSDIEDNLK FNKKLDLNLY CIKRPKQTCF IHITNPNMLA WGIESGDMLV VEKNDDLYSG DLVVLEENNE FHVYEFMAHS GNYLFMALDS TTQNINTKRL VKFTYYRHRD QYDSSNETSR // ID Y1564_HAEIN Reviewed; 50 AA. AC P44256; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1564; GN OrderedLocusNames=HI_1564; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23221.1; -; Genomic_DNA. DR PIR; E64036; E64036. DR RefSeq; NP_439713.1; NC_000907.1. DR RefSeq; WP_005688502.1; NC_000907.1. DR STRING; 71421.HI1564; -. DR EnsemblBacteria; AAC23221; AAC23221; HI_1564. DR GeneID; 950424; -. DR KEGG; hin:HI1564; -. DR PATRIC; 20191853; VBIHaeInf48452_1635. DR OrthoDB; EOG6FZ4D8; -. DR Proteomes; UP000000579; 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 SUPFAM; SSF100879; SSF100879; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_1564. FT /FTId=PRO_0000078087. SQ SEQUENCE 50 AA; 5837 MW; D49D1826A3417AA5 CRC64; MEKTGLPLSL ESFQQLLPQI FMRAKGRSIR LIGLHVNLPE ENKQEQMSLW // ID Y1656_HAEIN Reviewed; 119 AA. AC P45300; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=UPF0102 protein HI_1656; GN OrderedLocusNames=HI_1656; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0102 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23300.1; -; Genomic_DNA. DR PIR; C64174; C64174. DR RefSeq; NP_439798.1; NC_000907.1. DR RefSeq; WP_005694382.1; NC_000907.1. DR STRING; 71421.HI1656; -. DR DNASU; 950807; -. DR EnsemblBacteria; AAC23300; AAC23300; HI_1656. DR GeneID; 950807; -. DR KEGG; hin:HI1656; -. DR PATRIC; 20192061; VBIHaeInf48452_1734. DR eggNOG; ENOG41082RQ; Bacteria. DR eggNOG; COG0792; LUCA. DR KO; K07460; -. DR OMA; MSFITKN; -. DR OrthoDB; EOG6PP9TH; -. DR PhylomeDB; P45300; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_00048; UPF0102; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR InterPro; IPR003509; UPF0102. DR Pfam; PF02021; UPF0102; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00252; TIGR00252; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 119 UPF0102 protein HI_1656. FT /FTId=PRO_0000167354. SQ SEQUENCE 119 AA; 13812 MW; B7359D8181F31AE7 CRC64; MFSLKRQQGA SFEHQARLFL ESKGLIFIAA NQNFKCGELD LIMNDKETIV FVEVRQRSHS AYGSAIESVD WRKQQKWLDA ANLWLAKQNM SLEDANCRFD LIAFGKTPQD IQWIPNFLD // ID Y1663_HAEIN Reviewed; 212 AA. AC Q57544; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=Uncharacterized protein HI_1663; DE EC=3.-.-.-; GN OrderedLocusNames=HI_1663; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q16775}; CC Note=Binds 2 Zn(2+) ions per subunit. CC {ECO:0000250|UniProtKB:Q16775}; CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II 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; L42023; AAC23309.1; -; Genomic_DNA. DR PIR; D64174; D64174. DR RefSeq; NP_439805.1; NC_000907.1. DR RefSeq; WP_005694389.1; NC_000907.1. DR ProteinModelPortal; Q57544; -. DR STRING; 71421.HI1663; -. DR EnsemblBacteria; AAC23309; AAC23309; HI_1663. DR GeneID; 950497; -. DR KEGG; hin:HI1663; -. DR PATRIC; 20192075; VBIHaeInf48452_1741. DR eggNOG; ENOG4105C5X; Bacteria. DR eggNOG; COG0491; LUCA. DR OMA; TPDRWLE; -. DR OrthoDB; EOG69GZQ4; -. DR PhylomeDB; Q57544; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 212 Uncharacterized protein HI_1663. FT /FTId=PRO_0000192358. FT METAL 55 55 Zinc 1; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q16775}. FT METAL 57 57 Zinc 1; via pros nitrogen. FT {ECO:0000250|UniProtKB:Q16775}. FT METAL 59 59 Zinc 2. {ECO:0000250|UniProtKB:Q16775}. FT METAL 60 60 Zinc 2; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q16775}. FT METAL 132 132 Zinc 1; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q16775}. FT METAL 151 151 Zinc 1. {ECO:0000250|UniProtKB:Q16775}. FT METAL 151 151 Zinc 2. {ECO:0000250|UniProtKB:Q16775}. FT METAL 192 192 Zinc 2; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q16775}. SQ SEQUENCE 212 AA; 23882 MW; 409D4E7DA445F4AA CRC64; MNIEIIPVTA FQQNCSLIWD DEKNAAIIDP GGEAERLIQR IEELDLNLKV LLLTHGHLDH VGAAMQLKQH FGVEIWGSNE KDKFLFESLP EQAQRFGLPN IDAFLPDRWF NQEGEILKLD GFNFEILHLP GHTPGHIGFI EHEKKVAFTG DVLFQGGIGR TDFPRGDYET LISSIRTKLL PLNDDIIIIA GHGSYTTIGQ EKRSNPFLNS KS // ID Y1667_HAEIN Reviewed; 489 AA. AC P44285; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative L,D-transpeptidase HI_1667; DE EC=2.-.-.-; GN OrderedLocusNames=HI_1667; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the YkuD 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; L42023; AAC23312.1; -; Genomic_DNA. DR PIR; G64039; G64039. DR RefSeq; NP_439809.1; NC_000907.1. DR RefSeq; WP_005694392.1; NC_000907.1. DR ProteinModelPortal; P44285; -. DR STRING; 71421.HI1667; -. DR EnsemblBacteria; AAC23312; AAC23312; HI_1667. DR GeneID; 950498; -. DR KEGG; hin:HI1667; -. DR PATRIC; 20192083; VBIHaeInf48452_1745. DR eggNOG; ENOG4105DIT; Bacteria. DR eggNOG; COG2989; LUCA. DR OMA; YTIDWEN; -. DR OrthoDB; EOG686NH3; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR InterPro; IPR005490; LD_TPept_cat_dom. DR Pfam; PF03734; YkuD; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Glycosyltransferase; Hydrolase; Membrane; Peptidoglycan synthesis; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 489 Putative L,D-transpeptidase HI_1667. FT /FTId=PRO_0000168767. FT TRANSMEM 10 29 Helical. {ECO:0000255}. FT ACT_SITE 403 403 {ECO:0000255}. SQ SEQUENCE 489 AA; 55582 MW; 1276A5C79D7E3A56 CRC64; MVVFKSTLKL SLFALSLSMM MSGCVLVGLS KNDQSKSLYG INLSHLSLAE RKELEEAIYA DQQRLTEEKQ TLLNMTLTHE IGDHKLQFKP LLARLYASRK YAPLWTDNAA ARQLLRDYAA MVASGISKSS ATSLETLALV EQQGGLVYDV LLSDILLDYL YYTQNVRSQA SNWLYSSAQY QAQQPENDHI QRWLSAVENN QLLDFIQSLA GENHLYRQTI QSLPMFIPTS KESNITQKLA MNAQRLRVIP DFHNGIFVNI PSYKLQYYRD GDLILESRVI VGTNSRRTPV MYSKLSNVVV NPPWNAPIRL INEDLLPKMK ADPNYITEHN YSILDNQGNV VDPASIDWES IDNKFPYRVR QAAGDSALGN YKFNMPSSDA IYLHDTPNRG LFNRKNRALS SGCVRVEKSD QLASILLKEA GWTETRKNTV LASKKTTSAP IRSDNPVFLY YVTAWIENGN IVNLPDIYGY DRQINLAEIN WDLVKKYLQ // ID Y1680_HAEIN Reviewed; 718 AA. AC P44289; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 93. DE RecName: Full=Uncharacterized protein HI_1680; GN OrderedLocusNames=HI_1680; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the YccS/YhfK 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; L42023; AAC23326.1; -; Genomic_DNA. DR PIR; B64040; B64040. DR RefSeq; NP_439822.1; NC_000907.1. DR RefSeq; WP_005665016.1; NC_000907.1. DR STRING; 71421.HI1680; -. DR EnsemblBacteria; AAC23326; AAC23326; HI_1680. DR GeneID; 950508; -. DR KEGG; hin:HI1680; -. DR PATRIC; 20192111; VBIHaeInf48452_1759. DR eggNOG; ENOG4105EM2; Bacteria. DR eggNOG; COG1289; LUCA. DR OMA; YSTIAFG; -. DR OrthoDB; EOG6MSS1Z; -. DR PhylomeDB; P44289; -. DR Proteomes; UP000000579; 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; IPR010019; Integral_membrane_YccS. DR InterPro; IPR010020; Integral_membrane_YCCS_YHJK. DR InterPro; IPR032692; YccS_N. DR Pfam; PF12805; FUSC-like; 1. DR TIGRFAMs; TIGR01666; YCCS; 1. DR TIGRFAMs; TIGR01667; YCCS_YHJK; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 718 Uncharacterized protein HI_1680. FT /FTId=PRO_0000168794. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 391 411 Helical. {ECO:0000255}. FT TRANSMEM 506 526 Helical. {ECO:0000255}. SQ SEQUENCE 718 AA; 82374 MW; 59216219C81B014A CRC64; MNIRLNAKVI STIPVFIAVN IAAVGIWFFD ISSQSMPLIL GIIAGGLVDL DNRLTGRLKN VFFTLIAFSI SSFIVQLHIG KPIQYIVLMT VLTFIFTMIG AVGQRYSTIA FGSLVVALYT TLTYIPEVNV WFINPVMILC GTLLYSVVTL IVYLFFPNRP VQESVAKAFC ALGEYLDTKS CFFDPDEVAE IEKKHLNFAM KNANVVTAFN IVRTALFYRI RGQHRHPLTQ RMLRYYFAAQ DIHERANSTH FDYQQITEKL KNTDLIFRIQ RLLELQAQSC KEITASLREN KPYHFNKRVE RALLGTLHSF DLYRAQHLND QDELIDIQTL LDNLQSINWQ LRQLAQDTTV TEQLAQIHTE QITGLKNISA VIFSHFTFES PLFRHAVRLS IVVFLCCAIV EFFQFNLGYW ILLTTVFVCQ PNYSATKVRL RQRIIGTILG VVVGSLLPYL NPTLELKLGL VVLTSTLFFF FRSNNYSFST FFITLQVLLS FDVMGFDTAA ALMPRLLDTL LGAAISWFAV SYLWPDWKYL QLDKVSHQAL RSDAVYLLHI ISQLQFGKSD DLKYRIARRN AHQYAAALST TLSNMNNEPV KYKAYLQKGF DLLKLNYSLL SYISALGAYR DRMKNLQQTA QFLSGFYPVA KKIIYTLEHI EEIPEAIFNQ QQESIETHLK ELEKQEMTAE ERAVFSLPYQ QLNLITQLLP QFYGYFKKEI NCQSAGAL // ID Y1681_HAEIN Reviewed; 221 AA. AC P44290; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=UPF0319 protein HI_1681; DE Flags: Precursor; GN OrderedLocusNames=HI_1681; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0319 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; L42023; AAC23327.1; -; Genomic_DNA. DR PIR; C64040; C64040. DR RefSeq; NP_439823.1; NC_000907.1. DR RefSeq; WP_005654151.1; NC_000907.1. DR STRING; 71421.HI1681; -. DR EnsemblBacteria; AAC23327; AAC23327; HI_1681. DR GeneID; 950865; -. DR KEGG; hin:HI1681; -. DR PATRIC; 20192113; VBIHaeInf48452_1760. DR eggNOG; ENOG4108Q67; Bacteria. DR eggNOG; COG3110; LUCA. DR KO; K09909; -. DR OMA; YQQADKE; -. DR OrthoDB; EOG69D3D4; -. DR PhylomeDB; P44290; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00789; UPF0319; 1. DR InterPro; IPR018635; UPF0319. DR Pfam; PF09829; DUF2057; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 221 UPF0319 protein HI_1681. FT /FTId=PRO_0000036297. SQ SEQUENCE 221 AA; 23395 MW; D308BEAC9C0E03C6 CRC64; MKLRAVVLGL ATLCTSTATF AGMVSTSSNL EFLAIDGQKA SKSLGKAKTF TVDDTQNHQV VVRLNEIVGS GSNQSLFESN PVIVTFQGNA EDLVISAPVI RNLDSGDKFN QMPNITVKTK SGNAISAKVD VLKQEGLFPS GNVLNDLAEY NASGAAASVS KFAATTVASS VAVAPAGNAK ANKGKVVVQG ENVAEQQLQY WFQQADKETQ TRFLNWAKSH K // ID Y1728_HAEIN Reviewed; 397 AA. AC O05087; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized membrane protein HI_1728; GN OrderedLocusNames=HI_1728; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NRAMP 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; L42023; AAC23374.1; -; Genomic_DNA. DR PIR; G64138; G64138. DR RefSeq; NP_439869.1; NC_000907.1. DR RefSeq; WP_005694214.1; NC_000907.1. DR STRING; 71421.HI1728; -. DR EnsemblBacteria; AAC23374; AAC23374; HI_1728. DR GeneID; 950517; -. DR KEGG; hin:HI1728; -. DR PATRIC; 20192209; VBIHaeInf48452_1807. DR eggNOG; ENOG4105C5A; Bacteria. DR eggNOG; COG1914; LUCA. DR OMA; NIWRIVI; -. DR OrthoDB; EOG6V1M34; -. DR PhylomeDB; O05087; -. DR Proteomes; UP000000579; 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; IPR001046; NRAMP_fam. DR PANTHER; PTHR11706; PTHR11706; 2. DR Pfam; PF01566; Nramp; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 397 Uncharacterized membrane protein HI_1728. FT /FTId=PRO_0000099776. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 271 291 Helical. {ECO:0000255}. FT TRANSMEM 310 330 Helical. {ECO:0000255}. FT TRANSMEM 331 351 Helical. {ECO:0000255}. FT TRANSMEM 365 385 Helical. {ECO:0000255}. SQ SEQUENCE 397 AA; 41962 MW; 1868D392018BD492 CRC64; MASITHRRNA VLGAAFLMAT SAIGPGFLTQ TATFTNTLLA SFGFVILLSI LLDIGAQLNI WRIVIVSGKR AQDISNAVFP KAGYFLAALI VMGGLAFNIG NVGGAGLGLN SIFGIAPEMG AVISGIIAIL IFLRKEAGLL MDRFAQLMGF IMVVLTFYVM FKTEPPVVEA AYHSFIPEQI DPIAIVTLVG GTVGGYITFA GAHRLLDAGI QGEKAMAEVS RSSVSAILIA STMRVVLFLA VLGVVSKGVS LNPKNPAETP FEYVAGNFGQ VLFGVVIWAA SVTSVIGAAY TSVSFLTTLC PTIERNRNRW IIAFIVISTV VLVTVGKPAA VLVFVGTLNG LILPIALALI LLAAYRSDIV GTYKHPVFLA FSGWFVVIIM AILSGKTIIS YISSFFS // ID Y1730_HAEIN Reviewed; 309 AA. AC P44298; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_1730; GN OrderedLocusNames=HI_1730; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YbgK. {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YcsJ and yeast urea amidolyase (DUR1,2). 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; L42023; AAC23376.1; -; Genomic_DNA. DR PIR; B64041; B64041. DR RefSeq; NP_439871.1; NC_000907.1. DR RefSeq; WP_005694216.1; NC_000907.1. DR STRING; 71421.HI1730; -. DR EnsemblBacteria; AAC23376; AAC23376; HI_1730. DR GeneID; 950540; -. DR KEGG; hin:HI1730; -. DR PATRIC; 20192213; VBIHaeInf48452_1809. DR eggNOG; ENOG4107R7A; Bacteria. DR eggNOG; COG1984; LUCA. DR OMA; GPEYQEF; -. DR OrthoDB; EOG6D5G25; -. DR PhylomeDB; P44298; -. DR BioCyc; RETL1328306-WGS:GSTH-4393-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR003778; CT_A_B. DR InterPro; IPR029000; Cyclophilin-like_dom. DR Pfam; PF02626; AHS2; 1. DR SMART; SM00797; AHS2; 1. DR SUPFAM; SSF50891; SSF50891; 1. DR TIGRFAMs; TIGR00724; urea_amlyse_rel; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 309 Uncharacterized protein HI_1730. FT /FTId=PRO_0000168710. SQ SEQUENCE 309 AA; 34562 MW; E34D87B4C838EF1D CRC64; MIDILDVKSR ATIQDLGRFG LRRFGISHCG AMDKLALRAG NILLGNAENV PAIEVPLGGI TLQFQQDMNF CVTGAFYEMM LDDKPVFAYW RYQVRAGQIL KMARAKIGMY GYLCVQGGFV LPQALNSCST DLRAQIGGIE GRCLQAGDQL QTANDHILRS EIGIAPIPLR DVIRALPSSE YQAFKRKSQY YWWRNEWTLQ SNSDRMGYRF QGQTLELKQP LEMLSHAIQF GSVQVPPSGQ PIILMADAQT TGGYPKIANV IDADLGALAQ VRLGSTIKFE AVSLQEAAKL RRKNEIYLDQ IRRIVDEKN // ID Y1738_HAEIN Reviewed; 244 AA. AC P44302; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized membrane protein HI_1738; GN OrderedLocusNames=HI_1738; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the AzlC 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; L42023; AAC23382.1; -; Genomic_DNA. DR PIR; F64041; F64041. DR RefSeq; NP_439880.1; NC_000907.1. DR RefSeq; WP_010869284.1; NC_000907.1. DR STRING; 71421.HI1738; -. DR EnsemblBacteria; AAC23382; AAC23382; HI_1738. DR GeneID; 950553; -. DR KEGG; hin:HI1738; -. DR PATRIC; 20192233; VBIHaeInf48452_1819. DR eggNOG; ENOG4108UMN; Bacteria. DR eggNOG; COG1296; LUCA. DR OMA; FIVLFME; -. DR OrthoDB; EOG6K9QNJ; -. DR PhylomeDB; P44302; -. DR Proteomes; UP000000579; 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; IPR004471; Brnchd-chn_aa_trnsp_AzlC. DR InterPro; IPR011606; Brnchd-chn_aa_trnsp_permease. DR Pfam; PF03591; AzlC; 1. DR TIGRFAMs; TIGR00346; azlC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 244 Uncharacterized membrane protein HI_1738. FT /FTId=PRO_0000111782. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 165 185 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. SQ SEQUENCE 244 AA; 27360 MW; 7C61B72D4AF16021 CRC64; MNLSQQNQHS NPITEAAKAT FPYSVPMIAG FLFLGIAYGI YMKALGFGFL YPTLMALLIY AGSVEFIAAG ALIAPFSPIS VLLITLMISA RQIFYGISML EKYGIHIGKK RWYLITTLVD ESFSLNYMAK IPPHLDKGWY MFFVSLYLHI YWVLGAAMGN LFGTVLPFNL KGVEFSMTAL FLVIFAENWL KGKSHESSLL GLGIALVFLL IIGKEYFLIP TLIGIWLILT MRITKLETKL ESLK // ID Y183_HAEIN Reviewed; 481 AA. AC P44555; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Uncharacterized transporter HI_0183; GN OrderedLocusNames=HI_0183; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the sodium:alanine (SAF) symporter 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; L42023; AAC21852.1; -; Genomic_DNA. DR PIR; I64144; I64144. DR RefSeq; NP_438351.1; NC_000907.1. DR RefSeq; WP_005694103.1; NC_000907.1. DR STRING; 71421.HI0183; -. DR EnsemblBacteria; AAC21852; AAC21852; HI_0183. DR GeneID; 951094; -. DR KEGG; hin:HI0183; -. DR PATRIC; 20188861; VBIHaeInf48452_0187. DR eggNOG; ENOG4105BZG; Bacteria. DR eggNOG; COG1115; LUCA. DR KO; K03310; -. DR OMA; SIKLKFV; -. DR OrthoDB; EOG6D2KVD; -. DR PhylomeDB; P44555; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR30330; PTHR30330; 1. DR Pfam; PF01235; Na_Ala_symp; 1. DR PRINTS; PR00175; NAALASMPORT. DR TIGRFAMs; TIGR00835; agcS; 1. DR PROSITE; PS00873; NA_ALANINE_SYMP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 481 Uncharacterized transporter HI_0183. FT /FTId=PRO_0000161567. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. FT TRANSMEM 391 411 Helical. {ECO:0000255}. FT TRANSMEM 424 444 Helical. {ECO:0000255}. SQ SEQUENCE 481 AA; 52954 MW; 8BA7E44206A7E8EA CRC64; MIMEFEFSKM LEEVLTWIVA HLDGPLWDAT IIILLGTGLF FTITTGFVQF RLFPASLREM WFGRSVEGSS LTPFQAFTTG LASRVGVGNI GGVATAIALG GEGAVFWMWV TAFIGMSSAF AESTLAQLFK IQDKDGSFRG GPAYYIVQGL KSRCMAVAFA LALIFTFGFA FNSVQANSIV EATSNAWNWK GEYVGISLVI FTALIIFGGV KRIAIISSNL VPMMALFYLI MAVIILGMHI DMIPSVIHRI VQSAFSFDAA AGGMFGALVS KAMMMGIKRG LFSNEAGMGS APNSAAAAHV KHPVSQGLVQ MLGVFVDTMI VCTCTAVIIL LSNNYGSETL KSISLTQNAL QYHIGEFGAH FLAFILLLFA YSSIIGNYAY AESNIRFIKN KPWLVLLFRL MVLFFVYFGA VRSGNVVWNF ADTVMAVMAI INLIAILMLS PIVWKLMKDY QRQLKEGKTP EFKIDEYPEL RKKIFDSRIW K // ID Y198_HAEIN Reviewed; 255 AA. AC P46490; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=UPF0721 transmembrane protein HI_0198; GN OrderedLocusNames=HI_0198; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) 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 UPF0721 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; L42023; AAC21867.1; -; Genomic_DNA. DR RefSeq; NP_438367.1; NC_000907.1. DR RefSeq; WP_005664344.1; NC_000907.1. DR STRING; 71421.HI0198; -. DR EnsemblBacteria; AAC21867; AAC21867; HI_0198. DR GeneID; 951110; -. DR KEGG; hin:HI0198; -. DR PATRIC; 20188893; VBIHaeInf48452_0203. DR eggNOG; ENOG4105EJ9; Bacteria. DR eggNOG; COG0730; LUCA. DR KO; K07090; -. DR OMA; GTNKGQS; -. DR OrthoDB; EOG61VZ6K; -. DR PhylomeDB; P46490; -. DR Proteomes; UP000000579; 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; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 255 UPF0721 transmembrane protein HI_0198. FT /FTId=PRO_0000169190. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 191 211 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. SQ SEQUENCE 255 AA; 27608 MW; 7C0936C07F7B58F5 CRC64; MDIGIDLLAI LFCVGFVASF IDAIAGGGGL ITIPALLMTG MPPAMALGTN KLQAMGGALS ASLYFLRKRA VNLRDIWFIL IWVFLGSALG TLLIQSIDVA IFKKMLPFLI LAIGLYFLFT PKLGDEDRKQ RLSYLLFGLL VSPFLGFYDG FFGPGTGSIM SLACVTLLGF NLPKAAAHAK VMNFTSNLAS FALFLLGGQI LWKVGFVMMA GSILGANLGA KMVMTKGKTL IRPMVVIMSF MMTAKMVYDQ GWFHF // ID Y205_HAEIN Reviewed; 257 AA. AC P43963; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_0205; DE Flags: Precursor; GN OrderedLocusNames=HI_0205; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21878.1; -; Genomic_DNA. DR PIR; H64003; H64003. DR RefSeq; NP_438374.1; NC_000907.1. DR RefSeq; WP_005689698.1; NC_000907.1. DR STRING; 71421.HI0205; -. DR EnsemblBacteria; AAC21878; AAC21878; HI_0205. DR GeneID; 951114; -. DR KEGG; hin:HI0205; -. DR PATRIC; 20188907; VBIHaeInf48452_0210. DR eggNOG; ENOG4106W3N; Bacteria. DR eggNOG; ENOG410YQRV; LUCA. DR OMA; NDTTRYK; -. DR OrthoDB; EOG61GG6J; -. DR Proteomes; UP000000579; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 257 Uncharacterized protein HI_0205. FT /FTId=PRO_0000013954. SQ SEQUENCE 257 AA; 29411 MW; 889FF8AF60A9728B CRC64; MKISFHSVLI GLASFIGVQQ GVIANPSSHQ SISTESAEAL KQQFSMALAK QDKQQITNLQ KKLTALFSLP PQFLDNQIQI SEKILTRIFK TDKNLTPKFL DYLYFEPINT VDANLIQEMK KNLLVSFLAN DQAKIYIRQT DNSEQFVQTL MERGAKADQI ILLSLNAKGI FQKIIEQIRQ DFPNQTIFSI TENRISLITP SSEIKSRLAL ANMMFNRQFK GVEVDDFSYL DQPRENLQHN NDAIRYKTFQ AMLEGLN // ID Y241_HAEIN Reviewed; 97 AA. AC P44592; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=UPF0092 membrane protein HI_0241; GN OrderedLocusNames=HI_0241; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UPF0092 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21909.1; -; Genomic_DNA. DR PIR; A64146; A64146. DR RefSeq; NP_438411.1; NC_000907.1. DR RefSeq; WP_005648822.1; NC_000907.1. DR ProteinModelPortal; P44592; -. DR SMR; P44592; 5-39. DR STRING; 71421.HI0241; -. DR EnsemblBacteria; AAC21909; AAC21909; HI_0241. DR GeneID; 949367; -. DR KEGG; hin:HI0241; -. DR PATRIC; 20189007; VBIHaeInf48452_0256. DR eggNOG; ENOG4105VIE; Bacteria. DR eggNOG; COG1862; LUCA. DR KO; K03210; -. DR OMA; VIELNAN; -. DR OrthoDB; EOG6WQDDS; -. DR PhylomeDB; P44592; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR003849; Preprotein_translocase_YajC. DR Pfam; PF02699; YajC; 1. DR PRINTS; PR01853; YAJCTRNLCASE. DR SMART; SM01323; YajC; 1. DR TIGRFAMs; TIGR00739; yajC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 97 UPF0092 membrane protein HI_0241. FT /FTId=PRO_0000097017. FT TRANSMEM 5 25 Helical. {ECO:0000255}. SQ SEQUENCE 97 AA; 10754 MW; 86F9A683A1D28358 CRC64; MEAQSPMSTL FIFVIFGLIF YFMIYRPQAK RNKEHKKLMS ELAKGTEVLT AGGVIGKITK VTEGSDSIVI ALNDTTEITI NRNYIVSVLP KGSLKSL // ID Y242_HAEIN Reviewed; 73 AA. AC P44593; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=UPF0033 protein HI_0242; GN OrderedLocusNames=HI_0242; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0033 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21910.1; -; Genomic_DNA. DR PIR; B64146; B64146. DR RefSeq; NP_438412.1; NC_000907.1. DR RefSeq; WP_005634417.1; NC_000907.1. DR ProteinModelPortal; P44593; -. DR STRING; 71421.HI0242; -. DR EnsemblBacteria; AAC21910; AAC21910; HI_0242. DR GeneID; 949384; -. DR KEGG; hin:HI0242; -. DR PATRIC; 20189009; VBIHaeInf48452_0257. DR eggNOG; COG0425; LUCA. DR OMA; ELLCEEY; -. DR OrthoDB; EOG6D8BHJ; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.110.40; -; 1. DR InterPro; IPR001455; TusA-like. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS01148; UPF0033; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 73 UPF0033 protein HI_0242. FT /FTId=PRO_0000159069. SQ SEQUENCE 73 AA; 8362 MW; CDAF303DEBFAE3F1 CRC64; MKYQLNLTAL RCPIPLLSAK KALKNLDKND ELMLILNLES AVENFSIFAE ENSVALVEQY YASEKEFIVI LKK // ID Y246_HAEIN Reviewed; 148 AA. AC P43972; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_0246; DE Flags: Precursor; GN OrderedLocusNames=HI_0246; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 21-29, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21914.1; -; Genomic_DNA. DR PIR; H64004; H64004. DR RefSeq; NP_438416.1; NC_000907.1. DR RefSeq; WP_005686672.1; NC_000907.1. DR STRING; 71421.HI0246; -. DR EnsemblBacteria; AAC21914; AAC21914; HI_0246. DR GeneID; 949373; -. DR KEGG; hin:HI0246; -. DR PATRIC; 20189017; VBIHaeInf48452_0261. DR OMA; AVYQFEN; -. DR OrthoDB; EOG6742X6; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR016777; UCP020772. DR PIRSF; PIRSF020772; UCP020772; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Signal. FT SIGNAL 1 20 {ECO:0000269|PubMed:10675023}. FT CHAIN 21 148 Uncharacterized protein HI_0246. FT /FTId=PRO_0000013955. SQ SEQUENCE 148 AA; 15987 MW; C9BC4AE91C25AEF0 CRC64; MNLTKLLPAF AAAVVLSACA KDAPEMTKSS AQIAEMQTLP TITDKTVVYS CNKQTVTAVY QFENQEPVAA MVSVGDGIIA KDFTRDKSQN DFTSFVSGDY VWNVDSGLTL DKFDSVVPVN LIQKGKSSDN IIVKNCDVNV KATKKANL // ID Y275_HAEIN Reviewed; 551 AA. AC P43975; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 91. DE RecName: Full=Uncharacterized protein HI_0275; GN OrderedLocusNames=HI_0275; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21949.1; -; Genomic_DNA. DR PIR; B64005; B64005. DR RefSeq; NP_438444.1; NC_000907.1. DR RefSeq; WP_005694030.1; NC_000907.1. DR ProteinModelPortal; P43975; -. DR STRING; 71421.HI0275; -. DR EnsemblBacteria; AAC21949; AAC21949; HI_0275. DR GeneID; 949970; -. DR KEGG; hin:HI0275; -. DR PATRIC; 20189087; VBIHaeInf48452_0290. DR eggNOG; ENOG4107T7U; Bacteria. DR eggNOG; COG1368; LUCA. DR OMA; WTYFFAI; -. DR OrthoDB; EOG6XQ3GD; -. DR Proteomes; UP000000579; 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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IMP:BHF-UCL. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:BHF-UCL. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 551 Uncharacterized protein HI_0275. FT /FTId=PRO_0000077904. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. FT TRANSMEM 490 510 Helical. {ECO:0000255}. SQ SEQUENCE 551 AA; 62257 MW; BF08FE215695D610 CRC64; MIAYIFLALF TIAAVIFIVN SHYRWTYFFA ITLFTFLFGG MLMVSSQWQR ALNFSSVLFV VLMLFHRLKI HYYKQPLLIS DFFLVVDWRN WETLIHYKGA LFGVIGLLAL LGYAIFGFND VESLGVLGNS IGALLFIVSF SLMWHYSKNP SAVQVWLDSL PDDGRDVFLN LPMSCRGIFF KVPNFDGNSQ NFIEKMTALS SDANNLSETK PDIVVTLMES TLNPHQFAFS QQSIPPLSMF EPQNDTVFAS PLRVHTFAGA TWKSEFAFLA GVPSTDFGAL ASGVFYSVVP HLQSGLVKNL KAQGYFCVAL SPFTKGNYNA KSAYDHFGFD LMLQPQDLGY PAPISKNLWD ISSEEMMKYT RMILEKQHPA LENVDQPMFV YVLTMREHGP YELGMENTFN LQMPNLGAKS ISALNDYTQR IVALNDAIEG INNYLHERKK PFVLGYFGDH QVAFDNAIPP KKGDYAQPDY VTQFVVRSNC ASQFKQEQKF LDLAFAGGVL MNVAGLSAED EFMKANMAMC KLSDGKLEDS SDIQLLNNYR HYLYQTLAIA R // ID Y028_HAEIN Reviewed; 92 AA. AC P44465; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=UPF0250 protein HI_0028; GN OrderedLocusNames=HI_0028; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0250 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; L42023; AAC21706.1; -; Genomic_DNA. DR PIR; F64140; F64140. DR RefSeq; NP_438201.1; NC_000907.1. DR RefSeq; WP_005649857.1; NC_000907.1. DR ProteinModelPortal; P44465; -. DR SMR; P44465; 8-92. DR STRING; 71421.HI0028; -. DR EnsemblBacteria; AAC21706; AAC21706; HI_0028. DR GeneID; 950924; -. DR KEGG; hin:HI0028; -. DR PATRIC; 20188507; VBIHaeInf48452_0028. DR eggNOG; ENOG4108D64; Bacteria. DR eggNOG; COG2921; LUCA. DR KO; K09158; -. DR OMA; EFPCAFT; -. DR OrthoDB; EOG6BGP43; -. DR PhylomeDB; P44465; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.70.1460; -; 1. DR HAMAP; MF_00659; UPF0250; 1. DR InterPro; IPR007454; UPF0250. DR InterPro; IPR027471; YbeD-like. DR Pfam; PF04359; DUF493; 1. DR SUPFAM; SSF117991; SSF117991; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 92 UPF0250 protein HI_0028. FT /FTId=PRO_0000209300. SQ SEQUENCE 92 AA; 10506 MW; 07C8E384FE786C5A CRC64; MTIENDYAKL KELMEFPAKM TFKVAGINRE GLAQDLIQVV QKYIKGDYIP KEKRSSKGTY NSVSIDIIAE NFDQVETLYK ELAKVEGVKM VI // ID Y080_HAEIN Reviewed; 143 AA. AC P43936; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_0080; GN OrderedLocusNames=HI_0080; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YifN. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21755.1; -; Genomic_DNA. DR PIR; H64000; H64000. DR RefSeq; NP_438253.1; NC_000907.1. DR RefSeq; WP_005693840.1; NC_000907.1. DR ProteinModelPortal; P43936; -. DR STRING; 71421.HI0080; -. DR EnsemblBacteria; AAC21755; AAC21755; HI_0080. DR GeneID; 950976; -. DR KEGG; hin:HI0080; -. DR PATRIC; 20188615; VBIHaeInf48452_0081. DR eggNOG; ENOG4105UIH; Bacteria. DR eggNOG; COG3692; LUCA. DR OMA; WIKSELI; -. DR OrthoDB; EOG69WFKZ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 2.30.30.110; -; 1. DR InterPro; IPR003477; PemK-like. DR InterPro; IPR011067; Plasmid_toxin/cell-grow_inhib. DR Pfam; PF02452; PemK_toxin; 1. DR SUPFAM; SSF50118; SSF50118; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 143 Uncharacterized protein HI_0080. FT /FTId=PRO_0000169647. SQ SEQUENCE 143 AA; 16292 MW; D38D71A776669309 CRC64; MSIKQHRPKV GEILECDYGQ FSHTCHVDGH IPPEMVKKRL VVVLNAKLNG LILVAPISSK INLDGIKNGY HIEIDSELIK ATGFYDKRTR WIKSELIQSV SRLRLYHIYD KGTKITQYLP RDVVTKVQRA IIKAINASSL LDK // ID Y1012_HAEIN Reviewed; 210 AA. AC Q57199; O05040; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative aldolase class 2 protein HI_1012; GN OrderedLocusNames=HI_1012; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA 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; L42023; AAC22673.1; -; Genomic_DNA. DR PIR; B64108; B64108. DR RefSeq; NP_439173.1; NC_000907.1. DR RefSeq; WP_005647883.1; NC_000907.1. DR ProteinModelPortal; Q57199; -. DR STRING; 71421.HI1012; -. DR EnsemblBacteria; AAC22673; AAC22673; HI_1012. DR GeneID; 950005; -. DR KEGG; hin:HI1012; -. DR PATRIC; 20190687; VBIHaeInf48452_1056. DR eggNOG; ENOG4105FB2; Bacteria. DR eggNOG; COG0235; LUCA. DR OMA; VMKVGHV; -. DR OrthoDB; EOG6DG2PJ; -. DR PhylomeDB; Q57199; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 210 Putative aldolase class 2 protein FT HI_1012. FT /FTId=PRO_0000162931. FT METAL 74 74 Zinc. {ECO:0000250}. FT METAL 93 93 Zinc. {ECO:0000250}. FT METAL 95 95 Zinc. {ECO:0000250}. FT METAL 160 160 Zinc. {ECO:0000250}. SQ SEQUENCE 210 AA; 23243 MW; 4800CA987DBDF01F CRC64; MTDLAQKELM VQLGRSFYER GYTVGGAGNL SVRLDDNRVL VTPTGSSLGR LSVERLSVLD MEGNLLGGDK PSKEAVFHLA MYKKNPECKA IVHLHSTYLT ALSCLDNLDP NNAIEPFTPY YVMRVGKMQV IPYYRPGSPK IAEELSNRAL TGKAFLLANH GVVVTGSDLL DAADNTEELE ETAKLFFTLQ GQKIRYLTDT EVKDLENRGK // ID Y1013_HAEIN Reviewed; 258 AA. AC Q57151; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative hydroxypyruvate isomerase; DE EC=5.3.1.22; DE AltName: Full=Glyoxylate-induced protein; GN OrderedLocusNames=HI_1013; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible isomerization between CC hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed CC tartronate semialdehyde). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydroxypyruvate = 2-hydroxy-3-oxopropanoate. CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22674.1; -; Genomic_DNA. DR PIR; C64108; C64108. DR RefSeq; NP_439174.1; NC_000907.1. DR RefSeq; WP_005693349.1; NC_000907.1. DR ProteinModelPortal; Q57151; -. DR SMR; Q57151; 1-258. DR STRING; 71421.HI1013; -. DR EnsemblBacteria; AAC22674; AAC22674; HI_1013. DR GeneID; 950733; -. DR KEGG; hin:HI1013; -. DR PATRIC; 20190689; VBIHaeInf48452_1057. DR eggNOG; ENOG4105QG4; Bacteria. DR eggNOG; COG3622; LUCA. DR KO; K01816; -. DR OMA; CEYRPRA; -. DR OrthoDB; EOG6BS8PW; -. DR PhylomeDB; Q57151; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008903; F:hydroxypyruvate isomerase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR026040; HyI-like. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR PIRSF; PIRSF006241; HyI; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 258 Putative hydroxypyruvate isomerase. FT /FTId=PRO_0000209110. SQ SEQUENCE 258 AA; 29348 MW; 94555C63D1E0D69F CRC64; MPKFAANLTM MFNEVPFLDR FEAAAKAGFK YVEFLWPYDY PAQELKAILD KHGLKVVLFN TPAGDVNKGE WGGSAIPGRE ADSHRDIDLA LEYALALGCP NVHIMSAVVP EGASREEYKQ TFIKNVRYAS DKYKPYGIKI QLEALSPEVK PNYLLKSQFD TLEVVELVDR DNVFVQLDYF HAQNVDGNLA RLTDKLNGKF AHVQIASVPD RHEPDEGEIN YQYIFDKLDE IGYTGYVGCE YKPRGETVTG LDWFQKYK // ID Y101_HAEIN Reviewed; 146 AA. AC P43942; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-SEP-2015, entry version 61. DE RecName: Full=Uncharacterized protein HI_0101; GN OrderedLocusNames=HI_0101; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21782.1; -; Genomic_DNA. DR PIR; E64001; E64001. DR MEROPS; M15.024; -. DR EnsemblBacteria; AAC21782; AAC21782; HI_0101. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom. DR InterPro; IPR003709; Pept_M15B. DR Pfam; PF02557; VanY; 1. DR SUPFAM; SSF55166; SSF55166; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Uncharacterized protein HI_0101. FT /FTId=PRO_0000077889. SQ SEQUENCE 146 AA; 16836 MW; E02E4E8D40FF9AEE CRC64; MKLTPEMLTG KSREHLVNLP TTHSSNHFLQ TQAVQAFQAL QQSAAKNGFN LQPASSFRDF ERQQLIWNSK FKGERKVHDD AGKALDLNQL DDWQKCQAIL RWSALLRLVV IIGERKWIFL ILIFCHEVNL YNWSLGNMKK AATSLN // ID Y1028_HAEIN Reviewed; 328 AA. AC P44992; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Uncharacterized protein HI_1028; DE Flags: Precursor; GN OrderedLocusNames=HI_1028; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 262-266, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 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; L42023; AAC22688.1; -; Genomic_DNA. DR PIR; I64164; I64164. DR RefSeq; NP_439188.1; NC_000907.1. DR RefSeq; WP_005647844.1; NC_000907.1. DR ProteinModelPortal; P44992; -. DR STRING; 71421.HI1028; -. DR EnsemblBacteria; AAC22688; AAC22688; HI_1028. DR GeneID; 949528; -. DR KEGG; hin:HI1028; -. DR PATRIC; 20190719; VBIHaeInf48452_1072. DR eggNOG; ENOG4105DR6; Bacteria. DR eggNOG; COG1638; LUCA. DR OMA; TMENEVH; -. DR OrthoDB; EOG63588M; -. DR PhylomeDB; P44992; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR004682; TRAP_DctP. DR InterPro; IPR018389; TRAP_DctP/TeaA. DR Pfam; PF03480; DctP; 1. DR PIRSF; PIRSF006470; DctB; 1. DR TIGRFAMs; TIGR00787; dctP; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 328 Uncharacterized protein HI_1028. FT /FTId=PRO_0000031814. SQ SEQUENCE 328 AA; 36858 MW; A0FBDD8579E872A2 CRC64; MKLFNFKKLS MLIAGFTLVT SPALAEISLR FGYEAPRSDS QHSAAKKFND LLMKKTKGEI KLKLFPDSTL GNAQTMISSV RGGTIDLEMS GSPNFTGLEP KLNVIDIPFI FKDREHVYKV LDGEVGQNLL KDLEKQGLKG LAFWDVGFRA FSNSKQTVTK PEHIKGLKVR TNQNPMYIEA FKLLGSNPVP MPLAELYTAL ETRAVDAQEH PIGIFWSSKL YEVQKYLSLT NHGYTPLIVV MNKAKFDSLL PALQTAIIEA AKEAGQFQRD LNVKNEQNII SKLRKQGVEV IEKINTEPFK TLIEEKVRKS FIEKHGDDLL KKVDALSE // ID Y1034_HAEIN Reviewed; 163 AA. AC P44096; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 94. DE RecName: Full=UPF0234 protein HI_1034; GN OrderedLocusNames=HI_1034; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0234 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; L42023; AAC22694.1; -; Genomic_DNA. DR PIR; F64018; F64018. DR RefSeq; NP_439194.1; NC_000907.1. DR RefSeq; WP_005651674.1; NC_000907.1. DR PDB; 1IN0; X-ray; 2.14 A; A/B=1-163. DR PDBsum; 1IN0; -. DR ProteinModelPortal; P44096; -. DR SMR; P44096; 2-163. DR STRING; 71421.HI1034; -. DR EnsemblBacteria; AAC22694; AAC22694; HI_1034. DR GeneID; 950728; -. DR KEGG; hin:HI1034; -. DR PATRIC; 20190731; VBIHaeInf48452_1078. DR eggNOG; ENOG4108VPT; Bacteria. DR eggNOG; COG1666; LUCA. DR KO; K09767; -. DR OMA; SDFDRQE; -. DR OrthoDB; EOG6FZ4J6; -. DR PhylomeDB; P44096; -. DR EvolutionaryTrace; P44096; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00632; UPF0234; 1. DR InterPro; IPR007551; DUF520. DR Pfam; PF04461; DUF520; 1. DR SUPFAM; SSF89963; SSF89963; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 163 UPF0234 protein HI_1034. FT /FTId=PRO_0000106185. FT STRAND 3 7 {ECO:0000244|PDB:1IN0}. FT HELIX 12 26 {ECO:0000244|PDB:1IN0}. FT HELIX 30 32 {ECO:0000244|PDB:1IN0}. FT STRAND 37 42 {ECO:0000244|PDB:1IN0}. FT TURN 43 46 {ECO:0000244|PDB:1IN0}. FT STRAND 47 53 {ECO:0000244|PDB:1IN0}. FT HELIX 55 71 {ECO:0000244|PDB:1IN0}. FT HELIX 76 78 {ECO:0000244|PDB:1IN0}. FT STRAND 86 88 {ECO:0000244|PDB:1IN0}. FT STRAND 91 98 {ECO:0000244|PDB:1IN0}. FT HELIX 104 117 {ECO:0000244|PDB:1IN0}. FT STRAND 122 126 {ECO:0000244|PDB:1IN0}. FT STRAND 129 133 {ECO:0000244|PDB:1IN0}. FT HELIX 137 149 {ECO:0000244|PDB:1IN0}. FT STRAND 157 162 {ECO:0000244|PDB:1IN0}. SQ SEQUENCE 163 AA; 18551 MW; 1831F75A887A4717 CRC64; MPSFDIVSEI TLHEVRNAVE NANRVLSTRY DFRGVEAVIE LNEKNETIKI TTESDFQLEQ LIEILIGSCI KRGIEHSSLD IPAESEHHGK LYSKEIKLKQ GIETEMAKKI TKLVKDSKIK VQTQIQGEQV RVTGKSRDDL QAVIQLVKSA ELGQPFQFNN FRD // ID Y1037_HAEIN Reviewed; 294 AA. AC P44098; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Putative glutamine amidotransferase HI_1037; DE EC=2.4.2.-; GN OrderedLocusNames=HI_1037; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22697.1; -; Genomic_DNA. DR PIR; H64018; H64018. DR RefSeq; NP_439197.1; NC_000907.1. DR RefSeq; WP_010869111.1; NC_000907.1. DR ProteinModelPortal; P44098; -. DR STRING; 71421.HI1037; -. DR EnsemblBacteria; AAC22697; AAC22697; HI_1037. DR GeneID; 950020; -. DR KEGG; hin:HI1037; -. DR PATRIC; 20190737; VBIHaeInf48452_1081. DR eggNOG; ENOG4105E7A; Bacteria. DR eggNOG; COG0121; LUCA. DR KO; K07008; -. DR OMA; YWVFAHN; -. DR OrthoDB; EOG62K1T4; -. DR PhylomeDB; P44098; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR026869; Put_GATase_2. DR Pfam; PF13230; GATase_4; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Reference proteome; KW Transferase. FT CHAIN 1 294 Putative glutamine amidotransferase FT HI_1037. FT /FTId=PRO_0000168535. FT DOMAIN 18 266 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT ACT_SITE 18 18 {ECO:0000250}. SQ SEQUENCE 294 AA; 33182 MW; 3CCE11294D2F314D CRC64; MVLNHSHIVR LYLIKVMCQL LGMNCNTPTD IVFSFEGFRR RAGLTDCHSD GFGIAFFEGR GVRIFRDNQA ASLSPIADCI KQYNIKSLNV IAHIRKATQG EVNIENTHPF IREIWGQNWV FAHNGNLKNL PDMTDHFLQP IGSTDSEAAF CYMAEYLKNT FRKKPSEMEI FEAIQKVTKG LAQHGTFNFI LSNGEWMIAH CSTNLHYVMR KAPFGKAHRI DDDGVIDFSY YAKAGDKVNI ITTFPLTKNE SWTKMENGGF VFFKNGEKIA EVIGTPKEAI DDGTLGNRTI NSAI // ID Y103A_HAEIN Reviewed; 90 AA. AC O86232; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 55. DE RecName: Full=Uncharacterized protein HI_1037.1; GN OrderedLocusNames=HI_1037.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC22701.1; -; Genomic_DNA. DR EnsemblBacteria; AAC22701; AAC22701; HI_1037.1. DR Proteomes; UP000000579; 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 90 Uncharacterized protein HI_1037.1. FT /FTId=PRO_0000077993. FT TRANSMEM 46 62 Helical. {ECO:0000255}. SQ SEQUENCE 90 AA; 10780 MW; E6A87613F7868C51 CRC64; MYLELHFQFL FRFFSLIPIP CTIPNFRYHT RLLISRNXVF MNKLKMALLV VFLVSLFACT TIHQPKETVK SRFLKNNRLN KISIINIYTT // ID Y1042_HAEIN Reviewed; 617 AA. AC Q57195; P96337; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 99. DE RecName: Full=Uncharacterized protein HI_1042; GN OrderedLocusNames=HI_1042; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 AdoMet activation domain. CC {ECO:0000255|PROSITE-ProRule:PRU00346}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC -!- SIMILARITY: Contains 1 B12-binding N-terminal domain. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L42023; Type=Frameshift; Positions=126; 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; L42023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A61646; A61646. DR ProteinModelPortal; Q57195; -. DR OMA; RIGCELT; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro. DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IBA:GO_Central. DR GO; GO:0019353; P:protoporphyrinogen IX biosynthetic process from glutamate; IBA:GO_Central. DR Gene3D; 1.10.1240.10; -; 1. DR Gene3D; 3.10.196.10; -; 1. DR Gene3D; 3.20.20.330; -; 1. DR Gene3D; 3.40.50.280; -; 1. DR InterPro; IPR003759; Cbl-bd_cap. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR003726; HCY_dom. DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF02607; B12-binding_2; 1. DR Pfam; PF02965; Met_synt_B12; 1. DR SMART; SM01018; B12-binding_2; 1. DR SUPFAM; SSF47644; SSF47644; 1. DR SUPFAM; SSF52242; SSF52242; 1. DR SUPFAM; SSF56507; SSF56507; 1. DR SUPFAM; SSF82282; SSF82282; 1. DR PROSITE; PS50974; ADOMET_ACTIVATION; 1. DR PROSITE; PS51332; B12_BINDING; 1. DR PROSITE; PS51337; B12_BINDING_NTER; 1. PE 3: Inferred from homology; KW Cobalt; Complete proteome; Metal-binding; Reference proteome; Repeat; KW S-adenosyl-L-methionine. FT CHAIN 1 617 Uncharacterized protein HI_1042. FT /FTId=PRO_0000204544. FT DOMAIN 33 134 B12-binding N-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00666}. FT DOMAIN 136 272 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT DOMAIN 288 617 AdoMet activation. {ECO:0000255|PROSITE- FT ProRule:PRU00346}. FT REGION 224 225 Cobalamin-binding. {ECO:0000250}. FT REGION 583 584 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 149 149 Cobalt (cobalamin axial ligand). FT {ECO:0000250}. FT BINDING 194 194 Cobalamin. {ECO:0000250}. FT BINDING 337 337 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 528 528 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 532 532 Cobalamin; via carbonyl oxygen. FT {ECO:0000250}. SQ SEQUENCE 617 AA; 69414 MW; D49B2F91E5C5403F CRC64; MVNKTAQLKQ ALENRILILD GAMGTMIQKY KLTEDDFRGE KFKKSAVDSV AEWCTWPVGE LLKHALVKGI TTCQTLPSPL DVIEGPLMAG MDVVGDLFGD GKMFLPQVVK SARVMKQSVA YLEPFXNATK QKGSSNGKVV IATVKGDVHD IGKNIVSVVM QCNNFEVIDL GVMVPADKII QTAINQKTDI IALSGLITPS LDEMEYFLGE MTRLGLNLPV MIGGATTSKE HTAIKLYPKY KQHCVFYTSN ASRAVTVCAT LMNPEGRAAL WEQFKKDYEK IQQSFANSKP LRKQLSIEEA RDGFSGEWAD YVPPTPKQTG IVEFKNVPIA ELRKFIDWSP FFRIWGLMGC YPDAFDYPEG GEEARKVWND AQVVLDELEQ NHKLNPSGIL GIFPAERVGD DVVLFSDEER TQTIGTAYGL RQQTERGKNS KSPFNFCLSD FIADRQSGKK NWFGMFAVCV GVEEMELVEG YKAAGDDYNA ILLQAVGDRL AEAMAEYLHF ELRTRIWGYT QEEFDNQGLI NENYVGIRPA PGYPSWPEHT EKALIWDLLE VEQRIGMKLT ESYAMWPAAS VCGWYFTHPA SNYFTLGRID EDQAQDYAKR KGWDEREMMK WLGVAMK // ID Y1058_HAEIN Reviewed; 194 AA. AC P44106; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_1058; DE Flags: Precursor; GN OrderedLocusNames=HI_1058; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22722.1; -; Genomic_DNA. DR PIR; G64019; G64019. DR RefSeq; NP_439216.1; NC_000907.1. DR RefSeq; WP_010869120.1; NC_000907.1. DR STRING; 71421.HI1058; -. DR REBASE; 3701; M.HindVI. DR EnsemblBacteria; AAC22722; AAC22722; HI_1058. DR GeneID; 949400; -. DR KEGG; hin:HI1058; -. DR PATRIC; 20190779; VBIHaeInf48452_1102. DR eggNOG; ENOG41068I1; Bacteria. DR eggNOG; COG2189; LUCA. DR OMA; IHQINPK; -. DR OrthoDB; EOG6PGK5X; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR022221; TypeIII_RM_meth. DR Pfam; PF12564; TypeIII_RM_meth; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 194 Uncharacterized protein HI_1058. FT /FTId=PRO_0000013964. SQ SEQUENCE 194 AA; 21806 MW; 084B806553E093B2 CRC64; MKTDIQTELT QALLSHEKVW ANEEKTILAK NILLDLVEKT DPTIIGLLLG NDDLKRHFFV EVNGVLVFKL QDFRFFLDKH SINNSYTKYA NRIGLTDGNR FLKDSSDIVL DFPFKDCVLN GGQSTEEGEE IYFKRNNSQS VSQSVSQSVS QSVSQSVSQS VSQSVSQSVS QSVSQSVSQS IIHQINPKKT RNLF // ID Y1082_HAEIN Reviewed; 85 AA. AC P45026; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_1082; GN OrderedLocusNames=HI_1082; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the BolA/IbaG 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; L42023; AAC22738.1; -; Genomic_DNA. DR PIR; I64165; I64165. DR RefSeq; NP_439239.1; NC_000907.1. DR RefSeq; WP_005686372.1; NC_000907.1. DR ProteinModelPortal; P45026; -. DR STRING; 71421.HI1082; -. DR PRIDE; P45026; -. DR EnsemblBacteria; AAC22738; AAC22738; HI_1082. DR GeneID; 949428; -. DR KEGG; hin:HI1082; -. DR PATRIC; 20190829; VBIHaeInf48452_1127. DR eggNOG; ENOG4105VFK; Bacteria. DR eggNOG; COG5007; LUCA. DR OMA; TINAFTP; -. DR OrthoDB; EOG6VMTQ7; -. DR PhylomeDB; P45026; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.300.90; -; 1. DR InterPro; IPR002634; BolA. DR Pfam; PF01722; BolA; 1. DR PIRSF; PIRSF003113; BolA; 1. DR SUPFAM; SSF82657; SSF82657; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 85 Uncharacterized protein HI_1082. FT /FTId=PRO_0000201221. SQ SEQUENCE 85 AA; 9769 MW; 6CFB509428CF34C5 CRC64; MELQKIEQIL KDTLNIAEVY AQGENAHFGV IVVSDEIAAL SRVKQQQTIY APLMPYFSTG EIHALTIKTY TVEKWKRDRA LNQFN // ID Y1104_HAEIN Reviewed; 407 AA. AC P71369; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Putative metabolite transport protein HI_1104; GN OrderedLocusNames=HI_1104; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Aromatic CC acid:H(+) symporter (AAHS) (TC 2.A.1.15) 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; L42023; AAC22759.1; -; Genomic_DNA. DR PIR; C64167; C64167. DR RefSeq; NP_439261.1; NC_000907.1. DR RefSeq; WP_005693428.1; NC_000907.1. DR ProteinModelPortal; P71369; -. DR STRING; 71421.HI1104; -. DR EnsemblBacteria; AAC22759; AAC22759; HI_1104. DR GeneID; 950078; -. DR KEGG; hin:HI1104; -. DR PATRIC; 20190879; VBIHaeInf48452_1152. DR eggNOG; ENOG4107RGD; Bacteria. DR eggNOG; ENOG410ZVI6; LUCA. DR OMA; VIYVIDM; -. DR OrthoDB; EOG64JFK2; -. DR PhylomeDB; P71369; -. DR Proteomes; UP000000579; 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:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 407 Putative metabolite transport protein FT HI_1104. FT /FTId=PRO_0000050490. FT TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 17 37 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 38 48 Periplasmic. {ECO:0000255}. FT TRANSMEM 49 69 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 70 77 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 78 98 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 99 107 Periplasmic. {ECO:0000255}. FT TRANSMEM 108 128 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 129 138 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 139 159 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 160 160 Periplasmic. {ECO:0000255}. FT TRANSMEM 161 181 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 182 224 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 225 245 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 246 261 Periplasmic. {ECO:0000255}. FT TRANSMEM 262 282 Helical; Name=8. {ECO:0000255}. FT TOPO_DOM 283 288 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 289 309 Helical; Name=9. {ECO:0000255}. FT TOPO_DOM 310 312 Periplasmic. {ECO:0000255}. FT TRANSMEM 313 333 Helical; Name=10. {ECO:0000255}. FT TOPO_DOM 334 357 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 358 378 Helical; Name=11. {ECO:0000255}. FT TRANSMEM 379 399 Helical; Name=12. {ECO:0000255}. FT TOPO_DOM 400 407 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 407 AA; 43682 MW; 618588C6CB37C4A9 CRC64; MTNKVNSYGW KALIGSAVGY GMDGFDLLIL GFMLSAISAD LNLTPAQGGS LVTWTLIGAV FGGILFGALS DKYGRVRVLT WTILLFAVFT GLCAIAQGYW DLLIYRTIAG IGLGGEFGIG MALAAEAWPA RHRAKAASYV ALGWQVGVLG AALLTPLLLP HIGWRGMFLV GIFPAFVAWF LRSHLHEPEI FTQKQTALST QSSFTDKLRS FQLLIKDKAT SKISLGIVVL TSVQNFGYYG IMIWLPNFLS KQLGFSLTKS GLWTAVTVCG MMAGIWIFGQ LADRIGRKPS FLLFQLGAVI SIVVYSQLTD PDIMLLAGAF LGMFVNGMLG GYGALMAEAY PTEARATAQN VLFNIGRAVG GFGPVVVGSV VLAYSFQTAI ALLAIIYVID MLATIFLIPE LKGKALD // ID Y1119_HAEIN Reviewed; 292 AA. AC Q57273; O05045; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1119; GN OrderedLocusNames=HI_1119; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22773.1; -; Genomic_DNA. DR PIR; A64184; A64184. DR RefSeq; NP_439276.1; NC_000907.1. DR RefSeq; WP_005693441.1; NC_000907.1. DR STRING; 71421.HI1119; -. DR DNASU; 950085; -. DR EnsemblBacteria; AAC22773; AAC22773; HI_1119. DR GeneID; 950085; -. DR KEGG; hin:HI1119; -. DR PATRIC; 20190911; VBIHaeInf48452_1168. DR eggNOG; ENOG4108MJ5; Bacteria. DR eggNOG; COG2990; LUCA. DR KO; K09824; -. DR OMA; FEGSKEM; -. DR OrthoDB; EOG6TBHCV; -. DR PhylomeDB; Q57273; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007488; DUF535. DR Pfam; PF04393; DUF535; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 292 Uncharacterized protein HI_1119. FT /FTId=PRO_0000078004. SQ SEQUENCE 292 AA; 34446 MW; 24CB983EBFE1FA89 CRC64; MAIQMTTKTT YQWPQSKDIY PYRPGRFDAP KHWRYNLRSF LNRGSIRRFE QFINQHPFLI DIFNTHLDYS YPVACRFLDK RFNASQRFHA VCENLLFLPE KLTALSTPLW EKPLSFGEVI PDFEMTLSMT THQPMEGYWV LELWHKPRNE LVYLLTFAKL GDALLIAVVQ GPNFEGSKEM VKQLTKLCHG LRPAYLMVET MKSLTKILGY NKLLGIPQKY QNKSRFIQSK QYTVDYDAIF GESGGELKDY WELPLEMDRN LDDIPSKKRS MYRKRYAMLD DLAKVIEEKL GL // ID Y1168_HAEIN Reviewed; 114 AA. AC P44117; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=UPF0265 protein HI_1168; GN OrderedLocusNames=HI_1168; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0265 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; L42023; AAC22823.1; -; Genomic_DNA. DR PIR; I64020; I64020. DR RefSeq; NP_439326.1; NC_000907.1. DR RefSeq; WP_005653635.1; NC_000907.1. DR STRING; 71421.HI1168; -. DR EnsemblBacteria; AAC22823; AAC22823; HI_1168. DR GeneID; 950127; -. DR KEGG; hin:HI1168; -. DR PATRIC; 20191015; VBIHaeInf48452_1220. DR eggNOG; ENOG41090HJ; Bacteria. DR eggNOG; COG2926; LUCA. DR KO; K09802; -. DR OMA; IANMRSD; -. DR OrthoDB; EOG6KHG27; -. DR PhylomeDB; P44117; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00683; UPF0265; 1. DR InterPro; IPR007458; DUF496. DR Pfam; PF04363; DUF496; 1. DR PIRSF; PIRSF028773; UCP028773; 1. DR ProDom; PD030876; DUF496; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 114 UPF0265 protein HI_1168. FT /FTId=PRO_0000072764. SQ SEQUENCE 114 AA; 13867 MW; B1D3E628F90CC7AC CRC64; MEIVNKQSFQ DVLEYVRMYR LKNRIKRDME DNNRKIRDNQ KRILLLDNLN QYIRDDMTIA EVRGIIESMR DDYESRVDDY TIRNAELSKQ RREASTKMKE QKKAHAELLK NAEK // ID Y1170_HAEIN Reviewed; 328 AA. AC Q57527; O05047; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 22-JUL-2015, entry version 86. DE RecName: Full=Uncharacterized PabA-like protein HI_1170; GN OrderedLocusNames=HI_1170; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To the C-terminal of para-aminobenzoate synthase CC component I. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22834.1; -; Genomic_DNA. DR PIR; F64187; F64187. DR RefSeq; WP_005694271.1; NC_000907.1. DR RefSeq; YP_008530235.1; NC_000907.1. DR ProteinModelPortal; Q57527; -. DR EnsemblBacteria; AAC22834; AAC22834; HI_1170. DR GeneID; 950132; -. DR KEGG; hin:HI1169; -. DR KO; K01665; -. DR OMA; CDSPREI; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 328 Uncharacterized PabA-like protein FT HI_1170. FT /FTId=PRO_0000154153. SQ SEQUENCE 328 AA; 37734 MW; 1C02BCD0088957B0 CRC64; MAQSTMQHFI EQANHYGKQR TPFFFLIDFE KEKPLICPLE NSAQQGIYFD ILGKRNCTIS PRPLPLNFTK HPMPFSHYQQ GFKLVQSELQ KGNSYLLNLT YPTEISGNLS LEQIFHQTNA PYKLWLQDQF VCFSPECFVN IHDNNIFTYP MKGTINATLP DAENQLLTNE KEQREHYTIV DLMRNDLSMV AEHIQVKKFR YIDRIKTQKG KILQTSSEIY GKLNENWQNQ IGDILATLLP AGSISGAPKE KTTQIIQQAE KQKRGYYTGI FGIFDGKTLQ SAVAIRFISQ VDEKFYFHSG GGITIHSNAQ DEYEELLEKV YLPIEGAD // ID Y1202_HAEIN Reviewed; 167 AA. AC P44126; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=UPF0115 protein HI_1202; GN OrderedLocusNames=HI_1202; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0115 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Smr 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; L42023; AAC22856.1; -; Genomic_DNA. DR PIR; I64021; I64021. DR RefSeq; NP_439358.2; NC_000907.1. DR ProteinModelPortal; P44126; -. DR STRING; 71421.HI1202; -. DR DNASU; 950140; -. DR EnsemblBacteria; AAC22856; AAC22856; HI_1202. DR GeneID; 950140; -. DR KEGG; hin:HI1202; -. DR PATRIC; 20191083; VBIHaeInf48452_1254. DR eggNOG; ENOG4108DG9; Bacteria. DR eggNOG; COG2840; LUCA. DR OMA; EHVYCAS; -. DR OrthoDB; EOG66B3ZJ; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_01042; UPF0115; 1. DR InterPro; IPR002625; Smr_dom. DR InterPro; IPR022990; UPF0115. DR Pfam; PF01713; Smr; 1. DR SMART; SM00463; SMR; 1. DR SUPFAM; SSF160443; SSF160443; 1. DR PROSITE; PS50828; SMR; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 167 UPF0115 protein HI_1202. FT /FTId=PRO_0000214555. FT DOMAIN 91 166 Smr. SQ SEQUENCE 167 AA; 19393 MW; 3726C9DE68512BF2 CRC64; MQDEFDLFRT ETKGIKPIKQ DTFVAPRQKR DQKKIELKEL RAKEDTLFYF SDEYEPLLND NDGVVKYLRD GEDSHLLKQL RRGDFSPELF LDLHGLTREQ AKQELAALLL ACENEHVDCA SIMTGYGTFT LKKQIPRWLV QHPKVRALHQ APREWGGEAA ILILVDL // ID Y1236_HAEIN Reviewed; 367 AA. AC P44132; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein HI_1236; GN OrderedLocusNames=HI_1236; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YdgA and YihF. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22888.1; -; Genomic_DNA. DR PIR; F64022; F64022. DR STRING; 71421.HI1236; -. DR EnsemblBacteria; AAC22888; AAC22888; HI_1236. DR PATRIC; 20191151; VBIHaeInf48452_1288. DR eggNOG; COG5339; LUCA. DR OMA; LNIDEYS; -. DR OrthoDB; EOG6CGC8W; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010352; DUF945. DR Pfam; PF06097; DUF945; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 367 Uncharacterized protein HI_1236. FT /FTId=PRO_0000078010. FT TRANSMEM 6 26 Helical. {ECO:0000255}. SQ SEQUENCE 367 AA; 41355 MW; B00211C5F98C2585 CRC64; MKKSKIAAGV VVALAAVWCT SAWFTGKKAE EEYLYQLEQL NQLFTKTEAL EESKIFYKNI KFERGLFASH IQDQIEIHKA NETIIIPLSS TLYHGPLPLD RVAKLNFVPA IFSSQTLLGK NATTQAFFDI TESEKPLQLN FAMNYSLSGN AELKLASGQY HNEQSKTDFD WSNVVLNIDL NQNTPNNYVL SVDTFNSNAP NHAVSTASSI KIKDLVVQGS LQSTKWPFIY SGNINSKIGY FEQNTESAES GEKFSLIQKN SQANLTTQVE GDTVNIINKT NLDELHINGN NLGKVTNNVE FNHIDGNALQ ELLNILVAIG KADSECLYLK HWCKNYNKQA WPLRIISLKL SLPLFLFLMK KAKWHWI // ID Y1240_HAEIN Reviewed; 220 AA. AC P45122; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=UPF0126 membrane protein HI_1240; GN OrderedLocusNames=HI_1240; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0126 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; L42023; AAC22893.1; -; Genomic_DNA. DR PIR; E64169; E64169. DR RefSeq; NP_439396.1; NC_000907.1. DR RefSeq; WP_005694300.1; NC_000907.1. DR STRING; 71421.HI1240; -. DR EnsemblBacteria; AAC22893; AAC22893; HI_1240. DR GeneID; 950105; -. DR KEGG; hin:HI1240; -. DR PATRIC; 20191159; VBIHaeInf48452_1292. DR eggNOG; ENOG4105EN6; Bacteria. DR eggNOG; COG2860; LUCA. DR OMA; IFQKELY; -. DR OrthoDB; EOG6WMJ34; -. DR PhylomeDB; P45122; -. DR Proteomes; UP000000579; 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; IPR005115; UPF0126. DR Pfam; PF03458; UPF0126; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 220 UPF0126 membrane protein HI_1240. FT /FTId=PRO_0000166302. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. SQ SEQUENCE 220 AA; 24228 MW; 58506FAF1C5570BF CRC64; MLLSILYIIG ITAEGMTGAL AAGREKMDIF GVIIIASVTA IGGGSVRDVL LGHYPLGWVK HPEYFLMVAS AAVITVYVAP FINHFMRYFR TIFLVLDAMG LVVYSIIGAQ IAMDMGHSLT IVCIAGCITG AFGGVLRDML CNRIPLVFQK ELYASIALFA TLTYYALSTL QVEHTLAVLL TLINSFTLRL LAIHFEWGLP VFNYQELTSE EQDKQPNKKK // ID Y1250_HAEIN Reviewed; 101 AA. AC P44138; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_1250; GN OrderedLocusNames=HI_1250; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22909.1; -; Genomic_DNA. DR PIR; C64023; C64023. DR RefSeq; NP_439406.1; NC_000907.1. DR RefSeq; WP_005694311.1; NC_000907.1. DR STRING; 71421.HI1250; -. DR EnsemblBacteria; AAC22909; AAC22909; HI_1250. DR GeneID; 950243; -. DR KEGG; hin:HI1250; -. DR PATRIC; 20191181; VBIHaeInf48452_1302. DR eggNOG; ENOG41080ET; Bacteria. DR eggNOG; COG3549; LUCA. DR KO; K07334; -. DR OMA; WLRAFFV; -. DR OrthoDB; EOG6JQH8N; -. DR PhylomeDB; P44138; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007711; HigB-1. DR Pfam; PF05015; HigB-like_toxin; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 101 Uncharacterized protein HI_1250. FT /FTId=PRO_0000078014. SQ SEQUENCE 101 AA; 12249 MW; 1C4E4A04E6EED11B CRC64; MFNLKREHFR DDYLYRFYQY GDTHSKIPSN LYKVLARKLD MISASENIND LRSPPANHLE LLEPKENKIY SIRVNKQYCL IFKYENNEVN NLYLDPHSYN L // ID Y1292_HAEIN Reviewed; 261 AA. AC P44154; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1292; GN OrderedLocusNames=HI_1292; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22948.1; -; Genomic_DNA. DR PIR; A64025; A64025. DR RefSeq; NP_439444.1; NC_000907.1. DR RefSeq; WP_005694477.1; NC_000907.1. DR STRING; 71421.HI1292; -. DR EnsemblBacteria; AAC22948; AAC22948; HI_1292. DR GeneID; 949593; -. DR KEGG; hin:HI1292; -. DR PATRIC; 20191267; VBIHaeInf48452_1344. DR eggNOG; ENOG4105EXF; Bacteria. DR eggNOG; COG5595; LUCA. DR OMA; MYIQEIS; -. DR OrthoDB; EOG6GBM87; -. DR PhylomeDB; P44154; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR016908; UCP029037. DR Pfam; PF10071; DUF2310; 1. DR PIRSF; PIRSF029037; UCP029037_Zn_ribbon; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein HI_1292. FT /FTId=PRO_0000078022. SQ SEQUENCE 261 AA; 29818 MW; DE5DBAB18BB4334F CRC64; MYLIETYFRL TALENNIESQ SRLLNAVIDQ WRYNGQIIGR EIPLYLAEED GAQGFAMRVI CPEQDSLFPQ NNNAEVNRAL QEAEKCGVIF DGFQLVGDDF NSDQTAENAS PAWQVLYTTH LQSCSPIHSG ENFAPIPLYK QLKNQPHLTQ DLIKWQENWQ ACDQLQMNGA VLEQQSLAEI SDHQSTLSKH GRYLAQEIEK ETGIPTYYYL YRVGGQSLKS EKSRCCPSCG ANWALKDAIF DTFHFKCDTC RLVSNLSWNF L // ID Y1293_HAEIN Reviewed; 126 AA. AC P44156; P44155; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized SufE-like protein HI_1293; GN OrderedLocusNames=HI_1293; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the SufE 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; L42023; AAC22947.1; -; Genomic_DNA. DR PIR; T09422; B64025. DR RefSeq; NP_439445.1; NC_000907.1. DR RefSeq; WP_005694476.1; NC_000907.1. DR ProteinModelPortal; P44156; -. DR STRING; 71421.HI1293; -. DR EnsemblBacteria; AAC22947; AAC22947; HI_1293. DR GeneID; 950226; -. DR KEGG; hin:HI1293; -. DR PATRIC; 20191269; VBIHaeInf48452_1345. DR eggNOG; ENOG4105P9C; Bacteria. DR eggNOG; COG2166; LUCA. DR KO; K07125; -. DR OMA; KNWEERY; -. DR OrthoDB; EOG61047S; -. DR PhylomeDB; P44156; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003808; Fe-S_metab-assoc_dom. DR Pfam; PF02657; SufE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 126 Uncharacterized SufE-like protein FT HI_1293. FT /FTId=PRO_0000202138. SQ SEQUENCE 126 AA; 14643 MW; 42E1D49D6AA4AD48 CRC64; MIEQLKQAKN WEDRYRLIIQ AGKNLPRPSD NELAQMQPIT GCEAQMWFQI MPKNDRTFQF SGFSEARIMN GLLWILFNQI NGKTADELNT FDITVFFSEL GISQRLSEMR LNGLNQIGQQ LKNLCI // ID Y1307_HAEIN Reviewed; 210 AA. AC Q57320; O05057; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Uncharacterized membrane protein HI_1307; GN OrderedLocusNames=HI_1307; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the rht 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; L42023; AAC22954.1; -; Genomic_DNA. DR PIR; F64115; F64115. DR RefSeq; NP_439458.1; NC_000907.1. DR RefSeq; WP_005694463.1; NC_000907.1. DR STRING; 71421.HI1307; -. DR EnsemblBacteria; AAC22954; AAC22954; HI_1307. DR GeneID; 950239; -. DR KEGG; hin:HI1307; -. DR PATRIC; 20191297; VBIHaeInf48452_1359. DR eggNOG; ENOG4105CCF; Bacteria. DR eggNOG; COG1280; LUCA. DR OMA; NITEMWQ; -. DR OrthoDB; EOG63VC09; -. DR PhylomeDB; Q57320; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GOC. DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central. DR InterPro; IPR004778; Homoserine/Threonine_efflux. DR InterPro; IPR001123; LysE-type. DR PANTHER; PTHR30086; PTHR30086; 1. DR Pfam; PF01810; LysE; 1. DR TIGRFAMs; TIGR00949; 2A76; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 210 Uncharacterized membrane protein HI_1307. FT /FTId=PRO_0000094744. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. SQ SEQUENCE 210 AA; 23636 MW; 254D159014845473 CRC64; MMLNLIIVHL FGLMTPGPDF FYVSRMAASN SRRNTVCGIL GITLGIAFWG MLSMLGLAVL FVTIPALHGV IMLLGGSYLA YLGFLMARSK KYAKFESHSD TEFNQQTTIK KEILKGLLVN LSNAKVVVYF SSVMSLVLVN ITEMWQIILA FAVIVVETFC YFYVISLIFS RNIAKRLYSQ YSRYIDNMAG IVFLFFGCVL VYNGINEIIH // ID Y1341_HAEIN Reviewed; 203 AA. AC P44166; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_1341; GN OrderedLocusNames=HI_1341; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22993.1; -; Genomic_DNA. DR PIR; D64026; D64026. DR RefSeq; NP_439492.1; NC_000907.1. DR RefSeq; WP_005694017.1; NC_000907.1. DR STRING; 71421.HI1341; -. DR EnsemblBacteria; AAC22993; AAC22993; HI_1341. DR GeneID; 950616; -. DR KEGG; hin:HI1341; -. DR PATRIC; 20191365; VBIHaeInf48452_1393. DR eggNOG; ENOG4105EXF; Bacteria. DR eggNOG; COG5595; LUCA. DR OMA; ELQFECF; -. DR OrthoDB; EOG6GBM87; -. DR PhylomeDB; P44166; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR016908; UCP029037. DR Pfam; PF10071; DUF2310; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 203 Uncharacterized protein HI_1341. FT /FTId=PRO_0000078031. SQ SEQUENCE 203 AA; 23166 MW; 96B8B0055040DCDE CRC64; MLCWIGYKNG ILPQQNSTLY PWLNPSKCGV IFDGFQLVGD DFNSDQTAEN TSPAWQVLYT THLQSCSPIH SGENFAPIPL YKQLKNQPHL SQDLIKWQEN WQACDQLQMN GAVLEQQSLA EISDHQSTLS KHGRYLAQEI EKETGIPTYY YLYRVGGQSL ESEKSRCCPS CGANWALKDA IFDTFHFKCD TCRLVSNLSW NFL // ID Y1402_HAEIN Reviewed; 68 AA. AC P44177; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_1402; GN OrderedLocusNames=HI_1402; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23052.1; -; Genomic_DNA. DR PIR; G64027; G64027. DR STRING; 71421.HI1402; -. DR EnsemblBacteria; AAC23052; AAC23052; HI_1402. DR PATRIC; 20191503; VBIHaeInf48452_1462. DR eggNOG; ENOG4106D24; Bacteria. DR eggNOG; ENOG410Y78H; LUCA. DR OMA; EIEQWQF; -. DR OrthoDB; EOG65F8TJ; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020088; Uncharacterised_HI1402. DR ProDom; PD055258; Uncharacterised_HI1402; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 68 Uncharacterized protein HI_1402. FT /FTId=PRO_0000078040. SQ SEQUENCE 68 AA; 7841 MW; 396F3C4AA8DB7D29 CRC64; MLTQIARNRG VPFEILVEKV IEKSAQFAVV IGIIIGQRQA FEDRLLTFNP PEELTALEQE IEQWQFPT // ID Y1404_HAEIN Reviewed; 39 AA. AC P44179; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-SEP-2015, entry version 51. DE RecName: Full=Uncharacterized protein HI_1404; GN OrderedLocusNames=HI_1404; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23054.1; -; Genomic_DNA. DR PIR; I64027; I64027. DR EnsemblBacteria; AAC23054; AAC23054; HI_1404. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 39 Uncharacterized protein HI_1404. FT /FTId=PRO_0000078042. SQ SEQUENCE 39 AA; 4311 MW; 59E0DED12F777FEE CRC64; MTVSISVPSA STSDFKKFAI NHLDILPRQA GVQYLFNLT // ID Y1406_HAEIN Reviewed; 118 AA. AC P44181; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1406; GN OrderedLocusNames=HI_1406; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23056.1; -; Genomic_DNA. DR PIR; B64028; B64028. DR RefSeq; NP_439558.1; NC_000907.1. DR RefSeq; WP_005693956.1; NC_000907.1. DR STRING; 71421.HI1406; -. DR EnsemblBacteria; AAC23056; AAC23056; HI_1406. DR GeneID; 950830; -. DR KEGG; hin:HI1406; -. DR PATRIC; 20191511; VBIHaeInf48452_1466. DR eggNOG; ENOG410682P; Bacteria. DR eggNOG; ENOG410XV73; LUCA. DR OMA; KRDMDLV; -. DR OrthoDB; EOG6HB9WV; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019650; DUF2513. DR Pfam; PF10711; DUF2513; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 118 Uncharacterized protein HI_1406. FT /FTId=PRO_0000078044. SQ SEQUENCE 118 AA; 13325 MW; C1CAF33E6CBB3452 CRC64; MKRNWDLIRS ILLKLESQSE ARGSLLPDGF TGFDSETVSY HFKLLQSAGL IEAIDYSSLN EMSLIARLLT WQGHELLDKI RNDTVWNSLK TTIKSKSLDL SLDAIKQVAQ TIISQMLA // ID Y1407_HAEIN Reviewed; 447 AA. AC P71385; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_1407; GN OrderedLocusNames=HI_1407; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli plasmid IncP-alpha RP4 protein TraN. 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; L42023; AAC23048.1; -; Genomic_DNA. DR PIR; B64122; B64122. DR RefSeq; NP_439559.1; NC_000907.1. DR RefSeq; WP_005693955.1; NC_000907.1. DR STRING; 71421.HI1407; -. DR EnsemblBacteria; AAC23048; AAC23048; HI_1407. DR GeneID; 950320; -. DR KEGG; hin:HI1407; -. DR PATRIC; 20191513; VBIHaeInf48452_1467. DR eggNOG; ENOG4108C66; Bacteria. DR eggNOG; ENOG410XSV1; LUCA. DR OMA; HPLYENA; -. DR OrthoDB; EOG6QRWBC; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR006528; Phage_head_morphogenesis. DR Pfam; PF04233; Phage_Mu_F; 1. DR TIGRFAMs; TIGR01641; phageSPP1_gp7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 447 Uncharacterized protein HI_1407. FT /FTId=PRO_0000078045. SQ SEQUENCE 447 AA; 50114 MW; 814D0706EE828EE5 CRC64; MLMNLPEILK NQKARARKFK PVKMSKRTEL WYRQQLKQFV KMMTNDVERA LQQPQGSFFM DDAKGFQAIS AKALMKVLEK YEKSDRTSQA ENIANGFVSR GDAQNHAEVS TNLKNQTGID LSAYLRNSPN ITEKVNALTA GNIQLIKSIR SQYLDKVQNA VMQAMVRGSL NKDLAAQIKD LGKTTEKRAM FIARDQSSKL NAALTQARHE EVGIKKYMWS ASLDERVRES HAEKDGQIFE YANPPADTDH PGHDFNCRCV QIPVLDNNEQ IVKNSPIVSQ QEKQQMRSEW SDDFPDTIID RKLGDATSHP LYENAKKGSI EDAYQLAKDL VTDDAVNKLK QLVGNKNAIL IPVHAEEAVG QNMIPVAIAT VLSKKLHIPV DLSIVQATKV SRTGGDGWHR LVYSPAFDGI VPKDKYAIIL DDTQTQGGTL ASLKGYIIKE KLLHLML // ID Y1409_HAEIN Reviewed; 436 AA. AC P44183; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_1409; GN OrderedLocusNames=HI_1409; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23057.1; -; Genomic_DNA. DR PIR; D64028; D64028. DR RefSeq; NP_439560.1; NC_000907.1. DR RefSeq; WP_005693954.1; NC_000907.1. DR STRING; 71421.HI1409; -. DR DNASU; 950321; -. DR EnsemblBacteria; AAC23057; AAC23057; HI_1409. DR GeneID; 950321; -. DR KEGG; hin:HI1409; -. DR PATRIC; 20191515; VBIHaeInf48452_1468. DR eggNOG; ENOG4107ZQ5; Bacteria. DR eggNOG; COG3567; LUCA. DR KO; K09961; -. DR OMA; YHESIHR; -. DR OrthoDB; EOG622PPK; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR024459; DUF1073. DR InterPro; IPR006445; Phage-assoc_HI1409. DR Pfam; PF06381; DUF1073; 1. DR TIGRFAMs; TIGR01555; phge_rel_HI1409; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 436 Uncharacterized protein HI_1409. FT /FTId=PRO_0000078046. SQ SEQUENCE 436 AA; 48921 MW; EF32DEDD7BF17DE8 CRC64; MNILDGIKSL ALKLGSKQDQ TYYARGLSLT DDLMQIEALW RDNWIANKVC IKRSEDMVRN WRDIFSNDLK SEQLDEFTKL ERRLKLRETL TKALQWSSLY GAVGLLVVTD TINITSPLQP TERLKRLIIL PKWKISPTGQ RDDDVFSPNF GRYSEYTITG GTQSVSVHHS RLLIINANDA PLSDNDIWGV SDLEKIIDVL KRFDSASANV GDLIFESKID IFKIAGLSDK ISAGLENDVA HVISAVQSIK SATNSLLLDA ENEYDRKELS FGGLKDLLTE FRNAVAGAAD MPVTILFGQS VSGLASGDED IQNYHESIHR LQETRLRPVL EVLDTLLCNE LFGGQPDDWW FEFLPLTVVK QEQQVNMLNT FATAANTLIQ NGVVNEYQVA NELRESGLFA NISADDIEEM KNANELARNF EEPEGESTQV QASEDE // ID Y1421_HAEIN Reviewed; 92 AA. AC P44192; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 50. DE RecName: Full=Uncharacterized protein HI_1421; GN OrderedLocusNames=HI_1421; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23071.1; -; Genomic_DNA. DR PIR; D64029; D64029. DR EnsemblBacteria; AAC23071; AAC23071; HI_1421. DR OMA; HISRREY; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 92 Uncharacterized protein HI_1421. FT /FTId=PRO_0000078056. SQ SEQUENCE 92 AA; 11129 MW; 57556D010D9AA188 CRC64; MKCDARYAEK YRMRPISDEL GMEIDGYLGV IRKVTPELYD VFVLTYIKRW EKQGIWRYLH ISRREYFNRL KTVKTSLLLL LSTEGKQYLF IA // ID Y146A_HAEIN Reviewed; 345 AA. AC O86241; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 17-FEB-2016, entry version 67. DE RecName: Full=Uncharacterized TonB-dependent receptor HI_1466.1; GN OrderedLocusNames=HI_1466.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor 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; L42023; AAC23131.1; -; Genomic_DNA. DR ProteinModelPortal; O86241; -. DR EnsemblBacteria; AAC23131; AAC23131; HI_1466.1. DR OMA; NTANTTW; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0015344; F:siderophore uptake transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0044718; P:siderophore transmembrane transport; IBA:GOC. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF00593; TonB_dep_Rec; 1. PE 3: Inferred from homology; KW Complete proteome; Receptor; Reference proteome; TonB box. FT CHAIN 1 345 Uncharacterized TonB-dependent receptor FT HI_1466.1. FT /FTId=PRO_0000098337. FT MOTIF 328 345 TonB C-terminal box. SQ SEQUENCE 345 AA; 38745 MW; EAF83C55FCC9CB2A CRC64; MDLGPIYNTR DINDGKVINI DNPNYTNPVA IKKNENNNAY QFNHLKTLGL YIQNTTYFTD NFIITGGLRY EYFDQVVGRS TLKNIRSGYL AQKDGKLLYQ LGSVYKFTPN IATFFNHAES FRPQNNRTLI INGELPAEQG KSFETGLKYE NAYLNATVAL FNINKRNVAE TVNVNGTNEL QIVGKQRSRG IEFDLNGQLT DNLSIAANYT YTKVKNLENH NNKLAVGKQL SGVPKHQASL FLAYNIGEFD FGNIRVGGGA RYLGSWYAYN NTYTKAYKLP QAIVYDTFIA YDTKISGKKV SFQLNGKNLS NKVYSPSTSG NASRTLIPVA LGYAREVILN TKIEF // ID Y1490_HAEIN Reviewed; 71 AA. AC P44216; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 48. DE RecName: Full=Uncharacterized protein HI_1490; GN OrderedLocusNames=HI_1490; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23134.1; -; Genomic_DNA. DR PIR; A64032; A64032. DR EnsemblBacteria; AAC23134; AAC23134; HI_1490. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 71 Uncharacterized protein HI_1490. FT /FTId=PRO_0000078073. SQ SEQUENCE 71 AA; 8223 MW; B54F07C57476E9AE CRC64; MSQTLQQTGL FDDEHADIGA LFDHLDQIPS VELEKRWPSL LVEVIEVMQA EYCAKILQKI KQKRPLRSSW A // ID Y149A_HAEIN Reviewed; 102 AA. AC O86242; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_1498.1; GN OrderedLocusNames=HI_1498.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23152.1; -; Genomic_DNA. DR RefSeq; NP_439648.1; NC_000907.1. DR RefSeq; WP_010869227.1; NC_000907.1. DR STRING; 71421.HI1498.1; -. DR EnsemblBacteria; AAC23152; AAC23152; HI_1498.1. DR GeneID; 950365; -. DR KEGG; hin:HI1498.1; -. DR PATRIC; 20191717; VBIHaeInf48452_1568. DR OMA; ASITQRW; -. DR OrthoDB; EOG67MF79; -. DR PhylomeDB; O86242; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR013668; RNase_R_HTH_12. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF08461; HTH_12; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 102 Uncharacterized protein HI_1498.1. FT /FTId=PRO_0000078079. SQ SEQUENCE 102 AA; 11648 MW; 5A902DC34B050FF4 CRC64; MSFKELITQD QRLVVLRVLS EAGYDANESI INDGLDLYGH DISRDLVRTH LSWLEEQGLL TIERLKDGYM VASITQRWLR CSTRSCGSGR RKTPPPENLN TV // ID Y1594_HAEIN Reviewed; 223 AA. AC P44265; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1594; GN OrderedLocusNames=HI_1594; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23245.1; -; Genomic_DNA. DR PIR; E64037; E64037. DR EnsemblBacteria; AAC23245; AAC23245; HI_1594. DR Proteomes; UP000000579; 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 1 223 Uncharacterized protein HI_1594. FT /FTId=PRO_0000078095. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. SQ SEQUENCE 223 AA; 24714 MW; C7038E7E3A890F8F CRC64; MLIIGLCVVS MLLLSSNTFY LSGGVLGGSL VVNWFYPVLG KFGSILIGFV LALIGFIFCS GTSLIRLIVT FYHWLTMKNE QSENAEQEKS TEELEQIVIV KSDRSETENL DQNYLNVEQN SEIETVKPSL EAENISIGKS SSHLINISGL NPEVSIKSEY ELANEENEKP QFSFGFDSES LPSVNLSSDS DEQRVSKNDF VAVWNKPVKT VVQEDLAIKS KCG // ID Y159_HAEIN Reviewed; 174 AA. AC P43790; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0159; GN OrderedLocusNames=HI_0159; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YceD. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20229; AAA62139.1; -; Genomic_DNA. DR EMBL; L42023; AAC21828.1; -; Genomic_DNA. DR PIR; H64051; H64051. DR RefSeq; NP_438329.1; NC_000907.1. DR RefSeq; WP_010868949.1; NC_000907.1. DR STRING; 71421.HI0159; -. DR EnsemblBacteria; AAC21828; AAC21828; HI_0159. DR GeneID; 951069; -. DR KEGG; hin:HI0159; -. DR PATRIC; 20188817; VBIHaeInf48452_0165. DR eggNOG; ENOG4105FCQ; Bacteria. DR eggNOG; COG1399; LUCA. DR KO; K07040; -. DR OMA; TLLCQRC; -. DR OrthoDB; EOG61046G; -. DR PhylomeDB; P43790; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003772; DUF177. DR Pfam; PF02620; DUF177; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 174 Uncharacterized protein HI_0159. FT /FTId=PRO_0000168816. SQ SEQUENCE 174 AA; 19744 MW; 4BAAA34417F48CEA CRC64; MQKVKLPLTV DPIKDAQRRL DYVGYYAANQ LERLAESVVN VLSDAQVTLS FYVDPQKLVV MKGKVQIDVD LECQRCNEPY KQTLECEFTY SPVANWDQAD DLPEIYEPIE FNEFGEIDLI GTVEDELILA LPLVPMHSSE HCEVSAQEQV FGVLPEELAK KPNPFAVLAN LKQK // ID Y1605_HAEIN Reviewed; 203 AA. AC P44272; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 84. DE RecName: Full=Uncharacterized protein HI_1605; DE Flags: Precursor; GN OrderedLocusNames=HI_1605; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SH3b domain. {ECO:0000255|PROSITE- CC ProRule:PRU01117}. CC -!- SIMILARITY: To E.coli YgiM. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23249.1; -; Genomic_DNA. DR PIR; C64038; C64038. DR RefSeq; NP_439747.1; NC_000907.1. DR RefSeq; WP_010869256.1; NC_000907.1. DR STRING; 71421.HI1605; -. DR EnsemblBacteria; AAC23249; AAC23249; HI_1605. DR GeneID; 950458; -. DR KEGG; hin:HI1605; -. DR PATRIC; 20191941; VBIHaeInf48452_1678. DR eggNOG; COG3103; LUCA. DR KO; K07184; -. DR OMA; HKGREGW; -. DR OrthoDB; EOG6PCPX5; -. DR PhylomeDB; P44272; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003646; SH3-like_bac-type. DR InterPro; IPR016476; SH3_dom_pro. DR Pfam; PF08239; SH3_3; 1. DR PIRSF; PIRSF006158; UCP006158_SH3; 1. DR SMART; SM00287; SH3b; 1. DR TIGRFAMs; TIGR04211; SH3_and_anchor; 1. DR PROSITE; PS51781; SH3B; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 203 Uncharacterized protein HI_1605. FT /FTId=PRO_0000013901. FT TRANSMEM 167 189 Helical. {ECO:0000255}. FT DOMAIN 24 87 SH3b. {ECO:0000255|PROSITE- FT ProRule:PRU01117}. SQ SEQUENCE 203 AA; 23113 MW; FAFC5E229FD29C05 CRC64; MKKIYKALIS SLLLSTSINV AYAETQYVTE NLSTFLRRGA GEQFKIAGSI QAGEAVNVLD RQGKYTLIRD NKNREAWILN SDLSSTPSSK EENPKLKAQV QELTLKLSRL DGDWQQRTVE MQRRTKQAEQ QSAVLLEQNS QLKRELEMTK NKNRDLEAIL DAGKREIAIQ WFIYGGSVLG VGLLFGLLIP YVLPKRRRRD GWA // ID Y1620_HAEIN Reviewed; 167 AA. AC P44273; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_1620; GN OrderedLocusNames=HI_1620; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23270.1; -; Genomic_DNA. DR PIR; D64038; D64038. DR EnsemblBacteria; AAC23270; AAC23270; HI_1620. DR Proteomes; UP000000579; 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 1 167 Uncharacterized protein HI_1620. FT /FTId=PRO_0000078099. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 103 123 Helical. {ECO:0000255}. SQ SEQUENCE 167 AA; 19490 MW; C71C2B5E29FFC8CC CRC64; MKIHHLFQPH FRLIYLFIWG LIISGLSDLT WLIPLNVLAV SLFFISLQFS QKSFLPYLKR WFALVIFIVL MWATLSWKIG ENGIELNFQG IELAEKLSLR THLLLISLWL FLWNINDAVL VPSHWQIAFA RKINSTFCAD RTLHCTAWRI ASKNGYCHAR SWISSSA // ID Y1625_HAEIN Reviewed; 165 AA. AC P44277; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein HI_1625; GN OrderedLocusNames=HI_1625; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23273.1; -; Genomic_DNA. DR PIR; H64038; H64038. DR RefSeq; NP_439767.1; NC_000907.1. DR RefSeq; WP_010869261.1; NC_000907.1. DR ProteinModelPortal; P44277; -. DR STRING; 71421.HI1625; -. DR EnsemblBacteria; AAC23273; AAC23273; HI_1625. DR GeneID; 950478; -. DR KEGG; hin:HI1625; -. DR PATRIC; 20191985; VBIHaeInf48452_1700. DR eggNOG; COG0790; LUCA. DR KO; K07126; -. DR OMA; IGMAEES; -. DR OrthoDB; EOG6P3360; -. DR PhylomeDB; P44277; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF08238; Sel1; 2. DR SMART; SM00671; SEL1; 2. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 165 Uncharacterized protein HI_1625. FT /FTId=PRO_0000078101. FT TRANSMEM 7 24 Helical. {ECO:0000255}. SQ SEQUENCE 165 AA; 19037 MW; 6A8C974C9F5918BB CRC64; MKLKLFFHIV LLCFSLPIWA MKTVDVTASP KMDDQARMNL AQEFANKQQW IDVFNIMYPM ALEGNITAQS NLGMLYNLGR GTVRDYEKAY WWFSEAAEKG SVKGLNNLGV MYLRGDYVKQ NTEQAIKLFE RTAQAKDTDA MMMLSNIYRL QNQPEKIIGM AEESR // ID Y1657_HAEIN Reviewed; 194 AA. AC P52606; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1657; GN OrderedLocusNames=HI_1657; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the SIS family. DiaA subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23301.1; -; Genomic_DNA. DR RefSeq; NP_439799.1; NC_000907.1. DR RefSeq; WP_005694384.1; NC_000907.1. DR ProteinModelPortal; P52606; -. DR STRING; 71421.HI1657; -. DR EnsemblBacteria; AAC23301; AAC23301; HI_1657. DR GeneID; 950796; -. DR KEGG; hin:HI1657; -. DR PATRIC; 20192063; VBIHaeInf48452_1735. DR eggNOG; ENOG4105F55; Bacteria. DR eggNOG; COG0279; LUCA. DR KO; K03271; -. DR OMA; YELARPS; -. DR OrthoDB; EOG6384PC; -. DR PhylomeDB; P52606; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR001347; SIS. DR Pfam; PF13580; SIS_2; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 194 Uncharacterized protein HI_1657. FT /FTId=PRO_0000136565. FT DOMAIN 34 192 SIS. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. SQ SEQUENCE 194 AA; 21025 MW; D93DE51AF8C90600 CRC64; MLQKVKDIYS ESIQIQIAAS SMLSENITNA TQMVMQCLLG GNKVIACGVS RSYANAQFLV SNLLNRYDLV RPSFPSVLLS LESAVGSSLV FEQPPEELYC HQFNASAKSG DLLIAFAPLG TEKIVLNIIS HAVSKEVNVI VLTGSNNDAI QGILADKDLE ISIPATKESR ILENHLFVIN ALCELVDQTL FPSA // ID Y1677_HAEIN Reviewed; 223 AA. AC P45312; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Probable iron-sulfur cluster repair protein HI_1677; GN OrderedLocusNames=HI_1677; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Di-iron-containing protein involved in the repair of CC iron-sulfur clusters. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RIC 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; L42023; AAC23322.1; -; Genomic_DNA. DR PIR; F64174; F64174. DR RefSeq; NP_439819.1; NC_000907.1. DR RefSeq; WP_005694400.1; NC_000907.1. DR ProteinModelPortal; P45312; -. DR STRING; 71421.HI1677; -. DR EnsemblBacteria; AAC23322; AAC23322; HI_1677. DR GeneID; 950862; -. DR KEGG; hin:HI1677; -. DR PATRIC; 20192105; VBIHaeInf48452_1756. DR eggNOG; ENOG4105FJH; Bacteria. DR eggNOG; COG2846; LUCA. DR KO; K07322; -. DR OMA; ACTTWRV; -. DR OrthoDB; EOG68DD4M; -. DR PhylomeDB; P45312; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR012312; Haemerythrin-like. DR InterPro; IPR019903; RIC_family. DR Pfam; PF01814; Hemerythrin; 1. DR Pfam; PF04405; ScdA_N; 1. DR TIGRFAMs; TIGR03652; FeS_repair_RIC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Iron; Metal-binding; Reference proteome. FT CHAIN 1 223 Probable iron-sulfur cluster repair FT protein HI_1677. FT /FTId=PRO_0000169823. SQ SEQUENCE 223 AA; 25489 MW; 604EBEEC8D5CC29A CRC64; MSFAQQKLSE LAVSIPGATK IFREYDLDFC CGGSVLLEVA AQQKNLNLAE IEKRLTDLQQ SKAENNDKDW TSASYAEMID HIITRFHNRH REQLPELITL AEKVENIHGD RDDCPIGVVA QLEKIYAELS QHLMKEEQIL FPMIKMGNYA MASMPIRVME MEHDEAGQDV EVIKSLTNNC TPPADACFSW KALYSGINEF IDDLMHHIHL ENNILFPRVL NEK // ID Y1718_HAEIN Reviewed; 261 AA. AC P44296; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_1718; GN OrderedLocusNames=HI_1718; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23365.1; -; Genomic_DNA. DR PIR; I64040; I64040. DR STRING; 71421.HI1718; -. DR EnsemblBacteria; AAC23365; AAC23365; HI_1718. DR PATRIC; 20192189; VBIHaeInf48452_1797. DR OrthoDB; EOG6P332N; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.150.10.10; -; 1. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein HI_1718. FT /FTId=PRO_0000078109. SQ SEQUENCE 261 AA; 27435 MW; 8C57718BF91D2A59 CRC64; MEINREESDL TKYVKITNDT DLTASGTAQN NDAKIENSRL SIAIGHNALV KDSDTKYTHP KDKTPDNPAA SIAVGANANV TESPYSIALG KNAKVLNSEY SLAAGTNAKV EKSEKAIVQG VEANATNSNI SIVTDFAAKA ENSKDVIVLG SKTESIRSNS TVALGNRTSV TDSDSAFVGG DHASATTSAG ALVLGNGAKA KTVSLTADNG VLKAGDKTIF TEDNFKMLLK QLYTFEDGLK TKEKNGKTVV SLDKETIKQM A // ID Y1721_HAEIN Reviewed; 216 AA. AC O05086; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized transposase-like protein HI_1721; GN OrderedLocusNames=HI_1721; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the transposase IS3/IS150/IS904 family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 integrase catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU00457}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23367.1; -; Genomic_DNA. DR PIR; E64176; E64176. DR RefSeq; NP_439862.2; NC_000907.1. DR ProteinModelPortal; O05086; -. DR STRING; 71421.HI1721; -. DR EnsemblBacteria; AAC23367; AAC23367; HI_1721. DR GeneID; 950534; -. DR KEGG; hin:HI1721; -. DR PATRIC; 20192195; VBIHaeInf48452_1800. DR eggNOG; ENOG4105DQ6; Bacteria. DR eggNOG; COG2801; LUCA. DR KO; K07497; -. DR OMA; VKRLTQV; -. DR OrthoDB; EOG664CH4; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transposable element; Transposition. FT CHAIN 1 216 Uncharacterized transposase-like protein FT HI_1721. FT /FTId=PRO_0000075487. FT DOMAIN 54 215 Integrase catalytic. FT {ECO:0000255|PROSITE-ProRule:PRU00457}. SQ SEQUENCE 216 AA; 25541 MW; DC848863D9B23A2C CRC64; MTFKLRETIK INHKKVQRIM QWLGLKGKCK TQKYRSYQGE VGHIADNLLQ RDFTATQPNE KWTTDITEFK CAEGKLYLSP IKDLFNNEII AYDLARSPNF EQITRMMKQA VARLEGAKPI LHSDQGWQYQ MIGYQNILRE NGIQQSMSRK GNCLYNSAME SFFGRLKTEC YYGKRFETFE QLEKTIHEYI HYYNHERIQG KLKGLSPVNY RTQSLN // ID Y1737_HAEIN Reviewed; 109 AA. AC P44301; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_1737; GN OrderedLocusNames=HI_1737; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the AzlD/HI_1737/HP1330 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; L42023; AAC23381.1; -; Genomic_DNA. DR PIR; E64041; E64041. DR RefSeq; NP_439879.1; NC_000907.1. DR RefSeq; WP_005658306.1; NC_000907.1. DR STRING; 71421.HI1737; -. DR EnsemblBacteria; AAC23381; AAC23381; HI_1737. DR GeneID; 950881; -. DR KEGG; hin:HI1737; -. DR PATRIC; 20192231; VBIHaeInf48452_1818. DR eggNOG; ENOG4105KMT; Bacteria. DR eggNOG; COG1687; LUCA. DR OMA; YCFKDIH; -. DR OrthoDB; EOG6J1DMH; -. DR PhylomeDB; P44301; -. DR Proteomes; UP000000579; 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; IPR008407; Brnchd-chn_aa_trnsp_AzlD. DR Pfam; PF05437; AzlD; 1. DR PIRSF; PIRSF003203; AzlD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 109 Uncharacterized protein HI_1737. FT /FTId=PRO_0000078112. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 109 AA; 12423 MW; BCC25DB69F5005DF CRC64; MTLIEQIITI GICIVAVQFT RLLPFFVFPV NRPIPQYIRY LGKVLPPAMF GMLVVYCYKN IEILTGYHGI PDLLAGIVVL GLHFWKKNMF LSIAVGTLFY MALVQLIFI // ID Y217_HAEIN Reviewed; 176 AA. AC P43965; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Putative REP-associated tyrosine transposase; GN OrderedLocusNames=HI_0217; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the transposase 17 family. RAYT 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; L42023; AAC21884.1; -; Genomic_DNA. DR PIR; A64004; A64004. DR RefSeq; NP_438385.1; NC_000907.1. DR RefSeq; WP_005694080.1; NC_000907.1. DR ProteinModelPortal; P43965; -. DR STRING; 71421.HI0217; -. DR DNASU; 951128; -. DR EnsemblBacteria; AAC21884; AAC21884; HI_0217. DR GeneID; 951128; -. DR KEGG; hin:HI0217; -. DR PATRIC; 20188937; VBIHaeInf48452_0225. DR eggNOG; ENOG4108UK5; Bacteria. DR eggNOG; COG1943; LUCA. DR KO; K07491; -. DR OMA; HMIMTLP; -. DR OrthoDB; EOG65XN2G; -. DR PhylomeDB; P43965; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR Pfam; PF01797; Y1_Tnp; 1. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; KW Transposable element; Transposition. FT CHAIN 1 176 Putative REP-associated tyrosine FT transposase. FT /FTId=PRO_0000168537. SQ SEQUENCE 176 AA; 21403 MW; 5B49DED14510CC64 CRC64; MSNYRRDFTK GGLYFFTIVL QDRTKSYLTD YINEFRSAYK QTCEHYPFET VAICILPDHI HLLMQLPEND DNYAIRIAYL KTQFTRQLPK ECRQFNKNRQ KYRESGIWQR RFWEHLIRDD KDLANHLDYI YYNPVKHGYV EVVKDWPYSS FHRDVKAEIY PEDWGGNPDL KIKGDI // ID Y220B_HAEIN Reviewed; 214 AA. AC O86222; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_0220.2; GN OrderedLocusNames=HI_0220.2; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC21888.1; -; Genomic_DNA. DR RefSeq; NP_438390.2; NC_000907.1. DR ProteinModelPortal; O86222; -. DR STRING; 71421.HI0220.2; -. DR EnsemblBacteria; AAC21888; AAC21888; HI_0220.2. DR GeneID; 951123; -. DR KEGG; hin:HI0220.2; -. DR PATRIC; 20188949; VBIHaeInf48452_0231. DR eggNOG; ENOG4108RG0; Bacteria. DR eggNOG; COG1573; LUCA. DR OMA; QAPGRKV; -. DR OrthoDB; EOG6NKR46; -. DR BioCyc; RETL1328306-WGS:GSTH-2457-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.470.10; -; 1. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR Pfam; PF03167; UDG; 1. DR SMART; SM00986; UDG; 1. DR SUPFAM; SSF52141; SSF52141; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 214 Uncharacterized protein HI_0220.2. FT /FTId=PRO_0000077898. SQ SEQUENCE 214 AA; 25084 MW; 153813CE24ADCF74 CRC64; MIFHIFQIDF IYSFLISFIM LKNLDEITSS IIADPQNKDF TERGIFPLFS APKTARINIV GQAPGLKAEQ SRLYWNDKSG DRLREWLGVD YDYFYNSGIF AVLPMDFYYP GYGKSGDLPP RQGFAERWHP MILGNLPNIQ LTILIGQYAQ KYYLPENKDN VTNTVKNYRQ FLPHFMPLVH PSPRNQLWVT KNPWFEEQVI PELQILVKQI INKD // ID Y221A_HAEIN Reviewed; 163 AA. AC O86223; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Putative uncharacterized protein HI_0221.1; GN OrderedLocusNames=HI_0221.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. Corresponds to a CC tandem copy of the C-terminal region of GuaB (HI_0221). 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; L42023; AAC21895.1; -; Genomic_DNA. DR RefSeq; NP_438393.1; NC_000907.1. DR RefSeq; WP_010868961.1; NC_000907.1. DR ProteinModelPortal; O86223; -. DR SMR; O86223; 51-161. DR STRING; 71421.HI0221.1; -. DR EnsemblBacteria; AAC21895; AAC21895; HI_0221.1. DR GeneID; 951134; -. DR KEGG; hin:HI0221.1; -. DR PATRIC; 20188963; VBIHaeInf48452_0234. DR eggNOG; COG0516; LUCA. DR OMA; XIREFAP; -. DR OrthoDB; EOG6GTZPV; -. DR PhylomeDB; O86223; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 1. DR Pfam; PF00478; IMPDH; 1. DR SUPFAM; SSF52317; SSF52317; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 163 Putative uncharacterized protein FT HI_0221.1. FT /FTId=PRO_0000093788. SQ SEQUENCE 163 AA; 18407 MW; 04433231582FAC57 CRC64; MTNIHYHKIL ILDFGSQYTQ LIARRVREIG VYCELWAWDV TEQXIREFAP ELYQGRAFKS YRGMGSLGAM AKGSSDRYFQ SDNAADKLVP EGIEGRIPYK GYLKEIIHQQ MGGLRSCMGL TGCATIDELR TKAEFVRISG AGIKESHVHD VAITKEAPNY RMG // ID Y278_HAEIN Reviewed; 221 AA. AC P43976; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0278; GN OrderedLocusNames=HI_0278; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP CONCEPTUAL TRANSLATION. RX PubMed=8805245; DOI=10.1016/S0960-9822(02)00478-5; RA Tatusov R.L., Mushegian A.R., Bork P., Brown N.P., Hayes W.S., RA Borodovsky M., Rudd K.E., Koonin E.V.; RT "Metabolism and evolution of Haemophilus influenzae deduced from a RT whole-genome comparison with Escherichia coli."; RL Curr. Biol. 6:279-291(1996). CC -!- SIMILARITY: Contains 1 MOSC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00670}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC21950.1; Type=Frameshift; Positions=77; 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; L42023; AAC21950.1; ALT_FRAME; Genomic_DNA. DR PIR; C64005; C64005. DR EnsemblBacteria; AAC21950; AAC21950; HI_0278. DR OMA; SKFKQQG; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR Gene3D; 2.40.33.20; -; 1. DR InterPro; IPR005302; MoCF_Sase_C. DR InterPro; IPR015808; MoCF_Sase_C-like. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR Pfam; PF03473; MOSC; 1. DR SUPFAM; SSF50800; SSF50800; 1. DR PROSITE; PS51340; MOSC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 221 Uncharacterized protein HI_0278. FT /FTId=PRO_0000169689. FT DOMAIN 30 168 MOSC. {ECO:0000255|PROSITE- FT ProRule:PRU00670}. SQ SEQUENCE 221 AA; 24803 MW; C648A437DF48D6E6 CRC64; MNAKILVIKV GQVETLTFSD GSQYESAIRK KVVPSVKIHS LGAEGNDVGL KKHHGGVDKA LFFMSADSFN ELNALLXIKI FPYMDTATYG ENFVVSGLNE DNVCIGDRYQ IGSTILEVSQ PRKPCERLSK NTENEETRDI VYQTGLSGWY VRIIETGTIK QKDELKLLAR PYPQITIRHL NRLLSTPKNE AELDSALEIE VLAEAFKRSI RSQISKFKQQ G // ID Y326_HAEIN Reviewed; 87 AA. AC P43987; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_0326; GN OrderedLocusNames=HI_0326; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21991.1; -; Genomic_DNA. DR PIR; E64006; E64006. DR STRING; 71421.HI0326; -. DR EnsemblBacteria; AAC21991; AAC21991; HI_0326. DR PATRIC; 20189193; VBIHaeInf48452_0343. DR eggNOG; COG3923; LUCA. DR OrthoDB; EOG6H1Q0R; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010890; Primosomal_replicat_PriB/PriC. DR Pfam; PF07445; PriC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 87 Uncharacterized protein HI_0326. FT /FTId=PRO_0000077913. SQ SEQUENCE 87 AA; 10450 MW; 20FBBCC7E9F5A914 CRC64; MTVQQLIQRL DQKVQQLYQA HLSKREEKIF AKFDRTLFSE NGQNVSFYLK EINQTLDRIK TLESNDSNHY NFLAERLLAN VPFFRKL // ID Y355_HAEIN Reviewed; 245 AA. AC Q57306; O05017; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 2. DT 17-FEB-2016, entry version 104. DE RecName: Full=Probable ABC transporter permease protein HI_0355; GN OrderedLocusNames=HI_0355; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22015.1; -; Genomic_DNA. DR RefSeq; NP_438518.1; NC_000907.1. DR RefSeq; WP_005693804.1; NC_000907.1. DR ProteinModelPortal; Q57306; -. DR STRING; 71421.HI0355; -. DR TCDB; 3.A.1.17.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22015; AAC22015; HI_0355. DR GeneID; 949458; -. DR KEGG; hin:HI0355; -. DR PATRIC; 20189257; VBIHaeInf48452_0374. DR eggNOG; ENOG4105Y36; Bacteria. DR eggNOG; COG0600; LUCA. DR KO; K15599; -. DR OMA; ARMMIDE; -. DR OrthoDB; EOG6GR3CZ; -. DR PhylomeDB; Q57306; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 245 Probable ABC transporter permease protein FT HI_0355. FT /FTId=PRO_0000060279. FT TRANSMEM 9 29 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 61 81 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 92 112 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 115 135 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 170 190 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 217 237 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 50 234 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 245 AA; 27098 MW; F173BF70605FA170 CRC64; MKIRLLKPLL IVGVLLMIWQ MVATLGSFPH YIFPSPQAVR QQLFTHAELL WQHTQVTLLE ICLGLLLGFL FGLISALLLS FSRQISAVLL PILVISQAIP VFAIAPLLVL WFGYGMASKI VMSVLIIYFP VTAACYDGLR NTPQAWLDLA KTFNISPLRL LLKVRLPAAL PAFASGLRIA VSVAPIGAVV GEWVGSSEGL GYLMIHANAR MQVDLMFAAL LILVSISLCL YFSIDWLLHR FIWSV // ID Y362_HAEIN Reviewed; 293 AA. AC Q57449; O05018; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Uncharacterized periplasmic iron-binding protein HI_0362; DE Flags: Precursor; GN OrderedLocusNames=HI_0362; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 23-46, AND SUBCELLULAR LOCATION. RX PubMed=1556062; RA Harkness R.E., Chong P., Klein M.H.; RT "Identification of two iron-repressed periplasmic proteins in RT Haemophilus influenzae."; RL J. Bacteriol. 174:2425-2430(1992). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Part of an ATP-driven transport system CC HI_0359/HI_0360/HI_0361/HI_0362 for iron. Metal-binding component CC (Potential). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1556062}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22021.1; -; Genomic_DNA. DR PIR; G64063; G64063. DR RefSeq; NP_438524.1; NC_000907.1. DR RefSeq; WP_005656358.1; NC_000907.1. DR ProteinModelPortal; Q57449; -. DR SMR; Q57449; 19-291. DR STRING; 71421.HI0362; -. DR PRIDE; Q57449; -. DR EnsemblBacteria; AAC22021; AAC22021; HI_0362. DR GeneID; 950634; -. DR KEGG; hin:HI0362; -. DR PATRIC; 20189269; VBIHaeInf48452_0380. DR eggNOG; ENOG4105DSE; Bacteria. DR eggNOG; COG0803; LUCA. DR KO; K11604; -. DR OMA; HAWQNVA; -. DR OrthoDB; EOG6B3601; -. DR PhylomeDB; Q57449; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR InterPro; IPR006129; AdhesinB. DR InterPro; IPR006128; Lipoprotein_4. DR InterPro; IPR006127; ZnuA-like. DR Pfam; PF01297; ZnuA; 1. DR PRINTS; PR00691; ADHESINB. DR PRINTS; PR00690; ADHESNFAMILY. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Iron; Metal-binding; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 22 {ECO:0000269|PubMed:1556062}. FT CHAIN 23 293 Uncharacterized periplasmic iron-binding FT protein HI_0362. FT /FTId=PRO_0000031905. FT METAL 58 58 Iron. {ECO:0000250}. FT METAL 123 123 Iron. {ECO:0000250}. FT METAL 189 189 Iron. {ECO:0000250}. SQ SEQUENCE 293 AA; 32463 MW; 27FE3F9BACDFB508 CRC64; MRNSFKIMTA LALGLFAMQA NAKFKVVTTF TVIQDIAQNV AGNAATVESI TKPGAEIHEY EPTPKDIVKA QSADLILWNG LNLERWFERF FQNVKDKPAV VVTEGIQPLS IYEGPYKDAP NPHAWMSPSN ALIYIENIKN ALVKYDPQNA AVYEKNAADY AQKIKQLDEP LRAKLAQIPE AQRWLVTSEG AFSYLAKDYN LKEGYLWPIN AEQQGTPQQV RKVIDLVRKN NIPVVFSEST ISAKPAQQVA KESGAKYGGV LYVDSLSAKN GPVPTYIDLL NVTVSTIVKG FGK // ID Y396_HAEIN Reviewed; 404 AA. AC P44683; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Probable ribosomal oxygenase HI_0396; DE Short=ROX; DE EC=1.14.11.-; GN OrderedLocusNames=HI_0396; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Oxygenase that catalyzes the hydroxylation of a CC ribosomal protein. {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:P27431}; CC Note=Binds 1 Fe(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P27431}; CC -!- SIMILARITY: Belongs to the ROX family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 JmjC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00538}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22055.1; -; Genomic_DNA. DR PIR; A64151; A64151. DR RefSeq; NP_438558.1; NC_000907.1. DR RefSeq; WP_005693774.1; NC_000907.1. DR ProteinModelPortal; P44683; -. DR STRING; 71421.HI0396; -. DR DNASU; 950708; -. DR EnsemblBacteria; AAC22055; AAC22055; HI_0396. DR GeneID; 950708; -. DR KEGG; hin:HI0396; -. DR PATRIC; 20189343; VBIHaeInf48452_0415. DR eggNOG; ENOG4105EZE; Bacteria. DR eggNOG; COG2850; LUCA. DR KO; K18850; -. DR OMA; FTPIIDV; -. DR OrthoDB; EOG683S5N; -. DR PhylomeDB; P44683; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.260.20; -; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003380; Transform_Ski. DR Pfam; PF08007; Cupin_4; 1. DR SMART; SM00558; JmjC; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 404 Probable ribosomal oxygenase HI_0396. FT /FTId=PRO_0000168831. FT DOMAIN 102 231 JmjC. {ECO:0000255|PROSITE- FT ProRule:PRU00538}. FT METAL 135 135 Iron; via tele nitrogen; catalytic. FT {ECO:0000250|UniProtKB:P27431}. FT METAL 137 137 Iron; catalytic. FT {ECO:0000250|UniProtKB:P27431}. FT METAL 199 199 Iron; via tele nitrogen; catalytic. FT {ECO:0000250|UniProtKB:P27431}. SQ SEQUENCE 404 AA; 46419 MW; A3FF26064D3F8B4C CRC64; MTALSSVDFC LPEHITPEIF LRDYWQKKPL VIRNGLPEIV GQFEPQDIIE LAQNEDVTAR LVKTFSDDDW KVFFSPLSEK DFQKLPEKWS VLVQNLEQWS PELGQLWNKF GFIPQWQRDD IMVSYAPKGG SVGKHYDEYD VFLVQGYGHR RWQVGKWCDA STEFKPNQSI RIFDDMGELV IDEVMNPGDI LYIPARMAHY GVAEDDCLTF SFGLRYPNLS NLIDGISKGF CHQDPDLNLS EFDLPLRLSQ SEQRTGKLAD ENIQAMKQLL LDKLAHSEAF DTLFKQAVAS AVSSRRYELL VSDEMCDPDE VRSILEEDGA FLSQDNNCKL LYTENPLRIY ANGEWLDELN IIESEVLKRL SDGESLDWAF LSDLANKTED PETSMDLLLD SICNWVDDGW ALIE // ID Y409_HAEIN Reviewed; 475 AA. AC P44693; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uncharacterized metalloprotease HI_0409; DE EC=3.4.24.-; GN OrderedLocusNames=HI_0409; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M23B 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; L42023; AAC22068.1; -; Genomic_DNA. DR PIR; F64151; F64151. DR RefSeq; NP_438571.1; NC_000907.1. DR RefSeq; WP_005693760.1; NC_000907.1. DR ProteinModelPortal; P44693; -. DR STRING; 71421.HI0409; -. DR EnsemblBacteria; AAC22068; AAC22068; HI_0409. DR GeneID; 949412; -. DR KEGG; hin:HI0409; -. DR PATRIC; 20189369; VBIHaeInf48452_0428. DR eggNOG; ENOG4105DR5; Bacteria. DR eggNOG; COG0739; LUCA. DR OMA; EYQTVYM; -. DR OrthoDB; EOG61KBD1; -. DR PhylomeDB; P44693; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR007340; Opacity-associatedA. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF04225; OapA; 1. DR Pfam; PF01551; Peptidase_M23; 1. DR SUPFAM; SSF51261; SSF51261; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1 475 Uncharacterized metalloprotease HI_0409. FT /FTId=PRO_0000165905. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT METAL 348 348 Zinc. {ECO:0000255}. SQ SEQUENCE 475 AA; 53255 MW; 143C10F92233939D CRC64; MPVQHVKLAR DRRKKRAYIK VGVFFVAILL ILTGILLTIK SKPEENSIFS TFDSGEYHEL NTSPNENSTA LQPDENATSY DDELQAKDDE VDEVKLSSDD LDTLPQHAQD ALNGLLDAAD QAIRITDQFS YTVTEGDTLK DVLVLSGLDD SSVQPLIALD PELAHLKAGQ QFYWILDKND NLEYLNWLVS EKEERIYERL EDGKFKRQVI EKKSIWRKEV LKGEIQNSLN SSLREKGLDT RQISQLSNAL QWQVSLRKLK KGTQFAILVS REYLGDKLTG QGNVEALRIS SGGKNYYAVQ AANGRYYNQQ GETLGKGFAR YPLQRQARVS SPFNPNRRHP VTGRIRPHKG VDFSVSQGTP VIAPADGTVE KVAYQAGGAG RYVMLRHGRE YQTVYMHLSK SLVKAGQTVK KGERIALSGN TGISTGPHLH YEFHINGRAV NPLTVKLPGT SSGMTSAERK QFLVRVREAE RMLKP // ID Y1009_HAEIN Reviewed; 256 AA. AC P44978; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 09-DEC-2015, entry version 98. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1009; GN OrderedLocusNames=HI_1009; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 HTH deoR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00349}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22670.1; -; Genomic_DNA. DR PIR; A64108; A64108. DR RefSeq; NP_439170.1; NC_000907.1. DR RefSeq; WP_005693347.1; NC_000907.1. DR ProteinModelPortal; P44978; -. DR STRING; 71421.HI1009; -. DR EnsemblBacteria; AAC22670; AAC22670; HI_1009. DR GeneID; 950712; -. DR KEGG; hin:HI1009; -. DR PATRIC; 20190681; VBIHaeInf48452_1053. DR eggNOG; ENOG4105MVE; Bacteria. DR eggNOG; COG1349; LUCA. DR OMA; NAQARIA; -. DR OrthoDB; EOG6XSZXW; -. DR PhylomeDB; P44978; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR014036; DeoR_C. DR InterPro; IPR001034; DeoR_HTH. DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00455; DeoRC; 1. DR Pfam; PF08220; HTH_DeoR; 1. DR PRINTS; PR00037; HTHLACR. DR SMART; SM00420; HTH_DEOR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00894; HTH_DEOR_1; 1. DR PROSITE; PS51000; HTH_DEOR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 256 Uncharacterized HTH-type transcriptional FT regulator HI_1009. FT /FTId=PRO_0000050275. FT DOMAIN 7 62 HTH deoR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. FT DNA_BIND 24 43 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00349}. SQ SEQUENCE 256 AA; 28321 MW; 0EE880565E331663 CRC64; MEKKMIPAER QKTLLNLISK QSVISINNLV NILGVSHMTV RRDIQKLEED GKVISVSGGV QLLERLSSEP THDDKSLLAT TEKTAISKKA VELIQEHSTI YLDAGTTTLE IAKQIANRND LLVITNDFVI AHYLMVNSQC NIMHTGGLIN KSNRSSVGEF AAQFLHQISV DIAFISTSSW NLKGLTTPDE QKIPVKKAII QFSQKNILVT DSSKYGKVAT FLLYPLSSLD TIICDKGLPE NAQARIAEMN VELFLV // ID Y1017_HAEIN Reviewed; 213 AA. AC O86231; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Uncharacterized aquaporin-like protein HI_1017; GN OrderedLocusNames=HI_1017; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC22677.1; -; Genomic_DNA. DR ProteinModelPortal; O86231; -. DR EnsemblBacteria; AAC22677; AAC22677; HI_1017. DR OMA; HAIMPIK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015254; F:glycerol channel activity; IBA:GO_Central. DR GO; GO:0015250; F:water channel activity; IBA:GO_Central. DR GO; GO:0015793; P:glycerol transport; IBA:GOC. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central. DR GO; GO:0006833; P:water transport; IBA:GOC. DR Gene3D; 1.20.1080.10; -; 1. DR InterPro; IPR023271; Aquaporin-like. DR InterPro; IPR000425; MIP. DR PANTHER; PTHR19139; PTHR19139; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; SSF81338; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 213 Uncharacterized aquaporin-like protein FT HI_1017. FT /FTId=PRO_0000064096. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT MOTIF 43 45 NPA 1. FT MOTIF 164 166 NPA 2. SQ SEQUENCE 213 AA; 24053 MW; 2F80EFE512638963 CRC64; MCQYFLKKIR NVWERWFTYR LWFGLSMVSI AVIFGPLTGA HVNPAVTIDF WEVGKFPTEL VLVYIIAQCI GAFIVALIVW LLFKDHLDEE DNQNCQLGSF ATIATNSNNL RNLLSEIVTT FSLLFILFTL NHQQPTNGVA MFFVFTGVAG GVMSFGGLTS YAINPARDFM LRLIHAIMPI KNKGTSNFDY AWVPVLRPVI GAILAAWLYK ALF // ID Y1032_HAEIN Reviewed; 268 AA. AC P44996; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1032; GN OrderedLocusNames=HI_1032; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH iclR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00393}. CC -!- SIMILARITY: Contains 1 iclR-ED (iclR effector binding) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00394}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22692.1; -; Genomic_DNA. DR PIR; D64165; D64165. DR RefSeq; NP_439192.1; NC_000907.1. DR RefSeq; WP_005693366.1; NC_000907.1. DR ProteinModelPortal; P44996; -. DR SMR; P44996; 89-268. DR STRING; 71421.HI1032; -. DR EnsemblBacteria; AAC22692; AAC22692; HI_1032. DR GeneID; 950700; -. DR KEGG; hin:HI1032; -. DR PATRIC; 20190727; VBIHaeInf48452_1076. DR eggNOG; ENOG41069M3; Bacteria. DR eggNOG; COG1414; LUCA. DR OMA; KIFMAYG; -. DR OrthoDB; EOG6MWN8D; -. DR PhylomeDB; P44996; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.450.40; -; 1. DR InterPro; IPR029016; GAF_dom-like. DR InterPro; IPR014757; Tscrpt_reg_IclR_C. DR InterPro; IPR005471; Tscrpt_reg_IclR_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF09339; HTH_IclR; 1. DR Pfam; PF01614; IclR; 1. DR SMART; SM00346; HTH_ICLR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55781; SSF55781; 1. DR PROSITE; PS51077; HTH_ICLR; 1. DR PROSITE; PS51078; ICLR_ED; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 268 Uncharacterized HTH-type transcriptional FT regulator HI_1032. FT /FTId=PRO_0000201772. FT DOMAIN 15 77 HTH iclR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00393}. FT DOMAIN 92 265 IclR-ED. {ECO:0000255|PROSITE- FT ProRule:PRU00394}. FT DNA_BIND 37 56 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00393}. SQ SEQUENCE 268 AA; 30580 MW; AAAF3080ED39EA14 CRC64; MNIEVKMEKE KSLGNQALIR GLRLLDILSN YPNGCPLAKL AELANLNKST AHRLLQGLQN EGYVKPANAA GSYRLTIKCL SIGQKVLSSM NIIHVASPYL EQLNLKLGET INFSKREDDH AIMIYKLEPT NGMLKTRAYI GQYLKLYCSA MGKIFLAYEK KVDYLSHYWQ SHQREIKKLT RYTITELDDI KLELETIRQT AYAMDREENE LGVTCIACPI FDSFGQVEYA ISVSMSIYRL NKFGTDAFLQ EIRKTAEQIS LELGYENI // ID Y1038_HAEIN Reviewed; 400 AA. AC P44099; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1038; GN OrderedLocusNames=HI_1038; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To M.jannaschii MJ1544 and MJ1637. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22698.1; -; Genomic_DNA. DR PIR; I64018; I64018. DR RefSeq; NP_439198.1; NC_000907.1. DR RefSeq; WP_005693372.1; NC_000907.1. DR ProteinModelPortal; P44099; -. DR STRING; 71421.HI1038; -. DR DNASU; 950021; -. DR EnsemblBacteria; AAC22698; AAC22698; HI_1038. DR GeneID; 950021; -. DR KEGG; hin:HI1038; -. DR PATRIC; 20190739; VBIHaeInf48452_1082. DR eggNOG; ENOG4105E4P; Bacteria. DR eggNOG; COG1373; LUCA. DR KO; K07133; -. DR OMA; KEFLHAK; -. DR OrthoDB; EOG6RZB4G; -. DR PhylomeDB; P44099; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025420; DUF4143. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13635; DUF4143; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 400 Uncharacterized protein HI_1038. FT /FTId=PRO_0000077994. SQ SEQUENCE 400 AA; 46103 MW; 9094C1F75D4DF411 CRC64; MSKAMISREN YLQQLIQFKD TDFIKVISGV RRSGKSVLLM QYRDYLQQQG IASENILYLN FESFEYQWVK DAQDFQQLIQ EKMPSSQEKI YFLIDEIQFV EGWQKIVNAL RVSFNTDIVI TGSNANLLSG ELATLLSGRY VEIKIYPLSF KEFLHAKNVD SQSRLVDKLY SEYEKYGGFP SVVMADEPLK ETILSGIFDS IVLNDIAHRA GVKDTHILKS VILFLADNVG QLVNPSKISN TLTSERVPTS NHTISKYLDL LENAFLFYKA KQYDIRGKGY LKTNAKYFIV DNGLRRHAIG KKGANYANRL ENIVFIELLR RGYSVDVGKL DSKEIDFIAR KADEILYVQV AFEIPENTHE TDNLLHIKDN YKKILITGKY YEQTEIDGIE VIYVVDWLLQ // ID Y103_HAEIN Reviewed; 114 AA. AC P44515; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein HI_0103; GN OrderedLocusNames=HI_0103; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC21777.1; -; Genomic_DNA. DR PIR; F64142; F64142. DR RefSeq; NP_438277.1; NC_000907.1. DR RefSeq; WP_005693817.1; NC_000907.1. DR ProteinModelPortal; P44515; -. DR STRING; 71421.HI0103; -. DR EnsemblBacteria; AAC21777; AAC21777; HI_0103. DR GeneID; 951002; -. DR KEGG; hin:HI0103; -. DR PATRIC; 20188673; VBIHaeInf48452_0106. DR eggNOG; ENOG4105KUZ; Bacteria. DR eggNOG; COG1393; LUCA. DR OMA; FGIKNCD; -. DR OrthoDB; EOG6NSGMX; -. DR PhylomeDB; P44515; -. DR Proteomes; UP000000579; Chromosome. 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 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein HI_0103. FT /FTId=PRO_0000169230. SQ SEQUENCE 114 AA; 13060 MW; 08B9F319B456ACBA CRC64; MITVYGIKNC DTVKKALKWL ADHNIEHKLH DYRVDGLDLN FLTQAETQFG WDVLVNKRST TWRNLDEQVK NSLDKTTALS VLAENPTLIK RPIILQDGKA LIGFNEKEYQ AAFA // ID Y1049_HAEIN Reviewed; 97 AA. AC Q57347; O05042; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1049; GN OrderedLocusNames=HI_1049; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22707.1; -; Genomic_DNA. DR PIR; H64109; H64109. DR RefSeq; NP_439208.1; NC_000907.1. DR RefSeq; WP_010869116.1; NC_000907.1. DR STRING; 71421.HI1049; -. DR TCDB; 1.A.72.1.3; the mer superfamily. DR EnsemblBacteria; AAC22707; AAC22707; HI_1049. DR GeneID; 949946; -. DR KEGG; hin:HI1049; -. DR PATRIC; 20190763; VBIHaeInf48452_1094. DR KO; K08363; -. DR OMA; VASTLCC; -. DR OrthoDB; EOG6FFS8K; -. DR Proteomes; UP000000579; 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 97 Uncharacterized protein HI_1049. FT /FTId=PRO_0000077995. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. SQ SEQUENCE 97 AA; 11303 MW; 8FAD7F6D0373855D CRC64; MASTLCCIAP LIYLVFGVSS TWLIGLGEYD YLRIPMLIIS LCAFAYGFWL LMFSKKIICS KYISRKKLIV LYWIVFIVMI FFLTYPTILP WILELAN // ID Y1053_HAEIN Reviewed; 113 AA. AC Q57498; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1053; GN OrderedLocusNames=HI_1053; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22712.1; -; Genomic_DNA. DR PIR; E64165; E64165. DR RefSeq; NP_439212.1; NC_000907.1. DR RefSeq; WP_005651693.1; NC_000907.1. DR ProteinModelPortal; Q57498; -. DR STRING; 71421.HI1053; -. DR EnsemblBacteria; AAC22712; AAC22712; HI_1053. DR GeneID; 950030; -. DR KEGG; hin:HI1053; -. DR PATRIC; 20190771; VBIHaeInf48452_1098. DR eggNOG; COG0599; LUCA. DR OMA; RCESCIG; -. DR OrthoDB; EOG6W45V8; -. DR PhylomeDB; Q57498; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR004675; AhpD_core. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. DR TIGRFAMs; TIGR00778; ahpD_dom; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 113 Uncharacterized protein HI_1053. FT /FTId=PRO_0000077997. SQ SEQUENCE 113 AA; 11862 MW; 2EA29B9EEEFA5F24 CRC64; MFTDWKEHTS HVKKSFGELG KQYPKMLQAY QALGAAAAEG NVLDAKTREL IALAVAVTTR CESCISAHAE EAVKAGASEA EVAAALATAI ALNAGAAYTY SLRALEAYSV QKA // ID Y1054_HAEIN Reviewed; 460 AA. AC P44104; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_1054; GN OrderedLocusNames=HI_1054; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22713.1; -; Genomic_DNA. DR PIR; E64019; E64019. DR STRING; 71421.HI1054; -. DR REBASE; 2820; HindVIP. DR EnsemblBacteria; AAC22713; AAC22713; HI_1054. DR PATRIC; 20190773; VBIHaeInf48452_1099. DR eggNOG; COG3421; LUCA. DR OMA; NSGVNDE; -. DR OrthoDB; EOG6H7FCV; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 460 Uncharacterized protein HI_1054. FT /FTId=PRO_0000077998. SQ SEQUENCE 460 AA; 53472 MW; 0D80EA220AFDEDA8 CRC64; MKGKTAAVQI KNRAKAAATV SEKQLIGRGV RYFPFAFEDK QPNKRKFDND MQHELRILEE LFYYTHDEQS RYISELKAEL RKDGFIPEND KDKVLTTFKL KSEFADNENF KNLLIWANKK IPNPNAKANN ADSLKANPPP QPLPFPVHGK LLQETQFTAD ENDEKARQIG TQNNFTETIE MSEIERHIFN KALHIKGKNS QSLFHFDRLQ SKLNIQNRNE LQNNLLKDWQ IEFLGLGQDK QISPDDKLAG CLKILEMVEK HLNESDIPFI GTKEFTPKKL WEIFGTPKQK WVKKDDVKTA IATQNDWYVM DNFAGTSLEE ALIQFISERL GDLKSKYDVH LIRNEEVFKL NNFADGEGFM PDFILLLKDK QKSSSNGVND FLHYQIFIEP KGEHLVETDM WKKEFLEAIT AEYGKDKILQ KDTPHYRLIG LPFFTDNEKN PKEYEQFTKS FPLGEASLEK // ID Y107_HAEIN Reviewed; 420 AA. AC Q57017; P96330; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 106. DE RecName: Full=UPF0053 protein HI_0107; GN OrderedLocusNames=HI_0107; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC21785.1; 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; L42023; AAC21785.1; ALT_INIT; Genomic_DNA. DR PIR; H64142; H64142. DR RefSeq; NP_438281.1; NC_000907.1. DR PDB; 3LAE; X-ray; 1.45 A; A=343-420. DR PDBsum; 3LAE; -. DR ProteinModelPortal; Q57017; -. DR SMR; Q57017; 343-420. DR STRING; 71421.HI0107; -. DR EnsemblBacteria; AAC21785; AAC21785; HI_0107. DR GeneID; 951005; -. DR KEGG; hin:HI0107; -. DR PATRIC; 20188683; VBIHaeInf48452_0111. DR eggNOG; ENOG4108JU6; Bacteria. DR eggNOG; COG4536; LUCA. DR OMA; LSIMDLE; -. DR OrthoDB; EOG60W7V4; -. DR EvolutionaryTrace; Q57017; -. DR Proteomes; UP000000579; 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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR002550; DUF21. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 1. DR Pfam; PF03471; CorC_HlyC; 1. DR Pfam; PF01595; DUF21; 1. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure; CBS domain; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 420 UPF0053 protein HI_0107. FT /FTId=PRO_0000088358. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT DOMAIN 9 184 DUF21. FT DOMAIN 208 268 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 273 333 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT STRAND 350 353 {ECO:0000244|PDB:3LAE}. FT HELIX 358 365 {ECO:0000244|PDB:3LAE}. FT HELIX 377 384 {ECO:0000244|PDB:3LAE}. FT STRAND 394 397 {ECO:0000244|PDB:3LAE}. FT STRAND 400 408 {ECO:0000244|PDB:3LAE}. FT STRAND 411 419 {ECO:0000244|PDB:3LAE}. SQ SEQUENCE 420 AA; 46960 MW; 7CFFD76A12937231 CRC64; MDSIPLSTLF IILIICLVLS AYFSGSETGL LSLNKYRLRF LSEQGNKGAK KAEKLLEKPD TLLSFILIFN NLVNISASAI ATVIGMRLYG DAGVAIATGL LTFVMLVFSE IFPKTVAAMH AEKVSFFSSH ILTSLLKIFY PLVWLMNIFT KSLMQIVGLK LDMQKQVISS EELRSIVSEA GEATPNEQHP QMLLSILDME TVTVDDIMVP RNEIGGINID DDWRAIMRQL NHAAHNRVVL YKGSLDEQVL GILRVREAFR LLLEKNEFTK ETLIRAADEV YFIPESTPLK TQLANFRTNK ERIGLVVDEY GDIKGLVTLE DILEEIVGDF TTSTAPSIDK EVIQQSDGSM IIDGSANLRD LNKMFNWELD TEDARTFNGL ILEHLEEIPD EGTICEIDGL LITILEVGDN MIKQAKVVKL // ID Y1080_HAEIN Reviewed; 257 AA. AC P45024; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Probable amino-acid ABC transporter-binding protein HI_1080; DE Flags: Precursor; GN OrderedLocusNames=HI_1080; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system for an amino acid. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 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; L42023; AAC22736.1; -; Genomic_DNA. DR PIR; I64181; I64181. DR RefSeq; NP_439237.1; NC_000907.1. DR RefSeq; WP_005662813.1; NC_000907.1. DR ProteinModelPortal; P45024; -. DR STRING; 71421.HI1080; -. DR EnsemblBacteria; AAC22736; AAC22736; HI_1080. DR GeneID; 950096; -. DR KEGG; hin:HI1080; -. DR PATRIC; 20190825; VBIHaeInf48452_1125. DR eggNOG; ENOG4105EAB; Bacteria. DR eggNOG; COG0834; LUCA. DR KO; K02424; -. DR OMA; DAAYNDR; -. DR OrthoDB; EOG6JQH58; -. DR PhylomeDB; P45024; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR InterPro; IPR018313; SBP_3_CS. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR Pfam; PF00497; SBP_bac_3; 1. DR SMART; SM00062; PBPb; 1. DR PROSITE; PS01039; SBP_BACTERIAL_3; 1. PE 1: Evidence at protein level; KW Amino-acid transport; Complete proteome; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 257 Probable amino-acid ABC transporter- FT binding protein HI_1080. FT /FTId=PRO_0000031776. SQ SEQUENCE 257 AA; 28337 MW; B4CD7EADDAD9F3E1 CRC64; MKKLLFTTAL LTGAIAFSTF SHAGEIADRV EKTKTLLVGT EGTYAPFTFH DKSGKLTGFD VEVIRKVAEK LGLKVEFKET QWDAMYAGLN AKRFDVIANQ TNPSPERLKK YSFTTPYNYS GGVIVTKSSD NSIKSFEDLK GRKSAQSATS NWGKDAKAAG AQILVVDGLA QSLELIKQGR AEATINDKLA VLDYFKQHPN SGLKIAYDRG DKTPTAFAFL QGEDALITKF NQVLEALRQD GTLKQISIEW FGYDITQ // ID Y1159_HAEIN Reviewed; 217 AA. AC P43786; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Uncharacterized protein HI_1159; GN OrderedLocusNames=HI_1159; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22814.1; -; Genomic_DNA. DR PIR; H64186; H64186. DR RefSeq; NP_439317.2; NC_000907.1. DR ProteinModelPortal; P43786; -. DR STRING; 71421.HI1159m; -. DR DNASU; 950110; -. DR EnsemblBacteria; AAC22814; AAC22814; HI_1159. DR GeneID; 950110; -. DR KEGG; hin:HI1159m; -. DR PATRIC; 20190995; VBIHaeInf48452_1210. DR eggNOG; ENOG4107QR8; Bacteria. DR eggNOG; COG3118; LUCA. DR KO; K05838; -. DR OMA; EMEIASY; -. DR OrthoDB; EOG6QG8RK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR011990; TPR-like_helical_dom. DR PANTHER; PTHR10438; PTHR10438; 1. DR SUPFAM; SSF48452; SSF48452; 2. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 217 Uncharacterized protein HI_1159. FT /FTId=PRO_0000168641. SQ SEQUENCE 217 AA; 24500 MW; B9F98BBA7A366D61 CRC64; MIAAQFRIQA LPTTYLFKEA QALDAFPSVL DKSSLIQRLS IILPKEEDLK FQQALDFLQV ENYEAALPLL KDAWELSDKK NSDVALLYAE TYIAMKKTEP AQEILNQIPL QDRDSRWHGL QAQIELQIQA ADTPEIQQLQ ADYAKNPTAE IAIKLAVQLH QAGRNEEALT LLFGILKTDL GAQNGEVKQQ FLSILSAMGN ADPLTNKFRR LLYSLLY // ID Y1163_HAEIN Reviewed; 1027 AA. AC Q57252; O05046; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 101. DE RecName: Full=Uncharacterized protein HI_1163 {ECO:0000305}; GN OrderedLocusNames=HI_1163; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P77748}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P77748}; CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00718}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22818.1; -; Genomic_DNA. DR PIR; B64187; B64187. DR RefSeq; NP_439321.1; NC_000907.1. DR RefSeq; WP_005694279.1; NC_000907.1. DR ProteinModelPortal; Q57252; -. DR STRING; 71421.HI1163; -. DR EnsemblBacteria; AAC22818; AAC22818; HI_1163. DR GeneID; 950119; -. DR KEGG; hin:HI1163; -. DR PATRIC; 20191005; VBIHaeInf48452_1215. DR eggNOG; ENOG4105CQB; Bacteria. DR eggNOG; COG0247; LUCA. DR eggNOG; COG0277; LUCA. DR OMA; FKPNGKP; -. DR OrthoDB; EOG6TTVHX; -. DR PhylomeDB; Q57252; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 2. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; Reference proteome. FT CHAIN 1 1027 Uncharacterized protein HI_1163. FT /FTId=PRO_0000168995. FT DOMAIN 48 284 FAD-binding PCMH-type. FT {ECO:0000255|PROSITE-ProRule:PRU00718}. FT DOMAIN 665 696 4Fe-4S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. SQ SEQUENCE 1027 AA; 116743 MW; A53D3D966E264761 CRC64; MLPNLNRIPQ VEQYVLDYLD DLQCQHFEGD IATNYADRLS LATDNSVYQQ LPQAILFPKT VADIVRITKL ANLPEYQSIS FTPRGGGTGT NGQSINNNII VDLSRHMTAI LELNVKERWV RVQAGVVKDQ LNQFLKPHGL FFAPELSTSN RATLGGMINT DASGQGSLQY GKTSNHVLAL RAVLINGEIL DTSAVNSVDV LENIDALELS ESSKKLHQTI AQHCKEKRAA IIKDLPQLNR FLTGYDLKNV FNEDESEFNL TRILTGSEGS LAFICEAKLN LLLIPQYRTL INIKYRSFDA ALRNAPFMVK ANALSVETVD SKVLNLAKQD IIWHSVNELL TEDEKDPILG LNIVEFAGNN KEKIDRQVTA LCRLLDEKIE HNQDHIIGYQ VCSDLPSIER IYAMRKKAVG LLGNAKGAAK PIPFVEDTCV PPENLADYIS EFRALLDQHN LQYGMFGHVD AGVLHVRPAL DLCDKEQVKL FKQISDEVAE LTIKYGGLLW GEHGKGVRSH YGEKFFTPEL WHELRYIKTL FDPNNRLNPG KICTPLDSKD ELYSILSPMR ADKDRQIPIQ IRDEFKGAMN CNGNGLCFNF DEHSIMCPSM KVSKNRVFSP KGRAAMVREW LRLMANENVS PEQLDFRKTE IKLTALVKRL SNTVQKWRGN YDFSHEVKAA MDTCLACKAC ASQCPIKIDV PSFRAKFFHF YHSRYLRPTK DHIVANLEIA APYMAKQAKF FNYFTKLKVT QTLVEKTLGM TDLPLLSEPS LQQQLVEIHY QGKSLEELES LSAVEKNDIL FIVQDPYTSY YDAKVIRDFV MLTQKLGFKP ILLPFKPNGK AMHIKGFLKR FSKTAQNQAE FLNRMAKLGI PLVGVDPAIV LSYRDEYKEA LQEKRGDFHV LTAHEWLKQR LQNADLQEKL KNIAKTDRTL GWYLFPHCTE STFMPNSPKE WQEIFGRFGQ QLNVEKVGCC GMAGVFGHEV QNQKMSREIY DVSWHKKLHG KDPHFCLATG YSCRSQVKRY EHVVLKHPVQ ALLEVLK // ID Y1169_HAEIN Reviewed; 188 AA. AC P44118; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 14-OCT-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_1169; GN OrderedLocusNames=HI_1169; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22833.1; -; Genomic_DNA. DR PIR; A64021; A64021. DR RefSeq; WP_005694272.1; NC_000907.1. DR RefSeq; YP_008530234.1; NC_000907.1. DR ProteinModelPortal; P44118; -. DR SMR; P44118; 2-188. DR EnsemblBacteria; AAC22833; AAC22833; HI_1169. DR GeneID; 16830696; -. DR KEGG; hin:HI1168a; -. DR OMA; RCRIDYN; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR InterPro; IPR001544; Aminotrans_IV. DR Pfam; PF01063; Aminotran_4; 1. DR SUPFAM; SSF56752; SSF56752; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 188 Uncharacterized protein HI_1169. FT /FTId=PRO_0000078008. SQ SEQUENCE 188 AA; 22210 MW; 2F4FDE5EC3099DF6 CRC64; MYPLFETLCI ENGKIQNINL HQVRYERSLR EYYGKSAVKI FNLFSLIQLP TPLQNQLIRC RIDYNAETTQ IQYFEYQRKI YRTFQPVICD DIEYSLKYSD RSLINTLFAQ RGACDEIMII KNGKVTDCSI GNLIFRQGKK WYTPDTPLLL GTQREKLLQE GKIQERTIFQ EDIVNFDEIK IINAMNGL // ID Y131_HAEIN Reviewed; 346 AA. AC P43951; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_0131; DE Flags: Precursor; GN OrderedLocusNames=HI_0131; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21803.1; -; Genomic_DNA. DR PIR; D64002; D64002. DR PIR; E64002; E64002. DR RefSeq; NP_438300.1; NC_000907.1. DR RefSeq; WP_005694419.1; NC_000907.1. DR ProteinModelPortal; P43951; -. DR STRING; 71421.HI0131; -. DR EnsemblBacteria; AAC21803; AAC21803; HI_0131. DR GeneID; 951040; -. DR KEGG; hin:HI0131; -. DR PATRIC; 20188749; VBIHaeInf48452_0133. DR eggNOG; ENOG4105C4Y; Bacteria. DR eggNOG; COG1840; LUCA. DR KO; K02012; -. DR OMA; NILCETT; -. DR OrthoDB; EOG6VHZCM; -. DR PhylomeDB; P43951; -. DR BioCyc; RETL1328306-WGS:GSTH-2135-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-2136-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR026045; Ferric-bd. DR PIRSF; PIRSF002825; CfbpA; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 346 Uncharacterized protein HI_0131. FT /FTId=PRO_0000013951. SQ SEQUENCE 346 AA; 37898 MW; 233AD90C54E10710 CRC64; MKFNKISLSV STALLAAGLA VSGSANAKGR LVVYCSATNI LCETTTKAFG EKYDVKTSFI RNGSGSTFAK VEAEKNNPQA DVWFGGTFDP QAQAAELGLI EPYKSKHIDE IVERFREPAK TKGHYVSSIY MGILGFGVNT ERLAKLGIKE VPKCWKDLTD PRLKGEVQIA DPQSAGTAYT ALATFVQLWG EKEAFDFLKE LHPNVSQYTK SGITPSRNSA RGEATIGVGF LHDYALEKRN GAPLELVVPC EGTGYELGGV SILKGARNID NAKLFVDWAL SKEGQELAWK QGDSLQILTN TTAEQSPTAF DPNKLKLINY DFEKYGATEQ RKALIEKWVQ EVKLAK // ID Y132A_HAEIN Reviewed; 123 AA. AC O86236; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-MAY-2016, entry version 54. DE RecName: Full=Uncharacterized transposase-like protein HI_1328.1; GN OrderedLocusNames=HI_1328.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: To insertion element IS1016 transposase. 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; L42023; AAC22982.1; -; Genomic_DNA. DR EnsemblBacteria; AAC22982; AAC22982; HI_1328.1. DR OMA; GRYHING; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. DR SMART; SM01126; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome; DNA recombination; Reference proteome; KW Transposable element; Transposition. FT CHAIN 1 123 Uncharacterized transposase-like protein FT HI_1328.1. FT /FTId=PRO_0000078027. SQ SEQUENCE 123 AA; 14466 MW; 7EB8BCD207AC622A CRC64; MKCKVYTVVV PNVQSATLLP IIREKVKPDS IVYTDTFRSY DVLDVSEFSH FRINHSTHFA ENHNYINGIG NFWNHAKRHL QKFNGIPKEH FELYLKECEW RFNNSEIKSQ ISILKQLVKG SLV // ID Y1355_HAEIN Reviewed; 154 AA. AC P44168; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=UPF0260 protein HI_1355; GN OrderedLocusNames=HI_1355; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0260 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; L42023; AAC23002.1; -; Genomic_DNA. DR PIR; F64026; F64026. DR RefSeq; NP_439506.1; NC_000907.1. DR RefSeq; WP_005691957.1; NC_000907.1. DR STRING; 71421.HI1355; -. DR DNASU; 950283; -. DR EnsemblBacteria; AAC23002; AAC23002; HI_1355. DR GeneID; 950283; -. DR KEGG; hin:HI1355; -. DR PATRIC; 20191395; VBIHaeInf48452_1408. DR eggNOG; ENOG4108ZZ3; Bacteria. DR eggNOG; COG2983; LUCA. DR KO; K09160; -. DR OMA; TCQCSDY; -. DR OrthoDB; EOG6PZXBQ; -. DR PhylomeDB; P44168; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00676; UPF0260; 1. DR InterPro; IPR005358; Puta_zinc/iron-chelating_dom. DR InterPro; IPR008228; UCP006173. DR Pfam; PF03692; CxxCxxCC; 1. DR PIRSF; PIRSF006173; UCP006173; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 154 UPF0260 protein HI_1355. FT /FTId=PRO_0000214582. SQ SEQUENCE 154 AA; 18163 MW; 886CE6D467E8AB55 CRC64; MQSNMQLEPN FWQTKSLLEM TESEWEALCD GCGKCCYRKY IQGRGKRQKL YYTRIACNLL DLETGKCGNY SERFNIETDC TKLTKKNLPD FHWLPDTCAY RLLYEGKTLP EWHPLISGSP HSVKNADILI KNGIHERDVI DWFEFIIDED HTFK // ID Y1369_HAEIN Reviewed; 839 AA. AC P45182; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_1369; GN OrderedLocusNames=HI_1369; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YddB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23016.1; -; Genomic_DNA. DR PIR; F64171; F64171. DR RefSeq; NP_439520.1; NC_000907.1. DR RefSeq; WP_010869194.1; NC_000907.1. DR ProteinModelPortal; P45182; -. DR STRING; 71421.HI1369; -. DR EnsemblBacteria; AAC23016; AAC23016; HI_1369. DR GeneID; 950892; -. DR KEGG; hin:HI1369; -. DR PATRIC; 20191425; VBIHaeInf48452_1423. DR eggNOG; ENOG4105PE1; Bacteria. DR eggNOG; ENOG410XSVA; LUCA. DR OMA; NRYYGRS; -. DR OrthoDB; EOG6XDGR6; -. DR PhylomeDB; P45182; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.130.10; -; 1. DR Gene3D; 2.40.170.20; -; 2. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF07715; Plug; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 839 Uncharacterized protein HI_1369. FT /FTId=PRO_0000168942. SQ SEQUENCE 839 AA; 96411 MW; D419EFF3BF91E503 CRC64; MRFFIYLIPI LSRIPLAFIN LKNIMIIILI CIFILGNYTM YQKKPLMLLF CSTFVSPFVM GKTIETTNKN ILPEIVVYGD NNKSLSSVKT LSSDEISKTP TSNGNITDYL RSNPHIRYEN SDQNGFQRGE IKPENISING ADPNQSAYFV DNVNINNDLA IDSSIFDGAM QVVPGISHTQ AYFFDATMLS KVEVQDSNIS ASLGGFMGGA VIAKTKQYSG TDSIKLKYRT TNSSWAKMEA GDSVQKILKL VRPDDVGVAE LQPKYNKQTF NILAEKRLND NLGMVFGYSR RTSSIEQNRL IGFDKDANNK AQLDKQNHQR LSDNLLLNFN WTPQEKERIE FGLRYSNYKE LKYFKXNINN NVSDYHQALG ATLAWVHSFN SGVWTNTLAY DRFQDKRKSS SNSVEITSVL DEYYEPLYNF EKGGYGNSQL IQDNLHFSTE YVMDPFYLAS TEHSISVGGI YQATKYQFYR PQDVHSKIIL STLKSDGSME EPPTSTENTT SKGRVKTSYQ NIAIYAEDLI KWNKFELRPG IRIERDDYLK NNNIAPRFVA RYHPWDNTGF TLGLNRYYGR SFASLKLANG ILKLNNDSTR QHQNFSSLKS PYADELSLSF DQNMGNFALK LGYIHRDNKN RIILKREPIQ GERKTSYING HPFGVDIYTF QLNNIEPWKL GKTYWTTSLG FDWLNTKRAD VSNEFNPNEP VYLDGKLMTR SQMLQQVNSS TEDWIARLGI DMTIPDYNIT WSNKVYMKAP IRSYEELDGD NGDGISRFRS YHYGRHTQWD SSIRWQPTIR GKHSVYMQVD ILNVLNKTRK NKVTTISTSD EYGVYTPGRE FWLEVGYQF // ID Y1403_HAEIN Reviewed; 182 AA. AC P44178; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_1403; GN OrderedLocusNames=HI_1403; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23053.1; -; Genomic_DNA. DR PIR; H64027; H64027. DR RefSeq; NP_439556.1; NC_000907.1. DR RefSeq; WP_010869205.1; NC_000907.1. DR ProteinModelPortal; P44178; -. DR STRING; 71421.HI1403; -. DR EnsemblBacteria; AAC23053; AAC23053; HI_1403. DR GeneID; 950856; -. DR KEGG; hin:HI1403; -. DR PATRIC; 20191505; VBIHaeInf48452_1463. DR OrthoDB; EOG62RS7J; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR005068; Phage_lambda_Stf-r2. DR Pfam; PF03406; Phage_fiber_2; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 182 Uncharacterized protein HI_1403. FT /FTId=PRO_0000078041. SQ SEQUENCE 182 AA; 20536 MW; D92AC1FACE4D9A47 CRC64; MKAFLHHLQN EAKLIISLTY CVDGEFALNE IARATLQQYG IVQLSSATNS DSETEAATSK AVKTAYDKAV EAKTTADGKV GLNGNESING EKTFENRIVA KRNIRISDSP HYASRGDYLN IGANNGDCWF EYKLSNQEIG TLRMHANGDL TYKRQKIYLK MDCWQAIHKR KLKVFTAKRK KR // ID Y1412_HAEIN Reviewed; 173 AA. AC P45197; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_1412; GN OrderedLocusNames=HI_1412; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23060.1; -; Genomic_DNA. DR PIR; G64171; G64171. DR RefSeq; NP_439563.1; NC_000907.1. DR RefSeq; WP_010869207.1; NC_000907.1. DR STRING; 71421.HI1412; -. DR EnsemblBacteria; AAC23060; AAC23060; HI_1412. DR GeneID; 950722; -. DR KEGG; hin:HI1412; -. DR PATRIC; 20191521; VBIHaeInf48452_1471. DR eggNOG; ENOG4106050; Bacteria. DR eggNOG; COG3646; LUCA. DR OMA; NCHCSED; -. DR OrthoDB; EOG6B09SD; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR018877; Phage_P22_Orf201_C. DR InterPro; IPR014054; Phage_regulatory_Rha. DR Pfam; PF10549; ORF11CD3; 1. DR Pfam; PF09669; Phage_pRha; 1. DR TIGRFAMs; TIGR02681; phage_pRha; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 173 Uncharacterized protein HI_1412. FT /FTId=PRO_0000078049. SQ SEQUENCE 173 AA; 20512 MW; ABF59CCA6B962447 CRC64; MNLQTIENFE QFLKVNDKQR IVTNSRHIAT VFGKRHDNII RDIKALVIEQ DCGEFALLNF EETSYFDEWG RKQPMYQMTK NGFLLLVMGY RTQKAMKFKV EFIKAFDFMR EKLQQEGYSL MHKYNELCIE HKAKKAFASL CGKGLREWKG DKPVLEATLK LFEDKMQIEL PIK // ID Y1450_HAEIN Reviewed; 107 AA. AC P44199; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=UPF0263 protein HI_1450; GN OrderedLocusNames=HI_1450; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0263 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; L42023; AAC23100.1; -; Genomic_DNA. DR PIR; B64030; B64030. DR RefSeq; NP_439602.1; NC_000907.1. DR RefSeq; WP_005628170.1; NC_000907.1. DR PDB; 1NNV; NMR; -; A=1-107. DR PDBsum; 1NNV; -. DR ProteinModelPortal; P44199; -. DR SMR; P44199; 1-107. DR STRING; 71421.HI1450; -. DR EnsemblBacteria; AAC23100; AAC23100; HI_1450. DR GeneID; 950346; -. DR KEGG; hin:HI1450; -. DR PATRIC; 20191605; VBIHaeInf48452_1512. DR eggNOG; ENOG4105XW2; Bacteria. DR eggNOG; COG3099; LUCA. DR KO; K09901; -. DR OMA; QFEDRGA; -. DR OrthoDB; EOG6R2H2M; -. DR EvolutionaryTrace; P44199; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.10.450.140; -; 1. DR HAMAP; MF_00680; UPF0263; 1. DR InterPro; IPR007376; dsDNA_mimic_put. DR Pfam; PF04269; DUF440; 1. DR PIRSF; PIRSF004916; UCP004916; 1. DR ProDom; PD020447; dsDNA_mimic_put; 1. DR SUPFAM; SSF102816; SSF102816; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 107 UPF0263 protein HI_1450. FT /FTId=PRO_0000072779. FT HELIX 10 24 {ECO:0000244|PDB:1NNV}. FT HELIX 31 39 {ECO:0000244|PDB:1NNV}. FT STRAND 40 42 {ECO:0000244|PDB:1NNV}. FT STRAND 46 50 {ECO:0000244|PDB:1NNV}. FT TURN 55 58 {ECO:0000244|PDB:1NNV}. FT STRAND 59 62 {ECO:0000244|PDB:1NNV}. FT STRAND 68 75 {ECO:0000244|PDB:1NNV}. FT STRAND 86 92 {ECO:0000244|PDB:1NNV}. FT STRAND 94 98 {ECO:0000244|PDB:1NNV}. FT STRAND 101 105 {ECO:0000244|PDB:1NNV}. SQ SEQUENCE 107 AA; 12525 MW; B585C2B9E3E29A8B CRC64; MTTEIKKLDP DTAIDIAYDI FLEMAGENLD PADILLFNLQ FEERGGVEFV ETADDWEEEI GVLIDPEEYA EVWVGLVNEQ DEMDDVFAKF LISHREEDRE FHVIWKK // ID Y1470_HAEIN Reviewed; 253 AA. AC Q57399; O05064; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1470; GN OrderedLocusNames=HI_1470; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23118.1; -; Genomic_DNA. DR PIR; F64125; F64125. DR RefSeq; NP_439621.1; NC_000907.1. DR RefSeq; WP_005693486.1; NC_000907.1. DR PDB; 2NQ2; X-ray; 2.40 A; C/D=1-253. DR PDBsum; 2NQ2; -. DR ProteinModelPortal; Q57399; -. DR SMR; Q57399; 2-252. DR DIP; DIP-58990N; -. DR STRING; 71421.HI1470; -. DR TCDB; 3.A.1.14.11; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC23118; AAC23118; HI_1470. DR GeneID; 950600; -. DR KEGG; hin:HI1470; -. DR PATRIC; 20191655; VBIHaeInf48452_1537. DR eggNOG; ENOG4108W0P; Bacteria. DR eggNOG; COG1120; LUCA. DR KO; K02013; -. DR OMA; NINAHEA; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; Q57399; -. DR EvolutionaryTrace; Q57399; -. DR Proteomes; UP000000579; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 253 Uncharacterized ABC transporter ATP- FT binding protein HI_1470. FT /FTId=PRO_0000093207. FT DOMAIN 5 229 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT STRAND 3 14 {ECO:0000244|PDB:2NQ2}. FT TURN 15 18 {ECO:0000244|PDB:2NQ2}. FT STRAND 19 29 {ECO:0000244|PDB:2NQ2}. FT STRAND 33 37 {ECO:0000244|PDB:2NQ2}. FT STRAND 40 43 {ECO:0000244|PDB:2NQ2}. FT HELIX 44 51 {ECO:0000244|PDB:2NQ2}. FT STRAND 58 64 {ECO:0000244|PDB:2NQ2}. FT STRAND 68 71 {ECO:0000244|PDB:2NQ2}. FT HELIX 83 88 {ECO:0000244|PDB:2NQ2}. FT HELIX 89 94 {ECO:0000244|PDB:2NQ2}. FT HELIX 103 115 {ECO:0000244|PDB:2NQ2}. FT HELIX 119 121 {ECO:0000244|PDB:2NQ2}. FT HELIX 126 128 {ECO:0000244|PDB:2NQ2}. FT HELIX 131 144 {ECO:0000244|PDB:2NQ2}. FT STRAND 148 156 {ECO:0000244|PDB:2NQ2}. FT HELIX 161 176 {ECO:0000244|PDB:2NQ2}. FT STRAND 181 187 {ECO:0000244|PDB:2NQ2}. FT HELIX 189 195 {ECO:0000244|PDB:2NQ2}. FT STRAND 197 203 {ECO:0000244|PDB:2NQ2}. FT STRAND 206 211 {ECO:0000244|PDB:2NQ2}. FT HELIX 212 215 {ECO:0000244|PDB:2NQ2}. FT HELIX 218 225 {ECO:0000244|PDB:2NQ2}. FT STRAND 229 236 {ECO:0000244|PDB:2NQ2}. FT STRAND 239 246 {ECO:0000244|PDB:2NQ2}. FT HELIX 249 251 {ECO:0000244|PDB:2NQ2}. SQ SEQUENCE 253 AA; 28520 MW; AC54279C650C39F1 CRC64; MNKALSVENL GFYYQAENFL FQQLNFDLNK GDILAVLGQN GCGKSTLLDL LLGIHRPIQG KIEVYQSIGF VPQFFSSPFA YSVLDIVLMG RSTHINTFAK PKSHDYQVAM QALDYLNLTH LAKREFTSLS GGQRQLILIA RAIASECKLI LLDEPTSALD LANQDIVLSL LIDLAQSQNM TVVFTTHQPN QVVAIANKTL LLNKQNFKFG ETRNILTSEN LTALFHLPMF EQQAQYKESF FTHFVPLYKT LLK // ID Y1484_HAEIN Reviewed; 53 AA. AC P44211; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 51. DE RecName: Full=Putative uncharacterized protein HI_1484 in Mu-like prophage FluMu region; GN OrderedLocusNames=HI_1484; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23139.1; -; Genomic_DNA. DR PIR; E64031; E64031. DR EnsemblBacteria; AAC23139; AAC23139; HI_1484. DR OMA; DENAIAC; -. DR Proteomes; UP000000579; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 53 Putative uncharacterized protein HI_1484 FT in Mu-like prophage FluMu region. FT /FTId=PRO_0000078068. SQ SEQUENCE 53 AA; 6359 MW; BD868885A9E6DAE4 CRC64; MMDDLQDVSR LREAYQFYQK AKQDEDSIVC GCLNDAYEWL FSELKALFDE EEE // ID Y1486_HAEIN Reviewed; 57 AA. AC P44213; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Putative uncharacterized protein HI_1486 in Mu-like prophage FluMu region; GN OrderedLocusNames=HI_1486; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23141.1; -; Genomic_DNA. DR PIR; G64031; G64031. DR RefSeq; NP_439636.1; NC_000907.1. DR RefSeq; WP_005693505.1; NC_000907.1. DR STRING; 71421.HI1486; -. DR EnsemblBacteria; AAC23141; AAC23141; HI_1486. DR GeneID; 950578; -. DR KEGG; hin:HI1486; -. DR PATRIC; 20191689; VBIHaeInf48452_1554. DR OMA; FTHASIF; -. DR OrthoDB; EOG64V2KV; -. DR Proteomes; UP000000579; Chromosome. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Putative uncharacterized protein HI_1486 FT in Mu-like prophage FluMu region. FT /FTId=PRO_0000078070. SQ SEQUENCE 57 AA; 6588 MW; DCA9EE0991029E2D CRC64; MMTETRKNEL ENQLNQMIVM LKEAQKSLFK GQYTHAAIFV GNVSDQLPNM RMMLARG // ID Y1489_HAEIN Reviewed; 184 AA. AC P44215; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_1489; GN OrderedLocusNames=HI_1489; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23143.1; -; Genomic_DNA. DR PIR; I64031; I64031. DR RefSeq; NP_439639.1; NC_000907.1. DR RefSeq; WP_005693508.1; NC_000907.1. DR STRING; 71421.HI1489; -. DR EnsemblBacteria; AAC23143; AAC23143; HI_1489. DR GeneID; 950579; -. DR KEGG; hin:HI1489; -. DR PATRIC; 20191695; VBIHaeInf48452_1557. DR eggNOG; ENOG41065S5; Bacteria. DR eggNOG; ENOG4112ASJ; LUCA. DR OMA; PICHSDI; -. DR OrthoDB; EOG66MQSP; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 184 Uncharacterized protein HI_1489. FT /FTId=PRO_0000078072. SQ SEQUENCE 184 AA; 20782 MW; C298357DBED80211 CRC64; MKLCRCPICH SDIHLEALIE DDAGRELLGK ISQLTHGCAQ PMVGYLGLFK PAKSNLNNAR ALKILSEVLD LYPCSLLLAQ ALSETVASLR KKRQQALQTG QKIEPLTNHN YLKSVYETQK PHFAVIRSGK NQSETVKAQQ AEDKKVQDAI LYVERFVQLG QEEFVKNSPE YQIWLNHKAQ KQAL // ID Y148A_HAEIN Reviewed; 68 AA. AC O86220; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_0148.1; GN OrderedLocusNames=HI_0148.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC21832.1; -; Genomic_DNA. DR STRING; 71421.HI0148.1; -. DR EnsemblBacteria; AAC21832; AAC21832; HI_0148.1. DR PATRIC; 20188789; VBIHaeInf48452_0151. DR Proteomes; UP000000579; 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 68 Uncharacterized protein HI_0148.1. FT /FTId=PRO_0000077894. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. SQ SEQUENCE 68 AA; 7600 MW; E777D65E0BE995EB CRC64; MLFIPPPLLC LFIAIAMYFL PKIASYSVHF SVIVFVISLS FLIALSSVMQ SLYVKPPLIL VTLKAQQN // ID Y1493_HAEIN Reviewed; 94 AA. AC P44218; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_1493; GN OrderedLocusNames=HI_1493; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23145.1; -; Genomic_DNA. DR PIR; C64032; C64032. DR RefSeq; NP_439642.1; NC_000907.1. DR RefSeq; WP_010869225.1; NC_000907.1. DR STRING; 71421.HI1493; -. DR EnsemblBacteria; AAC23145; AAC23145; HI_1493. DR GeneID; 950360; -. DR KEGG; hin:HI1493; -. DR PATRIC; 20191703; VBIHaeInf48452_1561. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 94 Uncharacterized protein HI_1493. FT /FTId=PRO_0000078074. SQ SEQUENCE 94 AA; 10506 MW; D754498B3CA9B42F CRC64; MSLPITKIVV HCSATRNGKS IKQPGKNAAQ VIDGWHKQRG FKRQLSSQRA FNPHLSSIVI TLSLMWTAQS EPVAKWAKLV HTLRGTTKIQ WGFA // ID Y1497_HAEIN Reviewed; 75 AA. AC P44221; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=Uncharacterized protein HI_1497; GN OrderedLocusNames=HI_1497; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 dksA C4-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00510}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23137.1; -; Genomic_DNA. DR PIR; F64032; F64032. DR RefSeq; NP_439646.1; NC_000907.1. DR RefSeq; WP_005693516.1; NC_000907.1. DR ProteinModelPortal; P44221; -. DR STRING; 71421.HI1497; -. DR EnsemblBacteria; AAC23137; AAC23137; HI_1497. DR GeneID; 950363; -. DR KEGG; hin:HI1497; -. DR PATRIC; 20191713; VBIHaeInf48452_1566. DR eggNOG; COG1734; LUCA. DR OMA; AVRCICC; -. DR OrthoDB; EOG6PS62C; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR020460; Znf_C4-type_bac. DR InterPro; IPR012783; Znf_C4_TraR. DR InterPro; IPR000962; Znf_DskA_TraR. DR InterPro; IPR020458; Znf_DskA_TraR_CS. DR Pfam; PF01258; zf-dskA_traR; 1. DR PRINTS; PR00618; DKSAZNFINGER. DR TIGRFAMs; TIGR02419; C4_traR_proteo; 1. DR PROSITE; PS01102; ZF_DKSA_1; 1. DR PROSITE; PS51128; ZF_DKSA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 75 Uncharacterized protein HI_1497. FT /FTId=PRO_0000187552. FT ZN_FING 43 67 dksA C4-type. {ECO:0000255|PROSITE- FT ProRule:PRU00510}. SQ SEQUENCE 75 AA; 8405 MW; 9F6DAD6F2C02C626 CRC64; MADVLDQLNE REEALLQNIL APHLDTELSD DEVDAIAEAG RQCSECGLPI PTTRLRANPF AHRCVSCQQD WEEGR // ID Y1542_HAEIN Reviewed; 184 AA. AC P45244; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative NAD(P)H nitroreductase HI_1542; DE EC=1.-.-.-; GN OrderedLocusNames=HI_1542; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nitroreductase 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; L42023; AAC23192.1; -; Genomic_DNA. DR PIR; D64172; D64172. DR RefSeq; NP_439691.1; NC_000907.1. DR RefSeq; WP_005693567.1; NC_000907.1. DR ProteinModelPortal; P45244; -. DR STRING; 71421.HI1542; -. DR DNASU; 950405; -. DR EnsemblBacteria; AAC23192; AAC23192; HI_1542. DR GeneID; 950405; -. DR KEGG; hin:HI1542; -. DR PATRIC; 20191809; VBIHaeInf48452_1613. DR eggNOG; ENOG41069NU; Bacteria. DR eggNOG; COG0778; LUCA. DR OMA; QGIGAVW; -. DR OrthoDB; EOG69GZM0; -. DR PhylomeDB; P45244; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR026021; YdjA-like. DR Pfam; PF00881; Nitroreductase; 1. DR PIRSF; PIRSF000232; YdjA; 1. DR SUPFAM; SSF55469; SSF55469; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 184 Putative NAD(P)H nitroreductase HI_1542. FT /FTId=PRO_0000169004. FT NP_BIND 10 12 FMN. {ECO:0000250}. FT NP_BIND 122 127 NAD or NADP. {ECO:0000255}. FT NP_BIND 132 134 FMN. {ECO:0000250}. FT BINDING 35 35 FMN; shared with dimeric partner. FT {ECO:0000250}. FT BINDING 39 39 FMN; shared with dimeric partner. FT {ECO:0000250}. SQ SEQUENCE 184 AA; 20400 MW; F2EBDC99020C1025 CRC64; MDALTLLTTR KSNKKLTAPA PNAEQLERIF EAAMRAPDHG KLHPYHFIVM ENESLNKLET LLKAAVVEFD LGEEKLMKAE NLAHRAPMVI GVVAKIDPTI AKVPGWEQML SAGCATYGLQ LAAQAQGFDN VWISGKWVNG TALREAFGCR EQDRVIALVM IGTGMEKAER ECRVIDTKDF VTYL // ID Y1543_HAEIN Reviewed; 184 AA. AC P44248; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 81. DE RecName: Full=Uncharacterized protein HI_1543; GN OrderedLocusNames=HI_1543; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the TorD/DmsD 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; L42023; AAC23193.1; -; Genomic_DNA. DR PIR; F64035; F64035. DR RefSeq; NP_439692.1; NC_000907.1. DR RefSeq; WP_005693568.1; NC_000907.1. DR ProteinModelPortal; P44248; -. DR STRING; 71421.HI1543; -. DR EnsemblBacteria; AAC23193; AAC23193; HI_1543. DR GeneID; 950406; -. DR KEGG; hin:HI1543; -. DR PATRIC; 20191811; VBIHaeInf48452_1614. DR eggNOG; ENOG4107XHZ; Bacteria. DR eggNOG; COG3381; LUCA. DR OMA; EFSIVCR; -. DR OrthoDB; EOG6FZ4BH; -. DR PhylomeDB; P44248; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.10.3480.10; -; 1. DR InterPro; IPR026269; DmsD-type. DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone. DR PIRSF; PIRSF004690; DmsD; 1. DR SUPFAM; SSF89155; SSF89155; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 184 Uncharacterized protein HI_1543. FT /FTId=PRO_0000211658. SQ SEQUENCE 184 AA; 21059 MW; 21090267B7B32060 CRC64; MSEKQINNFS LISRLFGNLF YRFPTDKVLA DAFVWLQQEG LSQVWALDTD KESELALNSL QVKIDLNLLN EEYQKLFATN GKVMTAISAY GIDVEEFVNF RLVRNMPEVE SADHFALLLL TASWLEDNSD SLVAQQEFFE TFLLPCAAKF LTQVENQATL PFYRALALLT REILATMADE LEEE // ID Y1552_HAEIN Reviewed; 215 AA. AC P44251; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_1552; GN OrderedLocusNames=HI_1552; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23210.1; -; Genomic_DNA. DR PIR; I64035; I64035. DR RefSeq; NP_439701.1; NC_000907.1. DR RefSeq; WP_005693578.1; NC_000907.1. DR STRING; 71421.HI1552; -. DR ESTHER; haein-y1552; Duf_452. DR EnsemblBacteria; AAC23210; AAC23210; HI_1552. DR GeneID; 950563; -. DR KEGG; hin:HI1552; -. DR PATRIC; 20191829; VBIHaeInf48452_1623. DR eggNOG; ENOG4105HSA; Bacteria. DR eggNOG; COG2830; LUCA. DR KO; K09789; -. DR OMA; IVYFAGW; -. DR OrthoDB; EOG6S7XW4; -. DR BioCyc; MetaCyc:MONOMER-17845; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007398; DUF452. DR Pfam; PF04301; DUF452; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 215 Uncharacterized protein HI_1552. FT /FTId=PRO_0000078084. SQ SEQUENCE 215 AA; 25201 MW; EADF85CE2D1CFFBD CRC64; MKTKFYDYQG EHLILYFAGW GTPPDAVNHL ILPENHDLLI CYDYQDLNLD FDLSAYRHIR LVAWSMGVWV AERVLQGIRL KSATAVNGTG LPCDDSFGIP YAIFKGTLEN LTENTRLKFE RRICGDKASF ERYQLFPARP FDEIHQELTA LFAMIQQDKR IDLIHWANAW VSSRDKIFTP ANQHQYWALR CAVQEIEGEH YVFSRFTHWS ALWDH // ID Y1569_HAEIN Reviewed; 50 AA. AC P44258; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 48. DE RecName: Full=Uncharacterized protein HI_1569; GN OrderedLocusNames=HI_1569; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23223.1; -; Genomic_DNA. DR PIR; G64036; G64036. DR EnsemblBacteria; AAC23223; AAC23223; HI_1569. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_1569. FT /FTId=PRO_0000078089. SQ SEQUENCE 50 AA; 6132 MW; 06712E983668241E CRC64; MKDFADRYTF IRQGKMLVVK ILPKEIFVLS FRRIKDKELK KLLEKDYALR // ID Y156A_HAEIN Reviewed; 59 AA. AC O86243; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 46. DE RecName: Full=Uncharacterized protein HI_1564.1; GN OrderedLocusNames=HI_1564.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23222.1; -; Genomic_DNA. DR EnsemblBacteria; AAC23222; AAC23222; HI_1564.1. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 59 Uncharacterized protein HI_1564.1. FT /FTId=PRO_0000078088. SQ SEQUENCE 59 AA; 7066 MW; D0B32B05BF9F919B CRC64; MVGFSSCRVG FSPPTNNREI FWWAKAHPTL STHHSMRTSF YFRSNHYDDF MQKDSRTYT // ID Y1571_HAEIN Reviewed; 79 AA. AC P44260; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_1571; GN OrderedLocusNames=HI_1571; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC23225.1; -; Genomic_DNA. DR RefSeq; NP_439717.1; NC_000907.1. DR RefSeq; WP_005693594.1; NC_000907.1. DR STRING; 71421.HI1571; -. DR EnsemblBacteria; AAC23225; AAC23225; HI_1571. DR GeneID; 950428; -. DR KEGG; hin:HI1571; -. DR PATRIC; 20191865; VBIHaeInf48452_1641. DR eggNOG; COG4383; LUCA. DR OMA; ISESWVW; -. DR OrthoDB; EOG60PHGK; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009279; DUF935. DR Pfam; PF06074; DUF935; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 79 Uncharacterized protein HI_1571. FT /FTId=PRO_0000078091. SQ SEQUENCE 79 AA; 9048 MW; B60E4689C6AEB1D6 CRC64; MSLRHLAQII TQQIILPYLQ INVDPNIAPH RIPYFEFDTK EYEDLSVFAD AIPKLTGIGV QISESWVWDK LGIPEPQEG // ID Y1593_HAEIN Reviewed; 51 AA. AC P44264; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_1593; GN OrderedLocusNames=HI_1593; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23244.1; -; Genomic_DNA. DR PIR; D64037; D64037. DR EnsemblBacteria; AAC23244; AAC23244; HI_1593. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 51 Uncharacterized protein HI_1593. FT /FTId=PRO_0000078094. SQ SEQUENCE 51 AA; 6021 MW; 041BEAB9EF9AA3B2 CRC64; MPTVLLRPSH ESLNTEMVDN HFATQVNEKV DLEKDGVKFN LSYRMIWKPF N // ID Y1626_HAEIN Reviewed; 238 AA. AC P44278; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_1626; GN OrderedLocusNames=HI_1626; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YwiC. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23269.1; -; Genomic_DNA. DR PIR; I64038; I64038. DR RefSeq; NP_439768.1; NC_000907.1. DR RefSeq; WP_005693636.1; NC_000907.1. DR STRING; 71421.HI1626; -. DR EnsemblBacteria; AAC23269; AAC23269; HI_1626. DR GeneID; 950846; -. DR KEGG; hin:HI1626; -. DR PATRIC; 20191987; VBIHaeInf48452_1701. DR eggNOG; ENOG4108VTV; Bacteria. DR eggNOG; ENOG4111K10; LUCA. DR OMA; FAINPLC; -. DR OrthoDB; EOG6TR0CX; -. DR Proteomes; UP000000579; 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; IPR025576; YwiC. DR Pfam; PF14256; YwiC; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 238 Uncharacterized protein HI_1626. FT /FTId=PRO_0000078102. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. FT TRANSMEM 176 196 Helical. {ECO:0000255}. FT TRANSMEM 218 238 Helical. {ECO:0000255}. SQ SEQUENCE 238 AA; 27573 MW; 48B2034AB9F657A4 CRC64; MKLLISNQYG AIVMALVPFI YGMLLANPVW AHIFLLLGWF SLYLMTYPFL NLFKGKNLEL YKKWSVIYFA AAVIFAIPAL IYNWQVLYFM FAMLPFVAVN IYFTKKKDER NLWNDLAGIL IFALAGMGSY YFSDRTFDEK ILWVAIYPTL FFIGTTLYVK SMMRERKNPR YFWASVIFHL LCALIFVVSQ QFILALAFVP GLVRAVYLPT KKLSVMQVGL IEFAITAVFF ILLLVATL // ID Y1628_HAEIN Reviewed; 134 AA. AC P45279; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_1628; GN OrderedLocusNames=HI_1628; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YhcB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23275.1; -; Genomic_DNA. DR PIR; D64173; D64173. DR RefSeq; NP_439770.1; NC_000907.1. DR RefSeq; WP_005653154.1; NC_000907.1. DR STRING; 71421.HI1628; -. DR EnsemblBacteria; AAC23275; AAC23275; HI_1628. DR GeneID; 950472; -. DR KEGG; hin:HI1628; -. DR PATRIC; 20191991; VBIHaeInf48452_1703. DR eggNOG; ENOG4108W2Q; Bacteria. DR eggNOG; COG3105; LUCA. DR KO; K09908; -. DR OMA; QPRDYSE; -. DR OrthoDB; EOG683S9C; -. DR PhylomeDB; P45279; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009386; DUF1043. DR Pfam; PF06295; DUF1043; 1. DR PIRSF; PIRSF006318; YhcB; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 134 Uncharacterized protein HI_1628. FT /FTId=PRO_0000169480. SQ SEQUENCE 134 AA; 15314 MW; 0ECAB29449436F21 CRC64; MENWTNEIWV AIGIAFIVGL FIGYIIVRLT KGSVKHQAKT EAELKTVKTQ LDTQKAQIEK HFAESAELFK TLINDYQKLY RHYATSSNNL LGEKDQKGLF TQQLITATDK SQNEQPRDYS EGASGLFKEN KEEN // ID Y162_HAEIN Reviewed; 199 AA. AC P43782; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized lipoprotein HI_0162; DE Flags: Precursor; GN OrderedLocusNames=HI_0162; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Barcak G.J., Heimer S.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: To E.coli YajG. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20229; AAA62136.1; -; Genomic_DNA. DR EMBL; L42023; AAC21834.1; -; Genomic_DNA. DR PIR; B64144; B64144. DR RefSeq; NP_438332.1; NC_000907.1. DR RefSeq; WP_005694116.1; NC_000907.1. DR STRING; 71421.HI0162; -. DR EnsemblBacteria; AAC21834; AAC21834; HI_0162. DR GeneID; 951072; -. DR KEGG; hin:HI0162; -. DR PATRIC; 20188823; VBIHaeInf48452_0168. DR eggNOG; ENOG4105IEY; Bacteria. DR eggNOG; COG3056; LUCA. DR KO; K07286; -. DR OMA; DIVNNIY; -. DR OrthoDB; EOG679TC1; -. DR PhylomeDB; P43782; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR005619; Uncharacterised_YajG. DR Pfam; PF03923; Lipoprotein_16; 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 24 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 25 199 Uncharacterized lipoprotein HI_0162. FT /FTId=PRO_0000018038. 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 199 AA; 21657 MW; E92F4EECD0D7C233 CRC64; MALVNKIKTL SSVGILAATL FLAGCQAQSN ILAFTPPAPS ASMNVNRTAV VSVTTKDSRA IQEIASYTKH GELIKLNASP SVTQLFQQVM QQNLISKGFR VGQLNGSNAW VTVDVREFGT QVEQGNLRYK LNTKIQATVY VQGAKGSYNK SFNVTHSQEG VFNAGNDEIH KVLSQTFNDI VNNIYQDQEV AAAINQYSN // ID Y1637_HAEIN Reviewed; 470 AA. AC P44280; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_1637; GN OrderedLocusNames=HI_1637; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YcjX. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23282.1; -; Genomic_DNA. DR PIR; B64039; B64039. DR RefSeq; NP_439779.1; NC_000907.1. DR RefSeq; WP_005693645.1; NC_000907.1. DR STRING; 71421.HI1637; -. DR EnsemblBacteria; AAC23282; AAC23282; HI_1637. DR GeneID; 950851; -. DR KEGG; hin:HI1637; -. DR PATRIC; 20192019; VBIHaeInf48452_1713. DR eggNOG; ENOG4105CM6; Bacteria. DR eggNOG; COG3106; LUCA. DR KO; K06918; -. DR OMA; FDYPGEW; -. DR OrthoDB; EOG6B09PW; -. DR PhylomeDB; P44280; -. DR BioCyc; RETL1328306-WGS:GSTH-2341-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR007413; DUF463_YcjX. DR Pfam; PF04317; DUF463; 1. DR PIRSF; PIRSF019381; YcjX; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 470 Uncharacterized protein HI_1637. FT /FTId=PRO_0000168897. FT NP_BIND 27 34 ATP. {ECO:0000255}. SQ SEQUENCE 470 AA; 54251 MW; F487C88C0CF87A25 CRC64; MFNRVQKEIN QIINRGFDRT LRLAVTGLSR SGKTAFITSL INQLLSINQH SSQNLPLFEA ARNGSILAVK RVSQQDLSVP RFDYESNLND LSQNPPQWFQ STRGVSETRL AIRFQRQSGL LRHLKERGTL YLDIFDYPGE WLLDLPLLNL DFQQWSQEQI KVTTGVRAEL AQNWLSMLQN LDLSAVANED VLAKIAKSYT DYLHQCKAQG MQFIQPGRFV LPSDLEGAPA LQFFPLIHLS GEHWQTLKKT AKSNSYFAVL TKRYNYYRNK IVKGFYENYF STFDRQVILA DCLTPLNHSQ QAFLDMQMGL NQLFNNFHYG SRNFLHRLFS PQIDRLMFVA TKADHITRDQ IPNLVSLMRQ IVQEGGRHVE FEGIDTEYTA IAAVRTTKQV IVNQQGKEIK AIQGVRSIDK QLITLYPGTV PSKLPKTEFW QKQPHFDFDS FEPQPLEQGE SIPHLRMDAV LQFLLSDRFE // ID Y186_HAEIN Reviewed; 135 AA. AC P44558; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0186; GN OrderedLocusNames=HI_0186; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH merR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00254}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21856.1; -; Genomic_DNA. DR PIR; I64052; I64052. DR RefSeq; NP_438354.1; NC_000907.1. DR RefSeq; WP_005691542.1; NC_000907.1. DR ProteinModelPortal; P44558; -. DR STRING; 71421.HI0186; -. DR EnsemblBacteria; AAC21856; AAC21856; HI_0186. DR GeneID; 951087; -. DR KEGG; hin:HI0186; -. DR PATRIC; 20188867; VBIHaeInf48452_0190. DR eggNOG; ENOG4105VUF; Bacteria. DR eggNOG; COG0789; LUCA. DR OMA; CLKNSGM; -. DR OrthoDB; EOG6Z0QGQ; -. DR PhylomeDB; P44558; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR000551; MerR-type_HTH_dom. DR Pfam; PF13411; MerR_1; 1. DR PRINTS; PR00040; HTHMERR. DR SMART; SM00422; HTH_MERR; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR PROSITE; PS00552; HTH_MERR_1; 1. DR PROSITE; PS50937; HTH_MERR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 135 Uncharacterized HTH-type transcriptional FT regulator HI_0186. FT /FTId=PRO_0000098166. FT DOMAIN 2 71 HTH merR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. FT DNA_BIND 5 24 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. SQ SEQUENCE 135 AA; 15481 MW; B5F798D6A6584AD2 CRC64; MTYTTAKAAE KIGISAYTLR FYDKEGLLPN VGRDEYGNRR FTDKDLQWLS LLQCLKNTGM SLKDIKRFAE CTIIGDDTIE ERLSLFENQT KNVKCQIAEL KRYLDLLEYK LAFYQKAKAL GSVKAVNLPQ IPETS // ID Y223_HAEIN Reviewed; 300 AA. AC P44579; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized transporter HI_0223; GN OrderedLocusNames=HI_0223; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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 EamA transporter 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; L42023; AAC21892.1; -; Genomic_DNA. DR RefSeq; NP_438395.1; NC_000907.1. DR RefSeq; WP_010868962.1; NC_000907.1. DR STRING; 71421.HI0223; -. DR EnsemblBacteria; AAC21892; AAC21892; HI_0223. DR GeneID; 951139; -. DR KEGG; hin:HI0223; -. DR PATRIC; 20188967; VBIHaeInf48452_0236. DR eggNOG; ENOG4106KPZ; Bacteria. DR eggNOG; COG2962; LUCA. DR KO; K05786; -. DR OMA; WAPLNGE; -. DR OrthoDB; EOG6Z99ZH; -. DR PhylomeDB; P44579; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR000620; EamA_dom. DR InterPro; IPR004626; RarD. DR Pfam; PF00892; EamA; 1. DR TIGRFAMs; TIGR00688; rarD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 300 Uncharacterized transporter HI_0223. FT /FTId=PRO_0000108157. FT TRANSMEM 13 35 Helical. {ECO:0000255}. FT TRANSMEM 45 67 Helical. {ECO:0000255}. FT TRANSMEM 80 102 Helical. {ECO:0000255}. FT TRANSMEM 106 128 Helical. {ECO:0000255}. FT TRANSMEM 180 202 Helical. {ECO:0000255}. FT TRANSMEM 217 236 Helical. {ECO:0000255}. FT TRANSMEM 243 265 Helical. {ECO:0000255}. FT TRANSMEM 275 294 Helical. {ECO:0000255}. SQ SEQUENCE 300 AA; 34181 MW; 695BC144469089B7 CRC64; MKFKMKVVTQ GILLCIFSQC LFGILYLFSI WLQPLSGTDV FAWRMLTMIF GLLLILFPTI GCRSLLSLIT TTLGKSWTRW VLFLLGTLDA GSQFWLFMWA PLNGEGINIA MGYFLFPLIM AVLGWAWLKE RLSFIQKIAL LLAAAGVAHE LWHTQSFSWT SLWVCTVYPF YYLSRKWMKI PALQGITLDI ILISIPCFIY ILSQSDTLSL VTQEYRYWLL LPALGIVSAI SLSANLKSSQ QIPVSIFAVL SYIEPILLFL IAVFVLDNQI TTSDYFTYVP IWLSLIVIGI EGLLNKKKVR // ID Y228_HAEIN Reviewed; 124 AA. AC P43966; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_0228; GN OrderedLocusNames=HI_0228; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21902.1; -; Genomic_DNA. DR PIR; B64004; B64004. DR EnsemblBacteria; AAC21902; AAC21902; HI_0228. DR PATRIC; 20188979; VBIHaeInf48452_0242. DR OMA; GDISESW; -. DR OrthoDB; EOG6KMB8T; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 124 Uncharacterized protein HI_0228. FT /FTId=PRO_0000077899. SQ SEQUENCE 124 AA; 14299 MW; 263D8AEA34D09C01 CRC64; MMLIIFLNVE ITLKSLLMHN ENLSVFILHT GDISESWQND LQLYFAKRYS TLQLVHMISI NTLDTSPNIF HFTGPHKPLD NIFSENACVN AVISLFRLYA SISWQDICSL PLGTTRANWI NQER // ID Y290_HAEIN Reviewed; 722 AA. AC P77868; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-APR-2016, entry version 121. DE RecName: Full=Probable cation-transporting ATPase HI_0290; DE EC=3.6.3.-; GN OrderedLocusNames=HI_0290; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. 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 IB subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HMA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21955.1; -; Genomic_DNA. DR RefSeq; NP_438457.1; NC_000907.1. DR RefSeq; WP_010868972.1; NC_000907.1. DR ProteinModelPortal; P77868; -. DR STRING; 71421.HI0290; -. DR EnsemblBacteria; AAC21955; AAC21955; HI_0290. DR GeneID; 949726; -. DR KEGG; hin:HI0290; -. DR PATRIC; 20189119; VBIHaeInf48452_0306. DR eggNOG; ENOG4105C59; Bacteria. DR eggNOG; COG2217; LUCA. DR KO; K17686; -. DR OMA; AVERQAN; -. DR OrthoDB; EOG6742RM; -. DR PhylomeDB; P77868; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0019829; F:cation-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0098655; P:cation transmembrane transport; IBA:GOC. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR Gene3D; 2.70.150.10; -; 1. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR InterPro; IPR027256; P-typ_ATPase_IB. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR SUPFAM; SSF81660; SSF81660; 1. DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 722 Probable cation-transporting ATPase FT HI_0290. FT /FTId=PRO_0000046334. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 340 360 Helical. {ECO:0000255}. FT TRANSMEM 373 393 Helical. {ECO:0000255}. FT TRANSMEM 523 543 Helical. {ECO:0000255}. FT TRANSMEM 608 628 Helical. {ECO:0000255}. FT TRANSMEM 675 695 Helical. {ECO:0000255}. FT TRANSMEM 697 717 Helical. {ECO:0000255}. FT DOMAIN 10 76 HMA. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. FT ACT_SITE 422 422 4-aspartylphosphate intermediate. FT {ECO:0000250}. FT METAL 20 20 {ECO:0000255|PROSITE-ProRule:PRU00280}. FT METAL 23 23 {ECO:0000255|PROSITE-ProRule:PRU00280}. FT METAL 617 617 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. FT METAL 621 621 Magnesium. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. SQ SEQUENCE 722 AA; 78072 MW; E4FF0BA5642EDCDD CRC64; MLDLTPQSKK ISIQIGGMTC QSCANRIEKV LNKKPFVQQA GVNFAAEEAQ VVFDATQASE AQIIEIIHKT GFSAHIKQAN ELPIEENTSI PWRLIVLWII NIPFLIGMLG MIGGSHNLML PPIWQFALAS IVQLWLAIPF YRGAIGSIRG GLTNMDVLVS TGTLTIYLYS AFMLFYHANH AMGHVYFEAS VMVIGFVSLG KFLEDRTKKH SLNSLSMLLQ LTPKKVTVLR NEKWIEIALD QVNIGEIIRA NQGERIAADG VIESGNGWCD ESHLTGESRP EEKQKGGKVL AGAMVTEGSI IYRANQLGSQ TLLGDMMNAL SDAQGSKAPI ARFADKVTSV FVPVVLVISL VTFALTYILT NDSVSSLIHA VSVLVIACPC ALGLATPAAI MVGLGKAVNA GVWFKDAAAM EETAHVDTVV LDKTGTLTKG ELEISALWQP QSAVYSEDDL YRFAAAVERQ ANHPIAKAIV QAAEXKMLEI PTALFSKMEV GQGIQAELEQ VGTIKVGKPD YCGLILPKNL EDIWQIASIV AVSINDEPIG AFALTDTLKN DSLHAIQRLQ QQNIDVVIMS GDQQSVVDYI AKQLGIKKAF GKLTPRDKAE QIQKLKDLGH IVAMVGDGIN DAPALASANV SFAMKSSSDI AEQTASATLM QHSVNQLVDA LFIARATLKN IKQNLFFALI YNILGIPLAA FGFLSPIIAG AAMALSSISV LMNALRLKKV RF // ID Y315_HAEIN Reviewed; 246 AA. AC P44634; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Probable transcriptional regulatory protein HI_0315 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=HI_0315; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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; L42023; AAC21979.1; -; Genomic_DNA. DR PIR; G64147; G64147. DR RefSeq; NP_438481.1; NC_000907.1. DR RefSeq; WP_005649034.1; NC_000907.1. DR ProteinModelPortal; P44634; -. DR SMR; P44634; 3-246. DR STRING; 71421.HI0315; -. DR EnsemblBacteria; AAC21979; AAC21979; HI_0315. DR GeneID; 949441; -. DR KEGG; hin:HI0315; -. DR PATRIC; 20189171; VBIHaeInf48452_0332. DR eggNOG; ENOG4105CDY; Bacteria. DR eggNOG; COG0217; LUCA. DR OMA; MTRNGGS; -. DR OrthoDB; EOG6HJ29R; -. DR PhylomeDB; P44634; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.200; -; 1. DR Gene3D; 3.30.1270.10; -; 2. DR Gene3D; 3.30.70.980; -; 1. DR HAMAP; MF_00693; Transcrip_reg_TACO1; 1. DR InterPro; IPR017856; Integrase_Zn-bd_dom-like_N. DR InterPro; IPR002876; Transcrip_reg_TACO1-like. DR InterPro; IPR026563; Transcrip_reg_TACO1-like_dom2. DR InterPro; IPR026564; Transcrip_reg_TACO1-like_dom3. DR InterPro; IPR029072; YebC-like. DR PANTHER; PTHR12532; PTHR12532; 1. DR Pfam; PF01709; Transcrip_reg; 1. DR SUPFAM; SSF75625; SSF75625; 1. DR TIGRFAMs; TIGR01033; TIGR01033; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 246 Probable transcriptional regulatory FT protein HI_0315. FT /FTId=PRO_0000175818. SQ SEQUENCE 246 AA; 26383 MW; 847DD353F99A2CF8 CRC64; MAGHSKWANI KHRKAAQDAQ RGKIFTKLIR ELVTAAKIGG GDVSANPRLR AAVDKALSNN MTRDTINRAI DRGVGGGDDT NMETKIYEGY GPGGTAVMVE CLSDNANRTI SQVRPSFTKC GGNLGTEGSV GYLFSKKGLI LIAEADEDAL TEAAIEAGAD DIQPQDDGSF EIYTAWEDLG SVRDGIEAAG FKVQEAEVTM IPSTTVDLDI ETAPKLLRLI DMLEDCDDVQ NVYHNGEICD EVASQL // ID Y318_HAEIN Reviewed; 172 AA. AC P43984; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_0318; GN OrderedLocusNames=HI_0318; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21982.1; -; Genomic_DNA. DR PIR; B64006; B64006. DR RefSeq; NP_438484.1; NC_000907.1. DR RefSeq; WP_005649040.1; NC_000907.1. DR STRING; 71421.HI0318; -. DR EnsemblBacteria; AAC21982; AAC21982; HI_0318. DR GeneID; 949431; -. DR KEGG; hin:HI0318; -. DR PATRIC; 20189179; VBIHaeInf48452_0336. DR eggNOG; ENOG4108WWS; Bacteria. DR eggNOG; COG1755; LUCA. DR OMA; YWALCSL; -. DR OrthoDB; EOG6Z6FZS; -. DR PhylomeDB; P43984; -. DR Proteomes; UP000000579; 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:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity; IEA:InterPro. DR InterPro; IPR007269; ICMT_MeTrfase. DR Pfam; PF04140; ICMT; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 172 Uncharacterized protein HI_0318. FT /FTId=PRO_0000077908. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. SQ SEQUENCE 172 AA; 19725 MW; B6B97BF3BBBB90EB CRC64; MLFINITFAC ILAIRFYSLS ISIRHEKALI AKGAIQYGKR NSTLLSIAHV AFYFAAIIEA NKQNLSFNST SQIGLAILIF AIAMLFYVIY ELKEIWTVKI YILPEHQINR SFLFKYVRHP NYFLNIIPEL IGLSLFCQAK YTALVGLPIY LLILAVRIKQ EESAMSHLFP KS // ID Y367_HAEIN Reviewed; 303 AA. AC Q57065; O05019; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_0367; GN OrderedLocusNames=HI_0367; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22025.1; -; Genomic_DNA. DR PIR; A64150; A64150. DR RefSeq; NP_438528.1; NC_000907.1. DR RefSeq; WP_005693797.1; NC_000907.1. DR STRING; 71421.HI0367; -. DR EnsemblBacteria; AAC22025; AAC22025; HI_0367. DR GeneID; 949469; -. DR KEGG; hin:HI0367; -. DR PATRIC; 20189279; VBIHaeInf48452_0385. DR eggNOG; ENOG4105HSZ; Bacteria. DR eggNOG; COG1426; LUCA. DR KO; K15539; -. DR OMA; GMTGLWW; -. DR OrthoDB; EOG65XN0H; -. DR PhylomeDB; Q57065; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR InterPro; IPR025194; DUF4115. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF13464; DUF4115; 1. DR Pfam; PF13413; HTH_25; 1. DR SUPFAM; SSF47413; SSF47413; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 303 Uncharacterized protein HI_0367. FT /FTId=PRO_0000077916. SQ SEQUENCE 303 AA; 34011 MW; 4A3FEFB363D5653C CRC64; MNPTTEQVLS PGEIFRQTRE ALNLSLEDVA KEITLRPSIL EQLENNEFIQ KSTPAIFVKG YVRSYAKFLR LPDSVWENIV FAETEKNDLG KNARSTRAVN QYSSHNRWIG RLTAIVFMIV IGMTGLWWWQ SYQQNTQERD DLVQSYVAST ENNQPATALV TTEESNKTVP ETAAPVSQPV EITNNLLPEI AQENSVSQPK NDEKSVSEIQ SAVENPSISP TLPIAKGDLV IEILTNSSWI SVKDNARHVL AQKEYKQGEI LTFNGNEFSL IVGAPSNVRI TYKGENYPLK VDGRVAKFKL SQP // ID Y418_HAEIN Reviewed; 447 AA. AC P44699; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Putative metabolite transport protein HI_0418; GN OrderedLocusNames=HI_0418; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22076.1; -; Genomic_DNA. DR PIR; B64152; B64152. DR RefSeq; NP_438580.1; NC_000907.1. DR RefSeq; WP_005693746.1; NC_000907.1. DR ProteinModelPortal; P44699; -. DR STRING; 71421.HI0418; -. DR TCDB; 2.A.1.6.12; the major facilitator superfamily (mfs). DR EnsemblBacteria; AAC22076; AAC22076; HI_0418. DR GeneID; 950811; -. DR KEGG; hin:HI0418; -. DR PATRIC; 20189389; VBIHaeInf48452_0438. DR eggNOG; ENOG4105CSH; Bacteria. DR eggNOG; ENOG410XP7I; LUCA. DR OMA; THFKPFF; -. DR OrthoDB; EOG6SZ1HS; -. DR PhylomeDB; P44699; -. DR Proteomes; UP000000579; 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:0022857; F:transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR004736; Cit_H_symport. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport_like. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF00083; Sugar_tr; 2. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00883; 2A0106; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 447 Putative metabolite transport protein FT HI_0418. FT /FTId=PRO_0000050489. FT TOPO_DOM 1 28 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 29 49 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 50 63 Periplasmic. {ECO:0000255}. FT TRANSMEM 64 84 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 85 96 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 97 117 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 118 119 Periplasmic. {ECO:0000255}. FT TRANSMEM 120 140 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 141 167 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 168 188 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 189 194 Periplasmic. {ECO:0000255}. FT TRANSMEM 195 215 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 216 249 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 250 270 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 271 295 Periplasmic. {ECO:0000255}. FT TRANSMEM 296 316 Helical; Name=8. {ECO:0000255}. FT TOPO_DOM 317 325 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 326 346 Helical; Name=9. {ECO:0000255}. FT TOPO_DOM 347 354 Periplasmic. {ECO:0000255}. FT TRANSMEM 355 375 Helical; Name=10. {ECO:0000255}. FT TOPO_DOM 376 390 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 391 411 Helical; Name=11. {ECO:0000255}. FT TOPO_DOM 412 418 Periplasmic. {ECO:0000255}. FT TRANSMEM 419 439 Helical; Name=12. {ECO:0000255}. FT TOPO_DOM 440 447 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 447 AA; 48229 MW; EE9780E9060110CC CRC64; MCKPQQKHYG RQVMNTQNSL KQVATATMVG TAIEYFDNYI YAMAAVLVFN HQFFHAVDPL SGQIAALSTL ALTFIARPLG AILFGHFGDR FGRKNTFVMS LLLMGISTVV IGLLPTYDSI GIWATILLCL CRIGQGIGLG GEWGGAALVA VENAPEGKRG WYGTFPQLGA PLGLLLANGV FLGITAIFGQ EAMTEWAWRI PFLSSVILVA IGLYVRLKLT EAPIFLAALN KPKPKRLPML EVVTTHFKPF FLGMLVCIAG YVLFYIMIAF SQIYAKSAPT VSEAGYAMGL GFSPQIFTAL LMASAVSLAI TIAASGKYID KIGRRTWLIW TTVGVAIFGL SLPLFLENGT TTSLFWFLFI GMGLIGMGYG PLASFLPELF PTHARYSGAS LTYNIAGLFG ASVAAIIALP LNAHYGLKGV GIYLTLNAVL SLVGLWFISE TKDKLLS // ID Y449_HAEIN Reviewed; 178 AA. AC P43997; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_0449; DE Flags: Precursor; GN OrderedLocusNames=HI_0449; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22120.1; -; Genomic_DNA. DR PIR; F64007; F64007. DR RefSeq; NP_438610.1; NC_000907.1. DR RefSeq; WP_005691374.1; NC_000907.1. DR STRING; 71421.HI0449; -. DR EnsemblBacteria; AAC22120; AAC22120; HI_0449. DR GeneID; 949746; -. DR KEGG; hin:HI0449; -. DR PATRIC; 20189453; VBIHaeInf48452_0469. DR OMA; HAYYSGV; -. DR OrthoDB; EOG6X6RDB; -. DR Proteomes; UP000000579; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 24 178 Uncharacterized protein HI_0449. FT /FTId=PRO_0000013958. SQ SEQUENCE 178 AA; 19919 MW; 97E5964E2FAF485F CRC64; MTMFKKISVL FFTLILAGCS SWSSVTNYIP FMGNDKKVID LDKDKIDQKS YAAAYEATVA TYKGRVNENF FVDNFASGAN DWYLGRILVP VKQIQDKLYT GGHDSDVYAY YSGVLHAEAL QANLKRLSAN CWEKVDSQSM AQGIYDAMRD LQKGEARGEN DEYIVQGSEA LLKACTSK // ID Y454_HAEIN Reviewed; 260 AA. AC P44718; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Uncharacterized metal-dependent hydrolase HI_0454 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=HI_0454; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22112.1; -; Genomic_DNA. DR PIR; I64152; I64152. DR RefSeq; NP_438615.1; NC_000907.1. DR RefSeq; WP_010868988.1; NC_000907.1. DR ProteinModelPortal; P44718; -. DR STRING; 71421.HI0454; -. DR EnsemblBacteria; AAC22112; AAC22112; HI_0454. DR GeneID; 949545; -. DR KEGG; hin:HI0454; -. DR PATRIC; 20189463; VBIHaeInf48452_0474. DR eggNOG; ENOG4105F8V; Bacteria. DR eggNOG; COG0084; LUCA. DR KO; K03424; -. DR OMA; RAGGVFH; -. DR OrthoDB; EOG66QM1C; -. DR PhylomeDB; P44718; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004536; F:deoxyribonuclease activity; IBA:GO_Central. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central. 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; PS01090; TATD_2; 1. DR PROSITE; PS01091; TATD_3; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome. FT CHAIN 1 260 Uncharacterized metal-dependent hydrolase FT HI_0454. FT /FTId=PRO_0000201998. 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 95 95 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 95 95 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 131 131 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 156 156 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 206 206 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 260 AA; 29419 MW; 3A0F9966442AB56E CRC64; MFIVDSHCHL DALDYENLHK NISDVVEKAH ARDVKHLLAI GVTLSRFEQA YDSLREFNNV SLACGVHPLD FEEEPYDAER LLRLAQDPKV IAIGEIGLDY YYSADNKAAQ QAVFGSQIDI ANQLDKPVII HTRSAGDDTI AMLRQHRAEK CGGVIHCFTE TMEFXKKALD LGFYISCSGI VTFKNAEAIR EVIRYVPMER LLVETDSPYL APVPYRGKEN QPAYTREVCE YVATLKGVSA EAFAQITTQN FERLFKIRVE // ID Y461_HAEIN Reviewed; 291 AA. AC Q57144; O05022; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein HI_0461; GN OrderedLocusNames=HI_0461; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22119.1; -; Genomic_DNA. DR PIR; I64069; I64069. DR RefSeq; NP_438622.1; NC_000907.1. DR RefSeq; WP_005693704.1; NC_000907.1. DR STRING; 71421.HI0461; -. DR EnsemblBacteria; AAC22119; AAC22119; HI_0461. DR GeneID; 949548; -. DR KEGG; hin:HI0461; -. DR PATRIC; 20189477; VBIHaeInf48452_0481. DR eggNOG; ENOG4108MJ5; Bacteria. DR eggNOG; COG2990; LUCA. DR KO; K09824; -. DR OMA; PLHIERK; -. DR OrthoDB; EOG6TBHCV; -. DR PhylomeDB; Q57144; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007488; DUF535. DR Pfam; PF04393; DUF535; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 291 Uncharacterized protein HI_0461. FT /FTId=PRO_0000077925. SQ SEQUENCE 291 AA; 34846 MW; 699FDC4204A2E2A0 CRC64; MSTKNHFIFP TYVQMYPYSK DRPFLKQVRE KLRYYGYKWL YQKQCSQLVD FLNTETQWQS LFTQDYYRTN TILTTFCDKR FSASERLTAI TENLRLAEEK MGRSLCQQLL DQQHIVLTQL TEDLRLSLSI NHIDPFEGYF SINIRNQNNE RVYDSSFTFL SPNKLLIASI QGPSSDNAQE LVKQATKALH GMRPMFMLVN GFKMLAEKWQ CELVGIPHKA QGKYRLSARS KILFNYDEFW QENQGEYRHN YWQLPLHIER KQLEDIASKK RSMYRKRYEM LDQMALDIQQ L // ID Y1246_HAEIN Reviewed; 647 AA. AC P44135; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 97. DE RecName: Full=Uncharacterized protein HI_1246; GN OrderedLocusNames=HI_1246; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22900.1; -; Genomic_DNA. DR PIR; I64022; I64022. DR RefSeq; NP_439402.1; NC_000907.1. DR RefSeq; WP_005694307.1; NC_000907.1. DR ProteinModelPortal; P44135; -. DR STRING; 71421.HI1246; -. DR EnsemblBacteria; AAC22900; AAC22900; HI_1246. DR GeneID; 950184; -. DR KEGG; hin:HI1246; -. DR PATRIC; 20191171; VBIHaeInf48452_1298. DR eggNOG; ENOG4105E0M; Bacteria. DR eggNOG; COG1368; LUCA. DR OMA; FIETYDY; -. DR OrthoDB; EOG6SR8X1; -. DR PhylomeDB; P44135; -. DR Proteomes; UP000000579; 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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR012160; ltaS-like. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF00884; Sulfatase; 1. DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 647 Uncharacterized protein HI_1246. FT /FTId=PRO_0000078013. FT TRANSMEM 14 38 Helical. {ECO:0000255}. FT TRANSMEM 61 78 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 140 158 Helical. {ECO:0000255}. FT TRANSMEM 178 195 Helical. {ECO:0000255}. SQ SEQUENCE 647 AA; 72752 MW; 87A0469DDDD3896F CRC64; MLVVFTMKKA HSPLFPIFTF VLINLIILSL SRLGLAVWQS ERVSAVDGWL QLFLQGVRMD VVALCYLFGV PALLTTLFHS SKVWVKILRL WLTFGSVFII FMEIATPAFI ETYDYRPNRL FIEYLIYPKE VFSMLAEGHL SAVIFSLVFT ILAAVIYWKI SGWAVKNLRS MSWKLRPVIA LLVIVVSFLG ARSSFQHRGI NPAMVAFSSD ALVNSLVLNS GYSVIYAAQQ FKDEEKSSEM YGKMDADEMF RIVKASRGRP ESDYISDKYP TLTKNVATYQ GKPKNIVILL QESLGAQFIG TLGGKPLSPN VDQLAKEGWL FENLYATGTR SVRGIEATTA GFTPTPARAV VKLNNAQSGF FTIADLLHKQ GYNTSFIYGG EKHFDNMASF FYGNGFKDIW DQQDYQNPKF TGTWGVSDED LFDKANETFT KLQNEGKPFF SLVFSSSNHD PFEYPDGKIE LYEQPKATRN NAAKYADYAL GHFFKMAKQS NYWKDTIFLI IADHDSRVGG ASLVPIKHFH IPALILGDGI TPRRDSRLVS QIDMPTTLLS LAGVSGNYPM IGFDLTQDVN PDRAFMQYDQ TQAMMKGNND VVIQMPNKAA QGYHYDKSTE TLTPKDVPDA MKKEALAHAL LGSYLYKNRL YSSGENK // ID Y1269_HAEIN Reviewed; 38 AA. AC P44148; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 56. DE RecName: Full=Uncharacterized protein HI_1269; GN OrderedLocusNames=HI_1269; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22930.1; -; Genomic_DNA. DR PIR; D64024; D64024. DR STRING; 71421.HI1269; -. DR EnsemblBacteria; AAC22930; AAC22930; HI_1269. DR PATRIC; 20191219; VBIHaeInf48452_1321. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 38 Uncharacterized protein HI_1269. FT /FTId=PRO_0000078019. SQ SEQUENCE 38 AA; 4562 MW; DFF1140F18742BDF CRC64; MLNGKANADF VPEMQRFYKL FYHIDLTNEQ ALKLFQVK // ID Y1272_HAEIN Reviewed; 263 AA. AC Q57243; O05049; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1272; GN OrderedLocusNames=HI_1272; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22920.1; -; Genomic_DNA. DR PIR; F64113; F64113. DR RefSeq; NP_439425.1; NC_000907.1. DR RefSeq; WP_005694513.1; NC_000907.1. DR ProteinModelPortal; Q57243; -. DR STRING; 71421.HI1272; -. DR EnsemblBacteria; AAC22920; AAC22920; HI_1272. DR GeneID; 950689; -. DR KEGG; hin:HI1272; -. DR PATRIC; 20191223; VBIHaeInf48452_1323. DR eggNOG; ENOG4105E0A; Bacteria. DR eggNOG; COG1120; LUCA. DR KO; K02013; -. DR OMA; NQEKNLT; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; Q57243; -. DR Proteomes; UP000000579; 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 1 263 Uncharacterized ABC transporter ATP- FT binding protein HI_1272. FT /FTId=PRO_0000093205. FT DOMAIN 12 247 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 44 51 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 263 AA; 29583 MW; 1D86403EDABAEA12 CRC64; MVISARAKIM LLETQNLAIG YEGKTLVQHI QFTLEENQIC CLLGANGAGK STFLKTLLGL QPPIGGDIVW QGKSLSDYSP TELARHIAYV PQAHSHLFPF LVQDMVMMGR SAFLKWYQTP KKSDLDLALM ALQELEIAHL AQRYYHQLSG GEKQLVLIAR AIAQQAKLLI MDEPTSSLDF GNQIRVLEKI KQLQKQNIAL IISTHNPQQA AFLGDNIVLL DQQFGFQQGD KKHLLTLENL AKIYRTSPEL LHQHLNNHIE KSL // ID Y1309_HAEIN Reviewed; 82 AA. AC P45154; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized ferredoxin-like protein HI_1309; GN OrderedLocusNames=HI_1309; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000305}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305}; CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22956.1; -; Genomic_DNA. DR PIR; G64170; G64170. DR RefSeq; NP_439460.1; NC_000907.1. DR RefSeq; WP_005650353.1; NC_000907.1. DR ProteinModelPortal; P45154; -. DR STRING; 71421.HI1309; -. DR EnsemblBacteria; AAC22956; AAC22956; HI_1309. DR GeneID; 950234; -. DR KEGG; hin:HI1309; -. DR PATRIC; 20191301; VBIHaeInf48452_1361. DR eggNOG; ENOG4105XPH; Bacteria. DR eggNOG; COG0633; LUCA. DR KO; K11107; -. DR OMA; YCGSCRC; -. DR OrthoDB; EOG6BPDNN; -. DR PhylomeDB; P45154; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR012675; Beta-grasp_dom. DR Pfam; PF00111; Fer2; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Transport. FT CHAIN 1 82 Uncharacterized ferredoxin-like protein FT HI_1309. FT /FTId=PRO_0000189418. FT DOMAIN 1 82 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 35 35 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 40 40 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 43 43 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT METAL 72 72 Iron-sulfur (2Fe-2S). FT {ECO:0000255|PROSITE-ProRule:PRU00465}. SQ SEQUENCE 82 AA; 9588 MW; A9E68733F01BDB36 CRC64; MKIHLIRHNT TLEFNNETSL LDHLEKNNIH HEYQCRSGYC GSCRVKIKKG KVSYKEMPLA FIQPDEILLC CCHVESDIEI DL // ID Y1310_HAEIN Reviewed; 253 AA. AC P44158; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_1310; GN OrderedLocusNames=HI_1310; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22961.1; -; Genomic_DNA. DR PIR; E64025; E64025. DR RefSeq; NP_439461.1; NC_000907.1. DR RefSeq; WP_005694458.1; NC_000907.1. DR STRING; 71421.HI1310; -. DR EnsemblBacteria; AAC22961; AAC22961; HI_1310. DR GeneID; 949509; -. DR KEGG; hin:HI1310; -. DR PATRIC; 20191303; VBIHaeInf48452_1362. DR eggNOG; ENOG4106HX4; Bacteria. DR eggNOG; ENOG410Y8T4; LUCA. DR OMA; KMLGFIT; -. DR OrthoDB; EOG651ST4; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 253 Uncharacterized protein HI_1310. FT /FTId=PRO_0000078023. SQ SEQUENCE 253 AA; 29371 MW; B70DB899F34B663B CRC64; MLLYKEKMKL LIKTSLSQWI CLNFAKIPIF KMLGFITALF ITACSSISKE PVKTVDIYIK PYYSAENGKA ENVFVHKEID PMLRENTIKG YKSAVKFVEE NPARISPMTM FTLAARAYDF GLRDEAVTWF YRGQNRLITA LYVLDLPKQT VQDNTGFSHV VGQFVNAYAF CNFDKQSLAA ENAMKWTVAH PYEVVFLPAL PAKFADRQKA LKEAEEKLVQ RLQEQARFFA NPKNKEKWQK ERSENFVNER FCW // ID Y1333_HAEIN Reviewed; 99 AA. AC P71376; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 09-DEC-2015, entry version 101. DE RecName: Full=RNA-binding protein HI_1333; GN OrderedLocusNames=HI_1333; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 2-99. RX PubMed=12360533; DOI=10.1002/prot.10225; RA Willis M.A., Krajewski W., Chalamasetty V.R., Reddy P., Howard A., RA Herzberg O.; RT "Structure of HI1333 (YhbY), a putative RNA-binding protein from RT Haemophilus influenzae."; RL Proteins 49:423-426(2002). CC -!- SIMILARITY: Contains 1 CRM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00626}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22977.1; -; Genomic_DNA. DR RefSeq; NP_439484.1; NC_000907.1. DR RefSeq; WP_005650404.1; NC_000907.1. DR PDB; 1JO0; X-ray; 1.37 A; A/B=2-99. DR PDBsum; 1JO0; -. DR ProteinModelPortal; P71376; -. DR SMR; P71376; 2-98. DR STRING; 71421.HI1333; -. DR EnsemblBacteria; AAC22977; AAC22977; HI_1333. DR GeneID; 949671; -. DR KEGG; hin:HI1333; -. DR PATRIC; 20191349; VBIHaeInf48452_1385. DR eggNOG; ENOG4105HBR; Bacteria. DR eggNOG; COG1534; LUCA. DR KO; K07574; -. DR OMA; LSPIFQV; -. DR OrthoDB; EOG6SBT94; -. DR PhylomeDB; P71376; -. DR EvolutionaryTrace; P71376; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.110.60; -; 1. DR InterPro; IPR001890; RNA-binding_CRM. DR InterPro; IPR017924; RNA-binding_YhbY. DR Pfam; PF01985; CRS1_YhbY; 1. DR ProDom; PD010559; RNA-binding_CRM; 1. DR SMART; SM01103; CRS1_YhbY; 1. DR SUPFAM; SSF75471; SSF75471; 1. DR TIGRFAMs; TIGR00253; RNA_bind_YhbY; 1. DR PROSITE; PS51295; CRM; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 99 RNA-binding protein HI_1333. FT /FTId=PRO_0000202167. FT DOMAIN 2 98 CRM. {ECO:0000255|PROSITE- FT ProRule:PRU00626}. FT HELIX 6 16 {ECO:0000244|PDB:1JO0}. FT STRAND 22 25 {ECO:0000244|PDB:1JO0}. FT HELIX 32 45 {ECO:0000244|PDB:1JO0}. FT STRAND 46 52 {ECO:0000244|PDB:1JO0}. FT HELIX 57 71 {ECO:0000244|PDB:1JO0}. FT STRAND 74 79 {ECO:0000244|PDB:1JO0}. FT STRAND 82 86 {ECO:0000244|PDB:1JO0}. SQ SEQUENCE 99 AA; 10924 MW; 83F4FEE15E126AE5 CRC64; MTTLSTKQKQ FLKGLAHHLN PVVMLGGNGL TEGVLAEIEN ALNHHELIKV KVAGADRETK QLIINAIVRE TKAAQVQTIG HILVLYRPSE EAKIQLPRK // ID Y1364_HAEIN Reviewed; 288 AA. AC P43011; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 96. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_1364; DE AltName: Full=ORF2; GN OrderedLocusNames=HI_1364; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6; RA Chandler M.S., Smith R.A.; RT "Characterization of the Haemophilus influenzae topA locus: DNA RT topoisomerase I is required for genetic competence."; RL Gene 169:25-31(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20964; AAC43726.1; -; Genomic_DNA. DR EMBL; L42023; AAC23011.1; -; Genomic_DNA. DR PIR; D64171; D64171. DR RefSeq; NP_439515.1; NC_000907.1. DR RefSeq; WP_010869193.1; NC_000907.1. DR ProteinModelPortal; P43011; -. DR STRING; 71421.HI1364; -. DR EnsemblBacteria; AAC23011; AAC23011; HI_1364. DR GeneID; 950273; -. DR KEGG; hin:HI1364; -. DR PATRIC; 20191415; VBIHaeInf48452_1418. DR eggNOG; ENOG4105CC0; Bacteria. DR eggNOG; ENOG410XQWS; LUCA. DR OMA; AISIFCK; -. DR OrthoDB; EOG6Q8J00; -. DR PhylomeDB; P43011; -. DR BioCyc; RETL1328306-WGS:GSTH-3703-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-816-MONOMER; -. DR Proteomes; UP000000579; 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; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 288 Uncharacterized HTH-type transcriptional FT regulator HI_1364. FT /FTId=PRO_0000105798. FT DOMAIN 1 59 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 19 38 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT CONFLICT 281 288 VTGISLNF -> RAFIEFLSGLGLCSEIWENHEDNI (in FT Ref. 1). {ECO:0000305}. SQ SEQUENCE 288 AA; 32423 MW; EEF3C22374352980 CRC64; MDKLNAISIF CKVIETQSFT LAAKQQNISV AMASKLVSQL EEHLKTRLLQ RTTRKIMPTE AGMMYYQRCQ GILLDLDEAD SSITQLTSSL QGNLLISVPR DFGLLFIAPN LPTFMAKHPH LHIEVEFNDK KIDLLSEGYD LALRIGYMED SSLVSRKIGT TTVHFAASPN YLETNGIPQT PDDLEHHNGL LYKNAMNQVN WVGSRINQTQ RFKIQSKVVS NSGFALLNMA KAGLGIANLP KFILGRAFEK GELIEILPEY KQQKLEIHVV YPNRRHLPIK VTGISLNF // ID Y1375_HAEIN Reviewed; 302 AA. AC P44169; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein HI_1375; GN OrderedLocusNames=HI_1375; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23029.1; -; Genomic_DNA. DR PIR; H64026; H64026. DR RefSeq; NP_439527.1; NC_000907.1. DR RefSeq; WP_005693981.1; NC_000907.1. DR STRING; 71421.HI1375; -. DR DNASU; 950817; -. DR EnsemblBacteria; AAC23029; AAC23029; HI_1375. DR GeneID; 950817; -. DR KEGG; hin:HI1375; -. DR PATRIC; 20191439; VBIHaeInf48452_1430. DR eggNOG; ENOG4108HFV; Bacteria. DR eggNOG; COG3586; LUCA. DR OMA; KRNDVDW; -. DR OrthoDB; EOG64N9ZZ; -. DR PhylomeDB; P44169; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 302 Uncharacterized protein HI_1375. FT /FTId=PRO_0000078032. SQ SEQUENCE 302 AA; 35503 MW; 0EBD6ABE2B8B7E55 CRC64; MKIFTSKKGQ LSQLKQQKFK LEKDIQRLFE ENLTLLSGYI FIRSEFSIKN SRIDTLAFDP ETQAFVIIEY KRQQNSSVVD QGISYLNLML EYKADFIVEY NEKQKVPLKR NDVDWSQSKV IFVSPAFNDF QIQATNFKDL PIELWEVNRF DNDIITLNII NKSKSAPNIK AVSNEKREEF SILKEIKVYQ ESDHLADKTD FIQELYEDFK QGILNLDPDI EINTRKLYIA FKKDRNIADI RIQQKNLKIW INLPYGELDD PKNLAKNVSN TGHWGNGDYE ITIESTQYLE YIMSLIKQAI KD // ID Y1422_HAEIN Reviewed; 191 AA. AC P44193; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_1422; GN OrderedLocusNames=HI_1422; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23072.1; -; Genomic_DNA. DR PIR; E64029; E64029. DR RefSeq; NP_439571.1; NC_000907.1. DR RefSeq; WP_005693944.1; NC_000907.1. DR STRING; 71421.HI1422; -. DR DNASU; 949966; -. DR EnsemblBacteria; AAC23072; AAC23072; HI_1422. DR GeneID; 949966; -. DR KEGG; hin:HI1422; -. DR PATRIC; 20191539; VBIHaeInf48452_1480. DR eggNOG; ENOG4105XB7; Bacteria. DR eggNOG; COG3561; LUCA. DR KO; K07741; -. DR OrthoDB; EOG6GJBRQ; -. DR PhylomeDB; P44193; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR013557; AntA/B_antirep. DR InterPro; IPR018876; Phage_P22_antirepressor_C. DR Pfam; PF08346; AntA; 1. DR Pfam; PF10548; P22_AR_C; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 191 Uncharacterized protein HI_1422. FT /FTId=PRO_0000078057. SQ SEQUENCE 191 AA; 22701 MW; D1F632E60066E785 CRC64; MTHLNLIPVF NGLIQNQPVQ LCNARELHAF VESKQQYTDW IKNRINEYGF IQDEDYLVIT ERTNGRPRKE YHITLDMGKE LGMVERNERG RQIRQYFIRC ERTLKALQQP QQLALPEPEK FTHEFTEFEI ETLVWLLIGH HQMNTLLGQL EKPLDAIGSN LHPAVYSYWK EYGRQYKDAL PTIKRLMAPF K // ID Y1467_HAEIN Reviewed; 589 AA. AC P45221; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1467; GN OrderedLocusNames=HI_1467; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC23116.1; -; Genomic_DNA. DR PIR; D64125; D64125. DR RefSeq; NP_439618.1; NC_000907.1. DR RefSeq; WP_005693484.1; NC_000907.1. DR ProteinModelPortal; P45221; -. DR STRING; 71421.HI1467; -. DR EnsemblBacteria; AAC23116; AAC23116; HI_1467. DR GeneID; 950646; -. DR KEGG; hin:HI1467; -. DR PATRIC; 20191649; VBIHaeInf48452_1534. DR eggNOG; ENOG4105CQ0; Bacteria. DR eggNOG; COG4178; LUCA. DR OMA; FEIRWLE; -. DR OrthoDB; EOG61KBCN; -. DR PhylomeDB; P45221; -. DR Proteomes; UP000000579; 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; PF06472; ABC_membrane_2; 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 inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 589 Uncharacterized ABC transporter ATP- FT binding protein HI_1467. FT /FTId=PRO_0000093206. FT TRANSMEM 11 31 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 57 77 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 97 117 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 190 210 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 213 233 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 57 357 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 390 587 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 423 430 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 589 AA; 68306 MW; B3E409EEB193E7F1 CRC64; MNWQTELNNS LNWILTALFW VVLCFSVTML ALKQTTFGKK FWCIVSPSMD KKTSIKLILM LLVLFIMILL EVRFSVLNSF FYNGLYSSMQ ELNIEKFWFF AKLNALLVVA QVIHAIADYF FQQVFEIRWL ESFNATLVKR WLNKKKYYRL KYERDLPDNI DQRIEQDARE FITSTVQIVR GVINSVLTTI EFTIILWSLS GVLTLFGFNI EKGVVFFIYA FIIFATLMSV WIGRPLIKLN FTKEKLNGDY RYSLIRVRDN AESIAFYNGE PKEQTFLQHQ FRQIIHNRWS IVLKMLGLNS FNSGVTRVAK LLPLMLQAPR FFSGQIKLGD MHQTVQAFNR LMTALSFFRL FYEQFTLYQA RLNRLYGFIT KMDELDKQNV HHPFHCSHRV ALKNFGIKDE QGHVLLNNLN INLENGDALL IQGASGTGKT SLLKAIAGIY PFETIGIAEH PCMGSLFLPQ RPYMPQGTLR EAICYPNINP SHAELEQTMK DCALGKYIHA LNVKNDWQAI LSPGELQRVA FIRILLTKPD VVFLDETTSA LDETTENLLY QTIKERLPEM IILSVGHRST LQQFHNKQLK LDVCLLCEN // ID Y149_HAEIN Reviewed; 63 AA. AC P43953; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_0149; DE Flags: Precursor; GN OrderedLocusNames=HI_0149; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21830.1; -; Genomic_DNA. DR PIR; G64002; G64002. DR STRING; 71421.HI0149; -. DR EnsemblBacteria; AAC21830; AAC21830; HI_0149. DR PATRIC; 20188791; VBIHaeInf48452_0152. DR eggNOG; COG2020; LUCA. DR OMA; SGIYQYS; -. DR OrthoDB; EOG689HZB; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 63 Uncharacterized protein HI_0149. FT /FTId=PRO_0000013952. SQ SEQUENCE 63 AA; 7693 MW; D2939DA4AEB9A606 CRC64; MYLSLLLILL AWTLWLGNSL AWLGVIIFIL VINQFQIARE ETYLESKFGD EYRRYKQKVR RWL // ID Y1524_HAEIN Reviewed; 50 AA. AC P44244; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 49. DE RecName: Full=Uncharacterized protein HI_1524; GN OrderedLocusNames=HI_1524; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23181.1; -; Genomic_DNA. DR PIR; B64035; B64035. DR EnsemblBacteria; AAC23181; AAC23181; HI_1524. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_1524. FT /FTId=PRO_0000078082. SQ SEQUENCE 50 AA; 5265 MW; 67B0B4D7EEB5DCAE CRC64; MIPTGEKIHL LIKGSSSANI PCELKSRSKL SPVTNGGKTI GKSNKVSKND // ID Y1556_HAEIN Reviewed; 315 AA. AC P45250; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=Putative 2-hydroxyacid dehydrogenase HI_1556; DE EC=1.-.-.-; GN OrderedLocusNames=HI_1556; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23205.1; -; Genomic_DNA. DR PIR; F64129; F64129. DR RefSeq; NP_439705.1; NC_000907.1. DR RefSeq; WP_005693583.1; NC_000907.1. DR ProteinModelPortal; P45250; -. DR STRING; 71421.HI1556; -. DR EnsemblBacteria; AAC23205; AAC23205; HI_1556. DR GeneID; 950416; -. DR KEGG; hin:HI1556; -. DR PATRIC; 20191837; VBIHaeInf48452_1627. DR eggNOG; ENOG4105C5I; Bacteria. DR eggNOG; COG1052; LUCA. DR KO; K00018; -. DR OMA; GHGELGK; -. DR OrthoDB; EOG6VXFC3; -. DR PhylomeDB; P45250; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 315 Putative 2-hydroxyacid dehydrogenase FT HI_1556. FT /FTId=PRO_0000076034. FT NP_BIND 156 157 NAD. {ECO:0000250}. FT NP_BIND 231 233 NAD. {ECO:0000250}. FT NP_BIND 285 288 NAD. {ECO:0000250}. FT ACT_SITE 233 233 {ECO:0000250}. FT ACT_SITE 262 262 {ECO:0000250}. FT ACT_SITE 285 285 Proton donor. {ECO:0000250}. FT BINDING 73 73 NAD. {ECO:0000250}. FT BINDING 257 257 NAD. {ECO:0000250}. SQ SEQUENCE 315 AA; 34636 MW; 0023D28C3266689B CRC64; MKIVFLDSTA IPKHISIPRP SFEHTWTEYE HTSAEQTIER VKDADIVITS KVIFDRETLQ QLPKLKLIAI TATGTNNVDL VAAEEMGIAV RNVTGYSSTT VPEHVIGLIF SLKHSLAGWL RDQTEAKWAE SKQFCYFDYP ITDVRGSTLG VFGKGCLGTE VGRLANAVGM KVLYAEHKDA TVCREGYTPF DEVLKQADIV TLHCPLTETT KDLINAETLS KMKKGAFLIN TGRGPLIDEL ALVDALKTGH LGGAALDVMV KEPPEKDNPL ILAAKTMPNL IITPHIAWAS DSAVTTLVGK VMQNIEEFVQ QLHQK // ID Y1586_HAEIN Reviewed; 519 AA. AC P44263; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 90. DE RecName: Full=Uncharacterized protein HI_1586; GN OrderedLocusNames=HI_1586; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23234.1; -; Genomic_DNA. DR PIR; C64037; C64037. DR RefSeq; NP_439731.1; NC_000907.1. DR RefSeq; WP_005693603.1; NC_000907.1. DR STRING; 71421.HI1586; -. DR EnsemblBacteria; AAC23234; AAC23234; HI_1586. DR GeneID; 950450; -. DR KEGG; hin:HI1586; -. DR PATRIC; 20191905; VBIHaeInf48452_1660. DR eggNOG; ENOG4107S6Z; Bacteria. DR eggNOG; COG1757; LUCA. DR OMA; LVPISSW; -. DR OrthoDB; EOG6CGC8T; -. DR PhylomeDB; P44263; -. DR Proteomes; UP000000579; 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; IPR018461; Na/H_Antiport_NhaC-like_C. DR Pfam; PF03553; Na_H_antiporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 519 Uncharacterized protein HI_1586. FT /FTId=PRO_0000078093. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 270 290 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 345 365 Helical. {ECO:0000255}. FT TRANSMEM 386 406 Helical. {ECO:0000255}. FT TRANSMEM 413 433 Helical. {ECO:0000255}. FT TRANSMEM 475 495 Helical. {ECO:0000255}. FT TRANSMEM 496 516 Helical. {ECO:0000255}. SQ SEQUENCE 519 AA; 55499 MW; 0EBF908C0454E4B1 CRC64; MLSVLSINYR YYLMELIDFS SSVWSIVPAL LAIILAIATR RVLVSLSAGI IIGSLMLSDW QIGSAFNYLV KNVVSLVYAD GEINSNMNIV LFLLLLGVLT ALLTVSGSNR AFAEWAQSRI KGRRGAKLLA ASLVFVTFID DYFHSLAVGA IARPVTDRFK VSRAKLAYIL DSTAAPMCVM MPVSSWGAYI ITLIGGLLAT YSITEYTPIG AFVAMSSMNF YAIFSIIMVF FVAYFSFDIA SMVRHEKLAL KNTEDQLEEE TGTKGQVRNL ILPILVLIIA TVSMMIYTGA EALAADGKVF SVLGTFENTV VGTSLVVGGF CSIIISTLLI ILDRQVSVPE YVRSWIVGIK SMSGAIAILF FAWTINKIVG DMQTGKYLSS LVSGNIPMQF LPVILFVLGA AMAFSTGTSW GTFGIMLPIA AAMAANAAPE LLLPCLSAVM AGAVCGDHCS PVSDTTILSS TGAKCNHIDH VTTQLPYAAT VATATSIGYI VVGFTYSGLA GFAATAVSLI VIIFAVKKR // ID Y1595_HAEIN Reviewed; 107 AA. AC P44266; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_1595; GN OrderedLocusNames=HI_1595; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23246.1; -; Genomic_DNA. DR PIR; F64037; F64037. DR EnsemblBacteria; AAC23246; AAC23246; HI_1595. DR Proteomes; UP000000579; 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; IPR025199; FtsK_4TM. DR Pfam; PF13491; FtsK_4TM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 107 Uncharacterized protein HI_1595. FT /FTId=PRO_0000078096. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. SQ SEQUENCE 107 AA; 12171 MW; DAE19ED0F6E4F344 CRC64; MIKQITERFT PRQYLAEFLL GLTALFGLYL IVAWSSYTPL DNSWATVSAY GNTINKVGSF GAWIIDLFFV FLGYVAHIIP FTAFLVPIYL LKTKAVKQLS CTRIILR // ID Y1602_HAEIN Reviewed; 151 AA. AC P44270; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Uncharacterized protein HI_1602; GN OrderedLocusNames=HI_1602; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DoxX 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; L42023; AAC23261.1; -; Genomic_DNA. DR PIR; A64038; A64038. DR RefSeq; NP_439744.2; NC_000907.1. DR STRING; 71421.HI1602; -. DR EnsemblBacteria; AAC23261; AAC23261; HI_1602. DR GeneID; 950457; -. DR KEGG; hin:HI1602; -. DR PATRIC; 20191935; VBIHaeInf48452_1675. DR eggNOG; ENOG4109045; Bacteria. DR eggNOG; COG2259; LUCA. DR KO; K15977; -. DR OMA; LSMWAEL; -. DR OrthoDB; EOG61GGB6; -. DR Proteomes; UP000000579; 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; IPR032808; DoxX. DR Pfam; PF07681; DoxX; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 151 Uncharacterized protein HI_1602. FT /FTId=PRO_0000078098. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 82 102 Helical. {ECO:0000255}. FT TRANSMEM 113 133 Helical. {ECO:0000255}. SQ SEQUENCE 151 AA; 17217 MW; AF2BC7B725C4BDD7 CRC64; MKDCKMQGIG SGVSLLILRF FLAWEFFESG LEKWNGQNWF AEIQDRFPFP FNLIPADINW HVAMGSELIF PFLLIFGVLT RFSALSLTIL ISVAWYSIHA DSGYNVCDNG YKLPLIYVVT LLILITQGAG KLSLDTLIKK VYPTKSWLKF L // ID Y1618_HAEIN Reviewed; 217 AA. AC P45275; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_1618; GN OrderedLocusNames=HI_1618; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23266.1; -; Genomic_DNA. DR PIR; A64133; A64133. DR RefSeq; NP_439760.2; NC_000907.1. DR ProteinModelPortal; P45275; -. DR STRING; 71421.HI1618; -. DR EnsemblBacteria; AAC23266; AAC23266; HI_1618. DR GeneID; 950842; -. DR KEGG; hin:HI1618; -. DR PATRIC; 20191971; VBIHaeInf48452_1693. DR eggNOG; ENOG4108JJB; Bacteria. DR eggNOG; COG1122; LUCA. DR KO; K02006; -. DR OMA; NQVACAY; -. DR OrthoDB; EOG6VXF80; -. DR Proteomes; UP000000579; 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 1 217 Uncharacterized ABC transporter ATP- FT binding protein HI_1618. FT /FTId=PRO_0000093209. FT DOMAIN 14 217 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 46 53 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 217 AA; 24079 MW; 8C0675189A65012B CRC64; MVFSSAKREK NNMLAVNNLC IERNGRAIIQ DLSFTLEGQK RLFVQGEIGS GKTTLLLALL GFVPVTKGEI KLFGKVCRKE KDFAPFRGTI GICFQNADDQ LFGPTVLDDI AFGPLNQNVP REQAYHIAEQ QLERLGITRL KDRMVHTLSG GEKNFTALAG VLAMQPKILL LDEPTNGLDR KNTEKLTALL RELSLPILIS SHHHGFINEL ATEIISL // ID Y1622_HAEIN Reviewed; 161 AA. AC P44275; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_1622; DE Flags: Precursor; GN OrderedLocusNames=HI_1622; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23271.1; -; Genomic_DNA. DR PIR; F64038; F64038. DR RefSeq; NP_439764.1; NC_000907.1. DR RefSeq; WP_005693634.1; NC_000907.1. DR STRING; 71421.HI1622; -. DR EnsemblBacteria; AAC23271; AAC23271; HI_1622. DR GeneID; 950474; -. DR KEGG; hin:HI1622; -. DR PATRIC; 20191979; VBIHaeInf48452_1697. DR eggNOG; ENOG4108A51; Bacteria. DR eggNOG; ENOG4111ZTC; LUCA. DR KO; K16915; -. DR OMA; AAETYVE; -. DR OrthoDB; EOG6JX7M1; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 23 Or 21. {ECO:0000255}. FT CHAIN 24 161 Uncharacterized protein HI_1622. FT /FTId=PRO_0000013975. FT TRANSMEM 129 149 Helical. {ECO:0000255}. SQ SEQUENCE 161 AA; 17520 MW; C9303AA13FF25D36 CRC64; MKKFAFLTAL FAACYLPNAY AHALYVFAQY DGQTLSGKSY YSDMTPAAET YLEVFRSGVS DPVLTGKTDR QGVFKLSIAD VPHTTLKVVV EGDEGHRASV VAAHTSAENQ SGADLMLLRE DIAHLKDKIY LHDILGGIGY IVGIAGLIAL RNARKIKQGR I // ID Y1650_HAEIN Reviewed; 36 AA. AC P44281; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-SEP-2015, entry version 59. DE RecName: Full=Uncharacterized protein HI_1650; GN OrderedLocusNames=HI_1650; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23303.1; -; Genomic_DNA. DR PIR; C64039; C64039. DR RefSeq; NP_439792.1; NC_000907.1. DR RefSeq; WP_005650114.1; NC_000907.1. DR EnsemblBacteria; AAC23303; AAC23303; HI_1650. DR GeneID; 950489; -. DR KEGG; hin:HI1650; -. DR PATRIC; 20192045; VBIHaeInf48452_1726. DR OrthoDB; EOG63Z7FM; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 36 Uncharacterized protein HI_1650. FT /FTId=PRO_0000078103. SQ SEQUENCE 36 AA; 4285 MW; 248010DAD7898E33 CRC64; MPNERNIQNY HSTYNNIRDW LGYQKAGEEK AKSTIN // ID Y1658_HAEIN Reviewed; 193 AA. AC P45301; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_1658; DE Flags: Precursor; GN OrderedLocusNames=HI_1658; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Contains 2 BON domains. {ECO:0000255|PROSITE- CC ProRule:PRU00229}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23302.1; -; Genomic_DNA. DR PIR; A64135; A64135. DR RefSeq; NP_439800.1; NC_000907.1. DR RefSeq; WP_005657657.1; NC_000907.1. DR STRING; 71421.HI1658; -. DR EnsemblBacteria; AAC23302; AAC23302; HI_1658. DR GeneID; 950803; -. DR KEGG; hin:HI1658; -. DR PATRIC; 20192065; VBIHaeInf48452_1736. DR eggNOG; ENOG4105W4M; Bacteria. DR eggNOG; COG2823; LUCA. DR OMA; MLQGCIG; -. DR OrthoDB; EOG6C5RQ0; -. DR PhylomeDB; P45301; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR InterPro; IPR007055; BON_dom. DR InterPro; IPR014004; Transpt-assoc_nodulatn_dom_bac. DR Pfam; PF04972; BON; 2. DR SMART; SM00749; BON; 2. DR PROSITE; PS50914; BON; 2. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Periplasm; Reference proteome; Repeat; Signal. FT SIGNAL 1 33 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 34 193 Uncharacterized protein HI_1658. FT /FTId=PRO_0000013912. FT DOMAIN 48 117 BON 1. {ECO:0000255|PROSITE- FT ProRule:PRU00229}. FT DOMAIN 126 193 BON 2. {ECO:0000255|PROSITE- FT ProRule:PRU00229}. SQ SEQUENCE 193 AA; 20414 MW; EE16B6AAA5870D1E CRC64; MTLSPLKKLA ILLGATIFLQ GCVAAVIGGG AVAAKVATDP RTTGTQIDDE TLEFKVENAV EKDAQIKAEG RVNAVSYNGR VLLIGQVPNS DVKDTATALA KGVEGVNEVY NELTVSPKIS FAQISKDSWL TTQVKSKMFV DGRVKATDVK VISENGEVFL LGNVTQSQAN AAADIASKIS GVKKVIKVFK YLD // ID Y1665_HAEIN Reviewed; 40 AA. AC P44283; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_1665; GN OrderedLocusNames=HI_1665; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23313.1; -; Genomic_DNA. DR PIR; E64039; E64039. DR ProteinModelPortal; P44283; -. DR STRING; 71421.HI1665; -. DR DNASU; 950493; -. DR EnsemblBacteria; AAC23313; AAC23313; HI_1665. DR PATRIC; 20192079; VBIHaeInf48452_1743. DR eggNOG; COG3108; LUCA. DR OrthoDB; EOG6D5G60; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.1380.10; -; 1. DR InterPro; IPR010275; DUF882. DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_dom. DR Pfam; PF05951; Peptidase_M15_2; 1. DR SUPFAM; SSF55166; SSF55166; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 40 Uncharacterized protein HI_1665. FT /FTId=PRO_0000078105. SQ SEQUENCE 40 AA; 4363 MW; 888B1D57563429A5 CRC64; MPLIKVKSSA ESLRNGGVGY YPTSNFIHVD TGPVRTWKGV // ID Y1720_HAEIN Reviewed; 188 AA. AC Q57066; O05085; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_1720; GN OrderedLocusNames=HI_1720; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the IS150/IS1296 orfA 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; L42023; AAC23366.1; -; Genomic_DNA. DR PIR; D64176; D64176. DR RefSeq; NP_439861.2; NC_000907.1. DR ProteinModelPortal; Q57066; -. DR STRING; 71421.HI1720; -. DR EnsemblBacteria; AAC23366; AAC23366; HI_1720. DR GeneID; 950873; -. DR KEGG; hin:HI1720; -. DR PATRIC; 20192193; VBIHaeInf48452_1799. DR eggNOG; ENOG4105IYK; Bacteria. DR eggNOG; COG2963; LUCA. DR KO; K07483; -. DR OMA; NSKCTRY; -. DR OrthoDB; EOG6QRW8Q; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR SUPFAM; SSF46689; SSF46689; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 188 Uncharacterized protein HI_1720. FT /FTId=PRO_0000078110. SQ SEQUENCE 188 AA; 21747 MW; 3005CF9D44135F27 CRC64; MICTPKVGLN NQLTKVQFFM TKYNFLFKQQ VIEFYLQNDK NSSLTRRHFQ LAETTLERWI NQFNHSGING LALLGKKRNY SPEFKLNVIQ AVKNGKFSAE AACLHFGIAN SGVVSQWLQA FEKQGINGLI PKPKGRPTMK LQYPKMPPKP KTREEELELE NLRLRAENAI LKKLQELNQQ KMQKKPLS // ID Y1729_HAEIN Reviewed; 245 AA. AC P45347; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 04-AUG-2003, sequence version 2. DT 09-DEC-2015, entry version 82. DE RecName: Full=UPF0271 protein HI_1729; GN OrderedLocusNames=HI_1729; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0271 (lamB) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23375.1; 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; L42023; AAC23375.1; ALT_INIT; Genomic_DNA. DR PIR; H64138; H64138. DR RefSeq; NP_439870.1; NC_000907.1. DR RefSeq; WP_010869282.1; NC_000907.1. DR ProteinModelPortal; P45347; -. DR STRING; 71421.HI1729m; -. DR EnsemblBacteria; AAC23375; AAC23375; HI_1729. DR GeneID; 950524; -. DR KEGG; hin:HI1729m; -. DR PATRIC; 20192211; VBIHaeInf48452_1808. DR eggNOG; ENOG4105E7W; Bacteria. DR eggNOG; COG1540; LUCA. DR KO; K07160; -. DR OMA; AQVGYRD; -. DR OrthoDB; EOG6CZQJG; -. DR PhylomeDB; P45347; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR HAMAP; MF_00691; UPF0271; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR005501; UPF0271_LamB_YcsF. DR Pfam; PF03746; LamB_YcsF; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 245 UPF0271 protein HI_1729. FT /FTId=PRO_0000185014. SQ SEQUENCE 245 AA; 26822 MW; 09B5A2D90ADE0A54 CRC64; MKKIDLNADI AEGFPFDESL LQLLSSANVA CGLHAGGAKE MQSAVKFAKE NKVRIGAHPS FPDRENFGRT AMALSSQELI AHLRYQLGAL KAICDGEGAV ISYVKPHGAL YNQAAKDEKI ARLIAQTVYQ FDPNLKLMGL AGSLMLRIAE EEKLQTISEV FADRHYMPDG SLVPRSQPNA MVESDKEAIQ QVLQMVTKGQ VNAIDGSLVP VKAESICLHG DNQHSLQFAK RIVEELEKNH IKITA // ID Y173_HAEIN Reviewed; 86 AA. AC P43960; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein HI_0173; GN OrderedLocusNames=HI_0173; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21846.1; -; Genomic_DNA. DR PIR; E64003; E64003. DR RefSeq; NP_438341.1; NC_000907.1. DR RefSeq; WP_010868951.1; NC_000907.1. DR STRING; 71421.HI0173; -. DR EnsemblBacteria; AAC21846; AAC21846; HI_0173. DR GeneID; 951082; -. DR KEGG; hin:HI0173; -. DR PATRIC; 20188841; VBIHaeInf48452_0177. DR eggNOG; COG2991; LUCA. DR KO; K05952; -. DR OMA; IEKECDC; -. DR OrthoDB; EOG693GV2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007495; NqrM. DR Pfam; PF04400; DUF539; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 86 Uncharacterized protein HI_0173. FT /FTId=PRO_0000077895. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 86 AA; 9494 MW; B8E2888E892C10E9 CRC64; MQTLFFTLIA FVAIILLMSI GFIIKKQSLK GSCGGLSTLG IAKACDCDKP CDTHHSKLDA GDEQAKAEYE QKFAKKDDDS QFYQVK // ID Y219_HAEIN Reviewed; 213 AA. AC P44577; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_0219; GN OrderedLocusNames=HI_0219; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21887.1; -; Genomic_DNA. DR PIR; E64145; E64145. DR RefSeq; NP_438387.2; NC_000907.1. DR STRING; 71421.HI0219; -. DR EnsemblBacteria; AAC21887; AAC21887; HI_0219. DR GeneID; 951126; -. DR KEGG; hin:HI0219; -. DR PATRIC; 20188943; VBIHaeInf48452_0228. DR eggNOG; ENOG4108KBJ; Bacteria. DR eggNOG; COG3059; LUCA. DR OMA; TTPEVYV; -. DR OrthoDB; EOG6DG2XJ; -. DR Proteomes; UP000000579; 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; IPR007339; DUF417. DR Pfam; PF04224; DUF417; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 213 Uncharacterized protein HI_0219. FT /FTId=PRO_0000168567. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. SQ SEQUENCE 213 AA; 23338 MW; 6D3314505A4F727E CRC64; MEIYMSVFNT FVEFVARIVA PMQRQFINFI RIAIFIVMAW IGGLKVCQYE ADGIAHFVSN SPFFSYMYEK GPNLVPNDKG ELVMEYTLHK NPEGKMVAKN IEWHKENGTY TASYIIGAII VTVGILTLAG IWNATAGLAG GLLTFGMSIV TLSFLITTPE AWVPNLGGDL PTPAYGFPYL SGVGRLVIKD IIMMAGGLTA AAECANRILA RKK // ID Y233_HAEIN Reviewed; 50 AA. AC P43967; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 51. DE RecName: Full=Uncharacterized protein HI_0233; GN OrderedLocusNames=HI_0233; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21903.1; -; Genomic_DNA. DR PIR; C64004; C64004. DR EnsemblBacteria; AAC21903; AAC21903; HI_0233. DR OMA; VIQEICC; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_0233. FT /FTId=PRO_0000077900. SQ SEQUENCE 50 AA; 6140 MW; 38255FC9AE4BEA7C CRC64; MLKRKTFLKK KANLQQSSLS RNLRLRRLKH RKQQQFSRHS LQFVVQEICC // ID Y234_HAEIN Reviewed; 48 AA. AC P43968; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein HI_0234; GN OrderedLocusNames=HI_0234; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21904.1; -; Genomic_DNA. DR PIR; D64004; D64004. DR STRING; 71421.HI0234; -. DR EnsemblBacteria; AAC21904; AAC21904; HI_0234. DR PATRIC; 20188991; VBIHaeInf48452_0248. DR OrthoDB; EOG6GR3CQ; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 48 Uncharacterized protein HI_0234. FT /FTId=PRO_0000077901. SQ SEQUENCE 48 AA; 5499 MW; 69FEFA8808801F5E CRC64; MRKVEDQIKI QRSFTELNEL FKFLGDYFDP VSIGLVGVKI GNLGIKLE // ID Y243_HAEIN Reviewed; 172 AA. AC P43971; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein HI_0243; GN OrderedLocusNames=HI_0243; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21913.1; -; Genomic_DNA. DR PIR; G64004; G64004. DR RefSeq; NP_438413.1; NC_000907.1. DR RefSeq; WP_005648824.1; NC_000907.1. DR ProteinModelPortal; P43971; -. DR SMR; P43971; 10-169. DR STRING; 71421.HI0243; -. DR EnsemblBacteria; AAC21913; AAC21913; HI_0243. DR GeneID; 949380; -. DR KEGG; hin:HI0243; -. DR PATRIC; 20189011; VBIHaeInf48452_0258. DR eggNOG; ENOG4105NSG; Bacteria. DR eggNOG; ENOG4111WZE; LUCA. DR OMA; NQAVKND; -. DR OrthoDB; EOG6B09V1; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF01814; Hemerythrin; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 172 Uncharacterized protein HI_0243. FT /FTId=PRO_0000077902. SQ SEQUENCE 172 AA; 20408 MW; 3D3483945C03BD1A CRC64; MQILEPQQFA TWNEPIEMLY ACHSKVKRFC RQLSILPDYL EKHGYTQAVL NDVEQILSYF NRAAPLHHDD EELDFFPQLV KVAPQTQTSI DELEKQHEYL HENWNALSVQ LEELISEQRQ DIDKHLIERF IQGYDRHIAL EEPLFEMGRE CLSADILTEM GKHMSARRQV KE // ID Y258_HAEIN Reviewed; 330 AA. AC P43974; P44597; P71347; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 17-FEB-2016, entry version 83. DE RecName: Full=Putative glycosyltransferase HI_0258; DE EC=2.-.-.-; GN OrderedLocusNames=HI_0258; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the glycosyltransferase 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; L42023; AAC21924.1; -; Genomic_DNA. DR PIR; C64146; C64146. DR RefSeq; NP_438427.1; NC_000907.1. DR RefSeq; WP_010868968.1; NC_000907.1. DR ProteinModelPortal; P43974; -. DR STRING; 71421.HI0258; -. DR CAZy; GT8; Glycosyltransferase Family 8. DR EnsemblBacteria; AAC21924; AAC21924; HI_0258. DR GeneID; 949647; -. DR KEGG; hin:HI0258; -. DR PATRIC; 20189043; VBIHaeInf48452_0273. DR eggNOG; ENOG4105X1N; Bacteria. DR eggNOG; COG1442; LUCA. DR OMA; TIICTDI; -. DR OrthoDB; EOG6F293M; -. DR PhylomeDB; P43974; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR002495; Glyco_trans_8. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01501; Glyco_transf_8; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 330 Putative glycosyltransferase HI_0258. FT /FTId=PRO_0000206068. SQ SEQUENCE 330 AA; 39073 MW; C5A6CA0207F24F9A CRC64; MTDRQTDRQT DRQTDRQTDR QTDRQTDRQT DGRTVSQTMN IIFSSDHYYA PYLAVSIFSI IKNTPKKINF YILDMKINQE NKTIINNLAS AYSCKVFFLP VCESDFQNFP KTIDYISLAT YARLNLTKYI KNIEKAIYID VDTLTNSSLQ ELWNIDITNY YLAACRDTFI DVKNEAYKKT IGLEGYSYFN AGILLINLNK WKEENIFQKS INWMNKYNNV MKYQDQDILN GICKGKVKFI NNRFNFTPTD RDLIKKKNLL CVKMPIVISH YCGPNKFWHK KCSHLNCHIG NLLLKEMDKI IDIPSSWYDH FEKIPFLIKI KRLRKRIKDN // ID Y279_HAEIN Reviewed; 98 AA. AC P43977; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAY-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0279; GN OrderedLocusNames=HI_0279; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 MOSC domain. {ECO:0000255|PROSITE- CC ProRule:PRU00670}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21951.1; -; Genomic_DNA. DR PIR; D64005; D64005. DR ProteinModelPortal; P43977; -. DR EnsemblBacteria; AAC21951; AAC21951; HI_0279. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR Gene3D; 2.40.33.20; -; 1. DR InterPro; IPR005302; MoCF_Sase_C. DR InterPro; IPR015808; MoCF_Sase_C-like. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR SUPFAM; SSF50800; SSF50800; 1. DR PROSITE; PS51340; MOSC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein HI_0279. FT /FTId=PRO_0000077905. FT DOMAIN 30 98 MOSC. {ECO:0000255|PROSITE- FT ProRule:PRU00670}. SQ SEQUENCE 98 AA; 10965 MW; 05A56EC9C3C3AEE4 CRC64; MNAKILVIKV GQVETLTFSD GSQYESAIRK KVVPSVKIHS LGAEGNDVGL KKHHGGVDKA LFFMSADSFN ELNALLNKDF SLYGYCDIRR KFCRVRLE // ID Y392_HAEIN Reviewed; 245 AA. AC P43993; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein HI_0392; GN OrderedLocusNames=HI_0392; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the acyltransferase 3 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; L42023; AAC22051.1; -; Genomic_DNA. DR PIR; B64007; B64007. DR STRING; 71421.HI0392; -. DR EnsemblBacteria; AAC22051; AAC22051; HI_0392. DR PATRIC; 20189335; VBIHaeInf48452_0411. DR eggNOG; ENOG4105EXC; Bacteria. DR eggNOG; COG1835; LUCA. DR OMA; MDIFFVI; -. DR OrthoDB; EOG6HXJ1F; -. DR PhylomeDB; P43993; -. DR Proteomes; UP000000579; 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:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR InterPro; IPR002656; Acyl_transf_3. DR Pfam; PF01757; Acyl_transf_3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 245 Uncharacterized protein HI_0392. FT /FTId=PRO_0000208099. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. SQ SEQUENCE 245 AA; 28178 MW; 5C075EC673ADCB2E CRC64; MDIFFVISGF LITGIIITEI QQNSFSLKQF YTRRIKRIYP AFITVMALVS FIASAIFIYN DFNKLRKTIE LAIAFLSNFY LGLTQGYFDL SANENPVLHI WSLAVEGQYY LIFPLILILA YKKFREVKVL FIITLILFFI LLATSFVSAN FYKEVLHQPN IYYLSNLRFP ELLVGSLLAI YHNLSNKVQL SKQVNNILAI LSTLLLFSCL FLMNNNIAFI PGITLILPCI FTALIIHTTS QNNIR // ID Y400_HAEIN Reviewed; 95 AA. AC P44686; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=UPF0381 protein HI_0400; GN OrderedLocusNames=HI_0400; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0381 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; L42023; AAC22059.1; -; Genomic_DNA. DR PIR; C64151; C64151. DR RefSeq; NP_438562.1; NC_000907.1. DR RefSeq; WP_005693769.1; NC_000907.1. DR ProteinModelPortal; P44686; -. DR STRING; 71421.HI0400; -. DR EnsemblBacteria; AAC22059; AAC22059; HI_0400. DR GeneID; 950654; -. DR KEGG; hin:HI0400; -. DR PATRIC; 20189351; VBIHaeInf48452_0419. DR eggNOG; ENOG4105KZW; Bacteria. DR eggNOG; COG3691; LUCA. DR OMA; DPCEIKS; -. DR OrthoDB; EOG62RSGC; -. DR PhylomeDB; P44686; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR005272; CHP00743. DR Pfam; PF04175; DUF406; 1. DR TIGRFAMs; TIGR00743; TIGR00743; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 95 UPF0381 protein HI_0400. FT /FTId=PRO_0000077919. SQ SEQUENCE 95 AA; 10343 MW; 1B09AB38912AA953 CRC64; MTVKCKAEES LTCSCVDVGT IIDGSDCSVE VHQFYSTEAD ANAVLERLTK KARNTESDPC EIKSEIVAVE NGVQLNASFT FSCQAEAMIF ELANR // ID Y419_HAEIN Reviewed; 460 AA. AC P44700; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=Uncharacterized protease HI_0419; DE EC=3.4.-.-; GN OrderedLocusNames=HI_0419; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the peptidase U32 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; L42023; AAC22077.1; -; Genomic_DNA. DR PIR; G64066; G64066. DR RefSeq; NP_438581.1; NC_000907.1. DR RefSeq; WP_005693745.1; NC_000907.1. DR STRING; 71421.HI0419; -. DR MEROPS; U32.002; -. DR PRIDE; P44700; -. DR EnsemblBacteria; AAC22077; AAC22077; HI_0419. DR GeneID; 949394; -. DR KEGG; hin:HI0419; -. DR PATRIC; 20189391; VBIHaeInf48452_0439. DR eggNOG; ENOG4105CFP; Bacteria. DR eggNOG; COG0826; LUCA. DR KO; K08303; -. DR OMA; DFQVNGE; -. DR OrthoDB; EOG6GJBTC; -. DR PhylomeDB; P44700; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001539; Peptidase_U32. DR InterPro; IPR032525; Peptidase_U32_C. DR Pfam; PF01136; Peptidase_U32; 1. DR Pfam; PF16325; Peptidase_U32_C; 1. DR PROSITE; PS01276; PEPTIDASE_U32; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome. FT CHAIN 1 460 Uncharacterized protease HI_0419. FT /FTId=PRO_0000079185. SQ SEQUENCE 460 AA; 52126 MW; 8FDC8FFDECD1C537 CRC64; MTTQFKPELL SPAGSLKNMR YAFAYGADAV YAGQPRYSLR VRNNEFNHAN LKIGIDEAHS LGKKFYVVVN IAPHNSKLKT FIKDLQPVID MKPDALIMSD PGLIMLVREN FPNIDIHLSV QANAVNWATV KFWKQMGLTR VILSRELSID EIAEIRQQVP DIELEIFVHG ALCMAYSGRC LLSGYINKRD PNQGTCTNAC RWEYKMEEGT TDDVGNIVPK IDPAQQIEVK NVAPTLGEGA VTDKVFLYTE SQKPDEQMTA FEDKHGTYFM NSKDLRAVQH VEKLTALGVH SLKIEGRTKS FYYCARTAQV YRKAIDDAAA GKPFDESLMD TLESLAHRGY TEGFLRRHTH DEYQNYEYGY SISDRQQFVG EFTGKRNEQG MAEVAVKNKF LLGDNVEMMT PQGNINFKIE KMLNRKNETV DAALGDGHFV FLNVPQDINL NYALLMRNLV NTNTRNPHSN // ID Y424_HAEIN Reviewed; 351 AA. AC P44703; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase HI_0424; DE EC=2.1.1.-; GN OrderedLocusNames=HI_0424; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22080.1; -; Genomic_DNA. DR PIR; D64152; D64152. DR RefSeq; NP_438585.1; NC_000907.1. DR RefSeq; WP_005693740.1; NC_000907.1. DR ProteinModelPortal; P44703; -. DR STRING; 71421.HI0424; -. DR DNASU; 949529; -. DR EnsemblBacteria; AAC22080; AAC22080; HI_0424. DR GeneID; 949529; -. DR KEGG; hin:HI0424; -. DR PATRIC; 20189401; VBIHaeInf48452_0444. DR eggNOG; ENOG4105EIB; Bacteria. DR eggNOG; COG0566; LUCA. DR KO; K03214; -. DR OMA; IVRLWAT; -. DR OrthoDB; EOG6GBMDM; -. DR PhylomeDB; P44703; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR013123; SpoU_subst-bd. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR016479; YfiF_prd. DR Pfam; PF00588; SpoU_methylase; 1. DR Pfam; PF08032; SpoU_sub_bind; 1. DR PIRSF; PIRSF006280; YfiF_prd; 1. DR SMART; SM00967; SpoU_sub_bind; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 351 Uncharacterized tRNA/rRNA FT methyltransferase HI_0424. FT /FTId=PRO_0000159816. SQ SEQUENCE 351 AA; 39397 MW; 71FA2E679F64AE4C CRC64; MNDKRKPSFQ SAGKTFQERS VGEKYREKPT QNRPHFNDKF NGNRNEKSRF PRDKQEVKET RITQLSLSRA PSNKNAEQPK VQVTIKSTGT VYKTKEKKTG ALSPRAPEKI KKNRAEEMKV YGENACLALF AERPESIVRL WATVQMSHKI GEVLSYLAEN KKAYHVVDSE ELARVSGTEH HGGICLLVKK PRAFTLQGYL DIPRNEDCLV LLDNVNNAQN IGGVLRTCAY FGVKNIVADN VENLYSAASM RVAEGGAEYI RVLEADYIDS ALMQLRKSGY QIIHVSHNKQ GDPLDKVRLK NKVVFVLSES STESLATPED TQARLTLASP IKSGLNIAVN AGVLLAKWYF R // ID Y466_HAEIN Reviewed; 280 AA. AC P44000; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized protein HI_0466; GN OrderedLocusNames=HI_0466; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YgfZ (UP14) and B.aphidicola (subsp. CC Acyrthosiphon pisum) BU435. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22125.1; -; Genomic_DNA. DR PIR; I64007; I64007. DR RefSeq; NP_438627.1; NC_000907.1. DR RefSeq; WP_005693695.1; NC_000907.1. DR ProteinModelPortal; P44000; -. DR STRING; 71421.HI0466; -. DR EnsemblBacteria; AAC22125; AAC22125; HI_0466. DR GeneID; 949552; -. DR KEGG; hin:HI0466; -. DR PATRIC; 20189487; VBIHaeInf48452_0486. DR eggNOG; ENOG4106XY2; Bacteria. DR eggNOG; COG0354; LUCA. DR KO; K06980; -. DR OMA; WRKTGTI; -. DR OrthoDB; EOG6QP0ZT; -. DR PhylomeDB; P44000; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central. DR InterPro; IPR006222; GCV_T_N. DR InterPro; IPR029043; GcvT/YgfZ_C. DR InterPro; IPR017703; YgfZ/GcvT_CS. DR Pfam; PF01571; GCV_T; 1. DR SUPFAM; SSF101790; SSF101790; 1. DR TIGRFAMs; TIGR03317; ygfZ_signature; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 280 Uncharacterized protein HI_0466. FT /FTId=PRO_0000077926. SQ SEQUENCE 280 AA; 31549 MW; 3A9F200090B2221C CRC64; MSQFISLTQY QLIEVQGADA EKYLQGQLTS DVVRLASGAT TLTAHCDPKG KMNAIYRLFK VSSEQFFLLV KKDILPSGLD ALKKYAVFSK VSFDLRDWQI IGVIGEKCGK ITPNFSLEID EKRSILLNET ELPVNFNGDE KIWEVADIQA GLPNLSPQTQ NEFIPQALNL QAIEQAISFT KGCYIGQETV ARAKYRGANK RAMFIFKVQT QQEAEIGSEI EMQLEANWRK TGTITSAVNL DGVLWLQVVM NNDIDSEQQF RLLNSEILLE RVQLPYSITE // ID Y521_HAEIN Reviewed; 514 AA. AC P44744; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0521; GN OrderedLocusNames=HI_0521; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli YjjI. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22179.1; -; Genomic_DNA. DR PIR; C64154; C64154. DR RefSeq; NP_438679.1; NC_000907.1. DR RefSeq; WP_005694125.1; NC_000907.1. DR ProteinModelPortal; P44744; -. DR STRING; 71421.HI0521; -. DR DNASU; 950665; -. DR EnsemblBacteria; AAC22179; AAC22179; HI_0521. DR GeneID; 950665; -. DR KEGG; hin:HI0521; -. DR PATRIC; 20189595; VBIHaeInf48452_0540. DR eggNOG; ENOG4105G0K; Bacteria. DR eggNOG; ENOG410XNMQ; LUCA. DR OMA; TIIYHHV; -. DR OrthoDB; EOG61KBCM; -. DR PhylomeDB; P44744; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR016905; Glycyl_radical_HI0521_prd. DR Pfam; PF11230; DUF3029; 1. DR PIRSF; PIRSF028991; Glycl_rad_HI0521_prd; 1. DR TIGRFAMs; TIGR04040; glycyl_YjjI; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 514 Uncharacterized protein HI_0521. FT /FTId=PRO_0000169808. SQ SEQUENCE 514 AA; 58159 MW; 69472E231F9FB746 CRC64; MLASLQDILD TVKANNLTYH QKLMTLGNIA ERLFDPRDLL GYTDEEWGFL QNQMICDLCE GYAIYRPRYI LPDYNVYIQK GCEFLELPPP KDLDEALDGL LILYSHVPSI TTYPVYIGRL DVLLEPFITD EEKDYIKIKR FLNHIDKTVP DSFCHANIGP YDTKAGRLIL RAVIDLEAPT PNMTIRYDKS KTSREFAELA AKACLLVSKP SFANDAYYIS DLGEEYGVAS CYNALPECGG AYTLTRLRLG TIARTCKSAD EMLNELLPRV AKCALSTMDK RHKFVVEESN FFNSSFLEKE GFIKRTNFTG MFAIVGLADA TNHLLQCEGL NETFGKSVRG DEIATAIMDK LKEITDAHEG VYAERTGNRY LLHAQVGASN HEEDKRNAPA HRIRVGEEPT LLAHLKQSAP FHKYFPSGTG DLFAFDQTYV DHCDAVVDII DGAFSLGYRY ITTYLKNTDL IRVTGYLVKK SEVEKYRKGE VALRDTTWYG SGTDECANVF DRQLRDEKDV IAEK // ID Y527_HAEIN Reviewed; 86 AA. AC P44746; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Uncharacterized ferredoxin-like protein HI_0527; GN OrderedLocusNames=HI_0527; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22184.1; -; Genomic_DNA. DR PIR; E64074; E64074. DR RefSeq; NP_438685.1; NC_000907.1. DR RefSeq; WP_005649491.1; NC_000907.1. DR ProteinModelPortal; P44746; -. DR SMR; P44746; 2-80. DR STRING; 71421.HI0527; -. DR EnsemblBacteria; AAC22184; AAC22184; HI_0527. DR GeneID; 949590; -. DR KEGG; hin:HI0527; -. DR PATRIC; 20189607; VBIHaeInf48452_0546. DR eggNOG; ENOG4105K5D; Bacteria. DR eggNOG; COG1145; LUCA. DR OMA; CPVECII; -. DR OrthoDB; EOG6CVV7G; -. DR PhylomeDB; P44746; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 86 Uncharacterized ferredoxin-like protein FT HI_0527. FT /FTId=PRO_0000159301. FT DOMAIN 2 29 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 29 65 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 9 9 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 12 12 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 15 15 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 38 38 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 41 41 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 50 50 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 86 AA; 9795 MW; 68765CB7DA5CECA9 CRC64; MALLITSKCT NCDMCLPECP NEAISIGDEI YVIDPILCTE CVGHYDTPTC QKVCPITNCI KPDPEHQETE EQLWERFVMI HHSDKL // ID Y554_HAEIN Reviewed; 180 AA. AC P44014; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Uncharacterized protein HI_0554; GN OrderedLocusNames=HI_0554; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22217.1; -; Genomic_DNA. DR PIR; E64009; E64009. DR RefSeq; NP_438712.1; NC_000907.1. DR RefSeq; WP_005694149.1; NC_000907.1. DR ProteinModelPortal; P44014; -. DR STRING; 71421.HI0554; -. DR EnsemblBacteria; AAC22217; AAC22217; HI_0554. DR GeneID; 949606; -. DR KEGG; hin:HI0554; -. DR PATRIC; 20189663; VBIHaeInf48452_0574. DR eggNOG; ENOG41090HT; Bacteria. DR eggNOG; COG1943; LUCA. DR KO; K07491; -. DR OMA; FITICCK; -. DR OrthoDB; EOG61ZTFT; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004803; F:transposase activity; IEA:InterPro. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR Gene3D; 3.30.70.1290; -; 1. DR InterPro; IPR002686; Transposase_17. DR SMART; SM01321; Y1_Tnp; 1. DR SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 180 Uncharacterized protein HI_0554. FT /FTId=PRO_0000077931. SQ SEQUENCE 180 AA; 21605 MW; 495C2E527F95CA1B CRC64; MTTKYNAGIH HRRSIRLKHY NYRSEGFYFI TICCKNKECL FGHIINQQMQ LNDLGNYVKQ CWENIPMFFP QVRIDEFVIM PNHLHGIIEI IEQVKGKCNL PLQLRATQLP QKGTSQTIGS IVRRFKAGVT SWARKNSEIF DVWQRNYYEH IIRDEKSYLQ IYEYIQNNPI LWEQDQLYVD // ID Y555_HAEIN Reviewed; 79 AA. AC Q57409; O05025; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_0555; GN OrderedLocusNames=HI_0555; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22211.1; -; Genomic_DNA. DR RefSeq; NP_438713.1; NC_000907.1. DR RefSeq; WP_005694150.1; NC_000907.1. DR STRING; 71421.HI0555; -. DR EnsemblBacteria; AAC22211; AAC22211; HI_0555. DR GeneID; 950248; -. DR KEGG; hin:HI0555; -. DR eggNOG; COG3759; LUCA. DR KO; K08987; -. DR OrthoDB; EOG66B42M; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 79 Uncharacterized protein HI_0555. FT /FTId=PRO_0000077932. SQ SEQUENCE 79 AA; 9646 MW; 6FB7162B96EC0016 CRC64; MEILAYILTA LVTLEHFYIL YLEMFTIESK SGVRQSRVIQ RLFGSRDYFW LCHQPNFGDL FLFRLCDYRR SFWGSYDEE // ID Y570_HAEIN Reviewed; 205 AA. AC P44757; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0570; GN OrderedLocusNames=HI_0570; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00335}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22228.1; -; Genomic_DNA. DR PIR; H64154; H64154. DR RefSeq; NP_438727.1; NC_000907.1. DR RefSeq; WP_005629669.1; NC_000907.1. DR ProteinModelPortal; P44757; -. DR STRING; 71421.HI0570; -. DR EnsemblBacteria; AAC22228; AAC22228; HI_0570. DR GeneID; 949502; -. DR KEGG; hin:HI0570; -. DR PATRIC; 20189695; VBIHaeInf48452_0590. DR eggNOG; ENOG4105EJ2; Bacteria. DR eggNOG; COG1309; LUCA. DR OMA; AYWYRKE; -. DR OrthoDB; EOG6ZPT09; -. DR PhylomeDB; P44757; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR Pfam; PF00440; TetR_N; 1. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS01081; HTH_TETR_1; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 205 Uncharacterized HTH-type transcriptional FT regulator HI_0570. FT /FTId=PRO_0000070643. FT DOMAIN 11 71 HTH tetR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00335}. SQ SEQUENCE 205 AA; 22942 MW; 636BB08BC9D0C9F2 CRC64; MAGVRAVQKE KTRRALVDAA FNQLSAEKSF SNLSLREVAR EAGIAPTSFY RHFSDMDELG LEMVDEAGLM LRQLMRQARK RIDAGGSVIS VSVDTFFEFI TNSTNVFRLL LRESSGTSQA FRTAAAREIK HFVDELAEYI SYKHQYSQYV AYVQAEGIVT IVFTAGANAL DMSKAEREQL KARVILQLRM LAKGADFAAN KERGK // ID Y577_HAEIN Reviewed; 95 AA. AC P44017; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_0577; GN OrderedLocusNames=HI_0577; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22241.1; -; Genomic_DNA. DR PIR; H64009; H64009. DR RefSeq; NP_438735.1; NC_000907.1. DR RefSeq; WP_005649577.1; NC_000907.1. DR ProteinModelPortal; P44017; -. DR STRING; 71421.HI0577; -. DR EnsemblBacteria; AAC22241; AAC22241; HI_0577. DR GeneID; 949622; -. DR KEGG; hin:HI0577; -. DR PATRIC; 20189711; VBIHaeInf48452_0598. DR eggNOG; COG2168; LUCA. DR KO; K07237; -. DR OMA; IVLWQDG; -. DR OrthoDB; EOG6HB9TB; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR007215; Sulphur_relay_TusB/DsrH. DR Pfam; PF04077; DsrH; 1. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 95 Uncharacterized protein HI_0577. FT /FTId=PRO_0000077935. SQ SEQUENCE 95 AA; 10902 MW; DAB65C8DEFCE81B8 CRC64; MLYTFSQSDY PKTELDDYFS YITEKDAVVL WQDGVLLAIK YPDYFAKCKG NCMILKQDIL ARNLTALLPQ SSKIKLISIE ELVGITENYL PQLSL // ID Y656A_HAEIN Reviewed; 178 AA. AC P46494; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein HI_0656.1; GN OrderedLocusNames=HI_0656.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YrdD. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22316.1; -; Genomic_DNA. DR RefSeq; NP_438817.1; NC_000907.1. DR RefSeq; WP_005694485.1; NC_000907.1. DR STRING; 71421.HI0656.1; -. DR EnsemblBacteria; AAC22316; AAC22316; HI_0656.1. DR GeneID; 949423; -. DR KEGG; hin:HI0656.1; -. DR PATRIC; 20189929; VBIHaeInf48452_0686. DR eggNOG; ENOG4108WI1; Bacteria. DR eggNOG; COG0551; LUCA. DR KO; K07479; -. DR OMA; GRYGMFV; -. DR OrthoDB; EOG6JHRK9; -. DR PhylomeDB; P46494; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:InterPro. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR013498; Topo_IA_Znf. DR PANTHER; PTHR11390; PTHR11390; 1. DR Pfam; PF01396; zf-C4_Topoisom; 3. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 178 Uncharacterized protein HI_0656.1. FT /FTId=PRO_0000169507. SQ SEQUENCE 178 AA; 20304 MW; ABFFA2F267D27ADD CRC64; MNQSLFHHSK QQEYCPQCGA PLQIKQGKKG LFLGCSAYPE CDYLRPLQRS EHKVLKTLDE ICPKCGNLLQ LKQGSFGMFI GCSHYPECDF VVREESESEE KITCPECKTG HLISRRGRQG KIFYGCDNFP KCKFSLPAKP YSVPCPTCHF PLSLLKSEDG EKQIFQCANK TCRHIFEQ // ID Y680_HAEIN Reviewed; 298 AA. AC Q57389; O05030; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized transporter HI_0680; GN OrderedLocusNames=HI_0680; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the EamA transporter family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 EamA 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; L42023; AAC22339.1; -; Genomic_DNA. DR PIR; I64085; I64085. DR RefSeq; NP_438840.1; NC_000907.1. DR RefSeq; WP_010869031.1; NC_000907.1. DR STRING; 71421.HI0680; -. DR TCDB; 2.A.7.7.3; the drug/metabolite transporter (dmt) superfamily. DR EnsemblBacteria; AAC22339; AAC22339; HI_0680. DR GeneID; 949717; -. DR KEGG; hin:HI0680; -. DR PATRIC; 20189979; VBIHaeInf48452_0711. DR eggNOG; ENOG4105DTR; Bacteria. DR eggNOG; COG2962; LUCA. DR KO; K05786; -. DR OMA; FGWRTLL; -. DR OrthoDB; EOG6Z99ZH; -. DR PhylomeDB; Q57389; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR InterPro; IPR000620; EamA_dom. DR InterPro; IPR004626; RarD. DR Pfam; PF00892; EamA; 1. DR TIGRFAMs; TIGR00688; rarD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 298 Uncharacterized transporter HI_0680. FT /FTId=PRO_0000108159. FT TRANSMEM 5 23 Helical. {ECO:0000255}. FT TRANSMEM 33 52 Helical. {ECO:0000255}. FT TRANSMEM 72 91 Helical. {ECO:0000255}. FT TRANSMEM 101 120 Helical. {ECO:0000255}. FT TRANSMEM 127 145 Helical. {ECO:0000255}. FT TRANSMEM 149 166 Helical. {ECO:0000255}. FT TRANSMEM 175 194 Helical. {ECO:0000255}. FT TRANSMEM 207 229 Helical. {ECO:0000255}. FT TRANSMEM 238 260 Helical. {ECO:0000255}. FT TRANSMEM 265 284 Helical. {ECO:0000255}. FT DOMAIN 13 144 EamA. SQ SEQUENCE 298 AA; 33465 MW; 65DC2A9EB8F9EF02 CRC64; MFKGILVSLL ASFLFGYMYY FSTLLKPLSG TDIFGYRMIF TFPFVLLSVT LFKQKAALIE RLKRIQKRPH LALSYLLCGL LMGFQMWLFL WAPNNGSSLS VSFGYLLLPI VMVAAGRVFF KERISTFKFI AVIIATLGVI SNIVLKGGLS WEAIVICLGY TAYFSIRKAL KNTDLASFCL EMLSLMPVSI YFALQTDFAT VQQTNPFIWG XLVLLGLISG TALIAYVIAS NMLPMNLLGL LGYVETIMML CVSFLIGEQI DSESYPLFIC LVIAMILVMV DGVYKHTQKE VYKCHLKK // ID Y725_HAEIN Reviewed; 146 AA. AC P44043; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein HI_0725; GN OrderedLocusNames=HI_0725; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22383.1; -; Genomic_DNA. DR PIR; G64012; G64012. DR RefSeq; NP_438883.1; NC_000907.1. DR RefSeq; WP_005693128.1; NC_000907.1. DR STRING; 71421.HI0725; -. DR EnsemblBacteria; AAC22383; AAC22383; HI_0725. DR GeneID; 949753; -. DR KEGG; hin:HI0725; -. DR PATRIC; 20190083; VBIHaeInf48452_0757. DR eggNOG; ENOG4105XCT; Bacteria. DR eggNOG; ENOG411232A; LUCA. DR OMA; RCELSEG; -. DR OrthoDB; EOG63FW3T; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR019617; DUF2489. DR Pfam; PF10675; DUF2489; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 146 Uncharacterized protein HI_0725. FT /FTId=PRO_0000077950. FT TRANSMEM 7 24 Helical. {ECO:0000255}. SQ SEQUENCE 146 AA; 17054 MW; 3978AEA0CA327C2F CRC64; MIWIFFVIAL FLVTGLTLYA IRLLKQLKVQ KELIAKAKNN RVIRLKESID IIARAMQSGE CNLSEGVMRL TMLLRPFGKN LSSYPAMANL YEVVRDMPTH DDRKLLEKRE RMRLDLARES AEAQFEKNIK QELYILLEDI KSIELI // ID Y1479_HAEIN Reviewed; 90 AA. AC P44208; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 29-APR-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_1479; GN OrderedLocusNames=HI_1479; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23129.1; -; Genomic_DNA. DR PIR; B64031; B64031. DR RefSeq; NP_439630.1; NC_000907.1. DR RefSeq; WP_005693495.1; NC_000907.1. DR ProteinModelPortal; P44208; -. DR STRING; 71421.HI1479; -. DR EnsemblBacteria; AAC23129; AAC23129; HI_1479. DR GeneID; 950355; -. DR KEGG; hin:HI1479; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR015126; Mu_I-gamma. DR Pfam; PF09039; HTH_Tnp_Mu_2; 1. DR SUPFAM; SSF46689; SSF46689; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 90 Uncharacterized protein HI_1479. FT /FTId=PRO_0000078065. SQ SEQUENCE 90 AA; 10467 MW; 18F6FCFD95ECCF26 CRC64; MSNITLNENA MLYLKADYYR PEMPTFKACY FRLSKIAQEQ GWGTLPNLAQ TKALFKAAVP EIIWTREAFK RANTQKKHAH KATPYLEQVM // ID Y1480_HAEIN Reviewed; 156 AA. AC P44209; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 14-OCT-2015, entry version 72. DE RecName: Full=Uncharacterized protein HI_1480; GN OrderedLocusNames=HI_1480; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23130.1; -; Genomic_DNA. DR PIR; C64031; C64031. DR RefSeq; NP_439631.1; NC_000907.1. DR RefSeq; WP_005693497.1; NC_000907.1. DR PDB; 1MW5; X-ray; 2.10 A; A/B=1-156. DR PDBsum; 1MW5; -. DR ProteinModelPortal; P44209; -. DR SMR; P44209; 3-156. DR STRING; 71421.HI1480; -. DR EnsemblBacteria; AAC23130; AAC23130; HI_1480. DR GeneID; 950577; -. DR KEGG; hin:HI1480; -. DR PATRIC; 20191675; VBIHaeInf48452_1547. DR EvolutionaryTrace; P44209; -. DR Proteomes; UP000000579; Chromosome. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 156 Uncharacterized protein HI_1480. FT /FTId=PRO_0000078066. FT HELIX 4 11 {ECO:0000244|PDB:1MW5}. FT STRAND 15 18 {ECO:0000244|PDB:1MW5}. FT HELIX 20 36 {ECO:0000244|PDB:1MW5}. FT HELIX 48 60 {ECO:0000244|PDB:1MW5}. FT STRAND 64 66 {ECO:0000244|PDB:1MW5}. FT HELIX 70 77 {ECO:0000244|PDB:1MW5}. FT TURN 82 84 {ECO:0000244|PDB:1MW5}. FT HELIX 85 104 {ECO:0000244|PDB:1MW5}. FT HELIX 106 111 {ECO:0000244|PDB:1MW5}. FT STRAND 123 130 {ECO:0000244|PDB:1MW5}. FT HELIX 131 140 {ECO:0000244|PDB:1MW5}. FT STRAND 142 153 {ECO:0000244|PDB:1MW5}. FT HELIX 154 156 {ECO:0000244|PDB:1MW5}. SQ SEQUENCE 156 AA; 17736 MW; E0E0C6C120A94162 CRC64; MSETDLLLKM VRQPVKLYSV ATLFHEFSEV ITKLEHSVQK EPTSLLSEEN WHKQFLKFAQ ALPAHGSASW LNLDDALQAV VGNSRSAFLH QLIAKLKSRH LQVLELNKIG SEPLDLSNLP APFYVLLPES FAARITLLVQ DKALPYVRVS FEYWHA // ID Y1482_HAEIN Reviewed; 105 AA. AC P44210; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_1482; GN OrderedLocusNames=HI_1482; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23138.1; -; Genomic_DNA. DR PIR; D64031; D64031. DR RefSeq; NP_439633.1; NC_000907.1. DR RefSeq; WP_010869223.1; NC_000907.1. DR STRING; 71421.HI1482; -. DR EnsemblBacteria; AAC23138; AAC23138; HI_1482. DR GeneID; 950568; -. DR KEGG; hin:HI1482; -. DR PATRIC; 20191679; VBIHaeInf48452_1549. DR OMA; WEGEREY; -. DR OrthoDB; EOG628FGG; -. DR Proteomes; UP000000579; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 105 Uncharacterized protein HI_1482. FT /FTId=PRO_0000078067. SQ SEQUENCE 105 AA; 11985 MW; BE3DB8757718F6F5 CRC64; MQKVYNKMAG EMMSPRNAVI HNQLAMLELA TLECEALGIE VETVEWFDIG KPRLVVKDCS ALRHLIKTGK AFNYGSEVKN GIRIYLNQMM VKGVKFIWKS DVTKH // ID Y1487_HAEIN Reviewed; 186 AA. AC P44214; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_1487; GN OrderedLocusNames=HI_1487; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23142.1; -; Genomic_DNA. DR PIR; H64031; H64031. DR RefSeq; NP_439637.1; NC_000907.1. DR RefSeq; WP_005693506.1; NC_000907.1. DR STRING; 71421.HI1487; -. DR EnsemblBacteria; AAC23142; AAC23142; HI_1487. DR GeneID; 950580; -. DR KEGG; hin:HI1487; -. DR PATRIC; 20191691; VBIHaeInf48452_1555. DR OMA; SIFGIVC; -. DR OrthoDB; EOG67MFBM; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein HI_1487. FT /FTId=PRO_0000078071. SQ SEQUENCE 186 AA; 21637 MW; E4442ECB896E5A9B CRC64; MNAIQFRYFK GVMTKEPLKT IIDTWYKLRA ERDKKLTNIF NTIPFYESWL GDETSIFGIV CSYDNPARDE AVLTKGYRTE DYKGKCVVKP DRRYKVGKDF DKKLQAIRQI LKEAPDFSSY SLKELGMYLL VGNFSRLYFS VSGVQDDIYI AKIPVKEQGN FGDDFLEIHE CLTEIKESEF LSIQGL // ID Y1496_HAEIN Reviewed; 84 AA. AC P44220; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein HI_1496; GN OrderedLocusNames=HI_1496; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23147.1; -; Genomic_DNA. DR PIR; E64032; E64032. DR RefSeq; NP_439645.1; NC_000907.1. DR RefSeq; WP_005693513.1; NC_000907.1. DR STRING; 71421.HI1496; -. DR EnsemblBacteria; AAC23147; AAC23147; HI_1496. DR GeneID; 950362; -. DR KEGG; hin:HI1496; -. DR PATRIC; 20191709; VBIHaeInf48452_1564. DR OMA; LERMHND; -. DR OrthoDB; EOG6G4VQG; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR020274; Uncharacterised_HI1496. DR Pfam; PF10883; DUF2681; 1. DR ProDom; PD060859; Uncharacterised_HI1496; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 84 Uncharacterized protein HI_1496. FT /FTId=PRO_0000078077. FT TRANSMEM 7 23 Helical. {ECO:0000255}. SQ SEQUENCE 84 AA; 9773 MW; 7595F064F32D0558 CRC64; MMNLILAFSG VIALYGGYLY LRLRQSQKQA ATLQKEKEQL QTQKTVAETK VKNYQVKQKN EENLISRSRT SLLERMHNDG DLRD // ID Y1544_HAEIN Reviewed; 202 AA. AC P45245; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 87. DE RecName: Full=Uncharacterized NAD(P)H oxidoreductase HI_1544; DE EC=1.6.99.-; GN OrderedLocusNames=HI_1544; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) 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; L42023; AAC23194.1; -; Genomic_DNA. DR PIR; G64128; G64128. DR RefSeq; NP_439693.1; NC_000907.1. DR RefSeq; WP_005693569.1; NC_000907.1. DR ProteinModelPortal; P45245; -. DR STRING; 71421.HI1544; -. DR EnsemblBacteria; AAC23194; AAC23194; HI_1544. DR GeneID; 950407; -. DR KEGG; hin:HI1544; -. DR PATRIC; 20191813; VBIHaeInf48452_1615. DR eggNOG; ENOG4105DYS; Bacteria. DR eggNOG; COG2249; LUCA. DR OMA; WMGFPSI; -. DR OrthoDB; EOG6G7R2D; -. DR PhylomeDB; P45245; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 202 Uncharacterized NAD(P)H oxidoreductase FT HI_1544. FT /FTId=PRO_0000071631. SQ SEQUENCE 202 AA; 23160 MW; 702F7F4CF44E7BCA CRC64; MNHLIIFAHP NSVRSFGRAI ANRIEQISQE NGVNVFFRDL YEMNFNPILS HEELQNANNG IIPEDIQQEH DFILQADLIT LVYPLWWMGF PAILKGYLDR VLSHGFAYKT ENGESVGLLK NKQMQQFITI GSNVDKYKEF GVDKSLNHCL INGLFNYCGI ENVEFELFGD IHLIDDKARK AMIELAAQKT QAKLTALLKE KE // ID Y1570_HAEIN Reviewed; 169 AA. AC P44259; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_1570; GN OrderedLocusNames=HI_1570; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23224.1; -; Genomic_DNA. DR PIR; H64036; H64036. DR EnsemblBacteria; AAC23224; AAC23224; HI_1570. DR OMA; KQGNREK; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020388; Put_Mu_head. DR ProDom; PD097920; Uncharacterised_HI1570; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein HI_1570. FT /FTId=PRO_0000078090. SQ SEQUENCE 169 AA; 19264 MW; 5E066B111463FABD CRC64; MEVERPADKQ GNREKTVGFK LPDGTIRVTD KGFDYNVGRL NYKPNLDLYP EKLAHAFAKV EMKGGEFKHD FELLAKHMAE MKQTLSPEGK KLTAEQMLQV RDSLTKNFKF AAGVLSAESK DLLKSKTGTV WLSDDTLIKQ FNSRDGQDFG IDEYERCQIS SMLPSIYYK // ID Y1599_HAEIN Reviewed; 238 AA. AC P44267; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_1599; GN OrderedLocusNames=HI_1599; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC23258.1; -; Genomic_DNA. DR PIR; G64037; G64037. DR RefSeq; NP_439741.2; NC_000907.1. DR ProteinModelPortal; P44267; -. DR STRING; 71421.HI1599; -. DR EnsemblBacteria; AAC23258; AAC23258; HI_1599. DR GeneID; 950442; -. DR KEGG; hin:HI1599; -. DR PATRIC; 20191929; VBIHaeInf48452_1672. DR eggNOG; COG3219; LUCA. DR KO; K09929; -. DR OMA; PLNGYAE; -. DR OrthoDB; EOG6716MP; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR018640; DUF2063. DR Pfam; PF09836; DUF2063; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 238 Uncharacterized protein HI_1599. FT /FTId=PRO_0000078097. SQ SEQUENCE 238 AA; 27533 MW; 31B9F50AAA08D000 CRC64; MLPKSSLKET QQALANAIRL GNADPLNGYA ASRLAVYTRL VRNNAFGFID RCFVEAPLHI EPEYWKNAKE NFVQNGNAHS PYFQDIAGEF LLFCQEKEIF DTNILALMDF ENTQLLAEVS LAKVPEKFEW NRHSVMQLSG AAYLKSYDVD FLSSDFKQFD DTPIQAIIWR DSDFRIQQQI LSELDYWLLS YLQEQPNSLE NVLSALNTMV EDSTSIIPLL EQVWMKWVTS EVIYPEQR // ID Y1624_HAEIN Reviewed; 227 AA. AC P44276; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_1624; DE Flags: Precursor; GN OrderedLocusNames=HI_1624; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 22-32. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23272.1; -; Genomic_DNA. DR PIR; G64038; G64038. DR RefSeq; NP_439765.1; NC_000907.1. DR RefSeq; WP_005689200.1; NC_000907.1. DR STRING; 71421.HI1624; -. DR EnsemblBacteria; AAC23272; AAC23272; HI_1624. DR GeneID; 950470; -. DR KEGG; hin:HI1624; -. DR PATRIC; 20191981; VBIHaeInf48452_1698. DR eggNOG; ENOG4105UZ0; Bacteria. DR eggNOG; COG5266; LUCA. DR KO; K10094; -. DR OMA; QRRGNIE; -. DR OrthoDB; EOG6BCSV3; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019613; DUF4198. DR Pfam; PF10670; DUF4198; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Signal. FT SIGNAL 1 21 {ECO:0000269|PubMed:10675023}. FT CHAIN 22 227 Uncharacterized protein HI_1624. FT /FTId=PRO_0000013976. SQ SEQUENCE 227 AA; 25564 MW; 9990A51301824E4A CRC64; MELKKIAVGL TALLGMSVAN AHNVWLEPAS SQDEYVVKFG HEQTETYPES KLKSIQALNS QGKLTAVDYQ FRNGEAYLMP KSDLVFVHFD NGVWSKLPSG KYVEKTKREE PTAEFSTNPV KFGKAILKWD AESFKSHQQA YELIPQEKAQ ANKPLSILVL HNGKPVQGIK VGVSEDAPFN LTNEKGIAQF TPTKGFNKVW AEFEEKVTNN ADYDRRTVEY MLTFDAQ // ID Y1629_HAEIN Reviewed; 212 AA. AC P45280; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 84. DE RecName: Full=Uncharacterized membrane protein HI_1629; GN OrderedLocusNames=HI_1629; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DedA 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; L42023; AAC23276.1; -; Genomic_DNA. DR PIR; D64133; D64133. DR RefSeq; NP_439771.2; NC_000907.1. DR STRING; 71421.HI1629; -. DR EnsemblBacteria; AAC23276; AAC23276; HI_1629. DR GeneID; 950844; -. DR KEGG; hin:HI1629; -. DR PATRIC; 20191993; VBIHaeInf48452_1704. DR eggNOG; ENOG4108VD1; Bacteria. DR eggNOG; COG0586; LUCA. DR OMA; WVYLGDF; -. DR OrthoDB; EOG613091; -. DR Proteomes; UP000000579; 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; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 212 Uncharacterized membrane protein HI_1629. FT /FTId=PRO_0000161421. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. SQ SEQUENCE 212 AA; 24550 MW; 4B57ADD50DDD4FCC CRC64; MNQFFITSIN IIKKQEQMEF LIGFFTEYGY WAVLFVLIIC GFGVPIPEDI TLVSGGVIAG LYPENVNSHL MLLVSMIGVL AGDSCMYWLG RIYGTKILRF RPIRRIVTLQ RLRMVREKFS QYGNRVLFVA RFLPGLRAPI YMVSGITRRV SYVRFVLIDF CAAIISVPIW IYLGELGAKN LDWLHTQIQK GQIVIYIFIG YLYYSFLEME KI // ID Y1664_HAEIN Reviewed; 251 AA. AC P45305; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Uncharacterized metal-dependent hydrolase HI_1664 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=HI_1664; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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 -!- SEQUENCE CAUTION: CC Sequence=AAC23310.1; 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; L42023; AAC23310.1; ALT_INIT; Genomic_DNA. DR PIR; E64174; E64174. DR RefSeq; NP_439806.2; NC_000907.1. DR RefSeq; WP_005694391.1; NC_000907.1. DR ProteinModelPortal; P45305; -. DR STRING; 71421.HI1664; -. DR EnsemblBacteria; AAC23310; AAC23310; HI_1664. DR GeneID; 950504; -. DR KEGG; hin:HI1664; -. DR PATRIC; 20192077; VBIHaeInf48452_1742. DR eggNOG; ENOG4108RE7; Bacteria. DR eggNOG; COG0084; LUCA. DR KO; K03424; -. DR OMA; HFHWFKT; -. DR OrthoDB; EOG66QM1C; -. DR PhylomeDB; P45305; -. DR Proteomes; UP000000579; 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; 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 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 1 251 Uncharacterized metal-dependent hydrolase FT HI_1664. FT /FTId=PRO_0000202005. FT METAL 6 6 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 8 8 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 90 90 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 90 90 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 130 130 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 154 154 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 202 202 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 251 AA; 29335 MW; F95E9E6967CE9450 CRC64; MLFDSHLHLD QLSDENIQQT LAHSKIIGML AVSTNLNSAK KLLNLKQTYP KKLYIAAGFH PEQQLPSLEE QKKLFQWIDE HHSSISAIGE VGLPHYSKRE NPNLDYVPYI ELLERFILIA KKWDLPLNLH IVHNDVEIAL ELLQKHNIQR AHFHWFKTDE KSFQKFFSTP YFASLTPDIL WNSKTQYVAQ HLSLNRLMIE TDSPWQHEGF ERAGISEQLL AVLQKLAELK SLPLHSVQKQ ILLNTQQFYR L // ID Y1671_HAEIN Reviewed; 416 AA. AC P44287; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized protein HI_1671; GN OrderedLocusNames=HI_1671; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the PqiA 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; L42023; AAC23316.1; -; Genomic_DNA. DR PIR; I64039; I64039. DR RefSeq; NP_439813.1; NC_000907.1. DR RefSeq; WP_005667179.1; NC_000907.1. DR STRING; 71421.HI1671; -. DR EnsemblBacteria; AAC23316; AAC23316; HI_1671. DR GeneID; 950860; -. DR KEGG; hin:HI1671; -. DR PATRIC; 20192093; VBIHaeInf48452_1750. DR eggNOG; ENOG4105H2K; Bacteria. DR eggNOG; COG2995; LUCA. DR KO; K03808; -. DR OMA; PISIIYV; -. DR OrthoDB; EOG661H80; -. DR PhylomeDB; P44287; -. DR Proteomes; UP000000579; 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; IPR005219; CHP00155. DR InterPro; IPR007498; PqiA. DR Pfam; PF04403; PqiA; 2. DR TIGRFAMs; TIGR00155; pqiA_fam; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 416 Uncharacterized protein HI_1671. FT /FTId=PRO_0000169054. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. FT TRANSMEM 347 367 Helical. {ECO:0000255}. FT TRANSMEM 377 397 Helical. {ECO:0000255}. SQ SEQUENCE 416 AA; 47374 MW; 0609F96506FBF27B CRC64; MPKTKLTSPP FKILKCTECD ACINVPSILQ SNEQAECPRC HHLLASGTRW SLHRCAMIAL SILILMPFSL NYPLLSLHLL GIKIDASIWD GIWKMAVGGY EYTAFMIFIC AVVMPITFAL LVIMLWLAKI FQIKPRSVLL FLGYIKAWVM FDVYLVALGV TIFKVREYAT LEINIYLIPF IFTALLTTLL FIKLNLSALW QEFYPECTSV YTKQAVELCP ACHYTFTQKS IHYDHQQKIC CPRCQSPLNT SDKLKLQATW ATLIAGIIML FPANLLPISG IYLTGALSED TLISGVISFV KSGSYFVAFV VFFASIFVPI SKIFIMLYLL ACVHFKWQHS IKWQMRLLHL VHFVGRWSML DLFVLALMMS LVTRGEIINF TVGPGAFYFG AAVFCTMLST SQFDSKLIWK IYDREK // ID Y1672_HAEIN Reviewed; 881 AA. AC P44288; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein HI_1672; GN OrderedLocusNames=HI_1672; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the PqiB 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; L42023; AAC23317.1; -; Genomic_DNA. DR PIR; A64040; A64040. DR RefSeq; NP_439814.1; NC_000907.1. DR RefSeq; WP_005694394.1; NC_000907.1. DR STRING; 71421.HI1672; -. DR EnsemblBacteria; AAC23317; AAC23317; HI_1672. DR GeneID; 950502; -. DR KEGG; hin:HI1672; -. DR PATRIC; 20192095; VBIHaeInf48452_1751. DR eggNOG; ENOG4105DY2; Bacteria. DR eggNOG; COG3008; LUCA. DR OMA; RFWNISG; -. DR OrthoDB; EOG69WFM1; -. DR PhylomeDB; P44288; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003399; Mce/MlaD. DR Pfam; PF02470; MlaD; 3. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 881 Uncharacterized protein HI_1672. FT /FTId=PRO_0000169056. FT TRANSMEM 30 49 Helical. {ECO:0000255}. SQ SEQUENCE 881 AA; 96678 MW; C278E5822E6A4F55 CRC64; MTEKNNSSSI EEKYQERTAN LRKTKRISPF WLLPFIALCI GAILFFQIVK ERGTSITITF TNGSGIVADK TQIRYQGLQI GIVKEVHFTD NLQKVEVVAN INPEASSILR ENTKFWLVQP NVSLAGISGL DSLVSGNYIT LQPGDGDRED EFIAEEQGPI AQVSAGDLLI HLISDDLGSI SIGASVYFKK LPVGKIYDYR INKNNKVEID VVIDKAYAKF VKKDSRFWNI SGINANISPS GLNLNVESLN AVVQGAVSFD SPADSPKADE NSHFTLYTNL KAAKRGIEIK VTIPASSALI AGQTEVYSQD NAIGILAKLS AVENNDEILE GSLLIDPNQA SLFKANSKIV LRNKKIDLGN LAEPKKFFRG EYFDVIAGDG ETKHQFNVIK ENELLLNAPN TLVLTLTAPE NYGVSEGQNV FYNNMIIGQI VSQTIDVNGV QFKAAIASEY RNLIHENTQF VAATNFDISV GLDGLRFESA TPEKWLQGGV RVLTKQGLGK AKDSYPLYQN ISNAEHGITG NILTPTITLH TQTLPSIDKG SLVLYRQFEV GKILSIKPKT NNFDVDIYIY PAYQHLLTDK SRFWVESAAK IDVSPKGISI QATPLARSLK GAISFDNGGS GNNRTLYANE SYAKSIGFVI TLITDDATNL SKGMNLRYLG LDVGQIDSIQ LDAKAKRITA KALINPNYMN IIAKEGANFT IISPQISAGG IDNLDSLLQP YIDIEIGNGN TKTQFNLAQT APQRNKFSNG TPFILETRDA MNLSEGSPIL YRGVEVGTVK KFELNSLGDR VLVHIAIMPK YSHLVRQNTE FWIASGYDFS LGWKGAVFNT GSVQQLLKGG ISFSTPAEKE IQPQAQPNKR FLLQINRPEE VQTWGSGALS K // ID Y1696_HAEIN Reviewed; 294 AA. AC Q48214; O05082; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 17-FEB-2016, entry version 87. DE RecName: Full=Uncharacterized glycosyltransferase HI_1696; DE EC=2.4.-.-; GN OrderedLocusNames=HI_1696; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A2; RA McLaughlin R., Abu Kwaik Y., Young R., Spinola S., Apicella M.; RT "Characterization and sequence of the lsg locus from Haemophilus RT influenzae."; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; M94855; AAA24982.1; -; Genomic_DNA. DR EMBL; L42023; AAC23342.1; -; Genomic_DNA. DR PIR; D64175; D64175. DR RefSeq; NP_439838.1; NC_000907.1. DR RefSeq; WP_005694185.1; NC_000907.1. DR ProteinModelPortal; Q48214; -. DR STRING; 71421.HI1696; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC23342; AAC23342; HI_1696. DR GeneID; 950519; -. DR KEGG; hin:HI1696; -. DR PATRIC; 20192143; VBIHaeInf48452_1775. DR eggNOG; ENOG4108RJ9; Bacteria. DR eggNOG; ENOG4111G49; LUCA. DR OMA; IGGMPMI; -. DR OrthoDB; EOG6QRW62; -. DR PhylomeDB; Q48214; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 294 Uncharacterized glycosyltransferase FT HI_1696. FT /FTId=PRO_0000059234. FT CONFLICT 38 38 C -> Y (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 48 48 S -> R (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 70 70 V -> I (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 74 74 T -> A (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 88 88 C -> R (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 97 97 V -> I (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 106 106 N -> D (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 152 152 I -> V (in Ref. 1; AAA24982). FT {ECO:0000305}. FT CONFLICT 185 185 P -> S (in Ref. 1; AAA24982). FT {ECO:0000305}. SQ SEQUENCE 294 AA; 33646 MW; 8330F081BFF7A18B CRC64; MLSIIVPSYN RKAEVPALLE SLTQQTSSNF EVIIVDDCSK ERVVVEQSYS FPVTVIRNET NQGAAESRNV GARTSKGDWL LFLDDDDCFM PEKCEKVLQV IEQNPNINFI YHPAKCEMVN EGFTYVTQPI EPQEISTERI LLANKIGGMP MIAIKKEMFL KIGGLSTALR SLEDYDFLLK LLQEPSFTPY KINEPLTYCT FHTKRSSVST DTTNTQKAID YIREHYVKTV EQARNFDINA SYILAYPHIM NLSRKAAKYY FDIFKKTKSI KQFIITLVIL ISPKLAINLK RLGK // ID Y1709_HAEIN Reviewed; 121 AA. AC P44293; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Uncharacterized protein HI_1709; DE Flags: Precursor; GN OrderedLocusNames=HI_1709; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: To E.coli YgiW. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23355.1; -; Genomic_DNA. DR PIR; F64040; F64040. DR RefSeq; NP_439851.1; NC_000907.1. DR RefSeq; WP_005631924.1; NC_000907.1. DR ProteinModelPortal; P44293; -. DR STRING; 71421.HI1709; -. DR EnsemblBacteria; AAC23355; AAC23355; HI_1709. DR GeneID; 950526; -. DR KEGG; hin:HI1709; -. DR PATRIC; 20192169; VBIHaeInf48452_1788. DR eggNOG; ENOG4105WXI; Bacteria. DR eggNOG; COG3111; LUCA. DR OMA; RWDGQTI; -. DR OrthoDB; EOG6WQD91; -. DR PhylomeDB; P44293; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR Gene3D; 2.40.50.200; -; 1. DR InterPro; IPR005220; BOF. DR InterPro; IPR016052; Phage_933W_L0136. DR Pfam; PF04076; BOF; 1. DR SUPFAM; SSF101756; SSF101756; 1. DR TIGRFAMs; TIGR00156; TIGR00156; 1. PE 1: Evidence at protein level; KW Complete proteome; Periplasm; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 121 Uncharacterized protein HI_1709. FT /FTId=PRO_0000013903. SQ SEQUENCE 121 AA; 13231 MW; 0CC475D37C5E2C8F CRC64; MKKFALATIF ALATTSAFAG FNGNNSQGGF QQAAPAAISV KQALSAADNS MITLVGNITQ QIDDDEFWFT DGTGQIKIEI KKRVWNGLNV DSKDKVKIYG KLDNEVFEKA ELDVLRIEKA E // ID Y224_HAEIN Reviewed; 168 AA. AC P44580; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0224; GN OrderedLocusNames=HI_0224; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH asnC-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00319}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21893.1; -; Genomic_DNA. DR PIR; B64056; B64056. DR RefSeq; NP_438396.2; NC_000907.1. DR ProteinModelPortal; P44580; -. DR STRING; 71421.HI0224; -. DR EnsemblBacteria; AAC21893; AAC21893; HI_0224. DR GeneID; 951138; -. DR KEGG; hin:HI0224; -. DR PATRIC; 20188969; VBIHaeInf48452_0237. DR eggNOG; ENOG4105FKN; Bacteria. DR eggNOG; COG1522; LUCA. DR KO; K03719; -. DR OMA; ATMPIAE; -. DR OrthoDB; EOG6F29D2; -. DR BioCyc; RETL1328306-WGS:GSTH-5499-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-6439-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-6466-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 168 Uncharacterized HTH-type transcriptional FT regulator HI_0224. FT /FTId=PRO_0000111750. FT DOMAIN 19 80 HTH asnC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. FT DNA_BIND 38 57 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. SQ SEQUENCE 168 AA; 19577 MW; F13BE2CD6CF5EDBB CRC64; MIIFFSIVTF LRNYLMQTLD KLDRHILNVL QQDAMIPLKE LSEKVNSSVA TCQRRVQSLT DSGIITKRVA VVSPKAVGRT ISVFVMVEMD NQHSYYQEQF ERKMRQEDEV VSCYEISGDY DFMLLLHAKD MESYHAFTRR VLTGEFHVRT YKSLFVMNFT KADSGIIL // ID Y277_HAEIN Reviewed; 161 AA. AC P44609; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 81. DE RecName: Full=UPF0225 protein HI_0277; GN OrderedLocusNames=HI_0277; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0225 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; L42023; AAC21942.1; -; Genomic_DNA. DR PIR; I64146; I64146. DR RefSeq; NP_438446.1; NC_000907.1. DR RefSeq; WP_005694029.1; NC_000907.1. DR ProteinModelPortal; P44609; -. DR EnsemblBacteria; AAC21942; AAC21942; HI_0277. DR GeneID; 949404; -. DR KEGG; hin:HI0277; -. DR PATRIC; 20189091; VBIHaeInf48452_0292. DR eggNOG; ENOG4105K5B; Bacteria. DR eggNOG; COG3012; LUCA. DR KO; K09858; -. DR OMA; CCGHYHA; -. DR OrthoDB; EOG6WMJ4X; -. DR PhylomeDB; P44609; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.10.450.50; -; 1. DR HAMAP; MF_00612; UPF0225; 1. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR004027; SEC_C_motif. DR InterPro; IPR023006; UPF0225. DR Pfam; PF02810; SEC-C; 1. DR SUPFAM; SSF54427; SSF54427; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 161 UPF0225 protein HI_0277. FT /FTId=PRO_0000071806. SQ SEQUENCE 161 AA; 18372 MW; DA2A1A4DB82F7498 CRC64; MSEISTALSL ENCPCQSSHH YADCCGKFHL RQAFPETAEQ LMRSRYTAYV LKNIPYIVVT TVPSQQTLLK PRLLQEWADN TTWLGLEILK TESLTKTQSA VEFKAIFQGE ECEQAHQERS IFVKIEDRWY FVDPTVSLPT MKQPCVCGSG KKFKHCCGGF L // ID Y281_HAEIN Reviewed; 438 AA. AC P44610; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Putative metabolite transport protein HI_0281; GN OrderedLocusNames=HI_0281; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar CC transporter (TC 2.A.1.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21944.1; -; Genomic_DNA. DR PIR; A64147; A64147. DR RefSeq; NP_438449.1; NC_000907.1. DR RefSeq; WP_005660680.1; NC_000907.1. DR ProteinModelPortal; P44610; -. DR STRING; 71421.HI0281; -. DR EnsemblBacteria; AAC21944; AAC21944; HI_0281. DR GeneID; 950652; -. DR KEGG; hin:HI0281; -. DR PATRIC; 20189101; VBIHaeInf48452_0297. DR eggNOG; ENOG4105CSH; Bacteria. DR eggNOG; ENOG410XP7I; LUCA. DR OMA; GLLCAFK; -. DR OrthoDB; EOG6SZ1HS; -. DR PhylomeDB; P44610; -. DR Proteomes; UP000000579; 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:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004736; Cit_H_symport. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005829; Sugar_transporter_CS. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00883; 2A0106; 1. DR PROSITE; PS50850; MFS; 1. DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 438 Putative metabolite transport protein FT HI_0281. FT /FTId=PRO_0000050488. FT TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 18 38 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 39 52 Periplasmic. {ECO:0000255}. FT TRANSMEM 53 73 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 74 85 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 86 106 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 107 115 Periplasmic. {ECO:0000255}. FT TRANSMEM 116 136 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 137 156 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 157 177 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 178 181 Periplasmic. {ECO:0000255}. FT TRANSMEM 182 202 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 203 239 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 240 260 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 261 286 Periplasmic. {ECO:0000255}. FT TRANSMEM 287 307 Helical; Name=8. {ECO:0000255}. FT TOPO_DOM 308 314 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 315 336 Helical; Name=9. {ECO:0000255}. FT TOPO_DOM 337 342 Periplasmic. {ECO:0000255}. FT TRANSMEM 343 363 Helical; Name=10. {ECO:0000255}. FT TOPO_DOM 364 377 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 378 398 Helical; Name=11. {ECO:0000255}. FT TOPO_DOM 399 405 Periplasmic. {ECO:0000255}. FT TRANSMEM 406 426 Helical; Name=12. {ECO:0000255}. FT TOPO_DOM 427 438 Cytoplasmic. {ECO:0000255}. SQ SEQUENCE 438 AA; 46900 MW; D3A01A3EAF9DFCAB CRC64; MSTQLRNNPM KVALASMVGT AIEFFDYYIY AAAAVLVFNT QFFHSDDPLS NDLLSLSTLA LAFFARPIGS ALFGHFGDKI GRKKTLVASL VLMGGSTVVI GLLPNYAQIG IWAPILLCVC RVGQGIGLGG EWGGAALVAT ENAPEGKRAW YGTFPQLGAP IGLFVANGTF FLVSYLLGHN ALVEWAWRIP FVSSILLVAV GLYVRLTLHE SHVFVEAEQK GKKLNAPVSV VFTKHLKPMV IGTFIMVATY SLFYIMTAFA QAYSRTAPKL SEAGYALGLG IPANTFTGLL LISAIVFGIF ISISGFYADK IGRRKWLIWV TIAIGVLGLA MPLFLENGTP VSVFAFLVIG MAIMGMTFGP MAALLPELFP TEVRYSGASL AYNLASIIGA TIAAMISLKI NASFGVMGVG IYLAINALMT FLALLASKET KNVDLTEI // ID Y291_HAEIN Reviewed; 68 AA. AC P43979; Q57196; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized protein HI_0291; GN OrderedLocusNames=HI_0291; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Contains 1 HMA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21964.1; -; Genomic_DNA. DR PIR; F64005; F64005. DR RefSeq; NP_438458.1; NC_000907.1. DR RefSeq; WP_005656255.1; NC_000907.1. DR ProteinModelPortal; P43979; -. DR STRING; 71421.HI0291; -. DR EnsemblBacteria; AAC21964; AAC21964; HI_0291. DR GeneID; 949416; -. DR KEGG; hin:HI0291; -. DR PATRIC; 20189121; VBIHaeInf48452_0307. DR eggNOG; COG2608; LUCA. DR OMA; GMGCQNC; -. DR OrthoDB; EOG6742RM; -. DR PhylomeDB; P43979; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 68 Uncharacterized protein HI_0291. FT /FTId=PRO_0000077906. FT DOMAIN 3 68 HMA. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. FT METAL 13 13 {ECO:0000255|PROSITE-ProRule:PRU00280}. FT METAL 16 16 {ECO:0000255|PROSITE-ProRule:PRU00280}. SQ SEQUENCE 68 AA; 7378 MW; 4E2D11F03D4DD8B8 CRC64; MKTITLNIKG IHCGCCVKNL TQVLTELDGV QSADVQLEGK ANITFDENRV NVAQLIEVIE DAGFDATE // ID Y292_HAEIN Reviewed; 68 AA. AC O32622; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein HI_0292; GN OrderedLocusNames=HI_0292; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HMA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21956.1; -; Genomic_DNA. DR PIR; H64059; H64059. DR RefSeq; NP_438459.1; NC_000907.1. DR RefSeq; WP_005631184.1; NC_000907.1. DR ProteinModelPortal; O32622; -. DR STRING; 71421.HI0292; -. DR EnsemblBacteria; AAC21956; AAC21956; HI_0292. DR GeneID; 949615; -. DR KEGG; hin:HI0292; -. DR PATRIC; 20189123; VBIHaeInf48452_0308. DR eggNOG; COG2608; LUCA. DR KO; K07213; -. DR OMA; MANQTRI; -. DR OrthoDB; EOG6742RM; -. DR PhylomeDB; O32622; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030001; P:metal ion transport; IEA:InterPro. DR InterPro; IPR017969; Heavy-metal-associated_CS. DR InterPro; IPR006121; HMA_dom. DR Pfam; PF00403; HMA; 1. DR SUPFAM; SSF55008; SSF55008; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 68 Uncharacterized protein HI_0292. FT /FTId=PRO_0000077907. FT DOMAIN 3 68 HMA. {ECO:0000255|PROSITE- FT ProRule:PRU00280}. FT METAL 13 13 {ECO:0000255|PROSITE-ProRule:PRU00280}. FT METAL 16 16 {ECO:0000255|PROSITE-ProRule:PRU00280}. SQ SEQUENCE 68 AA; 7351 MW; 4E39972B447DD8B8 CRC64; MKTITLNIKG IHCGCCVKSL TQVLTELDGV QSADVQLEGK ANITFDENRV NVAQLIEVIE DAGFDATE // ID Y325_HAEIN Reviewed; 450 AA. AC P44640; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 95. DE RecName: Full=Uncharacterized membrane protein HI_0325; GN OrderedLocusNames=HI_0325; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21988.1; -; Genomic_DNA. DR PIR; A64148; A64148. DR RefSeq; NP_438490.1; NC_000907.1. DR RefSeq; WP_005694344.1; NC_000907.1. DR STRING; 71421.HI0325; -. DR EnsemblBacteria; AAC21988; AAC21988; HI_0325. DR GeneID; 950706; -. DR KEGG; hin:HI0325; -. DR PATRIC; 20189191; VBIHaeInf48452_0342. DR eggNOG; ENOG4105D3Y; Bacteria. DR eggNOG; COG2056; LUCA. DR KO; K07084; -. DR OMA; NHIYDTC; -. DR OrthoDB; EOG6D5G41; -. DR PhylomeDB; P44640; -. DR Proteomes; UP000000579; 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; IPR018461; Na/H_Antiport_NhaC-like_C. DR InterPro; IPR032813; Na_H_antiport_N. DR Pfam; PF13726; Na_H_antiport_2; 1. DR Pfam; PF03553; Na_H_antiporter; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 450 Uncharacterized membrane protein HI_0325. FT /FTId=PRO_0000077911. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 242 262 Helical. {ECO:0000255}. FT TRANSMEM 267 287 Helical. {ECO:0000255}. FT TRANSMEM 302 322 Helical. {ECO:0000255}. FT TRANSMEM 343 363 Helical. {ECO:0000255}. FT TRANSMEM 378 398 Helical. {ECO:0000255}. FT TRANSMEM 428 448 Helical. {ECO:0000255}. SQ SEQUENCE 450 AA; 47440 MW; AFD139E73FD6B061 CRC64; MLSNPVVISI IVLLALSLLR INVIIALVIA ALTAGFIGDL GLTKTIETFT GGLGGGAEVA MNYAILGAFA IAISKSGITD LIAYKIITKM NKTPTAGNLT WFKYFIFAVL ALFAISSQNL LPVHIAFIPI VVPPLLSIFN RLKIDRRAVA CVLTFGLTAT YILLPVGFGK IFIESILVKN INQAGATLGL QTNVAQVSLA MLLPVIGMIL GLLTAIFITY RKPREYNINV EEATTKDIEA HIANIKPKQI VASLIAIVAT FATQLVTSST IIGGLIGLII FVLCGIFKLK ESNDIFQQGL RLMAMIGFVM IAASGFANVI NATTGVTDLV QSLSSGVVQS KGIAALLMLV VGLLITMGIG SSFSTVPIIT SIYVPLCLSF GFSPLATISI VGVAAALGDA GSPASDSTLG PTSGLNMDGK HDHIWDSVVP TFIHYNIPLL VFGWIAAMYL // ID Y338_HAEIN Reviewed; 348 AA. AC P44646; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 93. DE RecName: Full=UPF0118 membrane protein HI_0338; GN OrderedLocusNames=HI_0338; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0118 (PerM) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22000.1; -; Genomic_DNA. DR PIR; E64148; E64148. DR RefSeq; NP_438502.1; NC_000907.1. DR RefSeq; WP_005694337.1; NC_000907.1. DR STRING; 71421.HI0338; -. DR EnsemblBacteria; AAC22000; AAC22000; HI_0338. DR GeneID; 949451; -. DR KEGG; hin:HI0338; -. DR PATRIC; 20189219; VBIHaeInf48452_0355. DR eggNOG; ENOG4105DSF; Bacteria. DR eggNOG; COG0628; LUCA. DR OMA; MGNMVEP; -. DR OrthoDB; EOG6VTK3P; -. DR PhylomeDB; P44646; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 348 UPF0118 membrane protein HI_0338. FT /FTId=PRO_0000148303. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 267 287 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. SQ SEQUENCE 348 AA; 38163 MW; 23548566252A0310 CRC64; MQNNLNLHRT LLGIAAVIII LAGVKLAAEI VVPFLLSLFI AIICSPIIKA MTQRRVPHWL AITLLFVLIS LVFFFLVGLI NSTAREFTQS IPQYKVLLSQ RVSDLTGLLQ RFNLPFTLSR ETIQENFDPS IIMNFVSRVL LNFSGVVSNV FVLVLVVIFM LAEAPTMKHK FAMVISSTPH DVAKEERHID RVLQGVIGYL GIKSITSLLT GVGVFILLEA CRVQYAILWA TLSFLLNYIP NIGSIIAAIP IIVQALLLNG FGIGFGVAIG VIAINMVVGN IIEPKMMGQR LGLSTLVVFL SLLFWGWLLG TVGMLLSVPL TMALKIALES SPNTAKYACL LGDVEDFK // ID Y361_HAEIN Reviewed; 306 AA. AC P44662; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Probable iron transport system ATP-binding protein HI_0361; GN OrderedLocusNames=HI_0361; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of an ATP-driven transport system CC HI_0359/HI_0360/HI_0361/HI_0362 for iron. Probably responsible for CC energy coupling to the transport system. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; CC Peripheral 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; L42023; AAC22020.1; -; Genomic_DNA. DR PIR; F64063; F64063. DR RefSeq; NP_438523.1; NC_000907.1. DR RefSeq; WP_005630123.1; NC_000907.1. DR ProteinModelPortal; P44662; -. DR STRING; 71421.HI0361; -. DR EnsemblBacteria; AAC22020; AAC22020; HI_0361. DR GeneID; 950559; -. DR KEGG; hin:HI0361; -. DR PATRIC; 20189267; VBIHaeInf48452_0379. DR eggNOG; ENOG4105DIK; Bacteria. DR eggNOG; COG1121; LUCA. DR KO; K11607; -. DR OMA; DWTFPVL; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; P44662; -. DR Proteomes; UP000000579; 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:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; 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; Cell inner membrane; Cell membrane; Complete proteome; KW Ion transport; Iron; Iron transport; Membrane; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 306 Probable iron transport system ATP- FT binding protein HI_0361. FT /FTId=PRO_0000093200. FT DOMAIN 8 243 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 41 48 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 306 AA; 34251 MW; 8A725B71E52C6C70 CRC64; MDSFSTSIWV NDVTVRYNNG HTAIHNMTFS LNSGTICALV GVNGSGKSTL FKSIMGLVKP QQGEIKLCDL PISQALKRNL VAYVPQSEEV DWQFPVSVYD VVMMGRYGYM NFLRIPKAID KQKVQEAMQR VNIEHLAHRQ IGELSGGQKK RVFLARALAQ QSPIILLDEP FTGVDVKTEN AIVDLLQQLR EEGHLILVST HNLGSVPDFC DQVVMINRTV IAAGKTEDTF NQHNLEIVFG GVLRHIKLLG ENLHNDEDKR SVTVLTDDEK AVVFYGETKQ DPPAPTTQNC HFEDCPYKSA VKNKRD // ID Y391_HAEIN Reviewed; 182 AA. AC P43992; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0391; GN OrderedLocusNames=HI_0391; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22050.1; -; Genomic_DNA. DR PIR; A64007; A64007. DR STRING; 71421.HI0391; -. DR EnsemblBacteria; AAC22050; AAC22050; HI_0391. DR PATRIC; 20189333; VBIHaeInf48452_0410. DR eggNOG; COG1835; LUCA. DR OrthoDB; EOG6D2KRT; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.50.1110; -; 1. DR InterPro; IPR013830; SGNH_hydro. DR SUPFAM; SSF52266; SSF52266; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 182 Uncharacterized protein HI_0391. FT /FTId=PRO_0000077918. SQ SEQUENCE 182 AA; 21053 MW; 96B5F1BB5205EDB0 CRC64; MDKNNKITPE CQGLLDEINS PKYKAIFISG FYDLRMGGQP VPRFNAQASF IDNFKTRFVE TVKLLAKSKS VYIFANNSSI SRSPIRGYLL GKYGLEKYLE PIRRMGDIDA SNKIIHDLVK DIPNVYWVDA QQYLPKDSVM AEGKYLYGDQ DHLTNFGAYY MAKEFSKYQR VMTPEQVKKL YE // ID Y420_HAEIN Reviewed; 99 AA. AC P43995; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_0420; GN OrderedLocusNames=HI_0420; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22082.1; -; Genomic_DNA. DR PIR; D64007; D64007. DR RefSeq; NP_438582.1; NC_000907.1. DR RefSeq; WP_005693744.1; NC_000907.1. DR ProteinModelPortal; P43995; -. DR STRING; 71421.HI0420; -. DR EnsemblBacteria; AAC22082; AAC22082; HI_0420. DR GeneID; 949520; -. DR KEGG; hin:HI0420; -. DR PATRIC; 20189393; VBIHaeInf48452_0440. DR eggNOG; ENOG4105UKP; Bacteria. DR eggNOG; COG4453; LUCA. DR OMA; LADQECF; -. DR OrthoDB; EOG6Q5P0V; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR014795; Vibrio_phage_ICP1_Orf50. DR Pfam; PF08681; DUF1778; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 99 Uncharacterized protein HI_0420. FT /FTId=PRO_0000077921. SQ SEQUENCE 99 AA; 11055 MW; D97590E0EE2057F6 CRC64; MKTQVTKARL EAKVNIDIYE LLKQAAAITG RTLTDFVVSV AYEEAKKTIS EHQVLRLAVN DQALLIESLS KPFEPNPSMK NALDVYEAYL SITGKNNDK // ID Y452_HAEIN Reviewed; 432 AA. AC P44717; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=UPF0053 protein HI_0452; GN OrderedLocusNames=HI_0452; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22110.1; -; Genomic_DNA. DR PIR; H64152; H64152. DR RefSeq; NP_438613.1; NC_000907.1. DR RefSeq; WP_010868987.1; NC_000907.1. DR ProteinModelPortal; P44717; -. DR SMR; P44717; 351-427. DR STRING; 71421.HI0452; -. DR EnsemblBacteria; AAC22110; AAC22110; HI_0452. DR GeneID; 949660; -. DR KEGG; hin:HI0452; -. DR PATRIC; 20189459; VBIHaeInf48452_0472. DR eggNOG; ENOG4105C37; Bacteria. DR eggNOG; COG1253; LUCA. DR OMA; QPHSKFL; -. DR OrthoDB; EOG60W7V4; -. DR PhylomeDB; P44717; -. DR Proteomes; UP000000579; 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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR002550; DUF21. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR005170; Transptr-assoc_dom. DR Pfam; PF00571; CBS; 1. DR Pfam; PF03471; CorC_HlyC; 1. DR Pfam; PF01595; DUF21; 1. DR SMART; SM01091; CorC_HlyC; 1. DR SUPFAM; SSF56176; SSF56176; 1. 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 1 432 UPF0053 protein HI_0452. FT /FTId=PRO_0000088365. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT DOMAIN 9 201 DUF21. FT DOMAIN 220 279 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 286 345 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 432 AA; 48708 MW; 828EBD30B046D96B CRC64; MIMELFHTIL AIVALILSSA VVSSAEISLA SPRKLKLQSL ANKGDVRPLQ VLKLQEHPGR FITVVQILLN MVAILGGGIG ESALSPYIAD ILNRSFEGSW IAPTASTIAF ILVTCLFILF ADLIPKRIAI TYPEMVALSV VGIMNFSMYV FKPLVWFFDT IANVFFRLFR ISTVREDGMT SEDIFAVVEA GAEAGVLKTQ EHYLIENIFD MQARTVTSTM TTRENIVYLD RTFSRQEVMD TLSRDSHSKI VICDNGLDKI LGYIESHTLL TMYLQNENVV LTDPKLLRKA LFVPDTLSLY EVLELFKSTG EDFAIIVNEY ALVVGIVTLN DVMSIVMGEL VSNEEEYIVS RDENSWLIDG ATPLEEVTRV LDIAYFPDEE NYETISGFMM YMLRKIPKKT DSVVYGKYKF EVIDTENFKI DQILVSLVKE QE // ID Y488_HAEIN Reviewed; 200 AA. AC P44004; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Uncharacterized protein HI_0488; GN OrderedLocusNames=HI_0488; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC CbbY/CbbZ/Gph/YieH 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; L42023; AAC22147.1; -; Genomic_DNA. DR PIR; D64008; D64008. DR RefSeq; NP_438649.1; NC_000907.1. DR RefSeq; WP_005652027.1; NC_000907.1. DR ProteinModelPortal; P44004; -. DR STRING; 71421.HI0488; -. DR DNASU; 949569; -. DR EnsemblBacteria; AAC22147; AAC22147; HI_0488. DR GeneID; 949569; -. DR KEGG; hin:HI0488; -. DR PATRIC; 20189531; VBIHaeInf48452_0508. DR eggNOG; ENOG4107VXZ; Bacteria. DR eggNOG; COG0637; LUCA. DR OMA; IECTHRV; -. DR OrthoDB; EOG6091HT; -. DR PhylomeDB; P44004; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 200 Uncharacterized protein HI_0488. FT /FTId=PRO_0000108064. SQ SEQUENCE 200 AA; 22522 MW; ED7C6B65F26C535D CRC64; MLDYEIFNPY EGLIFDMDGT LIDTMPVHAQ AWTMVGKKFG YEFDFQIMYN FGGATVRTIA GEMMKAANMP LDRIEDVLAA KRELSYQLIP TQSKLLPTFE IVKSFHQKKP IALGSGSHRK IIDMLMDKLA IAPYFNAIVS ADDVKEHKPH PETFLRCAEL IQANPSRCIV FEDADLGVQA GLSAGMDVFD VRTREIISPR // ID Y489_HAEIN Reviewed; 157 AA. AC P44005; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 87. DE RecName: Full=Uncharacterized protein HI_0489; GN OrderedLocusNames=HI_0489; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YqaA. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22148.1; -; Genomic_DNA. DR PIR; E64008; E64008. DR RefSeq; NP_438650.1; NC_000907.1. DR RefSeq; WP_005693683.1; NC_000907.1. DR STRING; 71421.HI0489; -. DR EnsemblBacteria; AAC22148; AAC22148; HI_0489. DR GeneID; 949626; -. DR KEGG; hin:HI0489; -. DR PATRIC; 20189533; VBIHaeInf48452_0509. DR eggNOG; ENOG4105W39; Bacteria. DR eggNOG; COG1238; LUCA. DR OMA; EHRLWIM; -. DR OrthoDB; EOG6VF37Q; -. DR PhylomeDB; P44005; -. DR Proteomes; UP000000579; 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; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 157 Uncharacterized protein HI_0489. FT /FTId=PRO_0000169308. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. SQ SEQUENCE 157 AA; 17492 MW; 11B3CFC32BE798EC CRC64; MDIFSFFSAD FWQANSLCFM FISAFLSATV LPGNSEVIFV ALAVPKLMLG SLFNVDILAL ILIATAGNSL GSLTTYGIGR WMPKFDPKNY RTLWAINQLR RYGAIALLLS WLPVVGDLFC AIAGWLRLNF VTSSLFIFLG KMVRYVALLF LSTPFLL // ID Y520_HAEIN Reviewed; 262 AA. AC P44743; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Putative glycyl-radical enzyme activating enzyme HI_0520 {ECO:0000305}; DE Short=GRE activating enzyme HI_0520 {ECO:0000305}; DE EC=1.97.1.- {ECO:0000305}; GN OrderedLocusNames=HI_0520; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0A9N4}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:P0A9N4}; CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes 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; L42023; AAC22178.1; -; Genomic_DNA. DR PIR; B64154; B64154. DR RefSeq; NP_438678.1; NC_000907.1. DR RefSeq; WP_005694124.1; NC_000907.1. DR ProteinModelPortal; P44743; -. DR STRING; 71421.HI0520; -. DR EnsemblBacteria; AAC22178; AAC22178; HI_0520. DR GeneID; 949583; -. DR KEGG; hin:HI0520; -. DR PATRIC; 20189593; VBIHaeInf48452_0539. DR eggNOG; ENOG41076CZ; Bacteria. DR eggNOG; COG1180; LUCA. DR OMA; TDKFLFD; -. DR OrthoDB; EOG6ZPSX5; -. DR PhylomeDB; P44743; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 262 Putative glycyl-radical enzyme activating FT enzyme HI_0520. FT /FTId=PRO_0000200543. FT REGION 40 42 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT REGION 130 132 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 34 34 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 81 81 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 262 AA; 29496 MW; D76E061F201AFC3F CRC64; MTALSEIFVP LHRIIPFSNV EGQGNRSSIF LQGCKLNCLY CHNPETIPRY TESAKLVSLQ YLYEQVMEAV PFIRGVTVSG GEPTIHHKKL VPLFKALRSQ GLTCYLDSSG FFEFDRVCSL IDVTDKFLFD LKGEGIGLQT LCFDRKNQAG IVPQQVIPER LHIKNDKLER NLQNLAALLP LNKVEEVRLV FLKHFFDAEH LVGKVAQLLR NYPDVALKII RVHSKGVRDE AGLSAYIPSV EETNALSAYA RQCGINKILT IL // ID Y586_HAEIN Reviewed; 145 AA. AC P44019; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative uncharacterized transporter HI_0586; GN OrderedLocusNames=HI_0586; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DcuC/DcuD transporter (TC 2.A.61) CC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22250.1; -; Genomic_DNA. DR PIR; A64010; A64010. DR STRING; 71421.HI0586; -. DR EnsemblBacteria; AAC22250; AAC22250; HI_0586. DR PATRIC; 20189729; VBIHaeInf48452_0607. DR eggNOG; COG3069; LUCA. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 5: Uncertain; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 145 Putative uncharacterized transporter FT HI_0586. FT /FTId=PRO_0000201634. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. SQ SEQUENCE 145 AA; 15226 MW; 211213504489AA7D CRC64; MELFKSIVAV IGIIATIYFL IKKAETRTVL IGVGLIMSIL TLNPMGALDA FAKSMTSGGL IMAICSSMGF AYVMKYTQCD THLVHLLTKP LSGLKFFLIP IATIITFFIN IAIPSAAGCA AAVGATLIPV LKSAGVRPAT AGQLF // ID Y592_HAEIN Reviewed; 64 AA. AC P44021; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 48. DE RecName: Full=Uncharacterized protein HI_0592; GN OrderedLocusNames=HI_0592; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22259.1; -; Genomic_DNA. DR PIR; C64010; C64010. DR EnsemblBacteria; AAC22259; AAC22259; HI_0592. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR021237; DUF2618. DR Pfam; PF10940; DUF2618; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 64 Uncharacterized protein HI_0592. FT /FTId=PRO_0000077937. SQ SEQUENCE 64 AA; 7776 MW; D058E8A5BAA2117D CRC64; MLFRTYIHRY VHTKALRFLR FNPIKGRSLM AHIRRTRHIM MPSYRSCFSY SLFASQNKPS NRAL // ID Y665_HAEIN Reviewed; 343 AA. AC P44033; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative kinase HI_0665; DE EC=2.-.-.-; GN OrderedLocusNames=HI_0665; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the HipA Ser/Thr 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; L42023; AAC22325.1; -; Genomic_DNA. DR PIR; F64011; F64011. DR RefSeq; NP_438824.1; NC_000907.1. DR RefSeq; WP_005694624.1; NC_000907.1. DR STRING; 71421.HI0665; -. DR DNASU; 949704; -. DR EnsemblBacteria; AAC22325; AAC22325; HI_0665. DR GeneID; 949704; -. DR KEGG; hin:HI0665; -. DR PATRIC; 20189945; VBIHaeInf48452_0694. DR eggNOG; ENOG4108KSB; Bacteria. DR eggNOG; COG3550; LUCA. DR KO; K07154; -. DR OMA; EQYVSYE; -. DR OrthoDB; EOG6Q2SGF; -. DR PhylomeDB; P44033; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR012893; HipA-like_C. DR InterPro; IPR012894; HipA_N2. DR Pfam; PF07804; HipA_C; 1. DR Pfam; PF07805; HipA_N; 1. PE 3: Inferred from homology; KW Complete proteome; Kinase; Reference proteome; Transferase. FT CHAIN 1 343 Putative kinase HI_0665. FT /FTId=PRO_0000077942. FT ACT_SITE 209 209 Proton acceptor. {ECO:0000255}. SQ SEQUENCE 343 AA; 39832 MW; 711D46887A97EF03 CRC64; MNFCRILLKP LKKNEALSGY SAEGLHYLTD NKHFNPELPF SRQEFITVKP QKQQGMSISG FQPKLQLIIK DEHFDSVNQQ GNYILKPSPE EYPFLAENEH ATMRIMKELG FDVPENGLVS FAGEQNHKEF AFVITRFDRD KQQKPMHQEQ LDGAMNIRDK YGKIGADNEQ YVSYEQIAKF ILQHTENHLA QQREIFRRII YAYLLGNNDL HLRNFSFIYP KNSHPKLAPI YDFVSVSPYP EIFNSTLLAL PLLAREEGNA TLAKGFNTQY GEYIGDDFVE FGENIGLNKN VIIQKLIPEI IQEKEKVEQI YSQSFMPQPH IDCVLKTYRK RLALLNLLNE PEL // ID Y687_HAEIN Reviewed; 304 AA. AC P71356; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized transporter HI_0687; GN OrderedLocusNames=HI_0687; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the EamA transporter family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 EamA domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22347.1; -; Genomic_DNA. DR PIR; H64156; H64156. DR RefSeq; NP_438847.1; NC_000907.1. DR RefSeq; WP_005694611.1; NC_000907.1. DR STRING; 71421.HI0687; -. DR EnsemblBacteria; AAC22347; AAC22347; HI_0687. DR GeneID; 949720; -. DR KEGG; hin:HI0687; -. DR PATRIC; 20189993; VBIHaeInf48452_0718. DR eggNOG; ENOG4108P11; Bacteria. DR eggNOG; COG0697; LUCA. DR OMA; EITYVMM; -. DR OrthoDB; EOG66HVHB; -. DR Proteomes; UP000000579; 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; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 304 Uncharacterized transporter HI_0687. FT /FTId=PRO_0000108191. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. FT TRANSMEM 222 242 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. FT TRANSMEM 278 298 Helical. {ECO:0000255}. FT DOMAIN 13 148 EamA 1. FT DOMAIN 171 298 EamA 2. SQ SEQUENCE 304 AA; 33887 MW; CC7095529E8E4FB3 CRC64; MNNENMVRVF YVLLMGLGFP IMRFMSIHFE TLNNNSVRFL SGGSLFVIIC LIKFRSELKK IIGEPKIILY LFIYLFILGI FMTGNMFFFI NGLKYTSALA GSIFGILAMP LAIIIAGIFF KDERDRIRQK EFYIGELLAI IGSLIFVINS SNNDGNTDFF LGAIFLFTAI FIQSVQNLIV KKVAKKINAV VISASTATIS GVLFLCLAFN TKQIYLLQDV GIGMLIGLVC AGFYGMLTGM LMAFYIVQKQ GITVFNILQL LIPLSTAIIG YLTLDERINI YQGISGIIVI IGCVLALKRK NKEC // ID Y688_HAEIN Reviewed; 103 AA. AC P44037; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein HI_0688; GN OrderedLocusNames=HI_0688; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Eagan / Serotype B, and HK695 / Serotype B; RA Song X.M., Janson H.; RT "Different organization and regulation of the glpTQ operons between RT type b and nontypeable Haemophilus influenzae."; RL Submitted (MAR-1999) 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; L42023; AAC22349.1; -; Genomic_DNA. DR EMBL; AF132899; AAD38340.1; -; Genomic_DNA. DR EMBL; AF132900; AAD38342.1; -; Genomic_DNA. DR PIR; A64012; A64012. DR RefSeq; NP_438848.1; NC_000907.1. DR RefSeq; WP_010869032.1; NC_000907.1. DR STRING; 71421.HI0688; -. DR EnsemblBacteria; AAC22349; AAC22349; HI_0688. DR GeneID; 949721; -. DR KEGG; hin:HI0688; -. DR PATRIC; 20189995; VBIHaeInf48452_0719. DR eggNOG; ENOG4106YKR; Bacteria. DR eggNOG; ENOG410YUEP; LUCA. DR OMA; HGINDFG; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 103 Uncharacterized protein HI_0688. FT /FTId=PRO_0000077945. SQ SEQUENCE 103 AA; 11730 MW; E60D900FF867294D CRC64; MFELDILGKD GRIKLLNNAE TYELYQYSNK NNSAGNDYKS LILTCREDND YQSERMIKAI KNIIHCMTNN HQPISSAETS LETIKIIHGI INSVKIGNDP NNI // ID Y703_HAEIN Reviewed; 192 AA. AC P44832; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 74. DE RecName: Full=Uncharacterized protein HI_0703; GN OrderedLocusNames=HI_0703; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22362.1; -; Genomic_DNA. DR PIR; E64087; E64087. DR RefSeq; NP_438862.1; NC_000907.1. DR RefSeq; WP_005694589.1; NC_000907.1. DR STRING; 71421.HI0703; -. DR EnsemblBacteria; AAC22362; AAC22362; HI_0703. DR GeneID; 949729; -. DR KEGG; hin:HI0703; -. DR PATRIC; 20190025; VBIHaeInf48452_0734. DR eggNOG; ENOG4108UM1; Bacteria. DR eggNOG; COG1238; LUCA. DR OMA; AAWGGEK; -. DR OrthoDB; EOG6384KV; -. DR PhylomeDB; P44832; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 192 Uncharacterized protein HI_0703. FT /FTId=PRO_0000077946. SQ SEQUENCE 192 AA; 21688 MW; 003F53DCA5273BE0 CRC64; MKIFGTMYDK TMEWSKHRFA VFWLSFVSFI EAIFFPIPPD VMLIPMSMSK PKSAVKFAFY TAIASVIGGI IGYAIGFYAT DWVENIVQQW GYAAHWAKAV SWFEQWGVLV VFVAGFSPIP YKVFTLCAGV MQMAFFPFVI TAFVSRLARF LLVAKLAAWG GEKFAAKLRK SIEIIGWSVV VLAVIAYFIL KN // ID Y719_HAEIN Reviewed; 130 AA. AC P44839; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 106. DE RecName: Full=RutC family protein HI_0719; GN OrderedLocusNames=HI_0719; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RutC 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; L42023; AAC22376.1; -; Genomic_DNA. DR PIR; C64157; C64157. DR RefSeq; NP_438877.1; NC_000907.1. DR RefSeq; WP_005633088.1; NC_000907.1. DR PDB; 1J7H; NMR; -; A/B/C=1-130. DR PDBsum; 1J7H; -. DR ProteinModelPortal; P44839; -. DR SMR; P44839; 1-130. DR STRING; 71421.HI0719; -. DR PRIDE; P44839; -. DR EnsemblBacteria; AAC22376; AAC22376; HI_0719. DR GeneID; 949739; -. DR KEGG; hin:HI0719; -. DR PATRIC; 20190061; VBIHaeInf48452_0751. DR eggNOG; ENOG4105KME; Bacteria. DR eggNOG; COG0251; LUCA. DR KO; K09022; -. DR OMA; DEMNETY; -. DR OrthoDB; EOG6QVRPF; -. DR PhylomeDB; P44839; -. DR EvolutionaryTrace; P44839; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.1330.40; -; 1. DR InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like. DR InterPro; IPR006056; RidA. DR InterPro; IPR019897; RidA_CS. DR InterPro; IPR006175; YjgF/YER057c/UK114. DR PANTHER; PTHR11803; PTHR11803; 1. DR Pfam; PF01042; Ribonuc_L-PSP; 1. DR SUPFAM; SSF55298; SSF55298; 1. DR TIGRFAMs; TIGR00004; TIGR00004; 1. DR PROSITE; PS01094; UPF0076; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 130 RutC family protein HI_0719. FT /FTId=PRO_0000170324. FT ACT_SITE 109 109 {ECO:0000255}. FT STRAND 9 12 {ECO:0000244|PDB:1J7H}. FT STRAND 16 18 {ECO:0000244|PDB:1J7H}. FT STRAND 20 23 {ECO:0000244|PDB:1J7H}. FT STRAND 25 30 {ECO:0000244|PDB:1J7H}. FT TURN 38 40 {ECO:0000244|PDB:1J7H}. FT HELIX 47 65 {ECO:0000244|PDB:1J7H}. FT HELIX 69 71 {ECO:0000244|PDB:1J7H}. FT STRAND 72 80 {ECO:0000244|PDB:1J7H}. FT TURN 82 84 {ECO:0000244|PDB:1J7H}. FT HELIX 85 96 {ECO:0000244|PDB:1J7H}. FT TURN 97 100 {ECO:0000244|PDB:1J7H}. FT HELIX 116 118 {ECO:0000244|PDB:1J7H}. FT STRAND 120 128 {ECO:0000244|PDB:1J7H}. SQ SEQUENCE 130 AA; 14024 MW; CC37B821735DF58A CRC64; MMTQIIHTEK APAAIGPYVQ AVDLGNLVLT SGQIPVNPAT GEVPADIVAQ ARQSLENVKA IIEKAGLTAA DIVKTTVFVK DLNDFAAVNA EYERFFKENN HPNFPARSCV EVARLPKDVG LEIEAIAVRK // ID Y722_HAEIN Reviewed; 206 AA. AC P44842; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=IMPACT family member HI_0722; GN OrderedLocusNames=HI_0722; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the IMPACT 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; L42023; AAC22380.1; -; Genomic_DNA. DR PIR; I64088; I64088. DR RefSeq; NP_438880.2; NC_000907.1. DR ProteinModelPortal; P44842; -. DR SMR; P44842; 1-203. DR STRING; 71421.HI0722; -. DR DNASU; 949742; -. DR EnsemblBacteria; AAC22380; AAC22380; HI_0722. DR GeneID; 949742; -. DR KEGG; hin:HI0722; -. DR PATRIC; 20190067; VBIHaeInf48452_0754. DR eggNOG; ENOG4108ZK7; Bacteria. DR eggNOG; COG1739; LUCA. DR OMA; HCWAAVA; -. DR OrthoDB; EOG6N685N; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.30.230.30; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR023582; Impact. DR InterPro; IPR015796; Impact_bac/arc. DR InterPro; IPR001498; Impact_N. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR015269; UPF0029_Impact_C. DR InterPro; IPR020569; UPF0029_Impact_CS. DR PANTHER; PTHR16301; PTHR16301; 1. DR Pfam; PF09186; DUF1949; 1. DR Pfam; PF01205; UPF0029; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR TIGRFAMs; TIGR00257; IMPACT_YIGZ; 1. DR PROSITE; PS00910; UPF0029; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 206 IMPACT family member HI_0722. FT /FTId=PRO_0000207660. SQ SEQUENCE 206 AA; 22710 MW; 6FAECEE7AFE53BE5 CRC64; MAEYLVPKSA VVFEEEIKKS RFITYLQHTE GLEDARAFWA KIKQEHPNAR HHCWAAVAGK PTDSLQLGFS DDGEPAGTAG KPMLSALQGS QLGEISAVVV RYYGGILLGT GGLVRAYGNG VQQALKLIES EIKVERTLFK LDCDYGQLRL VQQLCEKYQV EILSQGFQAN IHLILGISEK TIEAFSSELT EKSSGRLVIQ LLEIGE // ID Y740_HAEIN Reviewed; 485 AA. AC Q57290; O05032; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Probable phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; GN OrderedLocusNames=HI_0740; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22400.1; -; Genomic_DNA. DR PIR; I64157; I64157. DR RefSeq; NP_438900.2; NC_000907.1. DR ProteinModelPortal; Q57290; -. DR STRING; 71421.HI0740; -. DR EnsemblBacteria; AAC22400; AAC22400; HI_0740. DR GeneID; 949768; -. DR KEGG; hin:HI0740; -. DR PATRIC; 20190123; VBIHaeInf48452_0777. DR eggNOG; ENOG4107QSU; Bacteria. DR eggNOG; COG1109; LUCA. DR KO; K01840; -. DR OMA; GLHRTSQ; -. DR OrthoDB; EOG6103ZG; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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 1: Evidence at protein level; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 485 Probable phosphomannomutase. FT /FTId=PRO_0000148021. FT ACT_SITE 86 86 Phosphoserine intermediate. FT {ECO:0000250}. FT METAL 86 86 Magnesium; via phosphate group. FT {ECO:0000250}. FT METAL 236 236 Magnesium. {ECO:0000250}. FT METAL 238 238 Magnesium. {ECO:0000250}. FT METAL 240 240 Magnesium. {ECO:0000250}. SQ SEQUENCE 485 AA; 52568 MW; BBCF7D443623B34E CRC64; MGMNRVLVSQ AAGGLAEYLK GYDKEPSIVI GYDGRKNSDV FARDTAEIMA GAGVKAYLLP RKLPTPVLAY AIQYFDTTAG VMVTASHNPP EDNGYKVYLG KANGGGQIVS PADKDIAALI DKVAAGNIQD LPRSDNYVVL NDEVVDAYIT KTASLAKEPA CDINYVYTAM HGVGYEVLSK TLAKAGLPQP HVVADQVWPD GTFPTVNFPN PEEKGALDLA IKVAKEKNAE FIIANDPDAD RLAVAVPDAQ GNWKSLHGNV VGCFLGWYLA KQYQGKQGTL ACSLVSSPAL AEIAKKYSFQ SEETLTGFKY IGKVSGLLFG FEEALGYLVD PDKVRDKDGI SAAIVFLDLV RNLKKQGKTL ADYADEFTKE FGAYVSGQIS IRVSDLSEIG KLMTALRNNP PAEIAGVKVA QFIDHIKTDR QSDILVFNLE NGGRLIARPS GTEPKIKFYL DARGKDPKDA DRVLAEFDEG VRHILRQDAY GKQDC // ID Y804_HAEIN Reviewed; 129 AA. AC P44053; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_0804; GN OrderedLocusNames=HI_0804; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22464.1; -; Genomic_DNA. DR PIR; H64013; H64013. DR ProteinModelPortal; P44053; -. DR STRING; 71421.HI0804; -. DR DNASU; 950170; -. DR EnsemblBacteria; AAC22464; AAC22464; HI_0804. DR PATRIC; 20190261; VBIHaeInf48452_0844. DR eggNOG; COG0664; LUCA. DR OrthoDB; EOG69GZND; -. DR PhylomeDB; P44053; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR Pfam; PF00027; cNMP_binding; 1. DR SMART; SM00100; cNMP; 1. DR SUPFAM; SSF51206; SSF51206; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein HI_0804. FT /FTId=PRO_0000077956. SQ SEQUENCE 129 AA; 15008 MW; 1ED1331E5E778E82 CRC64; MFTLPYYLPQ NLNKCIISES KTLEKNSLIY AQGEKPKEFY FLKQGLVGLY HSLENGKETL TRLYHANEYF GFRTIFSETS YHCSAKVLME ADIVRIFPGN HANFIANNPD FSCYLMKQLS NELLMQNTE // ID Y806_HAEIN Reviewed; 268 AA. AC P44054; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=UPF0721 transmembrane protein HI_0806; GN OrderedLocusNames=HI_0806; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0721 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; L42023; AAC22465.1; -; Genomic_DNA. DR PIR; I64013; I64013. DR RefSeq; NP_438966.1; NC_000907.1. DR RefSeq; WP_005693174.1; NC_000907.1. DR STRING; 71421.HI0806; -. DR EnsemblBacteria; AAC22465; AAC22465; HI_0806. DR GeneID; 949820; -. DR KEGG; hin:HI0806; -. DR PATRIC; 20190267; VBIHaeInf48452_0847. DR eggNOG; COG0730; LUCA. DR KO; K07090; -. DR OMA; LLFFHKQ; -. DR OrthoDB; EOG6KT2NN; -. DR Proteomes; UP000000579; 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; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 268 UPF0721 transmembrane protein HI_0806. FT /FTId=PRO_0000077957. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255}. FT TRANSMEM 212 232 Helical. {ECO:0000255}. FT TRANSMEM 248 268 Helical. {ECO:0000255}. SQ SEQUENCE 268 AA; 29137 MW; 61BAE00422D1D705 CRC64; MAFSTIFILL ICGICTNMVS AIFGIGGGVL MVPILRTLFP ELPIQVISAT SLTIVMCTAL INLLFFHKQK IKIDYINMIL WSIAMVIGVQ IGFELSFYFS TAIISLIFTV SLSALAIKTF LNRSRIQIEV FNMSPIERAK GSISFCGGGL IAGITGIGGG SILAPLVGQL KGVKTQQIAV YTNYMMIIGG IGNLYGYLTR AFLYDASLSG QLGLNFLVVG VVTLGSFEMS FFSMKLRGLM NPVLTRKLLA IILFCIAAYM CILEFVFH // ID Y868_HAEIN Reviewed; 250 AA. AC Q57022; P96336; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 81. DE RecName: Full=Uncharacterized glycosyltransferase HI_0868; DE EC=2.4.-.-; GN OrderedLocusNames=HI_0868; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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; L42023; AAC22526.1; -; Genomic_DNA. DR PIR; A64099; A64099. DR RefSeq; NP_439028.1; NC_000907.1. DR RefSeq; WP_005648226.1; NC_000907.1. DR ProteinModelPortal; Q57022; -. DR STRING; 71421.HI0868; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC22526; AAC22526; HI_0868. DR GeneID; 949464; -. DR KEGG; hin:HI0868; -. DR PATRIC; 20190391; VBIHaeInf48452_0909. DR eggNOG; ENOG4105K64; Bacteria. DR eggNOG; COG0463; LUCA. DR OMA; RSCAFSF; -. DR OrthoDB; EOG6H7FKC; -. DR PhylomeDB; Q57022; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 250 Uncharacterized glycosyltransferase FT HI_0868. FT /FTId=PRO_0000059239. SQ SEQUENCE 250 AA; 28916 MW; A5D8220129782E98 CRC64; MNMPLISIIM PVYNAECYLN QGILSCLNQS YQNIELILID DGSTDKSIEI INNIIDKDKR VKLFFTPTNQ GPAAARNIGL EKAQGDYITF LDSDDFIAND KLEKQLNFML QNHLVMTHGN YAFCDLEGNQ IKLVTTSKKI DYLTLLQGNQ FKIMTVLVER ESIKLLRFPN IKHEDYAFFL DCLKEVKQSI LYSHQASSFV RIGKVSVSSN KFKSAIWTFN IYFKREKLGV VKSIYYFILY AYNGFIKYKK // ID Y956_HAEIN Reviewed; 83 AA. AC P44954; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 2. DT 09-DEC-2015, entry version 80. DE RecName: Full=UPF0270 protein HI_0956; GN OrderedLocusNames=HI_0956; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0270 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22617.1; Type=Frameshift; Positions=38; 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; L42023; AAC22617.1; ALT_FRAME; Genomic_DNA. DR PIR; E64162; E64162. DR ProteinModelPortal; P44954; -. DR STRING; 71421.HI0956; -. DR EnsemblBacteria; AAC22617; AAC22617; HI_0956. DR PATRIC; 20190571; VBIHaeInf48452_0998. DR eggNOG; COG3089; LUCA. DR OMA; IMPRGQF; -. DR OrthoDB; EOG67MF89; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.10.10.610; -; 1. DR HAMAP; MF_00690; UPF0270; 1. DR InterPro; IPR010648; UPF0270. DR Pfam; PF06794; UPF0270; 1. DR PIRSF; PIRSF006169; UCP006169; 1. DR ProDom; PD026997; UPF0270; 1. DR SUPFAM; SSF118001; SSF118001; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 83 UPF0270 protein HI_0956. FT /FTId=PRO_0000214851. SQ SEQUENCE 83 AA; 9716 MW; F6D586488C9E0A14 CRC64; MIIPWQELEA ETLDNIVESV ILREGTDYGI EELSLNQKKQ LLLTQIRNGI ALIVWSELHE SIDIKNKTEF LKQECKEQEC QMN // ID Y983_HAEIN Reviewed; 193 AA. AC P43907; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein HI_0983; GN OrderedLocusNames=HI_0983; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7768823; RA Karudapuram S., Zhao X., Barcak G.J.; RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a RT gene required for chromosomal but not plasmid DNA transformation."; RL J. Bacteriol. 177:3235-3240(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; U18657; AAA70113.1; -; Genomic_DNA. DR EMBL; L42023; AAC22652.1; -; Genomic_DNA. DR PIR; C57256; C57256. DR RefSeq; NP_439146.1; NC_000907.1. DR RefSeq; WP_005693323.1; NC_000907.1. DR STRING; 71421.HI0983; -. DR EnsemblBacteria; AAC22652; AAC22652; HI_0983. DR GeneID; 949986; -. DR KEGG; hin:HI0983; -. DR PATRIC; 20190627; VBIHaeInf48452_1026. DR OMA; FVQYQYS; -. DR OrthoDB; EOG6Q2SKJ; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 193 Uncharacterized protein HI_0983. FT /FTId=PRO_0000077988. FT CONFLICT 170 170 L -> F (in Ref. 1; AAA70113). FT {ECO:0000305}. SQ SEQUENCE 193 AA; 22749 MW; 6AECE7C7E75C5C9B CRC64; MNKIFVILTA LILSGCATKL TQLNVPTQLE YNGKHYVLTG SQDFETIARY VYIAKPDTLE NWQSEIEILF DRNQPERSIK ERIALRERIY RNTGVKDFHF DAIPENSTNP NELNGYVIYS PTKENPSWQV NVMKGRQLSQ CGFVQFQYSQ KIQQPTRSKH LSVNKVQRHL QKYIVDIERK HLQNLKWQLF CEK // ID Y984_HAEIN Reviewed; 258 AA. AC P43908; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 17-FEB-2016, entry version 79. DE RecName: Full=UPF0246 protein HI_0984; GN OrderedLocusNames=HI_0984; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7768823; RA Karudapuram S., Zhao X., Barcak G.J.; RT "DNA sequence and characterization of Haemophilus influenzae dprA+, a RT gene required for chromosomal but not plasmid DNA transformation."; RL J. Bacteriol. 177:3235-3240(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0246 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA70112.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAC22645.1; 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; U18657; AAA70112.1; ALT_INIT; Genomic_DNA. DR EMBL; L42023; AAC22645.1; ALT_INIT; Genomic_DNA. DR PIR; E64163; E64163. DR RefSeq; NP_439147.2; NC_000907.1. DR RefSeq; WP_010869102.1; NC_000907.1. DR STRING; 71421.HI0984; -. DR EnsemblBacteria; AAC22645; AAC22645; HI_0984. DR GeneID; 949993; -. DR KEGG; hin:HI0984; -. DR PATRIC; 20190629; VBIHaeInf48452_1027. DR eggNOG; ENOG4105D1Q; Bacteria. DR eggNOG; COG3022; LUCA. DR KO; K09861; -. DR OMA; GLMARYI; -. DR OrthoDB; EOG6423KT; -. DR PhylomeDB; P43908; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0033194; P:response to hydroperoxide; IBA:GO_Central. DR HAMAP; MF_00652; UPF0246; 1. DR InterPro; IPR005583; YaaA. DR Pfam; PF03883; DUF328; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 258 UPF0246 protein HI_0984. FT /FTId=PRO_0000203987. SQ SEQUENCE 258 AA; 29254 MW; 515F332542F64249 CRC64; MLAIISPAKT LDFESAVKNF PVSQPHFTDY SEQLIEVCRK LSPQDLSSLM SISDKLAGLN AARFAEWTKI HNENNSRPAL FAFKGDVYTG LDADSLSEDD VIFAQSHLRM LSGLYGLLKP LDLMQPYRLE MGTKLANPKG KDLYAFWGNV ITQAVQQAID EQGDNVLVNL ASDEYYKSVK ESQINAKIIK PVFLDNKNGK YKVISFYAKK ARGLMCRYII QHHLTEIEQL KEFDLGGYWF DSASSTETEF VFKRDINE // ID Y193_HAEIN Reviewed; 287 AA. AC Q57427; O05013; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Putative esterase/lipase HI_0193; DE EC=3.1.-.-; GN OrderedLocusNames=HI_0193; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the DmpD/TodF/XylF esterase 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; L42023; AAC21862.1; -; Genomic_DNA. DR PIR; E64053; E64053. DR RefSeq; NP_438361.2; NC_000907.1. DR ProteinModelPortal; Q57427; -. DR STRING; 71421.HI0193; -. DR ESTHER; haein-HI0193; 6_AlphaBeta_hydrolase. DR EnsemblBacteria; AAC21862; AAC21862; HI_0193. DR GeneID; 951100; -. DR KEGG; hin:HI0193; -. DR PATRIC; 20188881; VBIHaeInf48452_0197. DR eggNOG; ENOG4105EV9; Bacteria. DR eggNOG; COG0596; LUCA. DR KO; K01175; -. DR OMA; FQQGEWR; -. DR OrthoDB; EOG6PZXDZ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR Pfam; PF00561; Abhydrolase_1; 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 1 287 Putative esterase/lipase HI_0193. FT /FTId=PRO_0000207082. FT ACT_SITE 119 119 {ECO:0000250}. FT ACT_SITE 266 266 {ECO:0000250}. SQ SEQUENCE 287 AA; 32987 MW; F2B548619C060619 CRC64; MIFIFISLFA KIFFNYNDFF TNSHVKIMAK SLLNYQFHQV KQTINTPVLI FIHGLFGDMD NLGVIARAFS EHYSILRIDL RNHGHSFHSE KMNYQLMAED VIAVIRHLNL SKVILIGHSM GGKTAMKITA LCPELVEKLI VIDMSPMPYE GFGHKDVFNG LFAVKNAKPE NRQQAKPILK QEINDEDVVQ FMLKSFDVNS ADCFRFNLTA LFNNYANIMD WEKVRVFTPT LFIKGGNSSY IKIENSEKIL EQFPNATAFT INGSGHWVHA EKPDFVIRAI KRFLNKN // ID Y213_HAEIN Reviewed; 514 AA. AC P44572; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Putative binding protein HI_0213; DE Flags: Precursor; GN OrderedLocusNames=HI_0213; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of a binding-protein-dependent transport system. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 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; L42023; AAC21881.1; -; Genomic_DNA. DR PIR; B64055; B64055. DR RefSeq; NP_438381.1; NC_000907.1. DR RefSeq; WP_005694085.1; NC_000907.1. DR ProteinModelPortal; P44572; -. DR STRING; 71421.HI0213; -. DR EnsemblBacteria; AAC21881; AAC21881; HI_0213. DR GeneID; 951122; -. DR KEGG; hin:HI0213; -. DR PATRIC; 20188921; VBIHaeInf48452_0217. DR eggNOG; ENOG4107TSG; Bacteria. DR eggNOG; COG4166; LUCA. DR KO; K02035; -. DR OMA; QRSAVIF; -. DR OrthoDB; EOG6V7BH5; -. DR PhylomeDB; P44572; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0015197; F:peptide transporter activity; IBA:GO_Central. DR GO; GO:0015833; P:peptide transport; IBA:GOC. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR030678; Peptide/Ni-bd. DR InterPro; IPR023765; SBP_5_CS. DR InterPro; IPR000914; SBP_5_dom. DR Pfam; PF00496; SBP_bac_5; 1. DR PIRSF; PIRSF002741; MppA; 1. DR PROSITE; PS01040; SBP_BACTERIAL_5; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Signal; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 514 Putative binding protein HI_0213. FT /FTId=PRO_0000031808. FT LIPID 24 24 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 24 24 S-diacylglycerol cysteine. {ECO:0000305}. SQ SEQUENCE 514 AA; 58876 MW; 789188C4328BDEBC CRC64; MNNLFALCQR SAVIFSIIFT VVACDKLDSP KPISPQIETQ KNTQLESNRV ELKRGVYSDL TLQPWQAQSE EQTQLLRDLF EGLTAYDVQG NLVPAVAENW QTEDNKTWIF TLRENAKWSN GEPITASDFV QSWQTLSQSE SPLKNYLAFM NLKNAKAVLE KALPVESLGL FAENDRTLRI ELDKASPYLP SMLAHVSLLP HYAKSTEIFI SNGAYQLQRQ AENQHILTTN PYYWAKEKVI FQQVKYQKIS VDADLSDFDV VMNPKKVNQN IQDYPQLCTY FYEFNLSDPV LQKSAVRKAI VSMISTNNLV ADIAHLYPNN TFLPKSMLGE QESVWEPVVA EQLFSQNQIS ETRPLKLRIR YDDLSLNQTI AMRLNHQLSQ SDLLRVENQG MSWQELQTAR TKGDFQLIRS GWCADFNDPA AFLNLFYSKS PDNKNGYKNA EFDRLFESAM TTISEKVRLE NYAKLKGIVQ QEHLVLPIFQ YSTPVYLVPS IMGAQVNSVG VIYSKDLWRK VQSQ // ID Y276_HAEIN Reviewed; 269 AA. AC P44608; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=UPF0761 membrane protein HI_0276 {ECO:0000255|HAMAP-Rule:MF_00672}; GN OrderedLocusNames=HI_0276; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00672}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00672}. CC -!- SIMILARITY: Belongs to the UPF0761 family. {ECO:0000255|HAMAP- CC Rule:MF_00672}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21941.1; -; Genomic_DNA. DR PIR; H64146; H64146. DR RefSeq; NP_438445.1; NC_000907.1. DR RefSeq; WP_005656225.1; NC_000907.1. DR STRING; 71421.HI0276; -. DR EnsemblBacteria; AAC21941; AAC21941; HI_0276. DR GeneID; 949791; -. DR KEGG; hin:HI0276; -. DR PATRIC; 20189089; VBIHaeInf48452_0291. DR eggNOG; ENOG4107S2Z; Bacteria. DR eggNOG; COG1295; LUCA. DR KO; K07058; -. DR OMA; RWASELN; -. DR OrthoDB; EOG63NMKT; -. DR PhylomeDB; P44608; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00672; UPF0761; 1. DR InterPro; IPR023679; UPF0761_bac. DR InterPro; IPR017039; Virul_fac_BrkB. DR Pfam; PF03631; Virul_fac_BrkB; 1. DR PIRSF; PIRSF035875; RNase_BN; 1. DR TIGRFAMs; TIGR00765; yihY_not_rbn; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 269 UPF0761 membrane protein HI_0276. FT /FTId=PRO_0000200984. FT TRANSMEM 32 52 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 89 109 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 168 188 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 203 223 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 232 252 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00672}. SQ SEQUENCE 269 AA; 30225 MW; 34F587E02FB982A6 CRC64; MISLKNFGLL FWKRFSENKL NQVAGALTYS TMLAMVPLVM VIFSIFSAFP VFNEVTGELK EMIFTNFAPS ASDMVGEYID QFVSNSKKMS AVGIVSLIAV ALMLINNIDR TLNSIWHNSQ SRSPLSSFAI YWMILTLGPL IIGVSIGISS YIKIMFEQSE HLSLGLKLLS FVPFLFTWFI FTLIYTVVPN KKVKIKHSAY GAFLAAIFFT LGKQAFTWYI VTFPSYQLIY GAMATLPIML LWIQISWLVV LVGAQLASTL DEIGEQIEQ // ID Y293_HAEIN Reviewed; 128 AA. AC P44617; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Probable heavy metal-dependent transcriptional regulator HI_0293; GN OrderedLocusNames=HI_0293; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be a copper-dependent transcriptional activator of CC the ATPase HI_0290. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: It contains a N-terminal DNA binding region and a C- CC terminal metal binding region. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH merR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00254}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21957.1; -; Genomic_DNA. DR PIR; I64059; I64059. DR RefSeq; NP_438460.1; NC_000907.1. DR RefSeq; WP_005654127.1; NC_000907.1. DR ProteinModelPortal; P44617; -. DR STRING; 71421.HI0293; -. DR EnsemblBacteria; AAC21957; AAC21957; HI_0293. DR GeneID; 949535; -. DR KEGG; hin:HI0293; -. DR PATRIC; 20189125; VBIHaeInf48452_0309. DR eggNOG; ENOG4108Z6Z; Bacteria. DR eggNOG; COG0789; LUCA. DR OMA; HTLAFIK; -. DR OrthoDB; EOG6NKQXH; -. DR PhylomeDB; P44617; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR011789; CueR. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR000551; MerR-type_HTH_dom. DR InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd. DR Pfam; PF00376; MerR; 1. DR Pfam; PF09278; MerR-DNA-bind; 1. DR PRINTS; PR00040; HTHMERR. DR SMART; SM00422; HTH_MERR; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR TIGRFAMs; TIGR02044; CueR; 1. DR PROSITE; PS00552; HTH_MERR_1; 1. DR PROSITE; PS50937; HTH_MERR_2; 1. PE 3: Inferred from homology; KW Activator; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 128 Probable heavy metal-dependent FT transcriptional regulator HI_0293. FT /FTId=PRO_0000098167. FT DOMAIN 1 69 HTH merR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. FT DNA_BIND 4 23 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. SQ SEQUENCE 128 AA; 14589 MW; 84D1381E09174CAE CRC64; MNISEAAKLV GLSTKQIRDY EKMGLIKPAV RSLSGYRNYG ESDLERLHFI RHSRNVGFSL HQIAQLLALQ DNPKRSCREV KVLTAQHIAT LNQQIEQLQK MVQKLQHWHD SCQGNDNPEC LILNGLNG // ID Y304_HAEIN Reviewed; 186 AA. AC P43980; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=UPF0301 protein HI_0304; GN OrderedLocusNames=HI_0304; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0301 (AlgH) 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; L42023; AAC21969.1; -; Genomic_DNA. DR PIR; G64005; G64005. DR RefSeq; NP_438471.1; NC_000907.1. DR RefSeq; WP_005694360.1; NC_000907.1. DR ProteinModelPortal; P43980; -. DR STRING; 71421.HI0304; -. DR EnsemblBacteria; AAC21969; AAC21969; HI_0304. DR GeneID; 949387; -. DR KEGG; hin:HI0304; -. DR PATRIC; 20189149; VBIHaeInf48452_0321. DR eggNOG; ENOG4108UJU; Bacteria. DR eggNOG; COG1678; LUCA. DR KO; K07735; -. DR OMA; IYICAHS; -. DR OrthoDB; EOG6RVFX5; -. DR PhylomeDB; P43980; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00758; UPF0301; 1. DR InterPro; IPR003774; UPF0301. DR Pfam; PF02622; DUF179; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 186 UPF0301 protein HI_0304. FT /FTId=PRO_0000214327. SQ SEQUENCE 186 AA; 20921 MW; DB56EBB49CE787DD CRC64; MMELQGKFLI AMPHLDDYFN RTVVFMCEHN EQGSMGLVIN QPTDLSIAEL YSKLNFMMKN DRTFGNEMVV AGGPMHTERG FILHKNTLNA FQHTYKVTKE LSMTTSADVV ETLGSTFAPE KYLVALGCSS WGAGQLEKEI RDNAWLVVSS NDQILFDMPY EDRYAAANQL LGIHPYNFAL AQVGHS // ID Y341_HAEIN Reviewed; 114 AA. AC P44649; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0341; GN OrderedLocusNames=HI_0341; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli YggL. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22003.1; -; Genomic_DNA. DR PIR; G64148; G64148. DR RefSeq; NP_438505.1; NC_000907.1. DR RefSeq; WP_005694334.1; NC_000907.1. DR ProteinModelPortal; P44649; -. DR STRING; 71421.HI0341; -. DR EnsemblBacteria; AAC22003; AAC22003; HI_0341. DR GeneID; 949447; -. DR KEGG; hin:HI0341; -. DR PATRIC; 20189225; VBIHaeInf48452_0358. DR eggNOG; ENOG41090ED; Bacteria. DR eggNOG; COG3171; LUCA. DR KO; K09923; -. DR OMA; EYPTKVE; -. DR OrthoDB; EOG6JTCCK; -. DR PhylomeDB; P44649; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007416; DUF469. DR Pfam; PF04320; DUF469; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein HI_0341. FT /FTId=PRO_0000169369. SQ SEQUENCE 114 AA; 13385 MW; 7F69268DAFD9FF75 CRC64; MSKSYNQRQR KKLHLAEFQE LGFLVNFQFA EGTAIETVDE TVDRFINEVI QPNGLAYEGS GYLHWEGLVC LEKIGKCDES HRETVKKWLE TNGLQQIEVS ELFDIWWEYP TKVE // ID Y354_HAEIN Reviewed; 240 AA. AC P44656; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_0354; GN OrderedLocusNames=HI_0354; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22014.1; -; Genomic_DNA. DR PIR; B64063; B64063. DR RefSeq; NP_438517.1; NC_000907.1. DR RefSeq; WP_005693805.1; NC_000907.1. DR ProteinModelPortal; P44656; -. DR STRING; 71421.HI0354; -. DR TCDB; 3.A.1.17.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22014; AAC22014; HI_0354. DR GeneID; 949457; -. DR KEGG; hin:HI0354; -. DR PATRIC; 20189255; VBIHaeInf48452_0373. DR eggNOG; ENOG4108YI8; Bacteria. DR eggNOG; COG1116; LUCA. DR KO; K15600; -. DR OMA; GIETQGV; -. DR OrthoDB; EOG6SNDS1; -. DR PhylomeDB; P44656; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 240 Uncharacterized ABC transporter ATP- FT binding protein HI_0354. FT /FTId=PRO_0000093199. FT DOMAIN 2 223 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 34 41 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 240 AA; 26931 MW; 25245AABBA214915 CRC64; MVRIQDLSLA FNGQTLFEHL NLTLLPNEWV SLLGSSGVGK STLLRLLAGI ETQGMVQGKI LFEPKVRIAW LPQKETLYPW LSIVDNVQLQ AVLFGRKSVK TTEKAKMLLE KVGMAAHWHK PCSQLSGGQK QRVALARTLM QEVDLILLDE PFSALDAISR HQLQDLAFEL LEDKSVLLVT HDPQEALRLS QRIFVLRSPE THQTALSAVI LPEGNAPREL HQANLWTLQQ QLLQELGGEQ // ID Y358_HAEIN Reviewed; 215 AA. AC P44659; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein HI_0358; GN OrderedLocusNames=HI_0358; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the thiaminase-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; L42023; AAC22017.1; -; Genomic_DNA. DR PIR; D64063; D64063. DR RefSeq; NP_438520.1; NC_000907.1. DR RefSeq; WP_005662665.1; NC_000907.1. DR ProteinModelPortal; P44659; -. DR STRING; 71421.HI0358; -. DR DNASU; 949463; -. DR EnsemblBacteria; AAC22017; AAC22017; HI_0358. DR GeneID; 949463; -. DR KEGG; hin:HI0358; -. DR PATRIC; 20189261; VBIHaeInf48452_0376. DR eggNOG; ENOG4105ETU; Bacteria. DR eggNOG; COG0819; LUCA. DR KO; K03707; -. DR OMA; AMSPCMR; -. DR OrthoDB; EOG6JMMXP; -. DR PhylomeDB; P44659; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0050334; F:thiaminase activity; IEA:InterPro. DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro. DR Gene3D; 1.20.910.10; -; 1. DR InterPro; IPR016084; Haem_Oase-like_multi-hlx. DR InterPro; IPR004305; Thiaminase-2/PQQC. DR InterPro; IPR027574; Thiaminase_II. DR Pfam; PF03070; TENA_THI-4; 1. DR SUPFAM; SSF48613; SSF48613; 1. DR TIGRFAMs; TIGR04306; salvage_TenA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 215 Uncharacterized protein HI_0358. FT /FTId=PRO_0000192047. SQ SEQUENCE 215 AA; 24989 MW; E9F312503E1135DF CRC64; MIEQLIQQAQ PYWQQYIEHE FVQQLAKGTL PKACFQHYLK QDYLYLFHYS RAFALGVFKA KNFAEMETPR KTLEILCQEI QLHLNYCREW GISEQEIFTT QESAACIAYT RYLLDCGMTG SLAELYAAVT PCALGYAQVA RYITQHYPRL PNNPYQTWID TYASEEFQQA AQETVDFLTA LCKPLNPSQL AEIQQIFTTA TRMEIAFWQM GLDLA // ID Y370_HAEIN Reviewed; 204 AA. AC P43989; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=UPF0070 protein HI_0370; GN OrderedLocusNames=HI_0370; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0070 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; L42023; AAC22028.1; -; Genomic_DNA. DR PIR; G64006; G64006. DR RefSeq; NP_438531.1; NC_000907.1. DR RefSeq; WP_005693794.1; NC_000907.1. DR STRING; 71421.HI0370; -. DR EnsemblBacteria; AAC22028; AAC22028; HI_0370. DR GeneID; 949833; -. DR KEGG; hin:HI0370; -. DR PATRIC; 20189285; VBIHaeInf48452_0388. DR eggNOG; ENOG4105N21; Bacteria. DR eggNOG; COG2976; LUCA. DR OMA; VGWRFWQ; -. DR OrthoDB; EOG6MSS1R; -. DR PhylomeDB; P43989; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR018704; TPR_21. DR InterPro; IPR026039; UPF0070. DR Pfam; PF09976; TPR_21; 1. DR PIRSF; PIRSF006170; YfgM; 1. DR SUPFAM; SSF48452; SSF48452; 1. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 204 UPF0070 protein HI_0370. FT /FTId=PRO_0000214365. FT TRANSMEM 24 42 Helical. {ECO:0000255}. SQ SEQUENCE 204 AA; 22664 MW; D763A17EF99AA97A CRC64; MAYSIEEEQE INQLKDWWKE NGKTIIVAFI LGVGGMFGWR YWQTHQAEQI AQASAQYDTL INSVQQDEQA KKANIEQFVQ ANSKTAYAVF ALLDEAKKAT EKQDFSAAEA NLNQALTQSQ DEVLTSIVAL RLSAVQFQLG QLDNALSTLN QVKGESFNAR KAILTGDIQV AKGDKVAAKN SFEQAQQSGS QLEQQMAKMK LNNL // ID Y414_HAEIN Reviewed; 70 AA. AC Q57392; O05021; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0414; GN OrderedLocusNames=HI_0414; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the opacity porin 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; L42023; AAC22081.1; -; Genomic_DNA. DR PIR; F64066; F64066. DR RefSeq; NP_438576.1; NC_000907.1. DR RefSeq; WP_005693751.1; NC_000907.1. DR ProteinModelPortal; Q57392; -. DR STRING; 71421.HI0414; -. DR EnsemblBacteria; AAC22081; AAC22081; HI_0414. DR GeneID; 949402; -. DR KEGG; hin:HI0414; -. DR PATRIC; 20189381; VBIHaeInf48452_0434. DR eggNOG; COG3637; LUCA. DR OMA; YDITPNI; -. DR OrthoDB; EOG68M4G6; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0015288; F:porin activity; IEA:InterPro. DR Gene3D; 2.40.160.20; -; 1. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 70 Uncharacterized protein HI_0414. FT /FTId=PRO_0000077920. SQ SEQUENCE 70 AA; 7918 MW; 614F817B53E0B736 CRC64; MPIGGDVKAD QETSGSRSIK RIGFGFIGGI GYDITPNITL DLGYRYNDWG RLENVRFKTH EASFGVRYRF // ID Y431_HAEIN Reviewed; 196 AA. AC P44709; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_0431; GN OrderedLocusNames=HI_0431; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli YjaG. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22090.1; -; Genomic_DNA. DR PIR; E64152; E64152. DR RefSeq; NP_438592.1; NC_000907.1. DR RefSeq; WP_005693732.1; NC_000907.1. DR ProteinModelPortal; P44709; -. DR STRING; 71421.HI0431; -. DR DNASU; 950606; -. DR EnsemblBacteria; AAC22090; AAC22090; HI_0431. DR GeneID; 950606; -. DR KEGG; hin:HI0431; -. DR PATRIC; 20189415; VBIHaeInf48452_0451. DR eggNOG; ENOG4105R2J; Bacteria. DR eggNOG; COG3068; LUCA. DR KO; K09891; -. DR OMA; YPAMDAC; -. DR OrthoDB; EOG67T5K1; -. DR PhylomeDB; P44709; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.20.1590.10; -; 1. DR InterPro; IPR007338; DUF416. DR InterPro; IPR023381; YP001051499.1-like_dom. DR Pfam; PF04222; DUF416; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 196 Uncharacterized protein HI_0431. FT /FTId=PRO_0000169705. SQ SEQUENCE 196 AA; 22721 MW; 81F70B80D466A77A CRC64; MRNPIHKRLE NLESWQHLTF MAALCERMAP NFKLFCQMNE LSAETKTYQN ILNLVWEYLT VKDVKINFEN QLEKLETIIP DVNDYDSFGV VPALDACQAL AEILHAIIAG ETLEKAVEIS LISLGTIRVL LETETGRDWS ESKLKENEDI QTELDVQWQV YRLLKECEKR DIELILALKN EIRTEGISNI GIEFHQ // ID Y451_HAEIN Reviewed; 63 AA. AC P43998; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein HI_0451; GN OrderedLocusNames=HI_0451; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22109.1; -; Genomic_DNA. DR PIR; G64007; G64007. DR RefSeq; NP_438612.1; NC_000907.1. DR RefSeq; WP_005649350.1; NC_000907.1. DR STRING; 71421.HI0451; -. DR EnsemblBacteria; AAC22109; AAC22109; HI_0451. DR GeneID; 950826; -. DR KEGG; hin:HI0451; -. DR PATRIC; 20189457; VBIHaeInf48452_0471. DR eggNOG; ENOG41063ES; Bacteria. DR eggNOG; ENOG4112CIT; LUCA. DR OMA; WIENKIA; -. DR OrthoDB; EOG6HF65F; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 63 Uncharacterized protein HI_0451. FT /FTId=PRO_0000077923. SQ SEQUENCE 63 AA; 7047 MW; 36B14E60AC306B67 CRC64; MELRQQIPTG CIKQFGQFGV PYVVGEVAEF LPDGDVLVNI TLLQSGEKDI YRLSHLLEDP EAE // ID Y457_HAEIN Reviewed; 347 AA. AC P44720; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=UPF0755 protein HI_0457; GN OrderedLocusNames=HI_0457; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0755 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; L42023; AAC22115.1; -; Genomic_DNA. DR PIR; E64069; E64069. DR RefSeq; NP_438618.1; NC_000907.1. DR RefSeq; WP_005693707.1; NC_000907.1. DR ProteinModelPortal; P44720; -. DR STRING; 71421.HI0457; -. DR EnsemblBacteria; AAC22115; AAC22115; HI_0457. DR GeneID; 950653; -. DR KEGG; hin:HI0457; -. DR PATRIC; 20189469; VBIHaeInf48452_0477. DR eggNOG; ENOG4105HHA; Bacteria. DR eggNOG; COG1559; LUCA. DR KO; K07082; -. DR OMA; APYVKHT; -. DR OrthoDB; EOG67T5RG; -. DR PhylomeDB; P44720; -. DR BioCyc; RETL1328306-WGS:GSTH-1459-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.160.60; -; 2. DR InterPro; IPR003770; UPF0755_YceG-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR Pfam; PF02618; YceG; 1. DR TIGRFAMs; TIGR00247; TIGR00247; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 347 UPF0755 protein HI_0457. FT /FTId=PRO_0000168818. SQ SEQUENCE 347 AA; 39621 MW; A21D559C66308F3D CRC64; MKKFLIAILL LILILAGVAS FSYYKMTEFV KTPVNVQADE LLTIERGTTS SKLATLFEQE KLIADGKLLP YLLKLKPELN KIKAGTYSLE NVKTVQDLLD LLNSGKEVQF NVKWIEGKTF KDWRKDLENA PHLVQTLKDK SNEEIFALLD LPDIGQNLEL KNVEGWLYPD TYNYTPKSTD LELLKRSAER MKKALNKAWN ERDEDLPLAN PYEMLILASI VEKETGIANE RAKVASVFIN RLKAKMKLQT DPTVIYGMGE NYNGNIRKKD LETKTPYNTY VIDGLPPTPI AMPSESSLQA VANPEKTDFY YFVADGSGGH KFTRNLNEHN KAVQEYLRWY RSQKNAK // ID Y487_HAEIN Reviewed; 125 AA. AC P44003; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_0487; GN OrderedLocusNames=HI_0487; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 PRD domain. {ECO:0000255|PROSITE- CC ProRule:PRU00704}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22157.1; -; Genomic_DNA. DR PIR; C64008; C64008. DR RefSeq; NP_438648.1; NC_000907.1. DR RefSeq; WP_005693684.1; NC_000907.1. DR STRING; 71421.HI0487; -. DR EnsemblBacteria; AAC22157; AAC22157; HI_0487. DR GeneID; 950695; -. DR KEGG; hin:HI0487; -. DR PATRIC; 20189529; VBIHaeInf48452_0507. DR OMA; RIERGGC; -. DR OrthoDB; EOG6DVJW5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.1790.10; -; 1. DR InterPro; IPR011608; PRD. DR Pfam; PF00874; PRD; 1. DR SUPFAM; SSF63520; SSF63520; 1. DR PROSITE; PS51372; PRD_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 125 Uncharacterized protein HI_0487. FT /FTId=PRO_0000169535. FT DOMAIN 15 121 PRD. {ECO:0000255|PROSITE- FT ProRule:PRU00704}. SQ SEQUENCE 125 AA; 14737 MW; FC9A38AE0C92F02C CRC64; MRLFKQLERW KIRRQINQSI IDVIFRLRDR LAHYWQADVN TPQVDFMLLH IACSLGRIER GGCVSSLYSE MLEEMQSAVI FPQVLAIHQD LLKLMPFSIP EAEQTYFLAN IHSLVLEQKQ LKPLK // ID Y522_HAEIN Reviewed; 218 AA. AC Q57256; O05024; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_0522; GN OrderedLocusNames=HI_0522; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22180.1; -; Genomic_DNA. DR PIR; D64154; D64154. DR RefSeq; NP_438680.1; NC_000907.1. DR RefSeq; WP_005692076.1; NC_000907.1. DR STRING; 71421.HI0522; -. DR EnsemblBacteria; AAC22180; AAC22180; HI_0522. DR GeneID; 950631; -. DR KEGG; hin:HI0522; -. DR PATRIC; 20189597; VBIHaeInf48452_0541. DR eggNOG; ENOG4108VW9; Bacteria. DR eggNOG; COG2364; LUCA. DR KO; K07149; -. DR OMA; APWDVLH; -. DR OrthoDB; EOG6HTNZ4; -. DR PhylomeDB; Q57256; -. DR Proteomes; UP000000579; 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 1 218 Uncharacterized protein HI_0522. FT /FTId=PRO_0000077929. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 173 193 Helical. {ECO:0000255}. SQ SEQUENCE 218 AA; 23520 MW; 98769596764E5DEA CRC64; MKKKVRVIPR TSWAATSLWT AQYKTISILL FALSILGIGD GLIVLSGLGS TPWTVLSQGI AIQTNFDIGW SSFLISCAVM LVWKPLKLRL GLGTLLNIIV IALFLGITTK ILAPPTALFS RMIFCLIGIL LYGFGTALYL TCHLGAGPRD GLMVGICQRF HLSINVVRSS LEISVCLLGF LLGGVVGLGT VLFATSIGSV VQFFLNIIAR LPHIPYEK // ID Y561_HAEIN Reviewed; 633 AA. AC P44016; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative oligopeptide transporter HI_0561; GN OrderedLocusNames=HI_0561; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) 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 oligopeptide OPT transporter 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; L42023; AAC22215.1; -; Genomic_DNA. DR PIR; G64009; G64009. DR RefSeq; NP_438718.1; NC_000907.1. DR RefSeq; WP_010869006.1; NC_000907.1. DR STRING; 71421.HI0561; -. DR TCDB; 2.A.67.4.1; the oligopeptide transporter (opt) family. DR EnsemblBacteria; AAC22215; AAC22215; HI_0561. DR GeneID; 950224; -. DR KEGG; hin:HI0561; -. DR PATRIC; 20189677; VBIHaeInf48452_0581. DR eggNOG; ENOG4105EPD; Bacteria. DR eggNOG; COG1297; LUCA. DR OMA; GFPYWET; -. DR OrthoDB; EOG67DPKN; -. DR PhylomeDB; P44016; -. DR Proteomes; UP000000579; 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 GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004814; Oligopep_transpt. DR InterPro; IPR004813; OPT. DR Pfam; PF03169; OPT; 1. DR TIGRFAMs; TIGR00728; OPT_sfam; 1. DR TIGRFAMs; TIGR00733; TIGR00733; 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 1 633 Putative oligopeptide transporter FT HI_0561. FT /FTId=PRO_0000213790. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 345 365 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. FT TRANSMEM 420 440 Helical. {ECO:0000255}. FT TRANSMEM 483 503 Helical. {ECO:0000255}. FT TRANSMEM 515 535 Helical. {ECO:0000255}. FT TRANSMEM 564 584 Helical. {ECO:0000255}. FT TRANSMEM 604 624 Helical. {ECO:0000255}. SQ SEQUENCE 633 AA; 66616 MW; F907A0DAE53D9102 CRC64; MYLGLKVGVT FASSIPAAVI SMAVLKFFKD SSILENNMVQ TQASSAGTLS SVIFVLPGLL MMGYWQDFPF WQTMLICAAG GTLGVLFTIP LRRAMVVNSN LPYPEGVAAA EILKAGNHAD GDSGVKDIAY GGVLAGLVAF LTNGLRVMAD GASAWIQTGK AAFQLPMGFS LALLGAGYLI GIVGGIAMLI GVILTWGVAV PYFTMSEDIA ADASLIDSAM TVWKTKVRYI GVGTIGIAAI WTLLILMKPM IEGMVHSFRM LKGGQEASEH RIDIDLSPKT MIYILIATVA LIVISLHHFI AAAPISPELS ILLVVVCTFL AVFIGFFVAA ASGYMAGLVG SSSSPISGIG IISVIVISLV LVSIGNASGL FETVDGQKFL TALTLFTASI VITTACISND NLQDLKTGLL VEATPWRQQV ALIIGCFVGA LVIAPVLEIL YHAYGFSGAL PRPDMDPSQA LSAPQATLMT AISQGIFTNK LEWTYILTGV GLGAVLITID AFLKKVSNKV FSLPVIAVGI GIYLPPSINT PVIVGAFLAW IMARHIAKLG NKEVSAKAER FGTLFSAGLI VGESLMGVIL AFIIAASVTT GGSEAPLSLN LENWDTIGEW FGLIVFIVGI VIFASRVLRA KKI // ID Y588_HAEIN Reviewed; 411 AA. AC Q57051; O05027; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized hydrolase HI_0588; DE EC=3.-.-.-; GN OrderedLocusNames=HI_0588; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the peptidase M20 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; L42023; AAC22245.1; -; Genomic_DNA. DR PIR; D64079; D64079. DR RefSeq; NP_438746.1; NC_000907.1. DR RefSeq; WP_005694560.1; NC_000907.1. DR ProteinModelPortal; Q57051; -. DR STRING; 71421.HI0588; -. DR EnsemblBacteria; AAC22245; AAC22245; HI_0588. DR GeneID; 950643; -. DR KEGG; hin:HI0588; -. DR PATRIC; 20189733; VBIHaeInf48452_0609. DR eggNOG; ENOG4105CE7; Bacteria. DR eggNOG; COG0624; LUCA. DR KO; K06016; -. DR OMA; MARVSPM; -. DR OrthoDB; EOG6QVRFS; -. DR PhylomeDB; Q57051; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR010158; Amidase_hdtase/Cbmase. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01879; hydantase; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 411 Uncharacterized hydrolase HI_0588. FT /FTId=PRO_0000061963. SQ SEQUENCE 411 AA; 45091 MW; CA410B24651525AE CRC64; MSINLNRVQN LIEKLAFISS VPNELTRLAF TEEDEKAHNM IIELCKEYDL SIRRDSIGNL FIRKAGKEDF LPAVAFGSHI DTVVNAGKFD GPLGSVAGLE ILLQLCEQNI QTRYPLELII FTCEESSRFN FATLGSKVMC GIVNQEKLSS LRDKQGKGLS EAMAEVGMNF NLVNQAKRDA KEFKCFFELH IEQGPRLENE GKTIGVVTGI AAPIRAIVKI KGQADHSGAT AMHYRHDALL GGSELSLAIE RAAIQAGHST VATVGNITAK PGVMNVVPGY CELLVDIRGT HVQARDSVFE LLQEEISKVS EKRGLLIELQ LISKDNPIIL PENMVNQIAE TAHSLGYSYE IMPSGAGHDA MHMATLCPTG MIFIPSHLGI SHNPLEFTDW KDIEAGIKVL QKVILEQAEV C // ID Y594_HAEIN Reviewed; 509 AA. AC P44023; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Uncharacterized protein HI_0594; GN OrderedLocusNames=HI_0594; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YfcC. {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YcgA. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22251.1; -; Genomic_DNA. DR PIR; E64010; E64010. DR RefSeq; NP_438751.1; NC_000907.1. DR RefSeq; WP_005694568.1; NC_000907.1. DR STRING; 71421.HI0594; -. DR EnsemblBacteria; AAC22251; AAC22251; HI_0594. DR GeneID; 949632; -. DR KEGG; hin:HI0594; -. DR PATRIC; 20189745; VBIHaeInf48452_0615. DR eggNOG; ENOG4105CSX; Bacteria. DR eggNOG; COG1288; LUCA. DR OMA; FPIMIWG; -. DR OrthoDB; EOG6MM1HM; -. DR PhylomeDB; P44023; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR InterPro; IPR018385; C4_dicarb_anaerob_car-like. DR Pfam; PF03606; DcuC; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 509 Uncharacterized protein HI_0594. FT /FTId=PRO_0000169192. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 209 229 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. FT TRANSMEM 303 323 Helical. {ECO:0000255}. FT TRANSMEM 324 344 Helical. {ECO:0000255}. FT TRANSMEM 359 379 Helical. {ECO:0000255}. FT TRANSMEM 399 419 Helical. {ECO:0000255}. FT TRANSMEM 423 443 Helical. {ECO:0000255}. FT TRANSMEM 458 478 Helical. {ECO:0000255}. FT TRANSMEM 484 504 Helical. {ECO:0000255}. SQ SEQUENCE 509 AA; 55487 MW; 59FCE0242AE68F6E CRC64; MDASKKKKTF NFPSAFTILF AILILAVGLT WVIPSGSYSK LTYNSTDNVF VVKAYGVDDK TYPATTDTLD NLNIKIKLSN FTEGVIKKPI AIPGTYQRVE QHHKGIEDIT KSMVEGTIEA VDVMVFIFVL GGMIGVINRT GSFNAGLMAL VKKTKGNEFF IVFCVSVLMV LGGTTCGIEE EAVAFYPILV PVFLALGYDA IVCVGAIFLA ASMGTAFSTI NPFSVVIASN AAGIQFTEGI GFRALGLVLG ATCVIAYLYW YCKKIKADPS FSYTYDDREE FRQRYMKNFD PNTTIPFSAR RKLILTLFCI SFPIMIWGVM VGGWWFPQMA ASFLAITIII MFISGLSEKD IMESFTEGAS ELVGVSLIIG LARGVNLVLE QGMISDTILD YMSNVVSGMP GSVFILGQLV VFIFLGLIVP SSSGLAVLSM PIMAPLADSV GIPRDIVVSA YNWGQYAMLF LAPTGLVLVT LQMLQIPFDR WVKFVMPMIG CLLLIGSILL VVQVSLYSV // ID Y653_HAEIN Reviewed; 254 AA. AC P44029; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized glycosyltransferase HI_0653; DE EC=2.4.-.-; GN OrderedLocusNames=HI_0653; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. WaaE/KdtX 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; L42023; AAC22312.1; -; Genomic_DNA. DR PIR; B64011; B64011. DR RefSeq; NP_438813.1; NC_000907.1. DR RefSeq; WP_005694490.1; NC_000907.1. DR ProteinModelPortal; P44029; -. DR STRING; 71421.HI0653; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAC22312; AAC22312; HI_0653. DR GeneID; 950619; -. DR KEGG; hin:HI0653; -. DR PATRIC; 20189921; VBIHaeInf48452_0682. DR eggNOG; ENOG4106WTF; Bacteria. DR eggNOG; COG0463; LUCA. DR KO; K12984; -. DR OMA; DWPGFGK; -. DR OrthoDB; EOG6W19MV; -. DR PhylomeDB; P44029; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IBA:GO_Central. DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central. DR Gene3D; 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 1 254 Uncharacterized glycosyltransferase FT HI_0653. FT /FTId=PRO_0000059232. SQ SEQUENCE 254 AA; 29137 MW; 1F520A67EC07B149 CRC64; MPTISVAMII KNEAQDLANC LDTVKDWVDE IIILDSGSTD NTKEIALSYG AKFYENSDWQ GFGKQRQLAQ QYVTSDYVLW LDADERVTPK LQQAILSAVK NDRENTVYEI PRVSEVFGRE IRHSGWYPDY VVRLYRTNYA QYNDSLVHEK VEFPAGTKVE KLTGDLEHFT YKSIHHYLVK SAGYAKAWAD QRQAKGKKAT LWQGISHALG CFVKMYLLKA GFLDGKQGFL LAVLSAHSTF VKYADLWERD QHKH // ID Y664_HAEIN Reviewed; 552 AA. AC Q57538; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Probable ABC transporter ATP-binding protein HI_0664; GN OrderedLocusNames=HI_0664; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. MsbA CC family. {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; L42023; AAC22321.1; -; Genomic_DNA. DR PIR; A64085; A64085. DR RefSeq; NP_438823.1; NC_000907.1. DR RefSeq; WP_005667625.1; NC_000907.1. DR ProteinModelPortal; Q57538; -. DR STRING; 71421.HI0664; -. DR EnsemblBacteria; AAC22321; AAC22321; HI_0664. DR GeneID; 949703; -. DR KEGG; hin:HI0664; -. DR PATRIC; 20189943; VBIHaeInf48452_0693. DR eggNOG; ENOG4105BZ1; Bacteria. DR eggNOG; COG1132; LUCA. DR KO; K06148; -. DR OMA; NINTCSL; -. DR OrthoDB; EOG6T7N3V; -. DR PhylomeDB; Q57538; -. DR Proteomes; UP000000579; 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; IPR014223; ABC_CydC. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR02868; CydC; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 552 Probable ABC transporter ATP-binding FT protein HI_0664. FT /FTId=PRO_0000093202. FT TRANSMEM 22 42 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 52 72 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 139 159 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 162 182 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 253 273 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 278 298 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 23 307 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 340 552 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 372 379 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 552 AA; 61294 MW; B14E31CDB07AD857 CRC64; MRKNGFVVMG HLLKLVTPLA HIMAFTITMG TLGFLAAIFI MVLGATGLVN LLNFDTHLSF SGILTALIVL AVARGALRYL EQMSGHYIAF KLLALLRDKV FSSLRRLAFV KLQDKQAGQL VSLVTNDIEL LEVFYAHTIA PIMIAFFTSA ILLLVFAQLS SWFVLVALAA YLTVGVILPI ITTKLAREDG RRYRELVGEM NDFFLDSVRG MKEIQLFGYA KQRLDEIQQR SQKIDTAFER IKDQEAKVRV YTEVAVSVFN IIMLFTGLIL FSLDKIDFAA FLIGVILLMS SYGPVIALSN LSSNLLQTLA SGERVLSLLA EEPELKDVES AVDLKDVSRI DVENVNFAYG EEQILSDVSL SVKKGEILGI HGRSGSGKST LLKLLMRFYD PKSGSIKING ETLPNINTCS LRDNMAYITQ QTYIFNETIE ENIRLARRDA TLEEIMEAAK KASIHDFILS LPQGYQTKMT ELGGNLSDGE KQRIGIARAF LHNAPIILLD EPTSNLDSLN EAMILKSLLN VKAEKLIILV SHRQSTMAIC DQVIGIENGR MS // ID Y732_HAEIN Reviewed; 50 AA. AC P44045; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein HI_0732; GN OrderedLocusNames=HI_0732; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22393.1; -; Genomic_DNA. DR PIR; I64012; I64012. DR STRING; 71421.HI0732; -. DR EnsemblBacteria; AAC22393; AAC22393; HI_0732. DR PATRIC; 20190101; VBIHaeInf48452_0766. DR eggNOG; COG2132; LUCA. DR OrthoDB; EOG6TBHRP; -. DR Proteomes; UP000000579; Chromosome. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_0732. FT /FTId=PRO_0000077952. SQ SEQUENCE 50 AA; 5491 MW; 079ACE2B6E838AB7 CRC64; MLFSGDELAN NTVLELRAQG QLSAFNKQPN LTFETDAPAI LQQAVAQTRE // ID Y742_HAEIN Reviewed; 109 AA. AC P44047; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein HI_0742; GN OrderedLocusNames=HI_0742; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YtfG C-terminal region. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22407.1; -; Genomic_DNA. DR PIR; B64013; B64013. DR RefSeq; NP_438901.1; NC_000907.1. DR RefSeq; WP_005693146.1; NC_000907.1. DR STRING; 71421.HI0742; -. DR EnsemblBacteria; AAC22407; AAC22407; HI_0742. DR GeneID; 949769; -. DR KEGG; hin:HI0742; -. DR PATRIC; 20190125; VBIHaeInf48452_0778. DR eggNOG; COG0702; LUCA. DR OMA; CCRICEL; -. DR OrthoDB; EOG6ZD6CP; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein HI_0742. FT /FTId=PRO_0000077953. SQ SEQUENCE 109 AA; 11898 MW; CDCBFE5E5A198078 CRC64; MCNLLVAEQC CRICELRNGW YTENYTESVP TTLANNAFYG SVENGKISSA LRAELAEAAA DYAVALVQVG LGEGFAGLIA QWDMDTSNGA LTCCLKRVWY LVIKNLHLS // ID Y756_HAEIN Reviewed; 410 AA. AC P44864; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein HI_0756; GN OrderedLocusNames=HI_0756; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22415.1; -; Genomic_DNA. DR PIR; D64158; D64158. DR RefSeq; NP_438915.1; NC_000907.1. DR RefSeq; WP_005693155.1; NC_000907.1. DR ProteinModelPortal; P44864; -. DR STRING; 71421.HI0756; -. DR MEROPS; M23.950; -. DR EnsemblBacteria; AAC22415; AAC22415; HI_0756. DR GeneID; 950697; -. DR KEGG; hin:HI0756; -. DR PATRIC; 20190157; VBIHaeInf48452_0794. DR eggNOG; ENOG41063SB; Bacteria. DR eggNOG; COG4942; LUCA. DR OMA; PEKFART; -. DR OrthoDB; EOG61ZTBJ; -. DR PhylomeDB; P44864; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01551; Peptidase_M23; 1. DR SUPFAM; SSF51261; SSF51261; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 410 Uncharacterized protein HI_0756. FT /FTId=PRO_0000169612. SQ SEQUENCE 410 AA; 45984 MW; B28D93E4E813BCA9 CRC64; MLRFGVNQKT SLLLTALLSC GLLIFSPVSQ SSDLNQIQKQ IKQQESKIEK QKREQAKLQA NLKKHESKIN SVEGELLETE ISLKEIRKQI ADADKQLKQL EKQEREQKAR LTKQIDIIYR SGINPSLIER MFAQDPTKAE RMKVYYQHLN QVRIEMINNL KATQAQIAVQ KKAILSQQKN HRNQLSTQKK QQQALQKAQQ EHQSTLNELN KNLALDQDKL NTLKANEQAL RQEIQRAEQA AREQEKRERE ALAQRQKAEE KRTSKPYQPT VQERQLLNST SGLGAAKKQY SLPVSGSILH TFGSIQAGEV RWKGMVIGAS AGTPVKAIAA GRVILAGYLN GYGYMVIVKH GETDLSLYGF NQAVSVKVGQ LVSAGQVIAQ VGNTGEISRS ALYFGISRKG TPVNPAGWVR // ID Y867_HAEIN Reviewed; 404 AA. AC Q57484; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Uncharacterized membrane protein HI_0867; GN OrderedLocusNames=HI_0867; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polysaccharide synthase family. CC HI_0867/HI_1700 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; L42023; AAC22525.1; -; Genomic_DNA. DR PIR; H64160; H64160. DR RefSeq; NP_439027.1; NC_000907.1. DR RefSeq; WP_005693216.1; NC_000907.1. DR STRING; 71421.HI0867; -. DR EnsemblBacteria; AAC22525; AAC22525; HI_0867. DR GeneID; 950724; -. DR KEGG; hin:HI0867; -. DR PATRIC; 20190389; VBIHaeInf48452_0908. DR eggNOG; ENOG4108MY6; Bacteria. DR eggNOG; COG2244; LUCA. DR OMA; SEIMFYL; -. DR OrthoDB; EOG6GFGNX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 404 Uncharacterized membrane protein HI_0867. FT /FTId=PRO_0000166458. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 103 123 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. FT TRANSMEM 319 339 Helical. {ECO:0000255}. FT TRANSMEM 366 386 Helical. {ECO:0000255}. SQ SEQUENCE 404 AA; 46373 MW; 47367D0AF3C27D6B CRC64; MSLIKDSSIY LIGELSAKCV PFLLLPYLSR KLGVEGFGEL SYYQTFLPLF VIFIGLSQDG AVARYFYVYG KRSLNLVVKT GYAYTLSIGG LGLLFCWLMQ SEIMFYLVLS AIFQVFLSVQ LSIRQCQKQA IPYTFIQVSS TITNAALTIL MLEFYQTDLV EKRILAILIS NVFVALLSYL IYRKRVNNKK FYFLQYKTAF FYIMSFGFLM IFHHGSFFIR QLDRIFIFHR FSEAELGLYA MGAQIAFILS VFILAINKAL VPYLFEKLKQ GSVKLKDLHR WSLLSLLIVP IPSLVTLIVP EQWLLFFLGK HFIGVKYYII VFLLSTSLTI PYLFLVNYLF YHGKTKEISF CSVLSTMIYL GALGGLIFTD VVYIPYASVL GALGILPVLY KITKRVEENE YATH // ID Y931_HAEIN Reviewed; 161 AA. AC P44078; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein HI_0931; GN OrderedLocusNames=HI_0931; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22601.1; -; Genomic_DNA. DR PIR; F64016; F64016. DR RefSeq; NP_439091.2; NC_000907.1. DR STRING; 71421.HI0931; -. DR EnsemblBacteria; AAC22601; AAC22601; HI_0931. DR GeneID; 949933; -. DR KEGG; hin:HI0931; -. DR PATRIC; 20190519; VBIHaeInf48452_0972. DR eggNOG; ENOG4108VBH; Bacteria. DR eggNOG; COG4316; LUCA. DR OMA; QICWSED; -. DR OrthoDB; EOG6DZF1M; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR014449; UCP007050_HI0931. DR Pfam; PF10008; DUF2251; 1. DR PIRSF; PIRSF007050; UPC007050; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 161 Uncharacterized protein HI_0931. FT /FTId=PRO_0000077977. SQ SEQUENCE 161 AA; 18798 MW; C325062A5D7FEFF2 CRC64; MKSHRTLYKS AVFLYLIFKG KRMLHLTLED ELFLGTPKQV GTHSTVFEHF AVMFEDDGET GYFYALDMRQ NAQPIVDMLH VYNVDSTSNH HEARKLEICW DESGYVALLL INGYPHAVFD FARLVGYNSN KYPQPDLMSM WTREEITNKQ AEQWLGVKTI R // ID Y973_HAEIN Reviewed; 289 AA. AC Q57133; O05038; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0973; GN OrderedLocusNames=HI_0973; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22641.1; -; Genomic_DNA. DR PIR; G64105; G64105. DR RefSeq; NP_439134.1; NC_000907.1. DR RefSeq; WP_005693319.1; NC_000907.1. DR ProteinModelPortal; Q57133; -. DR STRING; 71421.HI0973; -. DR EnsemblBacteria; AAC22641; AAC22641; HI_0973. DR GeneID; 949511; -. DR KEGG; hin:HI0973; -. DR PATRIC; 20190603; VBIHaeInf48452_1014. DR eggNOG; ENOG4106ZV1; Bacteria. DR eggNOG; ENOG410YUTK; LUCA. DR OMA; VNINASI; -. DR OrthoDB; EOG6QP103; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR001677; Solute-bd_prot_TBP-like. DR Pfam; PF01298; Lipoprotein_5; 1. DR SUPFAM; SSF56925; SSF56925; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 289 Uncharacterized protein HI_0973. FT /FTId=PRO_0000077984. SQ SEQUENCE 289 AA; 30604 MW; 628ECD6B098983C0 CRC64; MTINLTKFSL TILVALTLTA CGSSGGSGDS QSAHTPSTSI HTQNNSTPNK NTSTPPVNVS NANNLEIKNN DKTGGAFIIS GEDGHVTLKK VDITTNSDLN VLYIDGTKIP LSSPSIKSNG WLNIRSGTGK VSIDGIETSR DLKVCCGKYT DTRIGKVLSK NKNEDTYFFY NGNLTRNMPV GGTVNYNTGD SILSSYHDEL GDTDEAVGTS QFSADFVNKK LTGSLSVNEK KLNINADISG NTFSGTTQSD AFKSQGIAEG KFYGENAKEL GGLVKANDNS WSGAFAAKK // ID Y996_HAEIN Reviewed; 146 AA. AC P44089; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_0996; GN OrderedLocusNames=HI_0996; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22658.1; -; Genomic_DNA. DR PIR; H64017; H64017. DR EnsemblBacteria; AAC22658; AAC22658; HI_0996. DR Proteomes; UP000000579; 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 1 146 Uncharacterized protein HI_0996. FT /FTId=PRO_0000077989. FT TRANSMEM 8 24 Helical. {ECO:0000255}. SQ SEQUENCE 146 AA; 16589 MW; 3AAB26348335821C CRC64; MKNGVKQLFL LSLIGLSLTN VAWAEVARPK NDTLTNTIQS AELKTSSFSS MPKKEIPNRH IISLSKSQLA HHPRLVLRGL IPALYQNNTQ AVQLLLPLYK QFPQQDNFLL TWAKAIEARE QGDLTQSIAY YRELFARDAS LLPLRY // ID YACG_HAEIN Reviewed; 64 AA. AC P44921; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 11-NOV-2015, entry version 91. DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN OrderedLocusNames=HI_0891; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Inhibits all the catalytic activities of DNA gyrase by CC preventing its interaction with DNA. Acts by binding directly to CC the C-terminal domain of GyrB, which probably disrupts DNA binding CC by the gyrase. {ECO:0000255|HAMAP-Rule:MF_00649}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00649}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00649}; CC -!- SUBUNIT: Interacts with GyrB. {ECO:0000255|HAMAP-Rule:MF_00649}. CC -!- SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family. CC {ECO:0000255|HAMAP-Rule:MF_00649}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22551.1; 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; L42023; AAC22551.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_439052.1; NC_000907.1. DR ProteinModelPortal; P44921; -. DR SMR; P44921; 2-62. DR STRING; 71421.HI0891m; -. DR EnsemblBacteria; AAC22551; AAC22551; HI_0891. DR GeneID; 949368; -. DR KEGG; hin:HI0891m; -. DR PATRIC; 20190439; VBIHaeInf48452_0933. DR eggNOG; ENOG41067SF; Bacteria. DR eggNOG; COG3024; LUCA. DR KO; K09862; -. DR OMA; PWINEST; -. DR OrthoDB; EOG65F8ZX; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008657; F:DNA topoisomerase (ATP-hydrolyzing) inhibitor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.30.50.10; -; 1. DR HAMAP; MF_00649; DNA_gyrase_inhibitor_YacG; 1. DR InterPro; IPR005584; DNA_gyrase_inhibitor_YacG. DR InterPro; IPR013088; Znf_NHR/GATA. DR Pfam; PF03884; DUF329; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 64 DNA gyrase inhibitor YacG. FT /FTId=PRO_0000211701. FT METAL 6 6 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 9 9 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 25 25 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. FT METAL 29 29 Zinc. {ECO:0000255|HAMAP-Rule:MF_00649}. SQ SEQUENCE 64 AA; 7275 MW; 018CC3C812D6BA66 CRC64; MIEVPCPICQ KSVPWINEST FRPFCSKRCQ LIDLGEWAAE EKAIPSDTAD FAMDPNVSDE WSIK // ID YBEY_HAEIN Reviewed; 154 AA. AC P71335; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009}; GN Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; GN OrderedLocusNames=HI_0004; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP STRUCTURE BY NMR, COFACTOR, AND ZINC BINDING. RX PubMed=15632286; DOI=10.1110/ps.041096705; RA Yeh D.C., Parsons L.M., Parsons J.F., Liu F., Eisenstein E., Orban J.; RT "NMR structure of HI0004, a putative essential gene product from RT Haemophilus influenzae, and comparison with the X-ray structure of an RT Aquifex aeolicus homolog."; RL Protein Sci. 14:424-430(2005). CC -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved CC in late-stage 70S ribosome quality control and in maturation of CC the 3' terminus of the 16S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00009}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00009, CC ECO:0000269|PubMed:15632286}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009, CC ECO:0000269|PubMed:15632286}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}. CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family. CC {ECO:0000255|HAMAP-Rule:MF_00009}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21683.1; -; Genomic_DNA. DR PIR; A64140; A64140. DR RefSeq; NP_438177.1; NC_000907.1. DR RefSeq; WP_005663323.1; NC_000907.1. DR PDB; 1XAX; NMR; -; A=1-154. DR PDBsum; 1XAX; -. DR ProteinModelPortal; P71335; -. DR SMR; P71335; 3-146. DR STRING; 71421.HI0004; -. DR EnsemblBacteria; AAC21683; AAC21683; HI_0004. DR GeneID; 950900; -. DR KEGG; hin:HI0004; -. DR PATRIC; 20188459; VBIHaeInf48452_0004. DR eggNOG; ENOG4105KGE; Bacteria. DR eggNOG; COG0319; LUCA. DR KO; K07042; -. DR OMA; EESHHLN; -. DR OrthoDB; EOG680X6D; -. DR PhylomeDB; P71335; -. DR EvolutionaryTrace; P71335; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.390.30; -; 1. DR HAMAP; MF_00009; Endoribonucl_YbeY; 1. DR InterPro; IPR023091; MetalPrtase_cat_dom_prd. DR InterPro; IPR002036; YbeY. DR InterPro; IPR020549; YbeY_CS. DR Pfam; PF02130; UPF0054; 1. DR TIGRFAMs; TIGR00043; TIGR00043; 1. DR PROSITE; PS01306; UPF0054; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; KW Metal-binding; Nuclease; Reference proteome; Ribosome biogenesis; KW rRNA processing; Zinc. FT CHAIN 1 154 Endoribonuclease YbeY. FT /FTId=PRO_0000102463. FT METAL 114 114 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 118 118 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT METAL 124 124 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00009}. FT STRAND 4 10 {ECO:0000244|PDB:1XAX}. FT HELIX 21 32 {ECO:0000244|PDB:1XAX}. FT STRAND 33 35 {ECO:0000244|PDB:1XAX}. FT STRAND 39 45 {ECO:0000244|PDB:1XAX}. FT HELIX 48 58 {ECO:0000244|PDB:1XAX}. FT STRAND 66 70 {ECO:0000244|PDB:1XAX}. FT STRAND 84 88 {ECO:0000244|PDB:1XAX}. FT HELIX 90 100 {ECO:0000244|PDB:1XAX}. FT HELIX 104 117 {ECO:0000244|PDB:1XAX}. FT TURN 118 120 {ECO:0000244|PDB:1XAX}. FT TURN 126 128 {ECO:0000244|PDB:1XAX}. FT HELIX 129 141 {ECO:0000244|PDB:1XAX}. FT TURN 142 145 {ECO:0000244|PDB:1XAX}. SQ SEQUENCE 154 AA; 17355 MW; C066F7AB7F9CA7AD CRC64; MGSVLVDLQI ATENIEGLPT EEQIVQWATG AVQPEGNEVE MTVRIVDEAE SHELNLTYRG KDRPTNVLSF PFECPDEVEL PLLGDLVICR QVVEREASEQ EKPLMAHWAH MVVHGSLHLL GYDHIEDDEA EEMESLETQI MQGLGFDDPY LAEK // ID Y227_HAEIN Reviewed; 155 AA. AC P44583; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Uncharacterized protein HI_0227; GN OrderedLocusNames=HI_0227; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the TabA/YhcH/YiaL 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; L42023; AAC21897.1; -; Genomic_DNA. DR PIR; F64145; F64145. DR RefSeq; NP_438399.1; NC_000907.1. DR RefSeq; WP_005660595.1; NC_000907.1. DR PDB; 1JOP; X-ray; 2.60 A; A/B/C/D=1-155. DR PDB; 1S4C; X-ray; 2.20 A; A/B/C/D=1-155. DR PDBsum; 1JOP; -. DR PDBsum; 1S4C; -. DR ProteinModelPortal; P44583; -. DR SMR; P44583; 1-143. DR STRING; 71421.HI0227; -. DR DNASU; 951142; -. DR EnsemblBacteria; AAC21897; AAC21897; HI_0227. DR GeneID; 951142; -. DR KEGG; hin:HI0227; -. DR PATRIC; 20188977; VBIHaeInf48452_0241. DR eggNOG; ENOG4108R66; Bacteria. DR eggNOG; COG2731; LUCA. DR OMA; AIFLPYE; -. DR OrthoDB; EOG60PHCB; -. DR PhylomeDB; P44583; -. DR EvolutionaryTrace; P44583; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 2.60.120.370; -; 1. DR InterPro; IPR004375; YhcH/YjgK/YiaL. DR Pfam; PF04074; DUF386; 1. DR TIGRFAMs; TIGR00022; TIGR00022; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein HI_0227. FT /FTId=PRO_0000169486. FT STRAND 2 5 {ECO:0000244|PDB:1S4C}. FT TURN 9 14 {ECO:0000244|PDB:1S4C}. FT HELIX 17 26 {ECO:0000244|PDB:1S4C}. FT HELIX 31 33 {ECO:0000244|PDB:1S4C}. FT STRAND 36 40 {ECO:0000244|PDB:1S4C}. FT STRAND 42 44 {ECO:0000244|PDB:1S4C}. FT STRAND 46 50 {ECO:0000244|PDB:1S4C}. FT HELIX 57 59 {ECO:0000244|PDB:1S4C}. FT STRAND 62 64 {ECO:0000244|PDB:1S4C}. FT STRAND 66 77 {ECO:0000244|PDB:1S4C}. FT STRAND 79 83 {ECO:0000244|PDB:1S4C}. FT HELIX 90 92 {ECO:0000244|PDB:1S4C}. FT TURN 98 101 {ECO:0000244|PDB:1S4C}. FT STRAND 102 106 {ECO:0000244|PDB:1S4C}. FT STRAND 112 116 {ECO:0000244|PDB:1S4C}. FT STRAND 120 124 {ECO:0000244|PDB:1S4C}. FT STRAND 130 134 {ECO:0000244|PDB:1S4C}. FT STRAND 144 151 {ECO:0000244|PDB:1S4C}. FT HELIX 152 154 {ECO:0000244|PDB:1S4C}. SQ SEQUENCE 155 AA; 17670 MW; DAC9FEEAE69B11C1 CRC64; MIISSLTNPN FKVGLPKVIA EVCDYLNTLD LNALENGRHD INDQIYMNVM EPETAEPSSK KAELHHEYLD VQVLIRGTEN IEVGATYPNL SKYEDYNEAD DYQLCADIDD KFTVTMKPKM FAVFYPYEPH KPCCVVNGKT EKIKKLVVKV PVKLI // ID Y261_HAEIN Reviewed; 347 AA. AC Q57336; O05014; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Putative glycosyltransferase HI_0261; DE EC=2.-.-.-; GN Name=opsX; OrderedLocusNames=HI_0261; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyltransferase 9 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; L42023; AAC21926.1; -; Genomic_DNA. DR PIR; B64058; B64058. DR RefSeq; NP_438430.1; NC_000907.1. DR RefSeq; WP_010868969.1; NC_000907.1. DR ProteinModelPortal; Q57336; -. DR STRING; 71421.HI0261; -. DR CAZy; GT9; Glycosyltransferase Family 9. DR DNASU; 950896; -. DR EnsemblBacteria; AAC21926; AAC21926; HI_0261. DR GeneID; 950896; -. DR KEGG; hin:HI0261; -. DR PATRIC; 20189049; VBIHaeInf48452_0276. DR eggNOG; ENOG4105DKP; Bacteria. DR eggNOG; COG0859; LUCA. DR KO; K12982; -. DR OMA; KDERNWL; -. DR OrthoDB; EOG60PH7W; -. DR PhylomeDB; Q57336; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008713; F:ADP-heptose-lipopolysaccharide heptosyltransferase activity; IBA:GO_Central. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central. DR InterPro; IPR002201; Glyco_trans_9. DR Pfam; PF01075; Glyco_transf_9; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 347 Putative glycosyltransferase HI_0261. FT /FTId=PRO_0000207266. SQ SEQUENCE 347 AA; 38938 MW; E2149186830B0461 CRC64; MPLFTEAPKS LCILRLSAVG DVCHALAVVQ HIQEYYPQTE MTWIVGKTEM GLLSSIPNIT LIPYDKKTGW KGVLSLWKQL KNKQFDALLN MQTAFRASIL SLGIKAKFKI GFGEKRSREG QWLFVNRRIR DPFSPHVLDG FMAFAEYIGV PKAEPKWELA ISQDDYKFAD QFIDFSRKNL LISPCSSKAE KDWLIEGYAE VANIAHQHNI NVIFCSSPAK RELEIVEKIT ALCHFTPTNI AGKTNLKQLT ALISKVDLVL SPDSGPAHIA TTQGTPVIGL YAYHNPLRTA PYNNLDNVVS VYEENAQKEF GKPSSELPWA TKLKGKNLMT EIQVEPVIGQ MKKLGLF // ID Y310_HAEIN Reviewed; 95 AA. AC P43982; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein HI_0310; DE Flags: Precursor; GN OrderedLocusNames=HI_0310; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC21977.1; -; Genomic_DNA. DR PIR; I64005; I64005. DR RefSeq; NP_438477.1; NC_000907.1. DR RefSeq; WP_005694353.1; NC_000907.1. DR STRING; 71421.HI0310; -. DR EnsemblBacteria; AAC21977; AAC21977; HI_0310. DR GeneID; 949975; -. DR KEGG; hin:HI0310; -. DR PATRIC; 20189163; VBIHaeInf48452_0328. DR OMA; VEMPKQC; -. DR OrthoDB; EOG6JHRNZ; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020493; Uncharacterised_HI0310. DR ProDom; PD065628; Uncharacterised_HI0310; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 95 Uncharacterized protein HI_0310. FT /FTId=PRO_0000013956. SQ SEQUENCE 95 AA; 10674 MW; C756A75DADF44856 CRC64; MKKITLFFTA LLCLFSTSVL AESNSIPKQC EQLFKETENL IAQAEKQPGT HIQVNKIKSK LNQSKQQILQ MELATQLKSC EVGLAKLSNL KSYSE // ID Y360_HAEIN Reviewed; 282 AA. AC P44661; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Probable iron transport system membrane protein HI_0360; GN OrderedLocusNames=HI_0360; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of an ATP-driven transport system CC HI_0359/HI_0360/HI_0361/HI_0362 for iron. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22019.1; -; Genomic_DNA. DR PIR; E64063; E64063. DR RefSeq; NP_438522.1; NC_000907.1. DR RefSeq; WP_005666620.1; NC_000907.1. DR ProteinModelPortal; P44661; -. DR STRING; 71421.HI0360; -. DR EnsemblBacteria; AAC22019; AAC22019; HI_0360. DR GeneID; 950649; -. DR KEGG; hin:HI0360; -. DR PATRIC; 20189265; VBIHaeInf48452_0378. DR eggNOG; ENOG4105CC5; Bacteria. DR eggNOG; COG1108; LUCA. DR KO; K11605; -. DR OMA; NAMWVSG; -. DR OrthoDB; EOG67Q9FM; -. DR PhylomeDB; P44661; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR001626; ABC_3. DR InterPro; IPR029022; ABC_BtuC-like. DR Pfam; PF00950; ABC-3; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Iron; Iron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 282 Probable iron transport system membrane FT protein HI_0360. FT /FTId=PRO_0000171173. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. SQ SEQUENCE 282 AA; 30293 MW; 5EB442874214748C CRC64; MLDLLLEPFS YDYMLKAMIL STAVGGICAF LSSYLMLKGW SLIGDALSHS VVPGVAIAYA FALPYALGAF FAGILAALSI LWIKSISKLK EDAVIGFIFS TFFALGLLIV SLNPTAVNVQ NIILGNILGI ADEDIYQVAI IIGVCLVLLL LFWKDLLLIF FDETQAITVG LSPLFYKILF FTLLSACVVA ALQTVGAILV IAMVVTPGAT AYLLTDKFKT LSIIAIILGA VTSFVGVYIS YYLDGATGGV IVTLQTLLFL VAFLFSPKYG LLTRNKKAVE NV // ID Y374_HAEIN Reviewed; 228 AA. AC P44670; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_0374; GN OrderedLocusNames=HI_0374; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YbfG. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22036.1; -; Genomic_DNA. DR PIR; C64150; C64150. DR RefSeq; NP_438535.1; NC_000907.1. DR RefSeq; WP_005693791.1; NC_000907.1. DR STRING; 71421.HI0374; -. DR EnsemblBacteria; AAC22036; AAC22036; HI_0374. DR GeneID; 950642; -. DR KEGG; hin:HI0374; -. DR PATRIC; 20189293; VBIHaeInf48452_0392. DR eggNOG; ENOG4108RF1; Bacteria. DR eggNOG; ENOG4111HZX; LUCA. DR OMA; RWDGWRE; -. DR OrthoDB; EOG6SV5BQ; -. DR PhylomeDB; P44670; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR021239; DUF2625. DR Pfam; PF10946; DUF2625; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 228 Uncharacterized protein HI_0374. FT /FTId=PRO_0000168692. SQ SEQUENCE 228 AA; 26195 MW; 3482A43A24D66478 CRC64; MQTLEQLTSP EHSAWITLSQ WIDNARNHCE VIKKDQSSAE RELFTMQMPT SSPMGAVIYE TGGILIHYGW LRILGSGSFK LPRGLMDWNF SKSFSESGEK PKYLLVADDV IGGYFALNGG SLGNNIGKIY YYSSKDLTWH NLNFTYTEFL AWVLNGDVEA FYQGLFWKNW QDDVKQLDGN QVFVFTPDLN QDRKIAIDER QKQEVNIETH YQANFAEKNK FDLAYSVA // ID Y380_HAEIN Reviewed; 241 AA. AC P44676; Q9RP31; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 13-APR-2016, entry version 96. DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase HI_0380; DE EC=2.1.1.-; GN OrderedLocusNames=HI_0380; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Bonander N., Eisenstein E.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC22038.1; -; Genomic_DNA. DR EMBL; AF174385; AAD54289.1; -; Genomic_DNA. DR PIR; G64150; G64150. DR RefSeq; NP_438541.1; NC_000907.1. DR RefSeq; WP_010868980.1; NC_000907.1. DR PDB; 3ILK; X-ray; 2.01 A; A/B=1-241. DR PDBsum; 3ILK; -. DR ProteinModelPortal; P44676; -. DR STRING; 71421.HI0380; -. DR DNASU; 949482; -. DR EnsemblBacteria; AAC22038; AAC22038; HI_0380. DR GeneID; 949482; -. DR KEGG; hin:HI0380; -. DR PATRIC; 20189305; VBIHaeInf48452_0398. DR eggNOG; ENOG4105CVS; Bacteria. DR eggNOG; COG0565; LUCA. DR KO; K15396; -. DR OMA; LMRPRNA; -. DR OrthoDB; EOG6XSZTC; -. DR EvolutionaryTrace; P44676; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IBA:GO_Central. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR004384; rRNA_MeTrfase_TrmH_1. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF004808; LasT; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00050; rRNA_methyl_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 241 Uncharacterized tRNA/rRNA FT methyltransferase HI_0380. FT /FTId=PRO_0000159830. FT CONFLICT 73 73 S -> P (in Ref. 1; AAC22038). FT {ECO:0000305}. FT STRAND 5 11 {ECO:0000244|PDB:3ILK}. FT HELIX 15 27 {ECO:0000244|PDB:3ILK}. FT STRAND 32 37 {ECO:0000244|PDB:3ILK}. FT HELIX 43 47 {ECO:0000244|PDB:3ILK}. FT TURN 48 51 {ECO:0000244|PDB:3ILK}. FT HELIX 53 58 {ECO:0000244|PDB:3ILK}. FT STRAND 60 64 {ECO:0000244|PDB:3ILK}. FT HELIX 65 68 {ECO:0000244|PDB:3ILK}. FT TURN 69 71 {ECO:0000244|PDB:3ILK}. FT STRAND 73 78 {ECO:0000244|PDB:3ILK}. FT HELIX 83 85 {ECO:0000244|PDB:3ILK}. FT TURN 86 88 {ECO:0000244|PDB:3ILK}. FT HELIX 92 101 {ECO:0000244|PDB:3ILK}. FT STRAND 106 110 {ECO:0000244|PDB:3ILK}. FT TURN 113 115 {ECO:0000244|PDB:3ILK}. FT HELIX 119 123 {ECO:0000244|PDB:3ILK}. FT STRAND 126 129 {ECO:0000244|PDB:3ILK}. FT HELIX 142 166 {ECO:0000244|PDB:3ILK}. FT HELIX 177 193 {ECO:0000244|PDB:3ILK}. FT HELIX 201 213 {ECO:0000244|PDB:3ILK}. FT HELIX 217 237 {ECO:0000244|PDB:3ILK}. SQ SEQUENCE 241 AA; 27241 MW; 82F6A9E5A17EC637 CRC64; MLENIRIVLI ETSHSGNIGS AARAMKTMGL TQLCLVSPKS VDEQSYALSA GAENIVKNAR VVDSFDEAVD DCSLVIGTSA RLRHLQNTLI EPRECAEKVV AYKGKIAIVF GRERIGLTNE ELLKCHYHLN IPANPDYSSL NLAMAVQLVS YELRMAFLVQ NNKKNSLSLI EKNYPTTDQL AYFFDYTERI YQSLGFIQNQ GVMRKLKRLY YRAKLEKNEL NILNGMLSAV EKRIDLTKED N // ID Y387_HAEIN Reviewed; 640 AA. AC P44680; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Probable ATP-dependent helicase HI_0387; DE EC=3.6.4.12; GN OrderedLocusNames=HI_0387; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. 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; L42023; AAC22045.1; -; Genomic_DNA. DR PIR; A64065; A64065. DR RefSeq; NP_438548.1; NC_000907.1. DR RefSeq; WP_005693783.1; NC_000907.1. DR ProteinModelPortal; P44680; -. DR STRING; 71421.HI0387; -. DR EnsemblBacteria; AAC22045; AAC22045; HI_0387. DR GeneID; 949750; -. DR KEGG; hin:HI0387; -. DR PATRIC; 20189323; VBIHaeInf48452_0405. DR eggNOG; ENOG4105DVT; Bacteria. DR eggNOG; COG1199; LUCA. DR KO; K03722; -. DR OMA; HRDLPLM; -. DR OrthoDB; EOG6742WF; -. DR PhylomeDB; P44680; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR010614; DEAD_2. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF06733; DEAD_2; 1. DR Pfam; PF13307; Helicase_C_2; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 640 Probable ATP-dependent helicase HI_0387. FT /FTId=PRO_0000102007. FT DOMAIN 16 278 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 458 634 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 51 58 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 231 234 DEAH box. SQ SEQUENCE 640 AA; 71531 MW; EC659D19C2F23D3C CRC64; MDYENQIANI FSLNGELSQN IKGFRPRAEQ LEMAYAVGKA IQNKSSLVIE AGTGTGKTFA YLAPALVFGK KTIISTGSKN LQDQLFNRDL PAIKKALNFT GKIALLKGRA NYLCLERLDQ VIAQGVLGDK SVLAELSKVR KWNNSTKTGD FTECIELAED SPIIPQLTST AESCLGTDCP NYSECYVASA RKKALNADLV VVNHHLFFAD MAVKESGFGE LIPNAEVIIF DEAHQLPDIA SQYFGQSLTS RQLFDLCKDI NIVYRTELKD MQQLGTTSDT LLKVVQDFRL LLGNGSNVRG NWRELYTQSA VKKAFELLQE KIDFLSEVIK LALGRSQTLD SIFERVESIK IQLKRLSETN IVGYCYWYEG NGRQFGLHIT PLTVADKFGA QLEAKEAAWI FTSATLEVGG TFNHFCQRLG IENATQKILY SPFNYPEQSL LCVPRYLPNT NQMNTLNSLG EILLPVIEAN KGRCFVLCTS YSMMRGLAEY FREKSHLSIL LQGETSKGKL LEQFIKETHS VLVATSSFWE GVDVRGDALS LVIIDKLPFT APDEPLLKAR IEDCRLQGGD PFNDIQIPEA VITLKQGVGR LIRDVTDRGV VIICDNRLVM RNYGETFLKS LPNSSRTRDL NKVIQFLQNK // ID Y389_HAEIN Reviewed; 183 AA. AC P43991; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_0389; GN OrderedLocusNames=HI_0389; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22047.1; -; Genomic_DNA. DR PIR; I64006; I64006. DR RefSeq; NP_438550.1; NC_000907.1. DR RefSeq; WP_005693781.1; NC_000907.1. DR STRING; 71421.HI0389; -. DR EnsemblBacteria; AAC22047; AAC22047; HI_0389. DR GeneID; 949490; -. DR KEGG; hin:HI0389; -. DR PATRIC; 20189327; VBIHaeInf48452_0407. DR eggNOG; ENOG4105R8X; Bacteria. DR eggNOG; COG3065; LUCA. DR KO; K07285; -. DR OMA; NGFVEPE; -. DR OrthoDB; EOG68Q0QH; -. DR PhylomeDB; P43991; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR InterPro; IPR004658; OMP_Slp. DR Pfam; PF03843; Slp; 1. DR PIRSF; PIRSF004982; SlP; 1. DR TIGRFAMs; TIGR00752; slp; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 183 Uncharacterized protein HI_0389. FT /FTId=PRO_0000077917. FT TRANSMEM 7 23 Helical. {ECO:0000255}. SQ SEQUENCE 183 AA; 21170 MW; 602C303C10A9B61B CRC64; MKGKITLFFT ALCFGLTGCI APPKGLEKER FSINSYREIS PQDLTCHCKT VRLGGKIVNT TVLANQTKIE VLSLPVSSIS AKPFVELQSD GRFIVYFNGF VEPENLKERY ITVGGQLAGT EKGKIEQADY TYPVVQADKY RIWTLSTTYD YPTDDWDEDD DWGFFRWRHR LWYVQPEIHY YLN // ID Y442_HAEIN Reviewed; 109 AA. AC P44711; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 108. DE RecName: Full=Nucleoid-associated protein HI_0442 {ECO:0000255|HAMAP-Rule:MF_00274}; GN OrderedLocusNames=HI_0442; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP DNA-BINDING, AND SUBUNIT. RX PubMed=19594923; DOI=10.1186/1471-2180-9-137; RA Cooley A.E., Riley S.P., Kral K., Miller M.C., DeMoll E., Fried M.G., RA Stevenson B.; RT "DNA-binding by Haemophilus influenzae and Escherichia coli YbaB, RT members of a widely-distributed bacterial protein family."; RL BMC Microbiol. 9:137-137(2009). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT. RX PubMed=12486730; DOI=10.1002/prot.10297; RA Lim K., Tempczyk A., Parsons J.F., Bonander N., Toedt J., Kelman Z., RA Howard A., Eisenstein E., Herzberg O.; RT "Crystal structure of YbaB from Haemophilus influenzae (HI0442), a RT protein of unknown function coexpressed with the recombinational DNA RT repair protein RecR."; RL Proteins 50:375-379(2003). CC -!- FUNCTION: Binds to DNA and alters its conformation. May be CC involved in regulation of gene expression, nucleoid organization CC and DNA protection. {ECO:0000255|HAMAP-Rule:MF_00274}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00274, CC ECO:0000269|PubMed:12486730, ECO:0000269|PubMed:19594923}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC -!- SIMILARITY: Belongs to the YbaB/EbfC family. {ECO:0000255|HAMAP- CC Rule:MF_00274}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22101.1; 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; L42023; AAC22101.1; ALT_INIT; Genomic_DNA. DR PIR; G64152; G64152. DR RefSeq; NP_438603.2; NC_000907.1. DR RefSeq; WP_005629464.1; NC_000907.1. DR PDB; 1J8B; X-ray; 1.75 A; A=1-109. DR PDBsum; 1J8B; -. DR ProteinModelPortal; P44711; -. DR SMR; P44711; 7-98. DR STRING; 71421.HI0442; -. DR PRIDE; P44711; -. DR EnsemblBacteria; AAC22101; AAC22101; HI_0442. DR GeneID; 950773; -. DR KEGG; hin:HI0442; -. DR PATRIC; 20189437; VBIHaeInf48452_0462. DR eggNOG; ENOG4105KDX; Bacteria. DR eggNOG; COG0718; LUCA. DR KO; K09747; -. DR OMA; EMGKLTG; -. DR OrthoDB; EOG6DVJWP; -. DR PhylomeDB; P44711; -. DR EvolutionaryTrace; P44711; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043590; C:bacterial nucleoid; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1310.10; -; 1. DR HAMAP; MF_00274; DNA_YbaB_EbfC; 1. DR InterPro; IPR004401; YbaB/EbfC. DR Pfam; PF02575; YbaB_DNA_bd; 1. DR PIRSF; PIRSF004555; UCP004555; 1. DR SUPFAM; SSF82607; SSF82607; 1. DR TIGRFAMs; TIGR00103; DNA_YbaB_EbfC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 109 Nucleoid-associated protein HI_0442. FT /FTId=PRO_0000170397. FT HELIX 10 28 {ECO:0000244|PDB:1J8B}. FT STRAND 31 37 {ECO:0000244|PDB:1J8B}. FT TURN 38 41 {ECO:0000244|PDB:1J8B}. FT STRAND 42 47 {ECO:0000244|PDB:1J8B}. FT STRAND 52 57 {ECO:0000244|PDB:1J8B}. FT HELIX 59 63 {ECO:0000244|PDB:1J8B}. FT HELIX 66 95 {ECO:0000244|PDB:1J8B}. SQ SEQUENCE 109 AA; 11969 MW; 4C6D43D6A9E51361 CRC64; MFGKGGLGGL MKQAQQMQEK MQKMQEEIAQ LEVTGESGAG LVKITINGAH NCRRIDIDPS LMEDDKEMLE DLIAAAFNDA VRRAEELQKE KMASVTAGMP LPPGMKFPF // ID Y485A_HAEIN Reviewed; 124 AA. AC O86225; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein HI_0485.1; GN OrderedLocusNames=HI_0485.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC22145.1; -; Genomic_DNA. DR RefSeq; NP_438646.1; NC_000907.1. DR RefSeq; WP_005659757.1; NC_000907.1. DR STRING; 71421.HI0485.1; -. DR EnsemblBacteria; AAC22145; AAC22145; HI_0485.1. DR GeneID; 950693; -. DR KEGG; hin:HI0485.1; -. DR PATRIC; 20189525; VBIHaeInf48452_0505. DR eggNOG; COG3312; LUCA. DR KO; K02116; -. DR OMA; FIYGWQR; -. DR OrthoDB; EOG6VQPWZ; -. DR Proteomes; UP000000579; 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; IPR005598; ATPase_I. DR Pfam; PF03899; ATP-synt_I; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 124 Uncharacterized protein HI_0485.1. FT /FTId=PRO_0000077928. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. SQ SEQUENCE 124 AA; 14546 MW; E4D867EDA4FB4C3E CRC64; MSRILSHAKK NYRKAIVIES LLLVVFYLLI YGWQRQSAVD FSYGFLSAFL PFCTFIFIIF YRKQNFSTKL TALYRAEAIK FILTMVFIII AIKWLFVINF IAFFVGFLLA LVLNNIIPLI LNKI // ID Y507_HAEIN Reviewed; 183 AA. AC P44010; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=UPF0114 protein HI_0507; GN OrderedLocusNames=HI_0507; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0114 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; L42023; AAC22165.1; -; Genomic_DNA. DR PIR; A64009; A64009. DR RefSeq; NP_438665.1; NC_000907.1. DR RefSeq; WP_005649445.1; NC_000907.1. DR STRING; 71421.HI0507; -. DR EnsemblBacteria; AAC22165; AAC22165; HI_0507. DR GeneID; 949655; -. DR KEGG; hin:HI0507; -. DR PATRIC; 20189567; VBIHaeInf48452_0526. DR eggNOG; ENOG4108TEB; Bacteria. DR eggNOG; COG2862; LUCA. DR OMA; FVSRMNL; -. DR OrthoDB; EOG6VHZH0; -. DR PhylomeDB; P44010; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00143; UPF0114; 1. DR InterPro; IPR005134; UPF0114. DR InterPro; IPR020761; UPF0114_bac. DR InterPro; IPR020765; UPF0114_gbac. DR Pfam; PF03350; UPF0114; 1. DR TIGRFAMs; TIGR00645; HI0507; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 183 UPF0114 protein HI_0507. FT /FTId=PRO_0000214370. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. SQ SEQUENCE 183 AA; 20814 MW; B97E2F235E49B267 CRC64; MKENKPVDPY AKYNEQSNII AKIIFASRWL QVPIYLGLIV TLAIYSYKFI KGLWELVINV NDMDSNTIML GVLNLIDVVM IANLLVMVTI GGYEIFVSKL RTRNHPDQPE WMSHVNATVL KVKLSMSIIG ISSIHMLQTF VNASNMPEKT MMWQLLLHLG FLVSAIALAY TDKILYSTSH KTH // ID Y523_HAEIN Reviewed; 346 AA. AC P44011; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2016, sequence version 2. DT 11-MAY-2016, entry version 80. DE RecName: Full=Putative glycosyltransferase HI_0523; DE EC=2.-.-.-; GN OrderedLocusNames=HI_0523; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyltransferase 9 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22181.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22181.1; ALT_INIT; Genomic_DNA. DR PIR; B64009; B64009. DR RefSeq; NP_438681.2; NC_000907.1. DR RefSeq; WP_010868996.1; NC_000907.1. DR ProteinModelPortal; P44011; -. DR STRING; 71421.HI0523; -. DR CAZy; GT9; Glycosyltransferase Family 9. DR EnsemblBacteria; AAC22181; AAC22181; HI_0523. DR GeneID; 950662; -. DR KEGG; hin:HI0523; -. DR PATRIC; 20189599; VBIHaeInf48452_0542. DR eggNOG; ENOG4105M5K; Bacteria. DR eggNOG; COG0859; LUCA. DR OMA; RNDKLGD; -. DR OrthoDB; EOG67Q978; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008713; F:ADP-heptose-lipopolysaccharide heptosyltransferase activity; IBA:GO_Central. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central. DR InterPro; IPR002201; Glyco_trans_9. DR Pfam; PF01075; Glyco_transf_9; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 346 Putative glycosyltransferase HI_0523. FT /FTId=PRO_0000013959. SQ SEQUENCE 346 AA; 38906 MW; 7F829B1370FDF76B CRC64; MEKILVIRND KLGDFMQAWP AFAMLKASNP KLKLTALVPS YTASLAEICP FIDHVIIDSK KNDKTDFKRL VQEIKAQQFD GMISFFSNTH NGKLAWKSGI KYRLAPATKW VQILYNHRLT QRRSRSEKSE AEYNQDLVRT FLQKHNMPVV EPKPPYLIFE KSAVENQRVF LQENLGLSAN KKWIFVHSGS GGSATNLSLA QYADLIKGLL AEFDCNVVLT AGPGESEKAY ELANLVNDLR VAIYDKNKGL VDFAHSLACA DLFIAGSTGP LHLSSAFNIP TIGFYPNSRS SQPRRWKPIN DVDKHIAFCP PAGKESQMNL ELISIDNALA EISLFIRNMW QTSNNI // ID Y607_HAEIN Reviewed; 271 AA. AC P44774; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=Shikimate 5-dehydrogenase-like protein HI_0607; DE Short=SDH-L; DE EC=1.1.1.-; GN OrderedLocusNames=HI_0607; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), FUNCTION, MUTAGENESIS OF RP LYS-67 AND ASP-103, AND SUBUNIT. RX PubMed=15735308; DOI=10.1074/jbc.M412753200; RA Singh S., Korolev S., Koroleva O., Zarembinski T., Collart F., RA Joachimiak A., Christendat D.; RT "Crystal structure of a novel shikimate dehydrogenase from Haemophilus RT influenzae."; RL J. Biol. Chem. 280:17101-17108(2005). CC -!- FUNCTION: The physiological substrate is not known. Has much lower CC activity towards shikimate than AroE. CC {ECO:0000269|PubMed:15735308}. CC -!- CATALYTIC ACTIVITY: Shikimate + NAD(P)(+) = 3-dehydroshikimate + CC NADH. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15735308}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22266.1; -; Genomic_DNA. DR PIR; H64080; H64080. DR RefSeq; NP_438765.1; NC_000907.1. DR RefSeq; WP_005694543.1; NC_000907.1. DR PDB; 1NPY; X-ray; 1.75 A; A/B/C/D=1-271. DR PDBsum; 1NPY; -. DR ProteinModelPortal; P44774; -. DR SMR; P44774; 1-270. DR STRING; 71421.HI0607; -. DR EnsemblBacteria; AAC22266; AAC22266; HI_0607. DR GeneID; 949659; -. DR KEGG; hin:HI0607; -. DR PATRIC; 20189793; VBIHaeInf48452_0631. DR eggNOG; ENOG4105F9E; Bacteria. DR eggNOG; COG0169; LUCA. DR KO; K00014; -. DR OMA; FVYKAFT; -. DR OrthoDB; EOG6DZDX4; -. DR PhylomeDB; P44774; -. DR BRENDA; 1.1.1.282; 2529. DR EvolutionaryTrace; P44774; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 271 Shikimate 5-dehydrogenase-like protein FT HI_0607. FT /FTId=PRO_0000136073. FT NP_BIND 126 130 NADP. {ECO:0000250}. FT NP_BIND 235 239 NADP. {ECO:0000250}. FT ACT_SITE 67 67 Proton acceptor. {ECO:0000255}. FT BINDING 103 103 Substrate. {ECO:0000305}. FT MUTAGEN 67 67 K->A,H,N: Loss of activity. FT {ECO:0000269|PubMed:15735308}. FT MUTAGEN 103 103 D->A,N: Loss of activity. FT {ECO:0000269|PubMed:15735308}. FT STRAND 7 12 {ECO:0000244|PDB:1NPY}. FT HELIX 19 31 {ECO:0000244|PDB:1NPY}. FT STRAND 35 40 {ECO:0000244|PDB:1NPY}. FT HELIX 45 55 {ECO:0000244|PDB:1NPY}. FT STRAND 59 62 {ECO:0000244|PDB:1NPY}. FT TURN 67 70 {ECO:0000244|PDB:1NPY}. FT HELIX 71 73 {ECO:0000244|PDB:1NPY}. FT STRAND 75 77 {ECO:0000244|PDB:1NPY}. FT HELIX 79 82 {ECO:0000244|PDB:1NPY}. FT TURN 83 85 {ECO:0000244|PDB:1NPY}. FT STRAND 89 93 {ECO:0000244|PDB:1NPY}. FT STRAND 96 100 {ECO:0000244|PDB:1NPY}. FT HELIX 102 113 {ECO:0000244|PDB:1NPY}. FT STRAND 122 125 {ECO:0000244|PDB:1NPY}. FT HELIX 131 140 {ECO:0000244|PDB:1NPY}. FT STRAND 146 149 {ECO:0000244|PDB:1NPY}. FT HELIX 153 163 {ECO:0000244|PDB:1NPY}. FT STRAND 166 169 {ECO:0000244|PDB:1NPY}. FT STRAND 177 181 {ECO:0000244|PDB:1NPY}. FT TURN 191 194 {ECO:0000244|PDB:1NPY}. FT HELIX 200 205 {ECO:0000244|PDB:1NPY}. FT STRAND 207 211 {ECO:0000244|PDB:1NPY}. FT STRAND 215 218 {ECO:0000244|PDB:1NPY}. FT HELIX 220 227 {ECO:0000244|PDB:1NPY}. FT STRAND 231 233 {ECO:0000244|PDB:1NPY}. FT HELIX 235 251 {ECO:0000244|PDB:1NPY}. FT HELIX 257 268 {ECO:0000244|PDB:1NPY}. SQ SEQUENCE 271 AA; 29932 MW; A7A6AC9B9388394E CRC64; MINKDTQLCM SLSGRPSNFG TTFHNYLYDK LGLNFIYKAF TTQDIEHAIK GVRALGIRGC AVSMPFKETC MPFLDEIHPS AQAIESVNTI VNDNGFLRAY NTDYIAIVKL IEKYHLNKNA KVIVHGSGGM AKAVVAAFKN SGFEKLKIYA RNVKTGQYLA ALYGYAYINS LENQQADILV NVTSIGMKGG KEEMDLAFPK AFIDNASVAF DVVAMPVETP FIRYAQARGK QTISGAAVIV LQAVEQFELY THQRPSDELI AEAAAFARTK F // ID Y636_HAEIN Reviewed; 96 AA. AC P44027; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=UPF0381 protein HI_0636; GN OrderedLocusNames=HI_0636; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0381 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; L42023; AAC22295.1; -; Genomic_DNA. DR PIR; I64010; I64010. DR RefSeq; NP_438796.1; NC_000907.1. DR RefSeq; WP_010869023.1; NC_000907.1. DR ProteinModelPortal; P44027; -. DR STRING; 71421.HI0636; -. DR EnsemblBacteria; AAC22295; AAC22295; HI_0636. DR GeneID; 949687; -. DR KEGG; hin:HI0636; -. DR PATRIC; 20189879; VBIHaeInf48452_0664. DR eggNOG; ENOG4105KZW; Bacteria. DR eggNOG; COG3691; LUCA. DR OMA; PCEIQSE; -. DR OrthoDB; EOG62RSGC; -. DR PhylomeDB; P44027; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR005272; CHP00743. DR Pfam; PF04175; DUF406; 1. DR TIGRFAMs; TIGR00743; TIGR00743; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 96 UPF0381 protein HI_0636. FT /FTId=PRO_0000077939. SQ SEQUENCE 96 AA; 10966 MW; 7719CB9CFD29587F CRC64; MAIQTEKPIE CVGCNTFDMK SLFDNRDCSQ VIEYIYDSEG QAQEALAFFT QKARDVESEP CEIQSEITKV DDGYLLKADF TFCCQAELVI FQMRIA // ID Y650_HAEIN Reviewed; 70 AA. AC P44028; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_0650; GN OrderedLocusNames=HI_0650; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22318.1; -; Genomic_DNA. DR PIR; A64011; A64011. DR RefSeq; NP_438810.1; NC_000907.1. DR RefSeq; WP_005672404.1; NC_000907.1. DR STRING; 71421.HI0650; -. DR EnsemblBacteria; AAC22318; AAC22318; HI_0650. DR GeneID; 949696; -. DR KEGG; hin:HI0650; -. DR PATRIC; 20189915; VBIHaeInf48452_0679. DR eggNOG; COG5645; LUCA. DR OMA; AAYDLEM; -. DR OrthoDB; EOG6FRD33; -. DR Proteomes; UP000000579; 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; IPR010780; DUF1375. DR Pfam; PF07119; DUF1375; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 70 Uncharacterized protein HI_0650. FT /FTId=PRO_0000077940. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. SQ SEQUENCE 70 AA; 7763 MW; 7018E9FCADE1FDFF CRC64; MIKIFIFLTA LIVLSGCGSV VKLIDPTEKY TAYAGVAYDL EMAQQWGLPI LDLPLSFLLD TVLLPYAWAQ // ID Y658_HAEIN Reviewed; 638 AA. AC P44808; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 102. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_0658; GN OrderedLocusNames=HI_0658; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF CC family. EF3 subfamily. {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; L42023; AAC22317.1; -; Genomic_DNA. DR PIR; C64156; C64156. DR RefSeq; NP_438818.1; NC_000907.1. DR RefSeq; WP_005694483.1; NC_000907.1. DR ProteinModelPortal; P44808; -. DR STRING; 71421.HI0658; -. DR EnsemblBacteria; AAC22317; AAC22317; HI_0658. DR GeneID; 949699; -. DR KEGG; hin:HI0658; -. DR PATRIC; 20189931; VBIHaeInf48452_0687. DR eggNOG; ENOG4105C5H; Bacteria. DR eggNOG; COG0488; LUCA. DR KO; K06158; -. DR OMA; FYLVHDK; -. DR OrthoDB; EOG6F297F; -. DR PhylomeDB; P44808; -. DR Proteomes; UP000000579; 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; IPR032781; ABC_tran_Xtn. 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 Pfam; PF12848; ABC_tran_Xtn; 1. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 638 Uncharacterized ABC transporter ATP- FT binding protein HI_0658. FT /FTId=PRO_0000093189. FT DOMAIN 2 246 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 313 531 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 34 41 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 349 356 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 638 AA; 72231 MW; D04082E4ACB60099 CRC64; MIIFSNLSLK RGQTELLENA SATINPKQKV GLVGKNGCGK SSLFALLKKE LMPEGGEVNY PANWRVSWVN QETPALDISA IDYVIQGDRE YCRLQQKLER ANERNDGNAI ARIHGQLETL DAWTIQSRAA SLLHGLGFSQ EETIQPVKAF SGGWRMRLNL AQALLCPSDL LLLDEPTNHL DLDAVIWLER WLVQYQGTLV LISHDRDFLD PIVTKILHIE NQKLNEYTGD YSSFEVQRAT KLAQQTAMYR QQQQKISHLQ KYIDRFKAKA TKAKQAQSRM KALERMELIA PAYVDNPFTF EFRPPQSLPN PLVMIEQASA GYGIGESAVE ILSKIKLNLV PGSRIGLLGK NGAGKSTLIK LLAGELTALS GTVQLAKGVQ LGYFAQHQLD TLRADESALW HMQKLAPEQT EQQVRDYLGS FAFHGDKVNQ AVKSFSGGEK ARLVLALIVW QRPNLLLLDE PTNHLDLDMR QALTEALVDY EGSLVVVSHD RHLLRNTVEE FYLVHDKKVE EFKGDLEDYQ KWLSEQNSTS ENKVSEKVGD NENSVQNRKE QKRREAELRQ QTAPLRKKIT QLEEKMNKFS SELANIENQL ADTELYNAEN KEKLTALLAQ QVDVKKALDD VETEWMTAQE ELEEMLQA // ID Y659_HAEIN Reviewed; 98 AA. AC P44030; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0659; GN OrderedLocusNames=HI_0659; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22323.1; -; Genomic_DNA. DR PIR; C64011; C64011. DR RefSeq; NP_438819.1; NC_000907.1. DR RefSeq; WP_005650837.1; NC_000907.1. DR ProteinModelPortal; P44030; -. DR STRING; 71421.HI0659; -. DR EnsemblBacteria; AAC22323; AAC22323; HI_0659. DR GeneID; 949700; -. DR KEGG; hin:HI0659; -. DR PATRIC; 20189933; VBIHaeInf48452_0688. DR eggNOG; ENOG4105KDP; Bacteria. DR eggNOG; ENOG4111TZA; LUCA. DR OMA; ARHEQGI; -. DR OrthoDB; EOG6TBHDR; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 98 Uncharacterized HTH-type transcriptional FT regulator HI_0659. FT /FTId=PRO_0000149769. FT DOMAIN 37 91 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 48 67 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 98 AA; 11093 MW; 989E4DA324103ECC CRC64; MNKISPLGSN WNEFEQQIFN EEEIRESNLR VALIKELITS RQQLGISQKQ LETLSGVKQP MIARIEKGQT NPQLETLLKL LAPLGKTLSI VPLRVKNA // ID Y660_HAEIN Reviewed; 119 AA. AC P44031; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 65. DE RecName: Full=Uncharacterized protein HI_0660; GN OrderedLocusNames=HI_0660; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22324.1; -; Genomic_DNA. DR PIR; D64011; D64011. DR RefSeq; NP_438820.1; NC_000907.1. DR RefSeq; WP_005694481.1; NC_000907.1. DR STRING; 71421.HI0660; -. DR EnsemblBacteria; AAC22324; AAC22324; HI_0660. DR GeneID; 950644; -. DR KEGG; hin:HI0660; -. DR PATRIC; 20189935; VBIHaeInf48452_0689. DR eggNOG; ENOG4105MRD; Bacteria. DR eggNOG; ENOG4111TQJ; LUCA. DR OMA; WELRPGN; -. DR OrthoDB; EOG6K402X; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009241; HigB-like. DR Pfam; PF05973; Gp49; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein HI_0660. FT /FTId=PRO_0000077941. SQ SEQUENCE 119 AA; 14322 MW; 42AA62D445EAE1F6 CRC64; MYEILFYRDQ NDIEPVKEYL LSLAQNESKD SRIKLNKIRD YVKLLSELGT SVGKPYVKHL DGEIWELRPI RDRILFARLM DGRFVLLHQF MKKTQKTPKR EIQTAQQRLS ELKERLKNE // ID Y663_HAEIN Reviewed; 560 AA. AC P71355; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein HI_0663; GN OrderedLocusNames=HI_0663; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass 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; L42023; AAC22320.1; -; Genomic_DNA. DR RefSeq; NP_438822.1; NC_000907.1. DR ProteinModelPortal; P71355; -. DR STRING; 71421.HI0663m; -. DR EnsemblBacteria; AAC22320; AAC22320; HI_0663. DR GeneID; 949702; -. DR KEGG; hin:HI0663m; -. DR PATRIC; 20189941; VBIHaeInf48452_0692. DR eggNOG; ENOG4108JJ9; Bacteria. DR eggNOG; COG4988; LUCA. DR KO; K06148; -. DR OMA; TMQLNSV; -. DR OrthoDB; EOG6T7N3V; -. DR Proteomes; UP000000579; 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:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0006869; P:lipid transport; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 560 Uncharacterized ABC transporter ATP- FT binding protein HI_0663. FT /FTId=PRO_0000093201. FT TRANSMEM 2 22 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 32 52 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 108 128 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 138 160 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 168 188 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 223 243 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 249 269 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 1 281 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. FT DOMAIN 314 547 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 347 354 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 560 AA; 62197 MW; 65ADC0D0BC1347DE CRC64; MLWNWVALVG GIISAVVFSY ILQAAYFHEL SLLSAVILGI VLIAALALRA FAGKKSVQAS YFASTKVKHE LRSLIYRKLA SMPLNQVNQQ STSSIIQVAS EGVEQLEIYF GRYLPQLFYS LLAPLTLFAF LIFFSFKTAI ILLICVPLIP MSIIAVNKIA KKLLAKYWSI YVGLGSSFLD NLQGLITLKI YQDDAYKAKA MDKEAEHFRK ITMKVLTMQL NSVSLMDLLA YGGAAIGILT ALLQFQNAQL SVLGVILFIL LSSEFFIPLR LLGSFFHVAM NGKAASDKIF TLLDTPVETQ QSAVDFEAKN NVQVEIKDLH FSYSEEKPAI TGLNLSILPN QLSVFVGKSG CGKSTLVSLL MGFNKAQQGE ILFNGQNALN IDRTSFYQKV SLVSHSSYVF KGTLRENMTM AKIDATDEQI YACLEQVNLA QFVRDNGGLD MQLLSRGANL SGGQIQRLAL ARALLHNAEL YIFDEATSNI DVESEEIILQ FIQQFKQQKT IVMISHRLAN AVNADCINVL DQGKLIEQGT HKELMEKQGA YAEMFQQQKD LEQIREVANA // ID Y666A_HAEIN Reviewed; 102 AA. AC O86228; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0666.1; GN OrderedLocusNames=HI_0666.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22327.1; -; Genomic_DNA. DR RefSeq; NP_438826.1; NC_000907.1. DR RefSeq; WP_010869030.1; NC_000907.1. DR STRING; 71421.HI0666.1; -. DR EnsemblBacteria; AAC22327; AAC22327; HI_0666.1. DR GeneID; 949707; -. DR KEGG; hin:HI0666.1; -. DR PATRIC; 20189949; VBIHaeInf48452_0696. DR eggNOG; ENOG4107A4G; Bacteria. DR eggNOG; COG1396; LUCA. DR OMA; ITYEQSQ; -. DR OrthoDB; EOG6CS06W; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 102 Uncharacterized HTH-type transcriptional FT regulator HI_0666.1. FT /FTId=PRO_0000149770. FT DOMAIN 48 102 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 59 78 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 102 AA; 11464 MW; 758B266497F9789B CRC64; MDNLSAQLEN QIDELKKLQK SVITYEQAQR QQLYAGKITD LKAFGKMLND KRKSLGIELS MLELQTGVSI STLNRLFQDP SQVRFTTVFL VAQTLGVSLC AI // ID Y775_HAEIN Reviewed; 315 AA. AC P44876; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0775; GN OrderedLocusNames=HI_0775; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22434.1; -; Genomic_DNA. DR PIR; C64092; C64092. DR RefSeq; NP_438934.2; NC_000907.1. DR ProteinModelPortal; P44876; -. DR STRING; 71421.HI0775; -. DR DNASU; 950670; -. DR EnsemblBacteria; AAC22434; AAC22434; HI_0775. DR GeneID; 950670; -. DR KEGG; hin:HI0775; -. DR PATRIC; 20190201; VBIHaeInf48452_0814. DR eggNOG; ENOG4105CMU; Bacteria. DR eggNOG; ENOG410XNYY; LUCA. DR OMA; KGIQQNM; -. DR OrthoDB; EOG686NKK; -. DR Proteomes; UP000000579; 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; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 315 Uncharacterized HTH-type transcriptional FT regulator HI_0775. FT /FTId=PRO_0000105810. FT DOMAIN 16 74 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 34 53 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 315 AA; 36679 MW; C38F209C599BDB9C CRC64; MLYFVKMAVL RGVKMMDIRH LRYFVSIVDN DFNLSRASQN LYVSQPALSM MITEFENREN IQIFKRASGK IIGLTFAGEN YYRDAKEVIK RYNDMRTNLY KSKDCKKGTI TIGIPPLVLS AVFSSVLPHL ILKNPDINFI IKEIGAYALK SELLLDKVDL AVLLYPERIS KNIIDSIEIH SSELALFLSP KHVLAKKQQI TWADLHQQKM AIFDQTFMIH HHLKEAFERN NCYPDIVLDS SCWDFLLSAV KTNKELLTIL PLPMAELYHS KEFLCRKIES PVPWKVTLCR QRKTVYTHLE EYIFDKLLEA FRPTK // ID Y842_HAEIN Reviewed; 276 AA. AC P44058; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=Uncharacterized protein HI_0842; DE Flags: Precursor; GN OrderedLocusNames=HI_0842; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22510.1; -; Genomic_DNA. DR PIR; D64014; D64014. DR ProteinModelPortal; P44058; -. DR STRING; 71421.HI0842; -. DR DNASU; 949857; -. DR EnsemblBacteria; AAC22510; AAC22510; HI_0842. DR PATRIC; 20190339; VBIHaeInf48452_0883. DR eggNOG; COG0402; LUCA. DR OMA; MRQAKMM; -. DR OrthoDB; EOG696BT4; -. DR PhylomeDB; P44058; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004131; F:cytosine deaminase activity; IBA:GO_Central. DR GO; GO:0035888; F:isoguanine deaminase activity; IBA:GO_Central. DR GO; GO:0006209; P:cytosine catabolic process; IBA:GO_Central. DR InterPro; IPR032466; Metal_Hydrolase. DR SUPFAM; SSF51556; SSF51556; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 276 Uncharacterized protein HI_0842. FT /FTId=PRO_0000013960. SQ SEQUENCE 276 AA; 31570 MW; 54E8C330886F7EF8 CRC64; MKSHVRSFKT YIRDEIIKKG GWVNAHAHAD RAFTMTPEKI GIYHSSNLQQ KWDLVDEVKR TSSVDDYYAR FCQSIELMIS QGVTAFGTFV DIDPICEDRA IIAAHKAREV YKHDIILKFA NQTLKGVIEP TARKWFDIGA EMVDMIGGLP YRDELDYGRG LEAMDILLDK AKSLGIMCHV HVDQFNNPSE KETEQLCDKT IEHGMEGRVV GIHGISIGSH SKEYRYKLYE KMRKAKMMMI ACPMAWIDSN RKEDLMPFHN ALTPADEMIP EVSLLP // ID Y845_HAEIN Reviewed; 88 AA. AC P44900; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0845; DE AltName: Full=ORF1; GN OrderedLocusNames=HI_0845; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1438213; DOI=10.1073/pnas.89.21.10252; RA Tomb J.-F.; RT "A periplasmic protein disulfide oxidoreductase is required for RT transformation of Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10252-10256(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YihD. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M94205; AAA24955.1; -; Genomic_DNA. DR EMBL; L42023; AAC22502.1; -; Genomic_DNA. DR PIR; G64159; A46411. DR RefSeq; NP_439005.1; NC_000907.1. DR RefSeq; WP_005693195.1; NC_000907.1. DR ProteinModelPortal; P44900; -. DR STRING; 71421.HI0845; -. DR EnsemblBacteria; AAC22502; AAC22502; HI_0845. DR GeneID; 950597; -. DR KEGG; hin:HI0845; -. DR PATRIC; 20190345; VBIHaeInf48452_0886. DR eggNOG; COG3084; LUCA. DR KO; K09896; -. DR OMA; KDEMIPG; -. DR OrthoDB; EOG6JB17F; -. DR PhylomeDB; P44900; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009383; DUF1040. DR Pfam; PF06288; DUF1040; 1. DR ProDom; PD029038; DUF1040; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 88 Uncharacterized protein HI_0845. FT /FTId=PRO_0000169673. SQ SEQUENCE 88 AA; 10282 MW; 52598B58E65F93E4 CRC64; MKCKRLNEVL ELLQSYWSKD SDLSLMEILQ KIANESGFQK PLNELTDEVI IYQLKMDGTD KYEPIPGLKK DYEEDFKTAL LRARGIIK // ID Y847_HAEIN Reviewed; 111 AA. AC P31811; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 81. DE RecName: Full=UPF0438 protein HI_0847; DE AltName: Full=ORF3; GN OrderedLocusNames=HI_0847; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=1438213; DOI=10.1073/pnas.89.21.10252; RA Tomb J.-F.; RT "A periplasmic protein disulfide oxidoreductase is required for RT transformation of Haemophilus influenzae Rd."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10252-10256(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Not known, a mutation in ORF3 causes a slight decrease CC in transformation efficiency. CC -!- SIMILARITY: Belongs to the UPF0438 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; M94205; AAA24957.1; -; Genomic_DNA. DR EMBL; L42023; AAC22504.1; -; Genomic_DNA. DR PIR; H64159; H64159. DR RefSeq; NP_439007.1; NC_000907.1. DR RefSeq; WP_005648303.1; NC_000907.1. DR STRING; 71421.HI0847; -. DR EnsemblBacteria; AAC22504; AAC22504; HI_0847. DR GeneID; 950632; -. DR KEGG; hin:HI0847; -. DR PATRIC; 20190349; VBIHaeInf48452_0888. DR eggNOG; ENOG4108WFC; Bacteria. DR eggNOG; COG3085; LUCA. DR KO; K09897; -. DR OMA; QFVAVCR; -. DR OrthoDB; EOG60KN53; -. DR PhylomeDB; P31811; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007335; DUF413. DR Pfam; PF04219; DUF413; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 111 UPF0438 protein HI_0847. FT /FTId=PRO_0000169645. FT CONFLICT 109 111 SGE -> PANKIR (in Ref. 1; AAA24957). FT {ECO:0000305}. SQ SEQUENCE 111 AA; 12805 MW; F410A609C2135066 CRC64; MAASFSVTRR FFDDKNYPRG FSRHGDYTIK ESQVLEQYGQ AFKALDLGER EPATKEEKDF VAFCRGERAA ETFFEKTWNK YRTRINTKKR VYTLSSDVSE AASGGEDYSG E // ID Y869_HAEIN Reviewed; 185 AA. AC P44064; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 69. DE RecName: Full=Uncharacterized protein HI_0869; GN OrderedLocusNames=HI_0869; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22528.1; -; Genomic_DNA. DR PIR; A64015; A64015. DR ProteinModelPortal; P44064; -. DR STRING; 71421.HI0869; -. DR EnsemblBacteria; AAC22528; AAC22528; HI_0869. DR PATRIC; 20190393; VBIHaeInf48452_0910. DR eggNOG; ENOG4107G2Y; Bacteria. DR eggNOG; ENOG410Z8ZC; LUCA. DR OrthoDB; EOG68SVW5; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 185 Uncharacterized protein HI_0869. FT /FTId=PRO_0000077963. SQ SEQUENCE 185 AA; 20858 MW; E0F7BC52B1A7FCC0 CRC64; MPIMDLLNTR NKNMISLLII SFGRYQEVLE TFACVNKYHG NKIELLFLDN NPERELEADL SSIVENNSGI LFSYFHTGEN LGVAEGRNFL IEKAQGDILI TLDDDVEIED ITLLIQKVTD YMANNAKVGA LAFNIKNYFT RKALSHEIPH GNKKLDFSQN LLTYYFIGAG HAIREKSLSK SGALP // ID Y871_HAEIN Reviewed; 306 AA. AC P44066; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_0871; GN OrderedLocusNames=HI_0871; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22537.1; -; Genomic_DNA. DR PIR; C64015; C64015. DR RefSeq; NP_439032.1; NC_000907.1. DR RefSeq; WP_005693221.1; NC_000907.1. DR STRING; 71421.HI0871; -. DR EnsemblBacteria; AAC22537; AAC22537; HI_0871. DR GeneID; 949881; -. DR KEGG; hin:HI0871; -. DR PATRIC; 20190397; VBIHaeInf48452_0912. DR eggNOG; ENOG41066S7; Bacteria. DR eggNOG; ENOG41129FM; LUCA. DR OMA; KVEYINI; -. DR OrthoDB; EOG67DPHN; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR012477; Glyco_transf_52. DR Pfam; PF07922; Glyco_transf_52; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 306 Uncharacterized protein HI_0871. FT /FTId=PRO_0000077966. SQ SEQUENCE 306 AA; 36173 MW; A6D7BD96D2B34F5C CRC64; MKFVSIISNS RMLFLFLLIT AKSDRESCLY IFDENIRGVN ITPTFVSTRA KGLFDLFIKK LRSRVALSFF LLKRKIKLEE TIVYGADHLS HSLLFLKKCS FFLIEDGTEN YHQKSYKRSW KNKLFSIPKF GMYKNVKRIY LTKRENVPDC IKSKVEYINI KDLWFKKTEE EKLEILYLLG IDMKKIQLLI GEPFILFTQP LSEDYILTEN EKIELYKSII DKYDASKLVI KPHPREKTDY SRIFPNVKVF DETYPSEVLD ILEVKFSRVI TLFSTAAFSY PKEKVDFYGT KIHPKLLAKF GNIEYE // ID Y930_HAEIN Reviewed; 206 AA. AC P44077; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_0930; GN OrderedLocusNames=HI_0930; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22600.1; -; Genomic_DNA. DR PIR; E64016; E64016. DR RefSeq; NP_439090.1; NC_000907.1. DR RefSeq; WP_010869088.1; NC_000907.1. DR STRING; 71421.HI0930; -. DR EnsemblBacteria; AAC22600; AAC22600; HI_0930. DR GeneID; 949932; -. DR KEGG; hin:HI0930; -. DR PATRIC; 20190517; VBIHaeInf48452_0971. DR OMA; KIELCEA; -. DR OrthoDB; EOG61042Z; -. DR Proteomes; UP000000579; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 206 Uncharacterized protein HI_0930. FT /FTId=PRO_0000077976. SQ SEQUENCE 206 AA; 21841 MW; B7D3950FEC6B9FAB CRC64; MARRKNHSIK IENNEKENQI LVSLSIVALL GGCSEEQVQR DVYQSLDDCL ADWKKIELCE ADKNTESTQK TATTQQQGLG LNIRDNGNAE SAVKNPAENN AQANQSENRA ESTTKAESTD PSLGAAIAGG VIGYMAARAI SSFLGPSYHP GNRAVTTPTG QVVQPQTNRS VGKPMLVKGN AGSMNSKPVS RGGFSSPNKT HRSSGG // ID Y938_HAEIN Reviewed; 170 AA. AC P44079; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=Uncharacterized protein HI_0938; GN OrderedLocusNames=HI_0938; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22602.1; -; Genomic_DNA. DR PIR; G64016; G64016. DR RefSeq; NP_439098.1; NC_000907.1. DR RefSeq; WP_005693285.1; NC_000907.1. DR STRING; 71421.HI0938; -. DR EnsemblBacteria; AAC22602; AAC22602; HI_0938. DR GeneID; 949906; -. DR KEGG; hin:HI0938; -. DR PATRIC; 20190533; VBIHaeInf48452_0979. DR eggNOG; COG2165; LUCA. DR KO; K02679; -. DR OMA; SACVNDE; -. DR OrthoDB; EOG6C5RP8; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR012902; N_methyl_site. DR Pfam; PF13633; N_methyl_3; 1. DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 170 Uncharacterized protein HI_0938. FT /FTId=PRO_0000077978. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 170 AA; 19835 MW; E7C78D84ED9D559C CRC64; MQKGMTLVEL LIGLAIISIA LNFAVPLWKT DSPKTILAKE QHRLYLFLRQ IQARAENSSE VWFLLINRNL ATQQWCLTAQ VKNNQTCDCL NPINCPKEVY AHFYYPYFPN KTMIQSHHIY PKEITRFDGI RNTIVTRCFI LQAENERTLF LFFNVGSIRV KTNQFDSACN // ID Y952_HAEIN Reviewed; 221 AA. AC P44952; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2003, sequence version 2. DT 09-DEC-2015, entry version 100. DE RecName: Full=UPF0758 protein HI_0952; GN OrderedLocusNames=HI_0952; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22613.1; 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; L42023; AAC22613.1; ALT_INIT; Genomic_DNA. DR PIR; F64104; F64104. DR RefSeq; NP_439113.2; NC_000907.1. DR RefSeq; WP_010869094.1; NC_000907.1. DR ProteinModelPortal; P44952; -. DR STRING; 71421.HI0952; -. DR EnsemblBacteria; AAC22613; AAC22613; HI_0952. DR GeneID; 949958; -. DR KEGG; hin:HI0952; -. DR PATRIC; 20190563; VBIHaeInf48452_0994. DR eggNOG; ENOG4105W5Q; Bacteria. DR eggNOG; COG2003; LUCA. DR KO; K03630; -. DR OMA; PHEEFWV; -. DR OrthoDB; EOG6RRKTV; -. DR PhylomeDB; P44952; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR001405; RadC. DR InterPro; IPR025657; RadC_JAB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR020891; UPF0758_CS. DR Pfam; PF04002; RadC; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00608; radc; 1. DR PROSITE; PS01302; UPF0758; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 221 UPF0758 protein HI_0952. FT /FTId=PRO_0000190703. SQ SEQUENCE 221 AA; 25028 MW; D76ACEF7BB8ED605 CRC64; MENNDELMPR EKLLAFGAKA LSDYELLAIF LRTGIKGCPV MSLSKNVLTH FGPLHALLSA DKKAFCSVKG LGITQFIQLQ AITEMTKRYL KQDMLSTPII NDPETVKLFL LTELQHEERE VFMVLFLDNQ HRLIKKERLF LGTIYVSAVY PREIIKEALY CNAAALILAH NHPSGITEPS YSDQLITKKI QDAAELMEIR VLDHLIVGKS DCYSFAENCL L // ID Y974A_HAEIN Reviewed; 85 AA. AC P46455; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein HI_0974.1; GN OrderedLocusNames=HI_0974.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA Koonin E.V., Rudd K.E.; RL Submitted (SEP-1995) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli YhdT. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22633.1; -; Genomic_DNA. DR RefSeq; NP_439136.1; NC_000907.1. DR RefSeq; WP_005647974.1; NC_000907.1. DR STRING; 71421.HI0974.1; -. DR EnsemblBacteria; AAC22633; AAC22633; HI_0974.1. DR GeneID; 949407; -. DR KEGG; hin:HI0974.1; -. DR PATRIC; 20190607; VBIHaeInf48452_1016. DR eggNOG; ENOG4105RG0; Bacteria. DR eggNOG; COG3924; LUCA. DR OMA; WFELACL; -. DR OrthoDB; EOG6J1DF7; -. DR PhylomeDB; P46455; -. DR Proteomes; UP000000579; 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; IPR010398; DUF997. DR Pfam; PF06196; DUF997; 1. DR ProDom; PD745092; DUF997; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 85 Uncharacterized protein HI_0974.1. FT /FTId=PRO_0000169498. FT TRANSMEM 16 34 Helical. {ECO:0000255}. FT TRANSMEM 50 71 Helical. {ECO:0000255}. SQ SEQUENCE 85 AA; 9818 MW; 847A3E2C627C11CF CRC64; MTLKQRYQQA GKEASWALSL SILYVIGWCL CAYLPKETQG PIGFPLWFEL SCIYLPILFI VIGHWIIKII FQDISLEIND QGNQK // ID Y976A_HAEIN Reviewed; 170 AA. AC O86230; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized transporter HI_0976.1; GN OrderedLocusNames=HI_0976.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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 EamA transporter family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 EamA 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; L42023; AAC22636.1; -; Genomic_DNA. DR STRING; 71421.HI0976.1; -. DR TCDB; 2.A.7.3.30; the drug/metabolite transporter (dmt) superfamily. DR EnsemblBacteria; AAC22636; AAC22636; HI_0976.1. DR PATRIC; 20190613; VBIHaeInf48452_1019. DR eggNOG; COG0697; LUCA. DR OrthoDB; EOG6M0T4B; -. DR PhylomeDB; O86230; -. DR Proteomes; UP000000579; 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; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 170 Uncharacterized transporter HI_0976.1. FT /FTId=PRO_0000108192. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT DOMAIN 35 161 EamA. SQ SEQUENCE 170 AA; 17972 MW; 64BD70D83E242603 CRC64; MAFIGVAILI NGGKNNEGID NISLFGCLLV LSAGIIFAAV LRWTQRVVAK VSTQAYTSVS IVLGTITTLP FTLLLTENWQ ISLNSTGIAG LLYLAIGCSW LAYWLWNKGL NSVDANISGV LVALEPLFGI LFAVSLLGET LSFSAALGIT IIMLATLGST LLPKLLKKSV // ID Y997_HAEIN Reviewed; 229 AA. AC P44090; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 52. DE RecName: Full=Uncharacterized protein HI_0997; GN OrderedLocusNames=HI_0997; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22659.1; -; Genomic_DNA. DR PIR; I64017; I64017. DR EnsemblBacteria; AAC22659; AAC22659; HI_0997. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 229 Uncharacterized protein HI_0997. FT /FTId=PRO_0000077990. SQ SEQUENCE 229 AA; 27240 MW; 86759D5D484F4E31 CRC64; MFNGNGKYYW DNKKYNEATV RIGGGLGYQT ASVEVSLFPF QEKRWYAGGS SGTNTMKQYA DKLGIRLENV DWLSKTWQIS TALEYGESRY KIRKHLDGNY YFVSSTLFYL PKSTQFWFVG MDFHRENTQA LDNAYQQKTL RLGWGQDWFY GISSRLTFSY ANRVYREKDL IGIQQKNREY TTTITLWHRN IHFMGLTPKL SWDYQKSTSN HAFYRYDKNR IYLEIGKIF // ID Y350_HAEIN Reviewed; 425 AA. AC P24326; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 17-FEB-2016, entry version 104. DE RecName: Full=Uncharacterized protein HI_0350; DE AltName: Full=ORF3; GN OrderedLocusNames=HI_0350; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1956282; DOI=10.1111/j.1365-2958.1991.tb01874.x; RA Maskell D.J., Szabo M.J., Butler P.D., Williams A.E., Moxon E.R.; RT "Molecular analysis of a complex locus from Haemophilus influenzae RT involved in phase-variable lipopolysaccharide biosynthesis."; RL Mol. Microbiol. 5:1013-1022(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: To E.coli AmpG and yeast YBR220c. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57315; CAA40569.1; -; Genomic_DNA. DR EMBL; L42023; AAC22011.1; -; Genomic_DNA. DR PIR; D64149; D64149. DR RefSeq; NP_438514.1; NC_000907.1. DR RefSeq; WP_005694326.1; NC_000907.1. DR ProteinModelPortal; P24326; -. DR STRING; 71421.HI0350; -. DR EnsemblBacteria; AAC22011; AAC22011; HI_0350. DR GeneID; 949456; -. DR KEGG; hin:HI0350; -. DR PATRIC; 20189247; VBIHaeInf48452_0369. DR eggNOG; ENOG4105EYM; Bacteria. DR eggNOG; COG0477; LUCA. DR KO; K08218; -. DR OMA; GYFSWIA; -. DR OrthoDB; EOG6PS5R8; -. DR PhylomeDB; P24326; -. DR Proteomes; UP000000579; 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:0015295; F:solute:proton symporter activity; IBA:GO_Central. DR GO; GO:0015835; P:peptidoglycan transport; IBA:GO_Central. DR GO; GO:0015992; P:proton transport; IBA:GOC. DR InterPro; IPR004752; AmpG_permease/AT-1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR TIGRFAMs; TIGR00901; 2A0125; 1. PE 4: Predicted; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 425 Uncharacterized protein HI_0350. FT /FTId=PRO_0000077914. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 174 194 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TRANSMEM 271 291 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TRANSMEM 331 351 Helical. {ECO:0000255}. FT TRANSMEM 370 390 Helical. {ECO:0000255}. FT TRANSMEM 395 415 Helical. {ECO:0000255}. FT VARIANT 5 5 L -> F (in strain: RM 7004). FT VARIANT 32 32 S -> L (in strain: RM 7004). FT VARIANT 271 271 A -> S (in strain: RM 7004). FT VARIANT 313 313 A -> S (in strain: RM 7004). FT VARIANT 415 415 L -> W (in strain: RM 7004). FT VARIANT 418 418 E -> K (in strain: RM 7004). SQ SEQUENCE 425 AA; 47354 MW; 2757C3F61B08FAB5 CRC64; MSNSLSSQIF TRKMLICAFT GFNSGLPLFV LSQMLPVWLT DKHLSIELIG AVTGVMLPYG LKFLWAPLLD RYFPSFLGRR RSWMLLSQVA LLILLYIISL FDPLTQLGTV ANIALLIAFF SATQDIVLDA YRREILSDHE LGLGNTIHIN AYRIAGLIPG GLSLYLAAIY PWETVFLWTA LCMLAGIFMT LFLAKEPKID MQQTNQPFYQ AFWIPLQEFF QRKGVIQAIG FLLFLFLYKF GDSFATTLQT KFIYDMGFSK EDIAIVVKST ALWSSILSGL AGGMIMLKLG INRALWLFGL VQMVTIGGFI WLAAFGHFDV ITSAELWKLG VVIAAEYIGV GLGTAAFVAF MARESNPLYT ATQLALFTSL SALPSKVLGI LSGYVVGAVG YYQYFWFCLF LAIPGMLCLF WVAPLKQENN KTSSV // ID Y359_HAEIN Reviewed; 271 AA. AC P44660; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Probable iron transport system membrane protein HI_0359; GN OrderedLocusNames=HI_0359; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of an ATP-driven transport system CC HI_0359/HI_0360/HI_0361/HI_0362 for iron. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22018.1; -; Genomic_DNA. DR PIR; G64149; G64149. DR RefSeq; NP_438521.1; NC_000907.1. DR RefSeq; WP_005666622.1; NC_000907.1. DR ProteinModelPortal; P44660; -. DR STRING; 71421.HI0359; -. DR EnsemblBacteria; AAC22018; AAC22018; HI_0359. DR GeneID; 949465; -. DR KEGG; hin:HI0359; -. DR PATRIC; 20189263; VBIHaeInf48452_0377. DR eggNOG; ENOG4105CC5; Bacteria. DR eggNOG; COG1108; LUCA. DR KO; K11606; -. DR OMA; SHSVMPG; -. DR OrthoDB; EOG67Q9FM; -. DR PhylomeDB; P44660; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR001626; ABC_3. DR InterPro; IPR029022; ABC_BtuC-like. DR Pfam; PF00950; ABC-3; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Iron; Iron transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 271 Probable iron transport system membrane FT protein HI_0359. FT /FTId=PRO_0000171172. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 221 241 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. SQ SEQUENCE 271 AA; 29392 MW; 061625ECA2927EAC CRC64; MFDWLLEPLQ FEFMQNALLT ALIVSIICAL LSCYLVLKGW SLMGDAISHA VLPGIVLAYL AGIPLAIGAF FSGIFCSLGV GYLKENSRIK EDTAMGIVFS GMFAIGLVMF TKIQTEEHLT HILFGNVLGV SHQELIQSAV ISAIIFCLIV FKRKDFLLYC FDPSHARVAG LSPKILHYGL LILLALTIVS TMQVVGVILV VAMLIAPGIT ALTLTKSFDK MLWVAIASSI ASSLIGVILS YHFDASTGAC IILLQAAFFV IALAYSKIRI R // ID Y366_HAEIN Reviewed; 179 AA. AC P43988; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Uncharacterized protein HI_0366; DE Flags: Precursor; GN OrderedLocusNames=HI_0366; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22024.1; -; Genomic_DNA. DR PIR; F64006; F64006. DR RefSeq; NP_438527.1; NC_000907.1. DR RefSeq; WP_005693799.1; NC_000907.1. DR ProteinModelPortal; P43988; -. DR STRING; 71421.HI0366; -. DR EnsemblBacteria; AAC22024; AAC22024; HI_0366. DR GeneID; 949468; -. DR KEGG; hin:HI0366; -. DR PATRIC; 20189277; VBIHaeInf48452_0384. DR eggNOG; ENOG41090FY; Bacteria. DR eggNOG; COG3063; LUCA. DR KO; K02656; -. DR OMA; AYYYQQI; -. DR OrthoDB; EOG6Q2SH3; -. DR PhylomeDB; P43988; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013360; Pilus_4_PilW. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. DR TIGRFAMs; TIGR02521; type_IV_pilW; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 27 Or 24. {ECO:0000255|PROSITE- FT ProRule:PRU00303}. FT CHAIN 28 179 Uncharacterized protein HI_0366. FT /FTId=PRO_0000013957. SQ SEQUENCE 179 AA; 20598 MW; 2E00E42625E8ADA4 CRC64; MKTISKQLSA VIFPFIFSAC VSQSASSLNH QTAAKARVEL ALSYLQQNNP QLAKINLDKA LQHDKNYYLV HSALAHYYQQ QGQIENAFRE YEIAVNLNHK QGDVHNNFGT FLCSQKKFEQ AQQQFELALN SPNYYHQADT FENIVLCAYS AQKMDIYQQT LEKLRQIDGK RAEKFNSLK // ID Y476_HAEIN Reviewed; 50 AA. AC P44002; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 51. DE RecName: Full=Uncharacterized protein HI_0476; GN OrderedLocusNames=HI_0476; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22144.1; -; Genomic_DNA. DR PIR; B64008; B64008. DR EnsemblBacteria; AAC22144; AAC22144; HI_0476. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 50 Uncharacterized protein HI_0476. FT /FTId=PRO_0000077927. SQ SEQUENCE 50 AA; 6005 MW; 7640A36378D5B83C CRC64; MVIKCIDKQQ NLGNIILFLL LKQQYSKEDS KKFTIYKFYL QTVNYTIQLS // ID Y493_HAEIN Reviewed; 118 AA. AC O05023; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized transposase-like protein HI_0493; GN OrderedLocusNames=HI_0493; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the transposase IS3/IS150/IS904 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; L42023; AAC22150.1; -; Genomic_DNA. DR PIR; D64153; D64153. DR RefSeq; NP_438652.1; NC_000907.1. DR RefSeq; WP_005693678.1; NC_000907.1. DR STRING; 71421.HI0493; -. DR DNASU; 949783; -. DR EnsemblBacteria; AAC22150; AAC22150; HI_0493. DR GeneID; 949783; -. DR KEGG; hin:HI0493; -. DR PATRIC; 20189537; VBIHaeInf48452_0511. DR eggNOG; COG2801; LUCA. DR KO; K07497; -. DR OMA; KRFETFK; -. DR OrthoDB; EOG664CH4; -. DR PhylomeDB; O05023; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Reference proteome; KW Transposable element; Transposition. FT CHAIN 1 118 Uncharacterized transposase-like protein FT HI_0493. FT /FTId=PRO_0000075488. SQ SEQUENCE 118 AA; 13997 MW; 040C20A2D5BAA5C7 CRC64; MRGRTRIGKF TTCGERNPKK VARTQPTKKD LKTQNPILHS DQGWLYQMVG YQAILRENSI QQNMSRKGNY LDNNAMENFF GRLKTECYYD KRFETFKQLK KQLMSIFIIT TMITFRGN // ID Y568_HAEIN Reviewed; 762 AA. AC P71353; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Uncharacterized protein HI_0568; GN OrderedLocusNames=HI_0568; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22226.1; -; Genomic_DNA. DR RefSeq; NP_438725.1; NC_000907.1. DR RefSeq; WP_010869009.1; NC_000907.1. DR ProteinModelPortal; P71353; -. DR SMR; P71353; 6-724. DR STRING; 71421.HI0568; -. DR EnsemblBacteria; AAC22226; AAC22226; HI_0568. DR GeneID; 949614; -. DR KEGG; hin:HI0568; -. DR PATRIC; 20189691; VBIHaeInf48452_0588. DR eggNOG; ENOG4105BZM; Bacteria. DR eggNOG; COG2183; LUCA. DR KO; K06959; -. DR OMA; GFLRIRD; -. DR OrthoDB; EOG6WT8CC; -. DR PhylomeDB; P71353; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 1.10.10.650; -; 1. DR Gene3D; 1.10.150.310; -; 1. DR Gene3D; 1.10.3500.10; -; 2. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.420.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR012337; RNaseH-like_dom. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR023323; Tex-like_dom. DR InterPro; IPR023319; Tex-like_HTH_dom. DR InterPro; IPR018974; Tex-like_N. DR InterPro; IPR023097; Tex_RuvX-like_dom. DR InterPro; IPR032639; Tex_YqgF. DR InterPro; IPR006641; YqgF/RNaseH-like_dom. DR Pfam; PF00575; S1; 1. DR Pfam; PF09371; Tex_N; 1. DR Pfam; PF16921; Tex_YqgF; 1. DR SMART; SM00316; S1; 1. DR SMART; SM00732; YqgFc; 1. DR SUPFAM; SSF47781; SSF47781; 2. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 762 Uncharacterized protein HI_0568. FT /FTId=PRO_0000215105. FT DOMAIN 651 720 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. SQ SEQUENCE 762 AA; 84425 MW; D5172BDD11F5736B CRC64; MLNQQISQII AAELTVQPQQ IFAAIQLLDD GNTIPFIARY RKEATGGLDD TQLRHFETRL IYLRELEDRR QTILKSIEEQ GKLTDELRDK IHATQSKTEL EDLYLPYKPK RRTKGQIAIE AGLEPLANLL WNEPKNDPES TALSFVDAEK GVADSKAALD GARIILMERF AEDAGLLAKV RDYLAKNAVI VSKVIEGKET EGAKFQDYFD HQELLKNVPS HRALAMFRGR NEGILQLSLN ADPDAEEGSR QSYCEEIIRD YLDVRFTGQP ADKWREQVIA WTWKIKVSLH LETELMASLR EKAEEEAIDV FARNLTALLM AAPAGAKSTM GLDPGLRTGV KVAMVDNTGK LLDTTTIYPH TGREAEAQVA IFSLIRKHNV ELIAIGNGTA SRETERFAKD VIKEIKENKP QTVVVSEAGA SVYSASEFAA NEFPNLDVSL RGAVSIARRL QDPLAELVKI EPKAIGVGQY QHDVNQTQLA RKLDAVVEDC VNAVGVDLNT ASAPLLARVA GMTKTLAQNI VEYRDENGRF ESRSELKKVP RLGPKAFEQC AGFMRIANGK NPLDASGVHP EAYPVVEKIL QATAQSIQDL MSNAGVVRQL DAKQFIDEQF GLPTVQDIFK ELEKPGRDPR GEFKTAVFAE GVEEITDLKS GMILEGTVTN VTNFGAFVDI GVHQDGLVHI SSLSDKFVED PHQVVKTGNI VKVKVLEVDV PRKRIALTMR LDESAVKNDS KSDRTLSTRP RGNMQREARN SRGNNVIGNA FA // ID Y647_HAEIN Reviewed; 238 AA. AC Q57424; O05028; 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=Uncharacterized protein HI_0647; GN OrderedLocusNames=HI_0647; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MgtC/SapB 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; L42023; AAC22307.1; -; Genomic_DNA. DR PIR; A64156; A64156. DR RefSeq; NP_438807.1; NC_000907.1. DR RefSeq; WP_005654516.1; NC_000907.1. DR STRING; 71421.HI0647; -. DR EnsemblBacteria; AAC22307; AAC22307; HI_0647. DR GeneID; 949408; -. DR KEGG; hin:HI0647; -. DR PATRIC; 20189909; VBIHaeInf48452_0676. DR eggNOG; ENOG4105KT7; Bacteria. DR eggNOG; COG1285; LUCA. DR KO; K07507; -. DR OrthoDB; EOG6RVFVG; -. DR PhylomeDB; Q57424; -. DR Proteomes; UP000000579; 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; IPR003416; MgtC/SapB/SrpB/YhiD_fam. DR Pfam; PF02308; MgtC; 1. DR PRINTS; PR01837; MGTCSAPBPROT. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 238 Uncharacterized protein HI_0647. FT /FTId=PRO_0000202034. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. SQ SEQUENCE 238 AA; 25892 MW; 923429C32EC630E8 CRC64; MENSSLLLTA LFNPDHLIIF SKMLLAMVLG SVIGLERELK RKPVGVKTCA IIAVTTCVLT IVSIQAAEHY AQVSENIRTD PMRLAAQVIS GIGFLGAGVI LHKKNDAISG LTTAAIIWAS AGIGIAAGAG FVFDAVIATV MILVSIRLSP LVQRWVHRKS QRRRTKFNIL VNDAESIGKV TQLLVNNQYR IEHIQVKDQS SGEVRLQIRC FSIDSTMLKD AYALLKAEDG VISVEVDN // ID Y704_HAEIN Reviewed; 61 AA. AC P44040; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0704; GN OrderedLocusNames=HI_0704; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22367.1; -; Genomic_DNA. DR PIR; D64012; D64012. DR RefSeq; NP_438863.1; NC_000907.1. DR RefSeq; WP_005658446.1; NC_000907.1. DR STRING; 71421.HI0704; -. DR EnsemblBacteria; AAC22367; AAC22367; HI_0704. DR GeneID; 949730; -. DR KEGG; hin:HI0704; -. DR PATRIC; 20190027; VBIHaeInf48452_0735. DR OMA; ALPDGIM; -. DR OrthoDB; EOG6NKR59; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 61 Uncharacterized protein HI_0704. FT /FTId=PRO_0000077948. SQ SEQUENCE 61 AA; 6302 MW; DDD5512ED25773AF CRC64; MNKLSLVLVA GFLLVGCASE SVKDPDALPN GIMQPVEGTG AVAGGSFMPE IQKNTIPTQM K // ID Y736_HAEIN Reviewed; 508 AA. AC P44849; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Uncharacterized sodium-dependent transporter HI_0736; GN OrderedLocusNames=HI_0736; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Putative sodium-dependent transporter. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) 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; L42023; AAC22395.1; -; Genomic_DNA. DR PIR; E64089; E64089. DR RefSeq; NP_438895.1; NC_000907.1. DR RefSeq; WP_005693140.1; NC_000907.1. DR ProteinModelPortal; P44849; -. DR EnsemblBacteria; AAC22395; AAC22395; HI_0736. DR GeneID; 949764; -. DR KEGG; hin:HI0736; -. DR PATRIC; 20190111; VBIHaeInf48452_0771. DR eggNOG; ENOG4105C8J; Bacteria. DR eggNOG; COG0733; LUCA. DR KO; K03308; -. DR OMA; NTFGWGM; -. DR OrthoDB; EOG6WT8F5; -. DR PhylomeDB; P44849; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR000175; Na/ntran_symport. DR PANTHER; PTHR11616; PTHR11616; 1. DR Pfam; PF00209; SNF; 2. DR PRINTS; PR00176; NANEUSMPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 508 Uncharacterized sodium-dependent FT transporter HI_0736. FT /FTId=PRO_0000214818. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 272 292 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. FT TRANSMEM 365 385 Helical. {ECO:0000255}. FT TRANSMEM 394 414 Helical. {ECO:0000255}. FT TRANSMEM 432 452 Helical. {ECO:0000255}. FT TRANSMEM 469 489 Helical. {ECO:0000255}. SQ SEQUENCE 508 AA; 55177 MW; 5CC50526DE854BB9 CRC64; MAHSAPKAQK RETFSGRRAF ILAAIGSAVG LGNIWRFPYT TYENGGGAFI IPYLIALLTA GIPLLFLDYA IGHRHRGGAP LSYRRFSPHF EVFGWWQMMV NVIIGLYYAV VLGWAASYTY FSFTGAWGDK PIDFFIGKFL KMGDIKNGIS FEFVGMVTAP LIAMWIVALG VLSMGVQKGI AKVSSVLMPV LVVMFMVLVI YSLFLPGAAK GLDALFTPDW SKLSNPSVWI AAYGQIFFSL SIGFGIMVTY ASYLKKESDL TGSGLVVGFA NSSFEVLAGI GVFAALGFIA TAQGQEVSEV AKGGIGLAFF AFPTIINKAP FGEVLGMLFF GSLTFAALTS FISVIEVIIS AIQDKIRISR GKVTFIVGVP MMLVSVILFG TTTGLPMLDV FDKFVNYFGI VAVAFASLIA IVANEKLGLL GNHLNETSSF KVGFFWRLCI VLTSGVLAFM LFSEGAKVFS EGYEGYPNWF VNTFGWGMSI SLLVVACFLS RLKWKSETKL TIDETKGE // ID Y744_HAEIN Reviewed; 148 AA. AC P44854; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein HI_0744; GN OrderedLocusNames=HI_0744; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 rhodanese domain. {ECO:0000255|PROSITE- CC ProRule:PRU00173}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22402.1; -; Genomic_DNA. DR PIR; A64158; A64158. DR RefSeq; NP_438903.1; NC_000907.1. DR RefSeq; WP_005693147.1; NC_000907.1. DR ProteinModelPortal; P44854; -. DR STRING; 71421.HI0744; -. DR EnsemblBacteria; AAC22402; AAC22402; HI_0744. DR GeneID; 949771; -. DR KEGG; hin:HI0744; -. DR PATRIC; 20190129; VBIHaeInf48452_0780. DR eggNOG; ENOG4107YZP; Bacteria. DR eggNOG; COG0607; LUCA. DR OMA; EIMQFVS; -. DR OrthoDB; EOG69GZQ4; -. DR PhylomeDB; P44854; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR001763; Rhodanese-like_dom. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 148 Uncharacterized protein HI_0744. FT /FTId=PRO_0000139427. FT DOMAIN 54 148 Rhodanese. {ECO:0000255|PROSITE- FT ProRule:PRU00173}. SQ SEQUENCE 148 AA; 16537 MW; 6CDC1E29CADEA06B CRC64; MQEFISMATE FAQKHTLLAV SWFAIFVMVI YTFYKGATSK FKVITHNEVI RLINSDEAIV VDLRSLEEFQ RGHIINSINV LPSEIKNQNI GKLESHKENA LILVDTNGTS ASASAVFLTK QGFNSVFVLK EGLSAWVAAN LPLVKKHK // ID Y817_HAEIN Reviewed; 182 AA. AC P44882; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=UPF0149 protein HI_0817; GN OrderedLocusNames=HI_0817; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0149 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; L42023; AAC22476.1; -; Genomic_DNA. DR PIR; I64158; I64158. DR RefSeq; NP_438977.1; NC_000907.1. DR RefSeq; WP_005693181.1; NC_000907.1. DR PDB; 1IZM; X-ray; 1.95 A; A=1-182. DR PDBsum; 1IZM; -. DR ProteinModelPortal; P44882; -. DR SMR; P44882; 2-171. DR STRING; 71421.HI0817; -. DR EnsemblBacteria; AAC22476; AAC22476; HI_0817. DR GeneID; 949830; -. DR KEGG; hin:HI0817; -. DR PATRIC; 20190289; VBIHaeInf48452_0858. DR eggNOG; COG3079; LUCA. DR KO; K09895; -. DR OMA; MRMSIQN; -. DR OrthoDB; EOG6358FQ; -. DR PhylomeDB; P44882; -. DR EvolutionaryTrace; P44882; -. DR Proteomes; UP000000579; Chromosome. DR HAMAP; MF_00346; UPF0149; 1. DR InterPro; IPR011978; UPF0149. DR Pfam; PF03695; UPF0149; 1. DR SUPFAM; SSF101327; SSF101327; 1. DR TIGRFAMs; TIGR02292; ygfB_yecA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 182 UPF0149 protein HI_0817. FT /FTId=PRO_0000207561. FT HELIX 5 14 {ECO:0000244|PDB:1IZM}. FT HELIX 21 33 {ECO:0000244|PDB:1IZM}. FT HELIX 41 49 {ECO:0000244|PDB:1IZM}. FT TURN 57 59 {ECO:0000244|PDB:1IZM}. FT HELIX 60 74 {ECO:0000244|PDB:1IZM}. FT TURN 75 78 {ECO:0000244|PDB:1IZM}. FT HELIX 92 113 {ECO:0000244|PDB:1IZM}. FT HELIX 117 119 {ECO:0000244|PDB:1IZM}. FT HELIX 122 134 {ECO:0000244|PDB:1IZM}. FT HELIX 146 170 {ECO:0000244|PDB:1IZM}. SQ SEQUENCE 182 AA; 20290 MW; EFFDC22E16D0E735 CRC64; MLISHSDLNQ QLKSAGIGFN ATELHGFLSG LLCGGLKDQS WLPLLYQFSN DNHAYPTGLV QPVTELYEQI SQTLSDVEGF TFELGLTEDE NVFTQADSLS DWANQFLLGI GLAQPELAKE KGEIGEAVDD LQDICQLGYD EDDNEEELAE ALEEIIEYVR TIAMLFYSHF NEGEIESKPV LH // ID Y825_HAEIN Reviewed; 244 AA. AC P44056; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0825; GN OrderedLocusNames=HI_0825; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22498.1; -; Genomic_DNA. DR PIR; B64014; B64014. DR RefSeq; NP_438985.1; NC_000907.1. DR RefSeq; WP_005648352.1; NC_000907.1. DR STRING; 71421.HI0825; -. DR EnsemblBacteria; AAC22498; AAC22498; HI_0825. DR GeneID; 949928; -. DR KEGG; hin:HI0825; -. DR PATRIC; 20190305; VBIHaeInf48452_0866. DR OMA; FIRNQHT; -. DR OrthoDB; EOG6RVFVD; -. DR Proteomes; UP000000579; 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 1 244 Uncharacterized protein HI_0825. FT /FTId=PRO_0000077958. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. SQ SEQUENCE 244 AA; 27745 MW; 7EADE866E90EF3A9 CRC64; MLINFTQVLQ DSWNFFRNQK KIMLQFVAIL FIVQSASALL SFSVNDENKN DVLNLANTDI TSFIFSVAIT QILTSFIAAW GLTSIHKISL QNYRTLGETF SLTLRRFAGV ILLDLLMVAP MLLGLGEAFA ALLTKKSPSI MSLIAMLVGV WFFVRLNLTV VHYLSTQEAL SQTIRKIWMR GNTRKGVLFI YTLLVYFLVP ILIFQLSAFS NNAVFDMVIG IFTALLNIFM LVVTYRFYSL FMKD // ID Y828_HAEIN Reviewed; 98 AA. AC P44887; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Uncharacterized protein HI_0828; GN OrderedLocusNames=HI_0828; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH ZINC CHLORIDE, RP AND SUBUNIT. RX PubMed=15779043; DOI=10.1002/prot.20411; RA Willis M.A., Song F., Zhuang Z., Krajewski W., Chalamasetty V.R., RA Reddy P., Howard A., Dunaway-Mariano D., Herzberg O.; RT "Structure of YciI from Haemophilus influenzae (HI0828) reveals a RT ferredoxin-like alpha/beta-fold with a histidine/aspartate centered RT catalytic site."; RL Proteins 59:648-652(2005). CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15779043}. CC -!- SIMILARITY: Belongs to the YciI 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; L42023; AAC22486.1; -; Genomic_DNA. DR PIR; B64097; B64097. DR RefSeq; NP_438988.1; NC_000907.1. DR RefSeq; WP_005648344.1; NC_000907.1. DR PDB; 1MWQ; X-ray; 0.99 A; A/B=1-98. DR PDBsum; 1MWQ; -. DR ProteinModelPortal; P44887; -. DR SMR; P44887; 1-98. DR STRING; 71421.HI0828; -. DR EnsemblBacteria; AAC22486; AAC22486; HI_0828. DR GeneID; 949842; -. DR KEGG; hin:HI0828; -. DR PATRIC; 20190311; VBIHaeInf48452_0869. DR eggNOG; ENOG4105K9H; Bacteria. DR eggNOG; COG2350; LUCA. DR KO; K09780; -. DR OMA; MWYMISS; -. DR OrthoDB; EOG6423NJ; -. DR PhylomeDB; P44887; -. DR EvolutionaryTrace; P44887; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR005545; YCII. DR Pfam; PF03795; YCII; 1. DR SUPFAM; SSF54909; SSF54909; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein HI_0828. FT /FTId=PRO_0000168879. FT STRAND 2 9 {ECO:0000244|PDB:1MWQ}. FT HELIX 14 19 {ECO:0000244|PDB:1MWQ}. FT HELIX 21 33 {ECO:0000244|PDB:1MWQ}. FT STRAND 37 50 {ECO:0000244|PDB:1MWQ}. FT HELIX 52 54 {ECO:0000244|PDB:1MWQ}. FT STRAND 56 64 {ECO:0000244|PDB:1MWQ}. FT HELIX 68 76 {ECO:0000244|PDB:1MWQ}. FT HELIX 79 82 {ECO:0000244|PDB:1MWQ}. FT STRAND 86 94 {ECO:0000244|PDB:1MWQ}. SQ SEQUENCE 98 AA; 10965 MW; 50D5C5508902A8D7 CRC64; MYYVIFAQDI PNTLEKRLAV REQHLARLKQ LQAENRLLTA GPNPAIDDEN PSEAGFTGST VIAQFENLQA AKDWAAQDPY VEAGVYADVI VKPFKKVF // ID Y874_HAEIN Reviewed; 399 AA. AC P44067; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein HI_0874; GN OrderedLocusNames=HI_0874; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22538.1; -; Genomic_DNA. DR PIR; D64015; D64015. DR RefSeq; NP_439035.1; NC_000907.1. DR RefSeq; WP_010869079.1; NC_000907.1. DR STRING; 71421.HI0874; -. DR EnsemblBacteria; AAC22538; AAC22538; HI_0874. DR GeneID; 949882; -. DR KEGG; hin:HI0874; -. DR PATRIC; 20190403; VBIHaeInf48452_0915. DR eggNOG; ENOG4105PF3; Bacteria. DR eggNOG; COG3307; LUCA. DR KO; K02847; -. DR OMA; FLAHNSG; -. DR OrthoDB; EOG625JV6; -. DR Proteomes; UP000000579; 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; IPR007016; O-antigen_ligase-related. DR Pfam; PF04932; Wzy_C; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 399 Uncharacterized protein HI_0874. FT /FTId=PRO_0000077967. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 173 193 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 362 382 Helical. {ECO:0000255}. SQ SEQUENCE 399 AA; 45281 MW; 56FD7C818FC2B2F8 CRC64; MIQEKHLTFT INLLVSLFFL TILIIPKGYN YAPIILSAIG LIYFIPLKKK LSFSSEDKKL IFSFLFYFFT FLLSIIINKD GIREIDNPSR LLLFIPLLLL FKNFPIKRKT ILYAIPSSAL ITGCVALFQK FALGYEKPFP ETMHIQMGNI AISLATFSIV ITLHFFIKKQ YKSTLFGFVA IILAIMTSAL SGARGGWIGL PVVVGIILFL YKEFINKKLI ITLIAIITIG LTALITSPKF GIEKRYNAAK SDIVSYLEKN NRNTSLGARF DMWENALIAI KEAPIFGHGS DGYDEFRHKQ VKSKQMAKTT LNFGSLHNQY LESWVKRGLV GFIALILIIL TPIFYFIKNL NTHNLETKCI CILGIIHIVS HIFYFTSQSF LAHNSGNIFY FSAMLCFIV // ID Y882_HAEIN Reviewed; 245 AA. AC P44068; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein HI_0882; GN OrderedLocusNames=HI_0882; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22546.1; -; Genomic_DNA. DR PIR; E64015; E64015. DR RefSeq; NP_439043.1; NC_000907.1. DR RefSeq; WP_005651413.1; NC_000907.1. DR STRING; 71421.HI0882; -. DR EnsemblBacteria; AAC22546; AAC22546; HI_0882. DR GeneID; 949886; -. DR KEGG; hin:HI0882; -. DR PATRIC; 20190421; VBIHaeInf48452_0924. DR eggNOG; ENOG4105WPN; Bacteria. DR eggNOG; COG1636; LUCA. DR KO; K09765; -. DR OMA; PNIHPYT; -. DR OrthoDB; EOG6S26FS; -. DR PhylomeDB; P44068; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003828; DUF208. DR Pfam; PF02677; DUF208; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 245 Uncharacterized protein HI_0882. FT /FTId=PRO_0000077968. SQ SEQUENCE 245 AA; 29072 MW; BC55B4EB8ED65491 CRC64; MNTELQPKLE KSAVNFQAKP RKQKIRKDPN APFIREKLEL PDGHNKLLLH SCCAPCSGEV MEAILASGIE FTIYFYNPNI HPLKEYLIRK EENIRFAKKF GIPFIDADYD RQNWFDRAKG MEWEPERGIR CTMCFDMRFE KAAEYAHKHG FPVFTSCLGI SRWKDMNQIN GCGHRAAEKY DDVIYWDYNW RKEGGSQRMI EISKRERFYQ QEYCGCVYSL RDSNKWREET GRQKIEIGKL YYSAD // ID Y896_HAEIN Reviewed; 204 AA. AC Q57434; O05035; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Uncharacterized protein HI_0896; GN OrderedLocusNames=HI_0896; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 SPOR domain. {ECO:0000305}. CC -!- SIMILARITY: To E.coli FtsN repeat regions. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22556.1; -; Genomic_DNA. DR PIR; I64100; I64100. DR RefSeq; NP_439057.1; NC_000907.1. DR RefSeq; WP_010869084.1; NC_000907.1. DR ProteinModelPortal; Q57434; -. DR STRING; 71421.HI0896; -. DR EnsemblBacteria; AAC22556; AAC22556; HI_0896. DR GeneID; 949899; -. DR KEGG; hin:HI0896; -. DR PATRIC; 20190449; VBIHaeInf48452_0938. DR eggNOG; ENOG41063M6; Bacteria. DR eggNOG; COG3087; LUCA. DR KO; K03591; -. DR OMA; KYGLQCG; -. DR OrthoDB; EOG6MD93F; -. DR PhylomeDB; Q57434; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR Gene3D; 3.30.70.1070; -; 1. DR InterPro; IPR007730; SPOR_dom. DR Pfam; PF05036; SPOR; 1. DR SUPFAM; SSF110997; SSF110997; 1. DR PROSITE; PS51724; SPOR; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 204 Uncharacterized protein HI_0896. FT /FTId=PRO_0000077970. FT DOMAIN 131 204 SPOR. SQ SEQUENCE 204 AA; 23185 MW; A15393761A0FE60D CRC64; MQQAITQQEK AQPKSVLPNR PEEVWSYIKA LETRTVPVDN NPASVEQNMR LTEEQRQVLI QIERDQKAAD EARKLAEQQR IEDATRTQSK TTEDMKNTEA EIVKSESIKK QDSQKIESAK KVEQIKTVNN VRDSKKFGLQ CGAFKNRAQA ENLQGRLQMT GLNAQIQTNG EWNRVRVASF DTRELAVQAQ SRAKTVTDCV VIGM // ID Y902_HAEIN Reviewed; 264 AA. AC P44070; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=UPF0721 transmembrane protein HI_0902; GN OrderedLocusNames=HI_0902; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0721 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; L42023; AAC22562.1; -; Genomic_DNA. DR PIR; G64015; G64015. DR RefSeq; NP_439063.1; NC_000907.1. DR RefSeq; WP_005693253.1; NC_000907.1. DR STRING; 71421.HI0902; -. DR EnsemblBacteria; AAC22562; AAC22562; HI_0902. DR GeneID; 949698; -. DR KEGG; hin:HI0902; -. DR PATRIC; 20190461; VBIHaeInf48452_0944. DR eggNOG; ENOG4105HF0; Bacteria. DR eggNOG; COG0730; LUCA. DR KO; K07090; -. DR OMA; SMFTANI; -. DR OrthoDB; EOG6RZB3C; -. DR PhylomeDB; P44070; -. DR Proteomes; UP000000579; 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; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 264 UPF0721 transmembrane protein HI_0902. FT /FTId=PRO_0000077971. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 183 203 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. SQ SEQUENCE 264 AA; 27542 MW; B5C18F4B6B9F0A43 CRC64; MFTFILLCLL VGALAGFLAG LFGIGGGLVI VPTLVYLLPI VDVPESLLMS TALGTSFATI VITGIGSAQR HHKLGNIVWQ AVRILAPVIM LSVFICGLFI GRLDREISAK IFACLVVYLA TKMVLSIKKD QVTTKSLTPL SSVIGGILIG MASSAAGIGG GGFIVPFLTA RGINIKQAIG SSAFCGMLLG ISGMFSFIVS GWGNPLMPEY SLGYIYLPAV LGITATSFFT SKLGASATAK LPVSTLKKGF ALFLIVVAIN MFLK // ID Y925_HAEIN Reviewed; 121 AA. AC P44075; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_0925; GN OrderedLocusNames=HI_0925; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YcjD and H.influenzae HI_1162. 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; L42023; AAC22585.1; -; Genomic_DNA. DR PIR; C64016; C64016. DR RefSeq; NP_439085.1; NC_000907.1. DR RefSeq; WP_005693271.1; NC_000907.1. DR ProteinModelPortal; P44075; -. DR STRING; 71421.HI0925; -. DR DNASU; 950812; -. DR EnsemblBacteria; AAC22585; AAC22585; HI_0925. DR GeneID; 950812; -. DR KEGG; hin:HI0925; -. DR PATRIC; 20190507; VBIHaeInf48452_0966. DR eggNOG; ENOG4105WDY; Bacteria. DR eggNOG; COG2852; LUCA. DR OMA; DFACHAK; -. DR OrthoDB; EOG6PKFM9; -. DR PhylomeDB; P44075; -. DR BioCyc; RETL1328306-WGS:GSTH-1435-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF04480; DUF559; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Uncharacterized protein HI_0925. FT /FTId=PRO_0000168893. SQ SEQUENCE 121 AA; 14589 MW; B232777F615BAFDD CRC64; MQPYEKYLKL NSQKLRADQT DTERKLWQRI NRDQLLGFRF NRQKPLLSYI VDFYCAKTKL IIELDGSQHY KPDYQEKDAL RDAELNSLGF TVMRFSNDEV MREIEAVVEQ IYLFLENVRT D // ID Y939_HAEIN Reviewed; 238 AA. AC P44080; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein HI_0939; GN OrderedLocusNames=HI_0939; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22603.1; -; Genomic_DNA. DR PIR; H64016; H64016. DR RefSeq; NP_439099.1; NC_000907.1. DR RefSeq; WP_005693287.1; NC_000907.1. DR STRING; 71421.HI0939; -. DR EnsemblBacteria; AAC22603; AAC22603; HI_0939. DR GeneID; 949939; -. DR KEGG; hin:HI0939; -. DR PATRIC; 20190535; VBIHaeInf48452_0980. DR eggNOG; COG4795; LUCA. DR KO; K02680; -. DR OMA; KNGCIGK; -. DR OrthoDB; EOG600DN7; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR016419; Prepilin_Pept-dep_B_prd. DR PIRSF; PIRSF004525; Pilin_peptidase-dep_B_prd; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 238 Uncharacterized protein HI_0939. FT /FTId=PRO_0000077979. FT TRANSMEM 10 33 Helical. {ECO:0000255}. SQ SEQUENCE 238 AA; 26787 MW; D75364993FB3D86C CRC64; MMKVLLKGQT LLALMISLSL SSLLLLSISH FYVQIQTQNQ HMLLHLKLQA ELQRTLQLIG KDLRRLGFRA LNAKLTESNL SLFELDEQGT AIFISQEDNA PPNSCVLFFY DLNKNGCIGK GSPKTCMKKG KNTSKSSTEE LFGYKVSNKM IKTKLTYQSV IPTNCTAETC KRAFQQTACN AGGGWADLLD NNEYEITRLQ FNWLIEGKGL EIKLKGNLKQ TPNISYETSL VVVLWNQK // ID Y966_HAEIN Reviewed; 188 AA. AC P44085; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_0966; GN OrderedLocusNames=HI_0966; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22629.1; -; Genomic_DNA. DR PIR; D64017; D64017. DR RefSeq; NP_439127.1; NC_000907.1. DR RefSeq; WP_005693313.1; NC_000907.1. DR STRING; 71421.HI0966; -. DR EnsemblBacteria; AAC22629; AAC22629; HI_0966. DR GeneID; 950444; -. DR KEGG; hin:HI0966; -. DR PATRIC; 20190591; VBIHaeInf48452_1008. DR OMA; IYPNLTR; -. DR OrthoDB; EOG6M9DW4; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 188 Uncharacterized protein HI_0966. FT /FTId=PRO_0000077982. SQ SEQUENCE 188 AA; 21442 MW; 075BD54CBF8933AD CRC64; MKLIATLGMA ALLSGCSMFD SQQSAIPAEF AGADYQLSDQ HAKQWAIASK QVEQCVYPNL TRILQQHFSK EDSYIHSQYV FFYPLEKIIG EQYVKIIQAD EKSMNYASYQ FKKFRTRVSN VEPLTKQSCL KLRNEARDDL AAVKGQYKNG MVEVQKNEDG TPKNSDGIAT NQNKFFFDII KWGSMLLL // ID YBAK_HAEIN Reviewed; 158 AA. AC P45202; Q9RP30; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 11-MAY-2016, entry version 111. DE RecName: Full=Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase YbaK; DE EC=4.2.-.-; GN Name=ybaK; OrderedLocusNames=HI_1434; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RA Bonander N., Eisenstein E.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION IN CYS-TRNA(PRO) EDITING, AND MUTAGENESIS OF LYS-46. RX PubMed=15322138; DOI=10.1074/jbc.C400304200; RA An S., Musier-Forsyth K.; RT "Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK RT protein."; RL J. Biol. Chem. 279:42359-42362(2004). RN [4] RP FUNCTION AS A DEACYLASE, AND SUBSTRATE SPECIFICITY. RX PubMed=15886196; DOI=10.1074/jbc.M502174200; RA Ruan B., Soll D.; RT "The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys RT deacylase."; RL J. Biol. Chem. 280:25887-25891(2005). RN [5] RP SUBUNIT. RX PubMed=16087664; DOI=10.1074/jbc.M507550200; RA An S., Musier-Forsyth K.; RT "Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel RT synthetase.YbaK.tRNA ternary complex."; RL J. Biol. Chem. 280:34465-34472(2005). RN [6] RP FUNCTION, REACTION MECHANISM, SUBSTRATE SPECIFICITY, AND MUTAGENESIS RP OF TYR-20; PHE-29; LYS-46; THR-47; GLY-101; SER-129; GLY-131; GLY-134 RP AND SER-136. RX PubMed=21768119; DOI=10.1074/jbc.M111.232611; RA So B.R., An S., Kumar S., Das M., Turner D.A., Hadad C.M., RA Musier-Forsyth K.; RT "Substrate-mediated fidelity mechanism ensures accurate decoding of RT proline codons."; RL J. Biol. Chem. 286:31810-31820(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=10813833; RX DOI=10.1002/(SICI)1097-0134(20000701)40:1<86::AID-PROT100>3.0.CO;2-Y; RA Zhang H., Huang K., Li Z., Banerjei L., Fisher K.E., Grishin N.V., RA Eisenstein E., Herzberg O.; RT "Crystal structure of YbaK protein from Haemophilus influenzae RT (HI1434) at 1.8-A resolution: functional implications."; RL Proteins 40:86-97(2000). CC -!- FUNCTION: Functions in trans to edit the amino acid from CC incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase CC activity. Probably compensates for the lack of Cys-tRNA(Pro) CC editing by ProRS. Is also able to deacylate Cys-tRNA(Cys), and CC displays weak deacylase activity in vitro against Gly-tRNA(Gly), CC as well as, at higher concentrations, some other correctly charged CC tRNAs. Does not cleave Pro-tRNA(Pro). CC {ECO:0000269|PubMed:15322138, ECO:0000269|PubMed:15886196, CC ECO:0000269|PubMed:21768119}. CC -!- SUBUNIT: May form a tertiary complex with ProRS and t-RNA(Pro), as CC it can be cross-linked to E.coli ProRS and to E.coli tRNA(Pro) in CC vitro. It cannot compete with Ef-Tu for aminoacyl-tRNA binding, CC suggesting it acts before release of the charged aminoacyl-tRNA CC from the synthetase. {ECO:0000269|PubMed:16087664}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: Reaction mechanism involves exclusion of catalytic CC water from the active site and substrate-mediated catalysis: the CC sulfhydryl side chain of the Cys substrate acts as a nucleophile CC and attacks the carbonyl center of the ester bond, leading to the CC cleavage of the Cys-tRNA ester bond and formation of a cyclic CC cysteine thiolactone intermediate. In contrast, the INS editing CC domain of ProRS catalyzes Ala-tRNA(Pro) hydrolysis via CC nucleophilic attack by a catalytic water molecule CC (PubMed:21768119). {ECO:0000305|PubMed:21768119}. CC -!- SIMILARITY: Belongs to the prolyl-tRNA editing family. YbaK/EbsC 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; L42023; AAC23081.1; -; Genomic_DNA. DR EMBL; AF174386; AAD54290.1; -; Genomic_DNA. DR PIR; H64171; H64171. DR RefSeq; NP_439583.1; NC_000907.1. DR PDB; 1DBU; X-ray; 1.80 A; A=1-158. DR PDB; 1DBX; X-ray; 1.80 A; A/B=1-158. DR PDBsum; 1DBU; -. DR PDBsum; 1DBX; -. DR ProteinModelPortal; P45202; -. DR SMR; P45202; 2-158. DR STRING; 71421.HI1434; -. DR EnsemblBacteria; AAC23081; AAC23081; HI_1434. DR GeneID; 949657; -. DR KEGG; hin:HI1434; -. DR PATRIC; 20191563; VBIHaeInf48452_1491. DR eggNOG; ENOG4108Z66; Bacteria. DR eggNOG; COG2606; LUCA. DR KO; K03976; -. DR OMA; FTVHAYD; -. DR OrthoDB; EOG6XDH1K; -. DR EvolutionaryTrace; P45202; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043906; F:Ala-tRNA(Pro) hydrolase activity; IDA:UniProtKB. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0006450; P:regulation of translational fidelity; IDA:GOC. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.90.960.10; -; 1. DR InterPro; IPR004369; Prolyl-tRNA_editing_YbaK/EbsC. DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom. DR Pfam; PF04073; tRNA_edit; 1. DR PIRSF; PIRSF006181; EbsC_YbaK; 1. DR SUPFAM; SSF55826; SSF55826; 1. DR TIGRFAMs; TIGR00011; YbaK_EbsC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lyase; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 158 Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase FT YbaK. FT /FTId=PRO_0000168623. FT SITE 29 29 Participates in proton transfer during FT catalysis. {ECO:0000250}. FT MUTAGEN 20 20 Y->A: 45-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 29 29 F->A: 29-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 46 46 K->A: 66-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:15322138, FT ECO:0000269|PubMed:21768119}. FT MUTAGEN 46 46 K->I: 38-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:15322138, FT ECO:0000269|PubMed:21768119}. FT MUTAGEN 46 46 K->R: 44-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:15322138, FT ECO:0000269|PubMed:21768119}. FT MUTAGEN 47 47 T->A: 21-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 101 101 G->A: 36-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 129 129 S->A: 5.6-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 131 131 G->A: 28-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 134 134 G->A: 7.4-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 136 136 S->A: 3.6-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT MUTAGEN 136 136 S->H: 16-fold decrease in Cys-tRNA(Pro) FT deacylation activity. FT {ECO:0000269|PubMed:21768119}. FT CONFLICT 117 117 N -> K (in Ref. 1; AAC23081). FT {ECO:0000305}. FT HELIX 3 11 {ECO:0000244|PDB:1DBU}. FT STRAND 16 19 {ECO:0000244|PDB:1DBU}. FT HELIX 32 37 {ECO:0000244|PDB:1DBU}. FT HELIX 41 43 {ECO:0000244|PDB:1DBU}. FT STRAND 44 52 {ECO:0000244|PDB:1DBU}. FT STRAND 58 65 {ECO:0000244|PDB:1DBU}. FT HELIX 72 78 {ECO:0000244|PDB:1DBU}. FT STRAND 84 86 {ECO:0000244|PDB:1DBU}. FT HELIX 89 96 {ECO:0000244|PDB:1DBU}. FT STRAND 105 107 {ECO:0000244|PDB:1DBU}. FT STRAND 114 117 {ECO:0000244|PDB:1DBU}. FT HELIX 118 122 {ECO:0000244|PDB:1DBU}. FT STRAND 126 129 {ECO:0000244|PDB:1DBU}. FT STRAND 135 139 {ECO:0000244|PDB:1DBU}. FT HELIX 141 148 {ECO:0000244|PDB:1DBU}. FT STRAND 151 153 {ECO:0000244|PDB:1DBU}. SQ SEQUENCE 158 AA; 17155 MW; 45723E9DFC99535A CRC64; MTPAIDLLKK QKIPFILHTY DHDPNNQHFG DEAAEKLGID PNRSFKTLLV AENGDQKKLA CFVLATANML NLKKAAKSIG VKKVEMADKD AAQKSTGYLV GGISPLGQKK RVKTVINSTA LEFETIYVSG GKRGLSVEIA PQDLAKVLGA EFTDIVDE // ID Y352_HAEIN Reviewed; 231 AA. AC P24324; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0352; DE AltName: Full=ORF1; GN OrderedLocusNames=HI_0352; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RM 7004 / Serotype B; RX PubMed=1956282; DOI=10.1111/j.1365-2958.1991.tb01874.x; RA Maskell D.J., Szabo M.J., Butler P.D., Williams A.E., Moxon E.R.; RT "Molecular analysis of a complex locus from Haemophilus influenzae RT involved in phase-variable lipopolysaccharide biosynthesis."; RL Mol. Microbiol. 5:1013-1022(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; X57315; CAA40567.1; -; Genomic_DNA. DR EMBL; L42023; AAC22013.1; -; Genomic_DNA. DR PIR; E64149; E64149. DR RefSeq; NP_438516.1; NC_000907.1. DR RefSeq; WP_010868978.1; NC_000907.1. DR ProteinModelPortal; P24324; -. DR STRING; 71421.HI0352; -. DR CAZy; GT42; Glycosyltransferase Family 42. DR EnsemblBacteria; AAC22013; AAC22013; HI_0352. DR GeneID; 949950; -. DR KEGG; hin:HI0352; -. DR PATRIC; 20189251; VBIHaeInf48452_0371. DR eggNOG; ENOG4105I85; Bacteria. DR eggNOG; ENOG4111TI4; LUCA. DR OMA; TICQSIN; -. DR OrthoDB; EOG6Z99Z7; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR009251; A-2_3-sialyltransferase. DR Pfam; PF06002; CST-I; 1. DR SUPFAM; SSF102414; SSF102414; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 231 Uncharacterized protein HI_0352. FT /FTId=PRO_0000077915. FT CONFLICT 1 27 MQLIKNNEYEYADIILSSFVNLGDSEL -> MNGTICQSIN FT QSINQSINQSINQSINQSINQSINQSKSVIIAGNGTSLKSI FT DYSLLPKDYDVFRCNQFYFEDHYFLG (in Ref. 1). FT {ECO:0000305}. SQ SEQUENCE 231 AA; 27279 MW; 0F6A8785F4D2AC73 CRC64; MQLIKNNEYE YADIILSSFV NLGDSELKKI KNVQKLLTQV DIGHYYLNKL PAFDAYLQYN ELYENKRITS GVYMCAVATV MGYKDLYLTG IDFYQEKGNP YAFHHQKENI IKLLPSFSQN KSQSDIHSME YDLNALYFLQ KHYGVNIYCI SPESPLCNYF PLSPLNNPIT FILEEKKNYT QDILIPPKFV YKKIGIYSKP RIYQNLIFRL IWDILRLPND IKHALKSRKW D // ID Y357_HAEIN Reviewed; 314 AA. AC P44658; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Putative thiamine biosynthesis protein HI_0357; GN OrderedLocusNames=HI_0357; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Probably involved in thiamine biosynthesis. CC -!- SIMILARITY: Belongs to the NMT1/THI5 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; L42023; AAC22016.1; -; Genomic_DNA. DR PIR; C64063; C64063. DR RefSeq; NP_438519.1; NC_000907.1. DR RefSeq; WP_005693803.1; NC_000907.1. DR ProteinModelPortal; P44658; -. DR STRING; 71421.HI0357; -. DR TCDB; 3.A.1.17.3; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAC22016; AAC22016; HI_0357. DR GeneID; 949462; -. DR KEGG; hin:HI0357; -. DR PATRIC; 20189259; VBIHaeInf48452_0375. DR eggNOG; ENOG4107Z6I; Bacteria. DR eggNOG; COG0715; LUCA. DR KO; K15598; -. DR OMA; CCFCTIL; -. DR OrthoDB; EOG6CZQPK; -. DR PhylomeDB; P44658; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR027939; NMT1/THI5. DR InterPro; IPR015168; SsuA/THI5. DR PANTHER; PTHR31528; PTHR31528; 1. DR Pfam; PF09084; NMT1; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Thiamine biosynthesis. FT CHAIN 1 314 Putative thiamine biosynthesis protein FT HI_0357. FT /FTId=PRO_0000211625. SQ SEQUENCE 314 AA; 34961 MW; BE86F4303D253C16 CRC64; MKTIIRYFSF VMGLMLTLPS FAKEKISIML DWYVNPDHAA IIVAQQKGFF EKNNLEVEII EPADPALPPK LAAAEKVDLA VSYQPQLYQQ VAEGLPLVRV GSLISNPLNS VVVLKKSNLK SLADLKGKKV GYSVSGFEDG LLDTMLHSIG LSNKDVELVN VNWSLSPSLL TGQVDAVIGA FRNFELNQLA LEKQEGIAFF PEQYGVPAYD ELILVANKNS VTDKKTSAFL TALEQATSYL QAHPNEAWQA FVSYKPNELN TPLNQLAWKD TLPFLANKPR QLDAKRYQQM AEFMQQKGLI PKALALKEYA VEIE // ID Y379_HAEIN Reviewed; 150 AA. AC P44675; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Putative HTH-type transcriptional regulator HI_0379; GN OrderedLocusNames=HI_0379; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH rrf2-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00540}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22037.1; -; Genomic_DNA. DR PIR; F64150; F64150. DR RefSeq; NP_438540.1; NC_000907.1. DR RefSeq; WP_005659892.1; NC_000907.1. DR ProteinModelPortal; P44675; -. DR STRING; 71421.HI0379; -. DR EnsemblBacteria; AAC22037; AAC22037; HI_0379. DR GeneID; 949480; -. DR KEGG; hin:HI0379; -. DR PATRIC; 20189303; VBIHaeInf48452_0397. DR eggNOG; ENOG4108ZF1; Bacteria. DR eggNOG; COG1959; LUCA. DR KO; K13643; -. DR OMA; MTHDLWS; -. DR OrthoDB; EOG63FW56; -. DR PhylomeDB; P44675; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR010242; TF_HTH_IscR. DR InterPro; IPR030489; TR_Rrf2-type_CS. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR02010; IscR; 1. DR TIGRFAMs; TIGR00738; rrf2_super; 1. DR PROSITE; PS01332; HTH_RRF2_1; 1. DR PROSITE; PS51197; HTH_RRF2_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 150 Putative HTH-type transcriptional FT regulator HI_0379. FT /FTId=PRO_0000109564. FT DOMAIN 2 131 HTH rrf2-type. {ECO:0000255|PROSITE- FT ProRule:PRU00540}. SQ SEQUENCE 150 AA; 16613 MW; 0D092D35392508FE CRC64; MKLTSKGRYA VTAVLDIALN ADGGPVSLAD ISERQHISLS YLEQLFAKLR KDGLVKSVRG PGGGYQLGLP SEQISVGMII AAVNENIHVT KCLGRENCKN GVECLTHELW EDLSLRIESF LNEITLAELV NKRNVKRQSH RDFNNLLVNQ // ID Y395_HAEIN Reviewed; 102 AA. AC P43994; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=UPF0125 protein HI_0395; GN OrderedLocusNames=HI_0395; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0125 (RnfH) 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; L42023; AAC22054.1; -; Genomic_DNA. DR PIR; C64007; C64007. DR RefSeq; NP_438557.1; NC_000907.1. DR RefSeq; WP_005649214.1; NC_000907.1. DR PDB; 2HJ1; X-ray; 2.10 A; B=1-87. DR PDBsum; 2HJ1; -. DR ProteinModelPortal; P43994; -. DR SMR; P43994; 2-78. DR STRING; 71421.HI0395; -. DR DNASU; 949524; -. DR EnsemblBacteria; AAC22054; AAC22054; HI_0395. DR GeneID; 949524; -. DR KEGG; hin:HI0395; -. DR PATRIC; 20189341; VBIHaeInf48452_0414. DR eggNOG; ENOG4105VDB; Bacteria. DR eggNOG; COG2914; LUCA. DR KO; K09801; -. DR OMA; GRINKIT; -. DR OrthoDB; EOG6Q8J4M; -. DR PhylomeDB; P43994; -. DR EvolutionaryTrace; P43994; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 3.10.20.280; -; 1. DR HAMAP; MF_00460; UPF0125_RnfH; 1. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR InterPro; IPR005346; RnfH. DR Pfam; PF03658; Ub-RnfH; 1. DR SUPFAM; SSF54285; SSF54285; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 102 UPF0125 protein HI_0395. FT /FTId=PRO_0000192491. FT STRAND 3 10 FT STRAND 17 24 FT HELIX 29 36 FT HELIX 38 41 FT TURN 47 49 FT STRAND 52 56 FT STRAND 70 74 SQ SEQUENCE 102 AA; 11584 MW; B16F83E91FECE3BC CRC64; MNQINIEIAY AFPERYYLKS FQVDEGITVQ TAITQSGILS QFPEIDLSTN KIGIFSRPIK LTDVLKEGDR IEIYRPLLAD PKEIRRKRAA EQAAAKDKEK GA // ID Y421_HAEIN Reviewed; 54 AA. AC P43996; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 47. DE RecName: Full=Uncharacterized protein HI_0421; GN OrderedLocusNames=HI_0421; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22083.1; -; Genomic_DNA. DR PIR; E64007; E64007. DR EnsemblBacteria; AAC22083; AAC22083; HI_0421. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 54 Uncharacterized protein HI_0421. FT /FTId=PRO_0000077922. SQ SEQUENCE 54 AA; 5919 MW; 10D253EE4ED2AA63 CRC64; MASAIRNFPY PCFWKFVSMA NRPIKTAGIL GYGTPLLIRS FGISVIGIDN ADKV // ID Y463_HAEIN Reviewed; 383 AA. AC P43899; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein HI_0463; DE EC=1.3.99.-; GN OrderedLocusNames=HI_0463; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the biosynthesis of porphyrin-containing CC compound. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III CC oxidase family. HemN-like 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; L42023; AAC22122.1; -; Genomic_DNA. DR PIR; B64070; B64070. DR RefSeq; NP_438624.1; NC_000907.1. DR RefSeq; WP_005693701.1; NC_000907.1. DR ProteinModelPortal; P43899; -. DR STRING; 71421.HI0463; -. DR EnsemblBacteria; AAC22122; AAC22122; HI_0463. DR GeneID; 949551; -. DR KEGG; hin:HI0463; -. DR PATRIC; 20189481; VBIHaeInf48452_0483. DR eggNOG; ENOG4105CSA; Bacteria. DR eggNOG; COG0635; LUCA. DR KO; K02495; -. DR OMA; PINHLSA; -. DR OrthoDB; EOG683S9D; -. DR PhylomeDB; P43899; -. DR UniPathway; UPA00251; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR004559; Coprogen_oxidase_HemN-rel. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR010723; HemN_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Porphyrin biosynthesis; Reference proteome; KW S-adenosyl-L-methionine. FT CHAIN 1 383 Oxygen-independent coproporphyrinogen-III FT oxidase-like protein HI_0463. FT /FTId=PRO_0000109957. FT REGION 71 72 S-adenosyl-L-methionine 2 binding. FT {ECO:0000250}. FT METAL 16 16 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 20 20 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 23 23 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT BINDING 10 10 S-adenosyl-L-methionine 1. {ECO:0000250}. FT BINDING 22 22 S-adenosyl-L-methionine 2; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 70 70 S-adenosyl-L-methionine 1; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000250}. FT BINDING 103 103 S-adenosyl-L-methionine 1. {ECO:0000250}. FT BINDING 130 130 S-adenosyl-L-methionine 2. {ECO:0000250}. FT BINDING 142 142 S-adenosyl-L-methionine 2. {ECO:0000250}. FT BINDING 167 167 S-adenosyl-L-methionine 2. {ECO:0000250}. SQ SEQUENCE 383 AA; 44105 MW; E07132657F4A5130 CRC64; MPKLPPLSLY IHIPWCVQKC PYCDFNSHAQ KSDIPEQDYI YHLLQDLQAD LQRFKDSIQQ RKLHSIFIGG GTPSLFSAES IAYLLKEIKK QIDFEDNIEI TLEANPGTVE AERFKGYVSA GIMRISMGIQ SFNDDKLQRL GRIHNAAEAK SAVNLAKVSG LKSFNLDLMH GLPNQTLEEA LDDLRQAIEL SPPHISWYQL TIEPNTMFAY RPPKLPDDDA LWDIFEQGHQ LLTMAGYQQY ETSAYAKAGF QCKHNLNYWR FGDYLAIGCG AHGKLTFPTG EITRFSKTKH PKGYLRGEYL YEEKNVPKID RPFEFFMNRF RLLEAVPKQE FEDYTGLSQS AVKNQIDFAI QQNYIVENAD SWQITEHGKL FLNELLELFL TEE // ID Y557_HAEIN Reviewed; 40 AA. AC P44015; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 47. DE RecName: Full=Uncharacterized protein HI_0557; GN OrderedLocusNames=HI_0557; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22218.1; -; Genomic_DNA. DR PIR; F64009; F64009. DR EnsemblBacteria; AAC22218; AAC22218; HI_0557. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 40 Uncharacterized protein HI_0557. FT /FTId=PRO_0000077933. SQ SEQUENCE 40 AA; 4870 MW; 0B782929EEB58B42 CRC64; MNYISFPTAQ HAVDKIAQEF VIYSQLNHSR TYFPFWWFDA // ID Y602A_HAEIN Reviewed; 174 AA. AC O86227; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_0602.1; GN OrderedLocusNames=HI_0602.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: To E.coli HemX C-terminal region. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22263.1; -; Genomic_DNA. DR RefSeq; NP_438761.2; NC_000907.1. DR STRING; 71421.HI0603m; -. DR EnsemblBacteria; AAC22263; AAC22263; HI_0602.1. DR GeneID; 949795; -. DR KEGG; hin:HI0603m; -. DR PATRIC; 20189783; VBIHaeInf48452_0626. DR eggNOG; ENOG4105ECF; Bacteria. DR eggNOG; COG2959; LUCA. DR KO; K02496; -. DR OrthoDB; EOG6QK4QM; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007470; HemX. DR Pfam; PF04375; HemX; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 174 Uncharacterized protein HI_0602.1. FT /FTId=PRO_0000135258. SQ SEQUENCE 174 AA; 20061 MW; B305A9003412D85E CRC64; MXVNFDETSK NNDKLSNNIT DWQQNIEKSA TSFLNHFIRI SPKQNSNKKE LLAPNQDIYL RENIRLRLQL AIMAVPRQQN ELYKQSLEAV SSWVRSYFDT NAEVTQNFLK LVDGLTDTSI YVDVPEQLKS LTLLDKYLNR TALDVQKVEI EADKAIDTMP QVEAVKPTQS ESQQ // ID Y603_HAEIN Reviewed; 230 AA. AC P44773; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein HI_0603; GN OrderedLocusNames=HI_0603; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli HemX N-terminal region. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22261.1; -; Genomic_DNA. DR PIR; D64080; D64080. DR STRING; 71421.HI0603m; -. DR EnsemblBacteria; AAC22261; AAC22261; HI_0603. DR eggNOG; ENOG4105ECF; Bacteria. DR eggNOG; COG2959; LUCA. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007470; HemX. DR Pfam; PF04375; HemX; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 230 Uncharacterized protein HI_0603. FT /FTId=PRO_0000135257. SQ SEQUENCE 230 AA; 25194 MW; D874DFA8B28B5664 CRC64; MAKEQPNDLT EQLTDTPKTA VEQAETMQSV PQTIVKKTGT ALSLLAILVA LGIGGAGYYF GQQQMAKIQQ KLTALENQTG ANLSSNNTNN NKRLTQLEQS LKTAQENIAQ LEQLIVSKTG EITSLQTQMK QVSQLAIAQQ PSDWLFSEAD FLLNNALRKL VLDNDVDTAV SLLKLADETL VKVNNSQANE IRSAINQDLK QLLSLSSVDQ NAIMQKLSQL ANTVDELQRL // ID Y677_HAEIN Reviewed; 146 AA. AC P44036; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Uncharacterized protein HI_0677; GN OrderedLocusNames=HI_0677; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22341.1; -; Genomic_DNA. DR PIR; I64011; I64011. DR RefSeq; NP_438837.1; NC_000907.1. DR RefSeq; WP_005655034.1; NC_000907.1. DR ProteinModelPortal; P44036; -. DR STRING; 71421.HI0677; -. DR EnsemblBacteria; AAC22341; AAC22341; HI_0677. DR GeneID; 950735; -. DR KEGG; hin:HI0677; -. DR PATRIC; 20189971; VBIHaeInf48452_0707. DR eggNOG; ENOG4108HYK; Bacteria. DR eggNOG; COG0454; LUCA. DR OMA; WQLTDIF; -. DR OrthoDB; EOG61CM21; -. DR PhylomeDB; P44036; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Uncharacterized protein HI_0677. FT /FTId=PRO_0000077944. FT DOMAIN 1 146 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 146 AA; 17193 MW; 38C64AB6ECE7E26E CRC64; MKLFKAEQWN IEVLLPLFEA YRQAYGQAEN PERTLAFLTN RMRFNESLFF IAVDENEKAI GFVQLFPRLS SLQLQRYWQI TDIFVLEHAQ QTEIYAALIS KAKDFVHFTQ SNRLVAELAQ NQYSMLESEG FKLNPKERLF ELSLSC // ID Y755_HAEIN Reviewed; 280 AA. AC P44863; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_0755; DE Flags: Precursor; GN OrderedLocusNames=HI_0755; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: To E.coli YibQ. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22414.1; 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; L42023; AAC22414.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_438914.2; NC_000907.1. DR RefSeq; WP_010869050.1; NC_000907.1. DR ProteinModelPortal; P44863; -. DR STRING; 71421.HI0755; -. DR EnsemblBacteria; AAC22414; AAC22414; HI_0755. DR GeneID; 949515; -. DR KEGG; hin:HI0755; -. DR PATRIC; 20190155; VBIHaeInf48452_0793. DR eggNOG; ENOG4105PXI; Bacteria. DR eggNOG; COG2861; LUCA. DR KO; K09798; -. DR OMA; YRPQTEN; -. DR OrthoDB; EOG6038TR; -. DR PhylomeDB; P44863; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.370; -; 1. DR InterPro; IPR006837; DUF610_YibQ. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR Pfam; PF04748; Polysacc_deac_2; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 280 Uncharacterized protein HI_0755. FT /FTId=PRO_0000013927. SQ SEQUENCE 280 AA; 30741 MW; C739E021613B53B8 CRC64; MNILIKSAVK NFIVFSTALY TSFSFAQSKL AIVIDDVGYH LKEDAAIFAM PREISVAIIP AAPYARARNQ EAKSQGRDIL IHMPMQPVSA VKIEDGGLHL GMSAAQVNDR VNTAKNIVRD AIGMNNHMGS AATADPQLMT YLMTALQEKH LFFLDSRTIG KSVAGKIAKE QGVRSLDRHI FLDDSNEFAD VQRQFKAAIH YARKHGSAIA IGHPRPNTIA VLQAGLRNLP EDIQLVGMGN LWRNEKVIPP KPFILLFSEV PAPTSIEPFE PVGLLRGIPK // ID Y843_HAEIN Reviewed; 45 AA. AC P44059; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein HI_0843; GN OrderedLocusNames=HI_0843; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22511.1; -; Genomic_DNA. DR PIR; E64014; E64014. DR STRING; 71421.HI0843; -. DR EnsemblBacteria; AAC22511; AAC22511; HI_0843. DR PATRIC; 20190341; VBIHaeInf48452_0884. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 45 Uncharacterized protein HI_0843. FT /FTId=PRO_0000077959. SQ SEQUENCE 45 AA; 4966 MW; B0412FE321DEC9E0 CRC64; MVPLCEGDLW QELSLLAAGC RFPHLDEMVN IASINGRKVL GLELI // ID Y870_HAEIN Reviewed; 34 AA. AC P44065; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 56. DE RecName: Full=Uncharacterized protein HI_0870; GN OrderedLocusNames=HI_0870; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22529.1; -; Genomic_DNA. DR PIR; B64015; B64015. DR STRING; 71421.HI0870; -. DR EnsemblBacteria; AAC22529; AAC22529; HI_0870. DR PATRIC; 20190395; VBIHaeInf48452_0911. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 34 Uncharacterized protein HI_0870. FT /FTId=PRO_0000077964. SQ SEQUENCE 34 AA; 4290 MW; 09E7D0C116875822 CRC64; MTYHKVSPDG RMSKEKENFF RYRNQLIVLN RYMH // ID Y872_HAEIN Reviewed; 471 AA. AC Q57491; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized sugar transferase HI_0872; DE EC=2.-.-.-; GN OrderedLocusNames=HI_0872; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May function as a sugar transferase. {ECO:0000250}. CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the bacterial sugar transferase 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; L42023; AAC22530.1; -; Genomic_DNA. DR PIR; B64099; B64099. DR RefSeq; NP_439033.1; NC_000907.1. DR RefSeq; WP_010869077.1; NC_000907.1. DR STRING; 71421.HI0872; -. DR DNASU; 949841; -. DR EnsemblBacteria; AAC22530; AAC22530; HI_0872. DR GeneID; 949841; -. DR KEGG; hin:HI0872; -. DR PATRIC; 20190399; VBIHaeInf48452_0913. DR eggNOG; ENOG4105D3Q; Bacteria. DR eggNOG; COG2148; LUCA. DR KO; K00996; -. DR OMA; ERYEENV; -. DR OrthoDB; EOG6ZD66R; -. DR PhylomeDB; Q57491; -. DR UniPathway; UPA00631; -. DR Proteomes; UP000000579; 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:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR003362; Bact_transf. DR InterPro; IPR017475; EPS_sugar_tfrase. DR InterPro; IPR017472; Undecaprenyl-P_galact_Ptfrase. DR Pfam; PF02397; Bac_transf; 1. DR TIGRFAMs; TIGR03025; EPS_sugtrans; 1. DR TIGRFAMs; TIGR03022; WbaP_sugtrans; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Exopolysaccharide synthesis; KW Membrane; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 471 Uncharacterized sugar transferase FT HI_0872. FT /FTId=PRO_0000166471. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. SQ SEQUENCE 471 AA; 55217 MW; EE3761FA499CC6CB CRC64; MNRLFFSKIA LWLLDFLTFN ISFLLSLFVI SYYHNGYEKY LPIYEIDDRT YIHAVLAGIC VGWFAIRLRH YTYRKPFWFE LKEIFRTLII FAIFELAIVA FPKLYFSRYL WALTWGITFL LFPLARVLVK KFLIKSGWFL RDTIMIGSGD NAFDVYNALR DEPYLGFQVT HFISVSNISN NVKELNIPIL NSMSSWTSVT KKTDQFIIAL EDDEEVDRNN WLRYFSTNGY RSVSVIPTLR GLPLYNTDMS FMFSHEIMLL QMNNNLAKLS SRILKRTMDI VVGSLAIIIF SPVLLYLYFA VKKDGGNAIY GHPRIGRNGK TFNCLKFRTM AVNSKEVLDE LLRTDPEARA EWEKDFKLKN DPRITKIGAF IRKTSLDELP QLFNVLKGEM SLVGPRPIVI DELERYEENV DYYLMARPGM TGLWQVSGRN NIDYNTRVYF DSWYVKNWSL WNDIAILFKT MNVVLNRDGA Y // ID Y878_HAEIN Reviewed; 306 AA. AC P71360; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized transporter HI_0878; GN OrderedLocusNames=HI_0878; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the EamA transporter family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 EamA domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22534.1; -; Genomic_DNA. DR RefSeq; NP_439039.1; NC_000907.1. DR RefSeq; WP_005693231.1; NC_000907.1. DR STRING; 71421.HI0878; -. DR EnsemblBacteria; AAC22534; AAC22534; HI_0878. DR GeneID; 949421; -. DR KEGG; hin:HI0878; -. DR PATRIC; 20190413; VBIHaeInf48452_0920. DR eggNOG; ENOG4105QYV; Bacteria. DR eggNOG; COG0697; LUCA. DR OMA; GHRLWGR; -. DR OrthoDB; EOG6GTZFQ; -. DR PhylomeDB; P71360; -. DR Proteomes; UP000000579; 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; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 306 Uncharacterized transporter HI_0878. FT /FTId=PRO_0000108172. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 35 55 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT DOMAIN 17 142 EamA 1. FT DOMAIN 166 296 EamA 2. SQ SEQUENCE 306 AA; 33893 MW; AAB056682DA10CDF CRC64; MKQQPLLGFT FALITAMAWG SLPIALKQVL SVMNAQTIVW YRFIIAAVSL LALLAYKKQL PELMKVRQYA WIMLIGVIGL TSNFLLFSSS LNYIEPSVAQ IFIHLSSFGM LICGVLIFKE KLGLHQKIGL FLLLIGLGLF FNDRFDAFAG LNQYSTGVIL GVGGALIWVA YGMAQKLMLR KFNSQQILLM MYLGCAIAFM PMADFSQVQE LTPLALICFI YCCLNTLIGY GSYAEALNRW DVSKVSVVIT LVPLFTILFS HIAHYFSPAD FAAPELNNIS YIGAFVVVCG AILSAIGHKL LPHKNH // ID Y929_HAEIN Reviewed; 393 AA. AC P44940; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Putative acid--amine ligase HI_0929; DE EC=6.3.1.-; GN OrderedLocusNames=HI_0929; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase CC activity (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP- CC grasp 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; L42023; AAC22589.1; -; Genomic_DNA. DR PIR; F64161; F64161. DR RefSeq; NP_439089.1; NC_000907.1. DR RefSeq; WP_010869087.1; NC_000907.1. DR ProteinModelPortal; P44940; -. DR STRING; 71421.HI0929; -. DR EnsemblBacteria; AAC22589; AAC22589; HI_0929. DR GeneID; 949927; -. DR KEGG; hin:HI0929; -. DR PATRIC; 20190515; VBIHaeInf48452_0970. DR eggNOG; ENOG4106032; Bacteria. DR eggNOG; COG0754; LUCA. DR OMA; WSEEAYY; -. DR OrthoDB; EOG66XB93; -. DR PhylomeDB; P44940; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF03738; GSP_synth; 1. DR SUPFAM; SSF52440; SSF52440; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 393 Putative acid--amine ligase HI_0929. FT /FTId=PRO_0000169404. FT NP_BIND 103 105 ATP. {ECO:0000250}. FT NP_BIND 378 380 ATP. {ECO:0000250}. FT METAL 105 105 Magnesium 1. {ECO:0000250}. FT METAL 117 117 Magnesium 1. {ECO:0000250}. FT METAL 119 119 Magnesium 2. {ECO:0000250}. FT BINDING 267 267 ATP. {ECO:0000250}. FT BINDING 303 303 ATP. {ECO:0000250}. FT BINDING 310 310 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 343 343 ATP. {ECO:0000250}. FT SITE 103 103 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 393 AA; 45792 MW; D2773A5BF35E8B38 CRC64; MKRVTGFPTR PDMVQQLLNV GFDYYNLPSS DGSHYWSDNV AYEFTLAEID RIEDTTNELH SMCLDFAADE IKKGDYENYH FTELQKQLIE TSWRNQEPYL YGRFDFGYDG NNLKMFEYNA DTPTSLLEAA VVQWQWLEQI EGLKHRDQFN WIHEELIKHF QFLKQQSGKT DFHLSAMQDA GREDWGNVDY LADVAYNAGW NIHQLAVEDI GYNSETKKFV DLNDQPIEML FKLYPLEWLS HAEFARHITT AETRFIEPAW KMLLSNKALL AKLWARYPNH PHLLPAYFTP FELPKDLSMW VKKPLLGREG ANVFYYEKNN GVEFAAKGSE HSTFYGNSGY VYQQKFELPS FDGMYPIIGS WVVGDVACGM GLREDFTAVT GNDSHFIPHY FVP // ID Y933_HAEIN Reviewed; 401 AA. AC P44941; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 103. DE RecName: Full=Uncharacterized protein HI_0933; GN OrderedLocusNames=HI_0933; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YhiN. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22591.1; -; Genomic_DNA. DR PIR; G64161; G64161. DR RefSeq; NP_439093.1; NC_000907.1. DR RefSeq; WP_005693280.1; NC_000907.1. DR PDB; 2GQF; X-ray; 2.70 A; A=1-401. DR PDBsum; 2GQF; -. DR ProteinModelPortal; P44941; -. DR SMR; P44941; 1-401. DR STRING; 71421.HI0933; -. DR EnsemblBacteria; AAC22591; AAC22591; HI_0933. DR GeneID; 949936; -. DR KEGG; hin:HI0933; -. DR PATRIC; 20190523; VBIHaeInf48452_0974. DR eggNOG; ENOG4105CBX; Bacteria. DR eggNOG; COG2081; LUCA. DR KO; K07007; -. DR OMA; RCNFTNM; -. DR OrthoDB; EOG6677RK; -. DR PhylomeDB; P44941; -. DR EvolutionaryTrace; P44941; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.10.8.260; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR004792; CHP00275_HI0933-like. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR023166; HI0933_dom. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR00275; TIGR00275; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 401 Uncharacterized protein HI_0933. FT /FTId=PRO_0000169566. FT STRAND 2 4 {ECO:0000244|PDB:2GQF}. FT STRAND 6 10 {ECO:0000244|PDB:2GQF}. FT HELIX 14 25 {ECO:0000244|PDB:2GQF}. FT STRAND 30 33 {ECO:0000244|PDB:2GQF}. FT STRAND 35 39 {ECO:0000244|PDB:2GQF}. FT HELIX 41 45 {ECO:0000244|PDB:2GQF}. FT HELIX 46 49 {ECO:0000244|PDB:2GQF}. FT STRAND 54 57 {ECO:0000244|PDB:2GQF}. FT HELIX 60 62 {ECO:0000244|PDB:2GQF}. FT HELIX 72 77 {ECO:0000244|PDB:2GQF}. FT HELIX 80 89 {ECO:0000244|PDB:2GQF}. FT STRAND 94 96 {ECO:0000244|PDB:2GQF}. FT STRAND 101 104 {ECO:0000244|PDB:2GQF}. FT HELIX 109 122 {ECO:0000244|PDB:2GQF}. FT STRAND 125 127 {ECO:0000244|PDB:2GQF}. FT STRAND 132 137 {ECO:0000244|PDB:2GQF}. FT STRAND 146 150 {ECO:0000244|PDB:2GQF}. FT STRAND 153 162 {ECO:0000244|PDB:2GQF}. FT HELIX 170 172 {ECO:0000244|PDB:2GQF}. FT HELIX 177 184 {ECO:0000244|PDB:2GQF}. FT STRAND 189 196 {ECO:0000244|PDB:2GQF}. FT HELIX 203 211 {ECO:0000244|PDB:2GQF}. FT STRAND 215 222 {ECO:0000244|PDB:2GQF}. FT STRAND 227 234 {ECO:0000244|PDB:2GQF}. FT STRAND 236 241 {ECO:0000244|PDB:2GQF}. FT HELIX 242 247 {ECO:0000244|PDB:2GQF}. FT TURN 248 250 {ECO:0000244|PDB:2GQF}. FT STRAND 257 261 {ECO:0000244|PDB:2GQF}. FT STRAND 263 265 {ECO:0000244|PDB:2GQF}. FT HELIX 267 277 {ECO:0000244|PDB:2GQF}. FT HELIX 283 287 {ECO:0000244|PDB:2GQF}. FT TURN 288 290 {ECO:0000244|PDB:2GQF}. FT HELIX 293 301 {ECO:0000244|PDB:2GQF}. FT HELIX 310 312 {ECO:0000244|PDB:2GQF}. FT HELIX 315 326 {ECO:0000244|PDB:2GQF}. FT STRAND 328 330 {ECO:0000244|PDB:2GQF}. FT STRAND 333 335 {ECO:0000244|PDB:2GQF}. FT TURN 338 340 {ECO:0000244|PDB:2GQF}. FT STRAND 342 348 {ECO:0000244|PDB:2GQF}. FT HELIX 350 352 {ECO:0000244|PDB:2GQF}. FT TURN 355 357 {ECO:0000244|PDB:2GQF}. FT STRAND 359 363 {ECO:0000244|PDB:2GQF}. FT STRAND 366 368 {ECO:0000244|PDB:2GQF}. FT HELIX 370 372 {ECO:0000244|PDB:2GQF}. FT TURN 379 381 {ECO:0000244|PDB:2GQF}. FT HELIX 382 399 {ECO:0000244|PDB:2GQF}. SQ SEQUENCE 401 AA; 44476 MW; 4B25CC8BB3CFE8D6 CRC64; MSQYSENIII GAGAAGLFCA AQLAKLGKSV TVFDNGKKIG RKILMSGGGF CNFTNLEVTP AHYLSQNPHF VKSALARYTN WDFISLVAEQ GITYHEKELG QLFCDEGAEQ IVEMLKSECD KYGAKILLRS EVSQVERIQN DEKVRFVLQV NSTQWQCKNL IVATGGLSMP GLGATPFGYQ IAEQFGIPVI PPRASLVPFT YRETDKFLTA LSGISLPVTI TALCGKSFYN QLLFTHRGIS GPAVLQISNY WQPTESVEID LLPNHNVEEE INQAKQSSPK QMLKTILVRL LPKKLVELWI EQGIVQDEVI ANISKVRVKN LVDFIHHWEF TPNGTEGYRT AEVTMGGVDT KVISSKTMES NQVSGLYFIG EVLDVTGWLG GYNFQWAWSS AYACALSISR Q // ID Y976_HAEIN Reviewed; 128 AA. AC Q57147; O05039; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein HI_0976; GN OrderedLocusNames=HI_0976; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 EamA 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; L42023; AAC22635.1; -; Genomic_DNA. DR PIR; B64163; B64163. DR STRING; 71421.HI0976; -. DR EnsemblBacteria; AAC22635; AAC22635; HI_0976. DR PATRIC; 20190611; VBIHaeInf48452_1018. DR eggNOG; COG0697; LUCA. DR OrthoDB; EOG6CS08B; -. DR Proteomes; UP000000579; 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; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 128 Uncharacterized protein HI_0976. FT /FTId=PRO_0000077986. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT DOMAIN 9 110 EamA. SQ SEQUENCE 128 AA; 15013 MW; 9D8C997B6D93EFE9 CRC64; MLYQILALLI WSSSLIVGKL TYSMMDPVLV VQVRLIIAMI IVMPLFLRRW KKIDKPMRKQ LWWLAFFNYT AVFLLQFIGL KYTSASSAVT MIGLEPLLVV FVGHFFFKTK QNGFTGYSVQ WHLLAWQF // ID YCIB_HAEIN Reviewed; 185 AA. AC P43810; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable intracellular septation protein A {ECO:0000255|HAMAP-Rule:MF_00189}; GN OrderedLocusNames=HI_0826; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in cell division; probably involved in CC intracellular septation. {ECO:0000255|HAMAP-Rule:MF_00189}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00189}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00189}. CC -!- SIMILARITY: Belongs to the YciB family. {ECO:0000255|HAMAP- CC Rule:MF_00189}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22484.1; -; Genomic_DNA. DR PIR; A64159; A64159. DR RefSeq; NP_438986.1; NC_000907.1. DR RefSeq; WP_005655641.1; NC_000907.1. DR STRING; 71421.HI0826; -. DR EnsemblBacteria; AAC22484; AAC22484; HI_0826. DR GeneID; 949918; -. DR KEGG; hin:HI0826; -. DR PATRIC; 20190307; VBIHaeInf48452_0867. DR eggNOG; ENOG4107835; Bacteria. DR eggNOG; COG2917; LUCA. DR KO; K06190; -. DR OMA; VAQFQFK; -. DR OrthoDB; EOG6JHRJS; -. DR PhylomeDB; P43810; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00189; Intracell_septation_prot_A; 1. DR InterPro; IPR006008; Intracell_sepatation_prot_A. DR Pfam; PF04279; IspA; 1. DR TIGRFAMs; TIGR00997; ispZ; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Septation; KW Transmembrane; Transmembrane helix. FT CHAIN 1 185 Probable intracellular septation protein FT A. FT /FTId=PRO_0000206535. FT TRANSMEM 27 47 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 53 73 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 76 96 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 118 138 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. FT TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00189}. SQ SEQUENCE 185 AA; 21216 MW; E50CAD86D0E03675 CRC64; MKQLLDFIPL ILFFITYKLG GVREAAIVLV VATILQIVIL KWKYGMVEKQ QKIMASAVVF FGLLTAYFNE IRYLQWKVTI INGLFAIVLL VAQFQFKTPL IKKLLGKELQ LPEKAWNTLN FGWAIFFIIC MLVNIYISHN MSEEAWVDFK SFGIIGMTVI ATIISGVYIY RYLPKDGSNS KDGEK // ID Y453_HAEIN Reviewed; 174 AA. AC P43999; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_0453; GN OrderedLocusNames=HI_0453; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22111.1; -; Genomic_DNA. DR PIR; H64007; H64007. DR RefSeq; NP_438614.1; NC_000907.1. DR RefSeq; WP_005652096.1; NC_000907.1. DR STRING; 71421.HI0453; -. DR EnsemblBacteria; AAC22111; AAC22111; HI_0453. DR GeneID; 949624; -. DR KEGG; hin:HI0453; -. DR PATRIC; 20189461; VBIHaeInf48452_0473. DR eggNOG; ENOG4105RX8; Bacteria. DR eggNOG; ENOG411201F; LUCA. DR OMA; RSVCTLF; -. DR OrthoDB; EOG6SV58G; -. DR PhylomeDB; P43999; -. DR Proteomes; UP000000579; 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; IPR011088; Phage_phiNM3_A0EWY4. DR Pfam; PF07509; DUF1523; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 174 Uncharacterized protein HI_0453. FT /FTId=PRO_0000077924. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. SQ SEQUENCE 174 AA; 20416 MW; 32A2F39303399B48 CRC64; MRKFFKYFLF IVVFLFHGFM FSVVNYVFPH YDVTRVTGVE VKRVDKDGPI TKSNPADGPT RDVYYINTQN DDGKIMVYRN EDTRWGFPFY FKFGSANLQA EAQALGNDNK LVQIKYYGWR ITMVDEYRNA TSIKEITADD TPSNPIVSWI LYVFLLATLF LSIQFIRGWF DSDK // ID Y467_HAEIN Reviewed; 287 AA. AC P44726; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=UPF0701 protein HI_0467; GN OrderedLocusNames=HI_0467; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- SIMILARITY: Belongs to the UPF0701 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; L42023; AAC22126.1; -; Genomic_DNA. DR PIR; C64153; C64153. DR RefSeq; NP_438628.3; NC_000907.1. DR RefSeq; WP_005693694.1; NC_000907.1. DR STRING; 71421.HI0467; -. DR EnsemblBacteria; AAC22126; AAC22126; HI_0467. DR GeneID; 949553; -. DR KEGG; hin:HI0467; -. DR PATRIC; 20189489; VBIHaeInf48452_0487. DR eggNOG; ENOG4105DSJ; Bacteria. DR eggNOG; COG1561; LUCA. DR OMA; QEMILLA; -. DR OrthoDB; EOG61KBKV; -. DR PhylomeDB; P44726; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR005229; CHP00255. DR InterPro; IPR013551; DUF1732. DR InterPro; IPR013527; YicC-like_N. DR Pfam; PF08340; DUF1732; 1. DR Pfam; PF03755; YicC_N; 1. DR TIGRFAMs; TIGR00255; TIGR00255; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 287 UPF0701 protein HI_0467. FT /FTId=PRO_0000169614. SQ SEQUENCE 287 AA; 33270 MW; BFC59630BC6F6BF3 CRC64; MIYSMTAFAR LEVKKDWGDA VWEIRSVNQR YLENFFRLPE QFRGLENTLR EKLRQNLTRG KIECSLRIET KKQANAELNL NKELANQVIQ SLQWIKAQAG EGEINLTDVL RYPGVVEAQE QDLDAISQDL LTAFDDLLTD FIAMRGREGE KLNDIIQQRL DSIAVETDKV RSQMPAVLQW QRERLLQRFE DAQLNLDPQR VEQEMILLAQ RIDVAEELDR LQMHVKETTN ILKKGGAVGR KLDFMMQELN RESNTLASKS INADITASAV ELKVLIEQMR EQIQNLE // ID Y519_HAEIN Reviewed; 417 AA. AC P44742; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 104. DE RecName: Full=Uncharacterized transporter HI_0519; GN OrderedLocusNames=HI_0519; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the concentrative nucleoside transporter CC (CNT) (TC 2.A.41) 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; L42023; AAC22177.1; -; Genomic_DNA. DR PIR; A64154; A64154. DR RefSeq; NP_438677.1; NC_000907.1. DR RefSeq; WP_005649475.1; NC_000907.1. DR STRING; 71421.HI0519; -. DR EnsemblBacteria; AAC22177; AAC22177; HI_0519. DR GeneID; 949656; -. DR KEGG; hin:HI0519; -. DR PATRIC; 20189591; VBIHaeInf48452_0538. DR eggNOG; ENOG4105D9N; Bacteria. DR eggNOG; COG1972; LUCA. DR KO; K03317; -. DR OMA; EFVAYMN; -. DR OrthoDB; EOG6V7BJ0; -. DR PhylomeDB; P44742; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005337; F:nucleoside transmembrane transporter activity; IBA:GO_Central. DR InterPro; IPR008276; C_nuclsd_transpt. DR InterPro; IPR018270; C_nuclsd_transpt_met_bac. DR InterPro; IPR011657; CNT_C_dom. DR InterPro; IPR002668; CNT_N_dom. DR InterPro; IPR011642; Gate_dom. DR PANTHER; PTHR10590; PTHR10590; 1. DR Pfam; PF07670; Gate; 1. DR Pfam; PF07662; Nucleos_tra2_C; 1. DR Pfam; PF01773; Nucleos_tra2_N; 1. DR TIGRFAMs; TIGR00804; nupC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 417 Uncharacterized transporter HI_0519. FT /FTId=PRO_0000070459. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. FT TRANSMEM 261 281 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. FT TRANSMEM 392 412 Helical. {ECO:0000255}. SQ SEQUENCE 417 AA; 42773 MW; 9075BFCFE7FC20A6 CRC64; MSVLSSILGM VVLIAIAVLL SNNRKAISIR TVVGALAIQV GFAALILYVP AGKQALGAAA DMVSNVIAYG NDGINFVFGG LADPSKPSGF IFAVKVLPII VFFSGLISVL YYLGIMQVVI KVLGGALQKA LGTSKAESMS AAANIFVGQT EAPLVVRPYI KNMTQSELFA IMVGGTASIA GSVMAGYAGM GVPLTYLIAA SFMAAPAGLL FAKLMFPQTE QFTDKQPEDN DSEKPTNVLE AMAGGASAGM QLALNVGAML IAFVGLIALI NGILSGVGGW FGYGDLTLQS IFGLIFKPLA YLIGVTDGAE AGIAGQMIGM KLAVNEFVGY LEFAKYLQPD SAIVLTEKTK AIITFALCGF ANFSSIAILI GGLGGMAPSR RSDVARLGIK AVIAGTLANL MSATIAGLFI GLGAAAL // ID Y552_HAEIN Reviewed; 207 AA. AC P44013; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0552; GN OrderedLocusNames=HI_0552; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22216.1; -; Genomic_DNA. DR PIR; D64009; D64009. DR RefSeq; NP_438710.1; NC_000907.1. DR RefSeq; WP_005694148.1; NC_000907.1. DR STRING; 71421.HI0552; -. DR EnsemblBacteria; AAC22216; AAC22216; HI_0552. DR GeneID; 949603; -. DR KEGG; hin:HI0552; -. DR PATRIC; 20189659; VBIHaeInf48452_0572. DR eggNOG; ENOG4105WV0; Bacteria. DR eggNOG; ENOG411248I; LUCA. DR OMA; FCPEDIP; -. DR OrthoDB; EOG6CCH4G; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR019722; G6PD_bac. DR Pfam; PF10786; G6PD_bact; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 207 Uncharacterized protein HI_0552. FT /FTId=PRO_0000077930. SQ SEQUENCE 207 AA; 24938 MW; 0E58735AD35BA0D1 CRC64; MLSLTAESCE LFNIPFYQFA QMKKFCPEDI PAIKADYKLH WDNWKAIIQS VSAQLGTPFA KPHIESWTNG WQVRAHFFAY FKYEFNQNSA AIFSVLLNRR RLRVCLDWHC YRADRSQINV QQYNQWLDQF DFKQFADFEI WREDESEYDD FRQVKVISEK NLILRSDEDF WCIGKSIEKA ELNQIDPVLF ITHTIQQLQP LYDRCHQ // ID Y575_HAEIN Reviewed; 221 AA. AC P44761; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0575; GN OrderedLocusNames=HI_0575; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YheO. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22233.1; -; Genomic_DNA. DR PIR; B64155; B64155. DR RefSeq; NP_438732.1; NC_000907.1. DR RefSeq; WP_005694171.1; NC_000907.1. DR STRING; 71421.HI0575; -. DR DNASU; 950683; -. DR EnsemblBacteria; AAC22233; AAC22233; HI_0575. DR GeneID; 950683; -. DR KEGG; hin:HI0575; -. DR PATRIC; 20189705; VBIHaeInf48452_0595. DR eggNOG; ENOG4105WWK; Bacteria. DR eggNOG; COG2964; LUCA. DR OMA; STIVYIK; -. DR OrthoDB; EOG6GJBRV; -. DR PhylomeDB; P44761; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR013559; YheO. DR Pfam; PF08348; PAS_6; 1. DR ProDom; PD037769; YheO; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 221 Uncharacterized protein HI_0575. FT /FTId=PRO_0000169512. SQ SEQUENCE 221 AA; 24850 MW; 238A8BCA80742105 CRC64; MTLNDKYPFT DEDQAIINSY KAVVDGVSAL IGEHCEIVLH SLENIEHSAI CIANGHNTNR QVGSPITDLA LRSLRNMQSE SVSKPYFTRA KGSVLMKSVT IAIRNKTQRI IGLLCININL DVPVSQFLQC FMLTEHTNET SSVNFANSVE DLVAQTIEKT IEEVNADRAV ANNTKNRQIV LSLYEKGIFD IKDAINLVAE RLDISRHTVY LYIRQIKQEQ E // ID Y585_HAEIN Reviewed; 279 AA. AC P44018; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Putative uncharacterized transporter HI_0585; GN OrderedLocusNames=HI_0585; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DcuC/DcuD transporter (TC 2.A.61) CC family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22249.1; -; Genomic_DNA. DR PIR; I64009; I64009. DR STRING; 71421.HI0585; -. DR TCDB; 2.A.61.1.3; the c4-dicarboxylate uptake c (dcuc) family. DR EnsemblBacteria; AAC22249; AAC22249; HI_0585. DR PATRIC; 20189727; VBIHaeInf48452_0606. DR eggNOG; COG3069; LUCA. DR OMA; VVMTRIS; -. DR OrthoDB; EOG6KMB42; -. DR Proteomes; UP000000579; 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:0015556; F:C4-dicarboxylate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR004669; C4_dicarb_anaerob_car. DR InterPro; IPR018385; C4_dicarb_anaerob_car-like. DR Pfam; PF03606; DcuC; 1. DR TIGRFAMs; TIGR00771; DcuC; 1. PE 5: Uncertain; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 279 Putative uncharacterized transporter FT HI_0585. FT /FTId=PRO_0000201633. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. SQ SEQUENCE 279 AA; 28990 MW; A724FFBD152476A9 CRC64; MMSPGSSHSA MISEMSGLTI TQVNLSHAPY NMIAGAIGAV VLTILALVFK DYGEQHRQAY LAEQKESEIK VIEGVNVLYA LAPLIPLVIL VIGGTSLQQV PGLEWTKMGV PQAMLIGAIY GIIVTRISPV KITEEFFNGM GNSYANVLGI IIAASVFVAG LKSTGAVDAA ISFLKESNEF VRWGATIGPF LMGLITGSGD AAAIAFNTAV TPHAVELGYT HVNLGMAAAI AGAIGRTASP IAGVTIVCAG LAMVSPVEMV KRTAPGMILA VLFLALFML // ID Y589_HAEIN Reviewed; 139 AA. AC P44020; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein HI_0589; GN OrderedLocusNames=HI_0589; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RseC 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; L42023; AAC22246.1; -; Genomic_DNA. DR PIR; B64010; B64010. DR RefSeq; NP_438747.1; NC_000907.1. DR RefSeq; WP_005694561.1; NC_000907.1. DR STRING; 71421.HI0589; -. DR EnsemblBacteria; AAC22246; AAC22246; HI_0589. DR GeneID; 949630; -. DR KEGG; hin:HI0589; -. DR PATRIC; 20189737; VBIHaeInf48452_0611. DR eggNOG; COG3086; LUCA. DR OMA; FSALLMY; -. DR OrthoDB; EOG6GBMHX; -. DR PhylomeDB; P44020; -. DR Proteomes; UP000000579; 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; IPR026268; RseC. DR InterPro; IPR007359; SigmaE_reg_RseC_MucC. DR Pfam; PF04246; RseC_MucC; 1. DR PIRSF; PIRSF004923; RseC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 139 Uncharacterized protein HI_0589. FT /FTId=PRO_0000077936. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. SQ SEQUENCE 139 AA; 15635 MW; 6C26821FAF4DF32D CRC64; MMSYDAETGI AKVKCQSQST CGACSARETC GTESLSELNG KRGEHIFTLE TITPLRTDQM VEIGLEEKSM LFSALLMYIV QLFTLLVATL LSSYISENEL IRAILIFMLT ALSFVMVKRY TRKLGQQTEF QSVLLRVLF // ID Y627_HAEIN Reviewed; 85 AA. AC P44025; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein HI_0627; GN OrderedLocusNames=HI_0627; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the CptB antitoxin family. {ECO:0000305}. CC -!- CAUTION: Although this protein belongs to an antitoxin family, the CC known cognate toxin is not found in this organism. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22287.1; -; Genomic_DNA. DR PIR; G64010; G64010. DR RefSeq; NP_438787.1; NC_000907.1. DR RefSeq; WP_005694645.1; NC_000907.1. DR ProteinModelPortal; P44025; -. DR SMR; P44025; 1-79. DR STRING; 71421.HI0627; -. DR EnsemblBacteria; AAC22287; AAC22287; HI_0627. DR GeneID; 950813; -. DR KEGG; hin:HI0627; -. DR PATRIC; 20189849; VBIHaeInf48452_0653. DR eggNOG; ENOG4105Y75; Bacteria. DR eggNOG; COG2938; LUCA. DR KO; K09159; -. DR OMA; DLFAWFM; -. DR OrthoDB; EOG63FW79; -. DR PhylomeDB; P44025; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.10.150.250; -; 1. DR InterPro; IPR005631; SDH. DR Pfam; PF03937; Sdh5; 1. DR SUPFAM; SSF109910; SSF109910; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 85 Uncharacterized protein HI_0627. FT /FTId=PRO_0000214400. SQ SEQUENCE 85 AA; 10430 MW; AADE707492162A1C CRC64; MKKYNKLRIE WDCRRGMLEL DKIIMPFYLT HFHELTDDKK DIFIRLLAST DLQLFSWFFN LAKSQDVELQ MMVEYIQKVQ KIIIN // ID Y633_HAEIN Reviewed; 98 AA. AC P44026; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein HI_0633; GN OrderedLocusNames=HI_0633; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22297.1; -; Genomic_DNA. DR PIR; H64010; H64010. DR RefSeq; NP_438793.2; NC_000907.1. DR ProteinModelPortal; P44026; -. DR STRING; 71421.HI0633; -. DR EnsemblBacteria; AAC22297; AAC22297; HI_0633. DR GeneID; 950781; -. DR KEGG; hin:HI0633; -. DR PATRIC; 20189869; VBIHaeInf48452_0659. DR eggNOG; COG0038; LUCA. DR OMA; IVIVMEM; -. DR OrthoDB; EOG6C0143; -. DR Proteomes; UP000000579; 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:0005247; F:voltage-gated chloride channel activity; IEA:InterPro. DR Gene3D; 1.10.3080.10; -; 1. DR InterPro; IPR014743; Cl-channel_core. DR InterPro; IPR001807; Cl-channel_volt-gated. DR Pfam; PF00654; Voltage_CLC; 1. DR SUPFAM; SSF81340; SSF81340; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 98 Uncharacterized protein HI_0633. FT /FTId=PRO_0000077938. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. SQ SEQUENCE 98 AA; 10922 MW; 2AC189CA314ABE17 CRC64; MLWDLSGGMV DQRFLVILCM VAFLAGCTQS PVTASVIVME MTGAQPVLIW LLISSIIASI ISHQFSPKPF YHFAAGCFLQ QMQARQAEEL RSKTEQEK // ID Y840_HAEIN Reviewed; 72 AA. AC P44897; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=UPF0352 protein HI_0840 {ECO:0000255|HAMAP-Rule:MF_00816}; GN OrderedLocusNames=HI_0840; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0352 family. {ECO:0000255|HAMAP- CC Rule:MF_00816}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22499.1; -; Genomic_DNA. DR PIR; E64159; E64159. DR RefSeq; NP_439000.1; NC_000907.1. DR RefSeq; WP_005693192.1; NC_000907.1. DR PDB; 2JUZ; NMR; -; A/B=1-72. DR PDBsum; 2JUZ; -. DR ProteinModelPortal; P44897; -. DR SMR; P44897; 1-72. DR STRING; 71421.HI0840; -. DR EnsemblBacteria; AAC22499; AAC22499; HI_0840. DR GeneID; 949854; -. DR KEGG; hin:HI0840; -. DR PATRIC; 20190335; VBIHaeInf48452_0881. DR eggNOG; ENOG4105YDX; Bacteria. DR eggNOG; COG3082; LUCA. DR KO; K09904; -. DR OMA; HQAPTDL; -. DR OrthoDB; EOG615VPH; -. DR PhylomeDB; P44897; -. DR EvolutionaryTrace; P44897; -. DR Proteomes; UP000000579; Chromosome. DR Gene3D; 1.10.3390.10; -; 1. DR HAMAP; MF_00816; UPF0352; 1. DR InterPro; IPR009857; UPF0352. DR InterPro; IPR023202; YejL_dom. DR Pfam; PF07208; DUF1414; 1. DR PIRSF; PIRSF006188; UCP006188; 1. DR ProDom; PD027794; UPF0352; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 72 UPF0352 protein HI_0840. FT /FTId=PRO_0000201789. FT HELIX 9 26 {ECO:0000244|PDB:2JUZ}. FT HELIX 31 45 {ECO:0000244|PDB:2JUZ}. FT HELIX 54 72 {ECO:0000244|PDB:2JUZ}. SQ SEQUENCE 72 AA; 7684 MW; 7220CB06FCC35BC2 CRC64; MAQHSKYSDA QLSAIVNDMI AVLEKHKAPV DLSLIALGNM ASNLLTTSVP QTQCEALAQA FSNSLINAVK TR // ID Y855_HAEIN Reviewed; 115 AA. AC P44904; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=UPF0597 protein HI_0855; GN OrderedLocusNames=HI_0855; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the UPF0597 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; L42023; AAC22514.1; -; Genomic_DNA. DR PIR; C64160; C64160. DR RefSeq; NP_439015.1; NC_000907.1. DR RefSeq; WP_005693202.1; NC_000907.1. DR STRING; 71421.HI0855; -. DR EnsemblBacteria; AAC22514; AAC22514; HI_0855. DR GeneID; 949868; -. DR KEGG; hin:HI0855; -. DR PATRIC; 20190365; VBIHaeInf48452_0896. DR eggNOG; COG3681; LUCA. DR OMA; VCNISID; -. DR OrthoDB; EOG64N9WK; -. DR Proteomes; UP000000579; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 115 UPF0597 protein HI_0855. FT /FTId=PRO_0000169449. SQ SEQUENCE 115 AA; 12248 MW; D2C1CB94ACC9BB8F CRC64; MNLERLNEIE KPLLHIVKHD VMPALGCTEP ISLALASATA AKYLGKTPER IEAKVSPNLM KNGLGVAVPG TGMVGLPIAA AMKVLSNTIL IELLIISVLL HQKVCSISTD RLSKL // ID Y862_HAEIN Reviewed; 235 AA. AC P44908; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein HI_0862; GN OrderedLocusNames=HI_0862; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YhhQ. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22521.1; -; Genomic_DNA. DR PIR; F64160; F64160. DR RefSeq; NP_439022.1; NC_000907.1. DR RefSeq; WP_005693208.1; NC_000907.1. DR STRING; 71421.HI0862; -. DR EnsemblBacteria; AAC22521; AAC22521; HI_0862. DR GeneID; 949874; -. DR KEGG; hin:HI0862; -. DR PATRIC; 20190379; VBIHaeInf48452_0903. DR eggNOG; ENOG4105EX9; Bacteria. DR eggNOG; COG1738; LUCA. DR KO; K09125; -. DR OMA; RSTDAFM; -. DR OrthoDB; EOG65J51G; -. DR PhylomeDB; P44908; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR003744; DUF165. DR Pfam; PF02592; Vut_1; 1. DR TIGRFAMs; TIGR00697; TIGR00697; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 235 Uncharacterized protein HI_0862. FT /FTId=PRO_0000169557. SQ SEQUENCE 235 AA; 26889 MW; C6FFCF79AB685CC1 CRC64; MKLTSPIFND QQKRRAIIWL SFFHIFIIAA SNYFVQIPFE ITLKLTALGA ANDFSFHSTW GTLTFPFIFL ATDLTVRIFG AEDARKIIFV VMFPALIVSY VISVLFSESK FQGFESLTHF DLFVFRIAIA SFAAYVVGQL LDVIVFNRLR QLKTWWVAPT SSMTFGSMAD TFVFFSIAFY QSADPFMAEH WAQLGFVDYL FKLFIGIILF VPAYGVVLNV ILRKLQMLVT ERVPA // ID Y886_HAEIN Reviewed; 134 AA. AC P44069; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 91. DE RecName: Full=Uncharacterized protein HI_0886; GN OrderedLocusNames=HI_0886; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DoxX 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; L42023; AAC22547.1; -; Genomic_DNA. DR PIR; F64015; F64015. DR RefSeq; NP_439047.1; NC_000907.1. DR RefSeq; WP_005693236.1; NC_000907.1. DR STRING; 71421.HI0886; -. DR EnsemblBacteria; AAC22547; AAC22547; HI_0886. DR GeneID; 949888; -. DR KEGG; hin:HI0886; -. DR PATRIC; 20190429; VBIHaeInf48452_0928. DR eggNOG; ENOG4105MGM; Bacteria. DR eggNOG; COG2259; LUCA. DR KO; K15977; -. DR OMA; GFPASQM; -. DR OrthoDB; EOG69SKFR; -. DR PhylomeDB; P44069; -. DR BioCyc; RETL1328306-WGS:GSTH-2240-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-5915-MONOMER; -. DR Proteomes; UP000000579; 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; IPR032808; DoxX. DR Pfam; PF07681; DoxX; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 134 Uncharacterized protein HI_0886. FT /FTId=PRO_0000077969. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. SQ SEQUENCE 134 AA; 14754 MW; B59EE67346F8EA86 CRC64; MNNLEKYRPY FLAFLRIVVA YMFILHGTAK FLEFPISMTG GNGAVGDPML LVAGVIEIVG SILLILGLFT RQAAFILSVE MAYAYFFLHV AGKGNLFFPI ANGGELALLY SLLFLYFVFS GAGACALDNK FFKK // ID Y893_HAEIN Reviewed; 187 AA. AC P44923; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator HI_0893; GN OrderedLocusNames=HI_0893; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Contains 1 HTH tetR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00335}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22553.1; -; Genomic_DNA. DR PIR; F64100; F64100. DR RefSeq; NP_439054.1; NC_000907.1. DR RefSeq; WP_005693244.1; NC_000907.1. DR PDB; 3QKX; X-ray; 2.35 A; A/B=1-187. DR PDBsum; 3QKX; -. DR ProteinModelPortal; P44923; -. DR STRING; 71421.HI0893; -. DR DNASU; 949896; -. DR EnsemblBacteria; AAC22553; AAC22553; HI_0893. DR GeneID; 949896; -. DR KEGG; hin:HI0893; -. DR PATRIC; 20190443; VBIHaeInf48452_0935. DR eggNOG; ENOG4105Y7M; Bacteria. DR eggNOG; COG1309; LUCA. DR KO; K18136; -. DR OMA; FEQYRQM; -. DR OrthoDB; EOG6DVJW9; -. DR PhylomeDB; P44923; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.357.10; -; 1. DR InterPro; IPR023772; DNA-bd_HTH_TetR-type_CS. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001647; HTH_TetR. DR InterPro; IPR015893; Tet_transcr_reg_TetR-like_C. DR Pfam; PF00440; TetR_N; 1. DR PRINTS; PR00455; HTHTETR. DR SUPFAM; SSF46689; SSF46689; 1. DR PROSITE; PS01081; HTH_TETR_1; 1. DR PROSITE; PS50977; HTH_TETR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1 187 Uncharacterized HTH-type transcriptional FT regulator HI_0893. FT /FTId=PRO_0000070657. FT DOMAIN 6 66 HTH tetR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00335}. FT DNA_BIND 29 48 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00335}. FT HELIX 5 22 {ECO:0000244|PDB:3QKX}. FT HELIX 30 37 {ECO:0000244|PDB:3QKX}. FT HELIX 41 47 {ECO:0000244|PDB:3QKX}. FT STRAND 48 50 {ECO:0000244|PDB:3QKX}. FT HELIX 51 71 {ECO:0000244|PDB:3QKX}. FT HELIX 80 97 {ECO:0000244|PDB:3QKX}. FT HELIX 99 108 {ECO:0000244|PDB:3QKX}. FT TURN 112 120 {ECO:0000244|PDB:3QKX}. FT HELIX 125 136 {ECO:0000244|PDB:3QKX}. FT HELIX 144 150 {ECO:0000244|PDB:3QKX}. FT HELIX 153 164 {ECO:0000244|PDB:3QKX}. FT HELIX 171 183 {ECO:0000244|PDB:3QKX}. SQ SEQUENCE 187 AA; 22022 MW; 53868EF738C024CD CRC64; MRQAKTDLAE QIFSATDRLM AREGLNQLSM LKLAKEANVA AGTIYLYFKN KDELLEQFAH RVFSMFMATL EKDFDETKPF FEQYRQMWKN IWYFLQENPT ILSNLKQYES LPNFKDICKN IKNCRWDLFC HQAQKAGLLA ELSEDILFLL SLKTAINLAS DAKFIDFDLK PEILESVIER SWRAIQK // ID Y894_HAEIN Reviewed; 382 AA. AC Q57500; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized protein HI_0894; GN OrderedLocusNames=HI_0894; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) CC (TC 8.A.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22554.1; -; Genomic_DNA. DR RefSeq; NP_439055.1; NC_000907.1. DR RefSeq; WP_010869083.1; NC_000907.1. DR ProteinModelPortal; Q57500; -. DR STRING; 71421.HI0894; -. DR EnsemblBacteria; AAC22554; AAC22554; HI_0894. DR GeneID; 949897; -. DR KEGG; hin:HI0894; -. DR PATRIC; 20190445; VBIHaeInf48452_0936. DR eggNOG; ENOG410624X; Bacteria. DR eggNOG; COG0845; LUCA. DR KO; K03585; -. DR OMA; APFDGKA; -. DR OrthoDB; EOG6ZWJFQ; -. DR PhylomeDB; Q57500; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR032317; HlyD_D23. DR InterPro; IPR006143; RND_pump_MFP. DR Pfam; PF16576; HlyD_D23; 1. DR TIGRFAMs; TIGR01730; RND_mfp; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 382 Uncharacterized protein HI_0894. FT /FTId=PRO_0000201893. FT TRANSMEM 1 21 Helical. {ECO:0000255}. SQ SEQUENCE 382 AA; 41409 MW; 7974AA9D53F0BB5E CRC64; MKIILVVFVL IFVGVIGFNM IKGVMISRAI AGMPESSSPV TALEVQPREW TPVINTTGLV RPNQGAMLST QNAGAVSQVL VQNGQNVKKG EVLVELDSSV ERANLQAAQA QLSALRQTYQ RYVGLLNSNA VSRQEMDNAK AAYDAQVASI ESLKAAIERR KIVAPFDGKA GIVKINVGQY VNVGTEIVRV EDTSSMKVDF ALSQNDLDKL HIGQRVTATT DARLGETFSA RITAIEPAIN SSTGLVDVQA TFDPEDGHKL LSGMFSRLRI ALPTETNQVV VPQVAISYNM YGEIAYLLEP LSEEEKGKMS GNEKLDRLYR AKQITVFTKD RQGVYAQLQG NEVKVGDKII TGGQQGIGNG SLVEWIKKDI VGAIEPAHKT PL // ID Y895_HAEIN Reviewed; 1032 AA. AC Q57124; O05034; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uncharacterized transporter HI_0895; GN OrderedLocusNames=HI_0895; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be a drug efflux pump. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division CC (RND) (TC 2.A.6) 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; L42023; AAC22555.1; -; Genomic_DNA. DR PIR; H64100; H64100. DR RefSeq; NP_439056.1; NC_000907.1. DR RefSeq; WP_005693247.1; NC_000907.1. DR ProteinModelPortal; Q57124; -. DR STRING; 71421.HI0895; -. DR EnsemblBacteria; AAC22555; AAC22555; HI_0895. DR GeneID; 949898; -. DR KEGG; hin:HI0895; -. DR PATRIC; 20190447; VBIHaeInf48452_0937. DR eggNOG; ENOG4105BZS; Bacteria. DR eggNOG; COG0841; LUCA. DR KO; K18138; -. DR OMA; RTIAINS; -. DR OrthoDB; EOG64R612; -. DR PhylomeDB; Q57124; -. DR Proteomes; UP000000579; 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 Gene3D; 3.30.2090.10; -; 2. DR InterPro; IPR027463; AcrB_DN_DC_subdom. DR InterPro; IPR001036; Acrflvin-R. DR Pfam; PF00873; ACR_tran; 1. DR PRINTS; PR00702; ACRIFLAVINRP. DR SUPFAM; SSF82714; SSF82714; 2. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1032 Uncharacterized transporter HI_0895. FT /FTId=PRO_0000161856. FT TOPO_DOM 1 17 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 18 36 Helical; Name=1. {ECO:0000250}. FT TOPO_DOM 37 337 Periplasmic. {ECO:0000250}. FT TRANSMEM 338 357 Helical; Name=2. {ECO:0000250}. FT TOPO_DOM 358 363 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 364 383 Helical; Name=3. {ECO:0000250}. FT TOPO_DOM 384 389 Periplasmic. {ECO:0000250}. FT TRANSMEM 390 411 Helical; Name=4. {ECO:0000250}. FT TOPO_DOM 412 438 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 439 457 Helical; Name=5. {ECO:0000250}. FT TOPO_DOM 458 470 Periplasmic. {ECO:0000250}. FT TRANSMEM 471 493 Helical; Name=6. {ECO:0000250}. FT TOPO_DOM 494 529 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 530 548 Helical; Name=7. {ECO:0000250}. FT TOPO_DOM 549 852 Periplasmic. {ECO:0000250}. FT TRANSMEM 853 872 Helical; Name=8. {ECO:0000250}. FT TOPO_DOM 873 878 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 879 898 Helical; Name=9. {ECO:0000250}. FT TOPO_DOM 899 910 Periplasmic. {ECO:0000250}. FT TRANSMEM 911 932 Helical; Name=10. {ECO:0000250}. FT TOPO_DOM 933 960 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 961 979 Helical; Name=11. {ECO:0000250}. FT TOPO_DOM 980 992 Periplasmic. {ECO:0000250}. FT TRANSMEM 993 1015 Helical; Name=12. {ECO:0000250}. FT TOPO_DOM 1016 1032 Cytoplasmic. {ECO:0000250}. SQ SEQUENCE 1032 AA; 111634 MW; C06658844C8F3C90 CRC64; MYEEIRMKFT DIFIRRPVLA VSISLLMIIL GLQAISKLAV REYPKMTTTV ITVSTAYPGA DANLIQAFVT SKLEESIAQA DNIDYMSSTS APSSSTITIK MKLNTDPAGA LADVLAKVNA VKSALPNGIE DPSVSSSSGG SGIMYISFRS KKLDSSQVTD YINRVVKPQF FTIEGVAEVQ VFGAAEYALR IWLDPQKMAA QNLSVPTVMS ALSANNVQTA AGNDNGYYVS YRNKVETTTK SVEQLSNLII SSNGDDLVRL RDIATVELNK ENDNSRATAN GAESVVLAIN PTSTANPLTV AEKIRPLYES IKTQLPDSME SDILYDRTIA INSSIHEVIK TIGEATLIVL VVILMFIGSF RAILIPILAI PISLIGVLML LQSFNFSINL MTLLALILAI GLVVDDAIVV LENIDRHIKA GETPFRAAII GTREIAVPVI SMTIALIAVY SPMALMGGIT GTLFKEFALT LAGAVFISGV VALTLSPMMS SKLLKSNAKP TWMEERVEHT LGKVNRVYEY MLDLVMLNRK SMLAFAVVIF STLPFLFNSL SSELTPNEDK GAFIAIGNAP SSVNVDYIQN AMQPYMKNVM ETPEVSFGMS IAGAPTSNSS LNIITLKDWK ERSRKQSAIM NEINEKAKSI PEVSVSAFNI PEIDTGEQGP PVSIVLKTAQ DYKSLANTAE KFLSAMKASG KFIYTNLDLT YDTAQMTISV DKEKAGTYGI TMQQISNTLG SFLSGATVTR VDVDGRAYKV ISQVKRDDRL SPESFQNYYL TASNGQSVPL SSVISMKLET QPTSLPRFSQ LNSAEISAVP MPGISSGDAI AWLQQQATDN LPQGYTFDFK SEARQLVQEG NALAVTFALA VIIIFLVLAI QFESIRDPMV IMISVPLAVS GALVSLNILS FFSIAGTTLN IYSQVGLITL VGLITKHGIL MCEVAKEEQL NHGKTRIEAI THAAKVRLRP ILMTTAAMVA GLIPLLYATG AGAVSRFSIG IVIVAGLSIG TIFTLFVLPV VYSYVATEHK PLPVFDENKT TH // ID Y907_HAEIN Reviewed; 104 AA. AC P44072; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_0907; GN OrderedLocusNames=HI_0907; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22569.1; -; Genomic_DNA. DR PIR; I64015; I64015. DR RefSeq; NP_439067.1; NC_000907.1. DR RefSeq; WP_005693258.1; NC_000907.1. DR STRING; 71421.HI0907; -. DR EnsemblBacteria; AAC22569; AAC22569; HI_0907. DR GeneID; 949909; -. DR KEGG; hin:HI0907; -. DR PATRIC; 20190469; VBIHaeInf48452_0948. DR eggNOG; COG4701; LUCA. DR OMA; MENKAER; -. DR OrthoDB; EOG6SZ1NZ; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR007922; DUF721/UPF0232. DR Pfam; PF05258; DUF721; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein HI_0907. FT /FTId=PRO_0000077972. SQ SEQUENCE 104 AA; 12030 MW; FD70906A29D80399 CRC64; MENKAERYQK AVNITDVLEQ SPFAKIIKKG LAINEINQKF NRIFPQEFHG KFRIGNMTDN SIFIETANAI VRQGILFRQT ELLKLIQEEF PQVTGFEITI NPGF // ID Y926_HAEIN Reviewed; 86 AA. AC P44076; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_0926; GN OrderedLocusNames=HI_0926; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22588.1; -; Genomic_DNA. DR PIR; D64016; D64016. DR RefSeq; NP_439086.1; NC_000907.1. DR RefSeq; WP_005693272.1; NC_000907.1. DR STRING; 71421.HI0926; -. DR EnsemblBacteria; AAC22588; AAC22588; HI_0926. DR GeneID; 949651; -. DR KEGG; hin:HI0926; -. DR PATRIC; 20190509; VBIHaeInf48452_0967. DR eggNOG; ENOG41063VX; Bacteria. DR eggNOG; COG4545; LUCA. DR OMA; CPDTEPF; -. DR OrthoDB; EOG6NGVZZ; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017167; UCP037291_glutaredoxin-rel. DR PIRSF; PIRSF037291; UCP037291_gluthr; 1. DR SUPFAM; SSF52833; SSF52833; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 86 Uncharacterized protein HI_0926. FT /FTId=PRO_0000077975. SQ SEQUENCE 86 AA; 9564 MW; 23D854A7643C42CC CRC64; MSKPILFYAE TCPDTAPFVA ELDRLGVDYD EVEIMTSLPN LKQFIRLRDS SAEFDNSKAN GYLGIPALLL PNGDVVLDLS KLKVIF // ID Y940_HAEIN Reviewed; 227 AA. AC P44081; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0940; GN OrderedLocusNames=HI_0940; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22604.1; -; Genomic_DNA. DR PIR; I64016; I64016. DR RefSeq; NP_439100.1; NC_000907.1. DR RefSeq; WP_010869091.1; NC_000907.1. DR STRING; 71421.HI0940; -. DR EnsemblBacteria; AAC22604; AAC22604; HI_0940. DR GeneID; 949941; -. DR KEGG; hin:HI0940; -. DR PATRIC; 20190537; VBIHaeInf48452_0981. DR OMA; CKHISST; -. DR OrthoDB; EOG62ZHT3; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR022543; DUF2572. DR Pfam; PF10833; DUF2572; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 227 Uncharacterized protein HI_0940. FT /FTId=PRO_0000077980. FT TRANSMEM 7 26 Helical. {ECO:0000255}. SQ SEQUENCE 227 AA; 25484 MW; 576A870A3160A275 CRC64; MTIQKGIITL TILIFISGLL TAFLLLDDSH LSFFRAQQNQ RKHYVERTLQ LQKMTATKKQ TACLDLPLNN NESVKQISIA LEGSTDAIQY FLWCERMSLF KKSPKKGDNQ GALKDFVTDE KLAYFRPHFS SPPRILNANK MPKLYWFSDS QAEVEINGTV SAVLIAEGDL KLTGKGRISG AVITSGNLTL DGVTLAYGKK TVVALVQQYS QWQLAEKSWS DFNVQDE // ID Y941_HAEIN Reviewed; 101 AA. AC P44082; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_0941; DE Flags: Precursor; GN OrderedLocusNames=HI_0941; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22605.1; -; Genomic_DNA. DR PIR; A64017; A64017. DR RefSeq; NP_439101.1; NC_000907.1. DR RefSeq; WP_010869092.1; NC_000907.1. DR STRING; 71421.HI0941; -. DR EnsemblBacteria; AAC22605; AAC22605; HI_0941. DR GeneID; 950292; -. DR KEGG; hin:HI0941; -. DR PATRIC; 20190539; VBIHaeInf48452_0982. DR KO; K02681; -. DR OMA; CENERII; -. DR OrthoDB; EOG6V4GG9; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020511; Uncharacterised_HI0941. DR ProDom; PD068240; Uncharacterised_HI0941; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 101 Uncharacterized protein HI_0941. FT /FTId=PRO_0000013961. SQ SEQUENCE 101 AA; 11830 MW; 58C475D1AB339CF4 CRC64; MILMFRMNKG MSFITLLFSL ALFSVLFLVF NQWTASQRKS TVKTYQDFQA IQVAENQAQR QFLGLACEQL IQQNGLTFRI QCENERIIVR YPTSEILIKT Q // ID Y974_HAEIN Reviewed; 368 AA. AC P44087; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_0974; GN OrderedLocusNames=HI_0974; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22642.1; -; Genomic_DNA. DR PIR; F64017; F64017. DR EnsemblBacteria; AAC22642; AAC22642; HI_0974. DR OMA; NEAAKDQ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 368 Uncharacterized protein HI_0974. FT /FTId=PRO_0000077985. FT TRANSMEM 7 23 Helical. {ECO:0000255}. SQ SEQUENCE 368 AA; 41886 MW; 979072CE13CD6891 CRC64; MSIQTKFILF LSSSLFLTPY SVATEKSPQP HDGRLDEQLH LAKPNLPQKT PALLTNNNPS KLSITKEELA KHPDLIIRGL IPAVLQNNGE AVQLLLPLYQ PLPKKDPFLL EWAEAIDLRE KGYFSDSVKA YRHLFSQKTD LLPLRYQLAQ ALFLNNDNEA AKDQFQKLRA EQVSSDSVKI IEQYLSALNQ RDQWKIQGGF SFLNESNINN APKAGTKIGN WTAWEKESAR GFSYFGNAEK KWSLPHNHFT KLSLEGSGKY YWDNKKYNEF NARAGVGLGY QTARFELSLM PFTEKRWYAG GSSGGNAMKQ YSKNSGARLD LSNWLNEKWQ ISTALEYGEQ RYETRKHLNG NNYLASATLL YLAKSGQY // ID Y559A_HAEIN Reviewed; 115 AA. AC O86226; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein HI_0559.1; GN OrderedLocusNames=HI_0559.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC22219.1; -; Genomic_DNA. DR RefSeq; NP_438717.1; NC_000907.1. DR RefSeq; WP_010869005.1; NC_000907.1. DR STRING; 71421.HI0559.1; -. DR EnsemblBacteria; AAC22219; AAC22219; HI_0559.1. DR GeneID; 949585; -. DR KEGG; hin:HI0559.1; -. DR PATRIC; 20189675; VBIHaeInf48452_0580. DR OMA; FWGWLTE; -. DR OrthoDB; EOG65XN3H; -. DR Proteomes; UP000000579; 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 HI_0559.1. FT /FTId=PRO_0000077934. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. SQ SEQUENCE 115 AA; 12826 MW; C01960F9E217DD1D CRC64; MKSYLKTLIF FPLILQIVVT ALLIWFDDDS SGVIVPFSSY ALTAFLLAAI PAFLTALLAA KFRYTRYNIA SIVLVSSIIS FVYCNMASYF YLLLLGEQDT SFWGWLTEGG LSLGL // ID Y597_HAEIN Reviewed; 272 AA. AC P44771; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative phosphatase HI_0597; DE EC=3.1.3.-; GN OrderedLocusNames=HI_0597; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22254.1; -; Genomic_DNA. DR PIR; D64155; D64155. DR RefSeq; NP_438754.1; NC_000907.1. DR RefSeq; WP_005694570.1; NC_000907.1. DR ProteinModelPortal; P44771; -. DR STRING; 71421.HI0597; -. DR DNASU; 950123; -. DR EnsemblBacteria; AAC22254; AAC22254; HI_0597. DR GeneID; 950123; -. DR KEGG; hin:HI0597; -. DR PATRIC; 20189751; VBIHaeInf48452_0618. DR eggNOG; ENOG4105DQF; Bacteria. DR eggNOG; COG0561; LUCA. DR KO; K07024; -. DR OMA; RHHVDVA; -. DR OrthoDB; EOG6K13W0; -. DR PhylomeDB; P44771; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0044283; P:small molecule biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR000150; Hypothet_cof. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR00099; Cof-subfamily; 1. DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1. DR PROSITE; PS01228; COF_1; 1. DR PROSITE; PS01229; COF_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 272 Putative phosphatase HI_0597. FT /FTId=PRO_0000054428. FT REGION 45 46 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 218 218 Magnesium. {ECO:0000250}. FT BINDING 12 12 Phosphate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 195 195 Phosphate. {ECO:0000250}. FT BINDING 221 221 Phosphate. {ECO:0000250}. SQ SEQUENCE 272 AA; 30523 MW; 5BC412A9B2892A52 CRC64; MNLPFRAMVS DLDGTLLTPE HLVGDLTIDT LRALEQKGVD IILATGRNHT DVSSILGKIG AERAVMITSN GARVRDLQGN LLYSNSLPEE LVLELYKTPF DTSKVCMNSY QDEGWFTNKD IPAMRQFHKE SGFDYNVVDF SKHHGRGTEK VFFIGKTPED LVEVETYLRD KFGDVTTIVY SALACLEVMN KNVSKGDALK HLLESREYEL KDCIAFGDGM NDVEMLSWAG KGCIMKDADI RLKMACPELE VIGSNKEESV ARYLRTQFGL DY // ID Y608_HAEIN Reviewed; 461 AA. AC Q57486; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Uncharacterized transporter HI_0608; GN OrderedLocusNames=HI_0608; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) CC family. NADC 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; L42023; AAC22267.1; -; Genomic_DNA. DR PIR; I64080; I64080. DR RefSeq; NP_438766.1; NC_000907.1. DR RefSeq; WP_010869019.1; NC_000907.1. DR STRING; 71421.HI0608; -. DR EnsemblBacteria; AAC22267; AAC22267; HI_0608. DR GeneID; 949996; -. DR KEGG; hin:HI0608; -. DR PATRIC; 20189795; VBIHaeInf48452_0632. DR eggNOG; ENOG4105C8P; Bacteria. DR eggNOG; COG0471; LUCA. DR KO; K14445; -. DR OMA; RTNFSIC; -. DR OrthoDB; EOG6GN72M; -. DR PhylomeDB; Q57486; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR InterPro; IPR001898; Na/sul_symport. DR InterPro; IPR031312; Na/sul_symport_CS. DR Pfam; PF00939; Na_sulph_symp; 1. DR TIGRFAMs; TIGR00785; dass; 1. DR PROSITE; PS01271; NA_SULFATE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 461 Uncharacterized transporter HI_0608. FT /FTId=PRO_0000172505. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 170 190 Helical. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TRANSMEM 256 276 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 349 369 Helical. {ECO:0000255}. FT TRANSMEM 377 397 Helical. {ECO:0000255}. FT TRANSMEM 399 419 Helical. {ECO:0000255}. FT TRANSMEM 439 459 Helical. {ECO:0000255}. SQ SEQUENCE 461 AA; 49762 MW; B5E6F6965B38EF06 CRC64; MGEMASLRSH KNGIIFILDI VLFFVLLNVL PFEPKANSGL ALLAFIAVLW LSEALHVTIT ALLVPLLAVA LGLVSTKQAL VGFADPTIFL FFGGFSLATA LHIQKLDKLI ANKIMALARG NLFIAVIYLF LITAFLSMWM SNTATAAMML PLAMGILSQL DREKDHNTYV FVLLGIAYSA SIGGMGTLVG SPPNAIVASN LNLTFSDWLW YGLPIMIILL PLMIGILYII FKPKLHLNFE QTFENIEMNP MRILTFIIFP VIALTWIFSG KINPFISGLL GLQKNIASFD SIVALLAAIV ICSTGVASWK QIQSNTDWGV LMLFGGGLTL SAVLKDSGAS KILADSIVFM IDGQHFYLIG LLVAAFIIFL TEFTSNTASA ALLVPIFISI AQSLGMPEIG LALIIGIGAS CAFMLPVATP PNAIVFGSGQ VKQSEMVKVG FLLNLVCVVV IATMGYMFWL K // ID Y666_HAEIN Reviewed; 106 AA. AC P44034; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein HI_0666; GN OrderedLocusNames=HI_0666; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22326.1; -; Genomic_DNA. DR PIR; G64011; G64011. DR RefSeq; NP_438825.1; NC_000907.1. DR RefSeq; WP_005672747.1; NC_000907.1. DR STRING; 71421.HI0666; -. DR EnsemblBacteria; AAC22326; AAC22326; HI_0666. DR GeneID; 949708; -. DR KEGG; hin:HI0666; -. DR PATRIC; 20189947; VBIHaeInf48452_0695. DR eggNOG; ENOG4105MHH; Bacteria. DR eggNOG; COG3550; LUCA. DR KO; K07154; -. DR OMA; LNNGENM; -. DR OrthoDB; EOG6ZSP44; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR017508; HipA_N1. DR Pfam; PF13657; Couple_hipA; 1. DR TIGRFAMs; TIGR03071; couple_hipA; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 106 Uncharacterized protein HI_0666. FT /FTId=PRO_0000077943. SQ SEQUENCE 106 AA; 12453 MW; 8F57014F866D9F3F CRC64; MRDLVRSGKV FLYGEFIGLL REDHRGFHFS YNPDYQGIPL SLSFPIEQSP FHSDTLFPYF ASLVPEGWLK HKYALHQRID ESDMFRFLLN NGENMLGAVQ IQEEKQ // ID Y731_HAEIN Reviewed; 127 AA. AC P44044; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 07-JAN-2015, entry version 62. DE RecName: Full=Uncharacterized protein HI_0731; GN OrderedLocusNames=HI_0731; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22392.1; -; Genomic_DNA. DR PIR; H64012; H64012. DR ProteinModelPortal; P44044; -. DR EnsemblBacteria; AAC22392; AAC22392; HI_0731. DR OMA; YNKPLHK; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR008972; Cupredoxin. DR Pfam; PF07731; Cu-oxidase_2; 1. DR SUPFAM; SSF49503; SSF49503; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 127 Uncharacterized protein HI_0731. FT /FTId=PRO_0000077951. SQ SEQUENCE 127 AA; 14566 MW; E0C7C7A88F2DE3C8 CRC64; MHQQYYNKPL HKLENNIDVT NGLINQRRFD PRKVDVMARK GTIERWILNA SLPVGFTIQG AKFVVESQGE HQLQAEELAW KDTVWVKNKT QILVKFDQAS SGNYPFLFGV SNLMLEDMGC LGVLMVQ // ID Y737_HAEIN Reviewed; 265 AA. AC O05031; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative uncharacterized protein HI_0737; GN OrderedLocusNames=HI_0737; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Truncated acetolactase synthase; no longer catalytically CC active. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22396.1; -; Genomic_DNA. DR PIR; F64089; F64089. DR RefSeq; NP_438896.1; NC_000907.1. DR RefSeq; WP_005693141.1; NC_000907.1. DR ProteinModelPortal; O05031; -. DR STRING; 71421.HI0737; -. DR EnsemblBacteria; AAC22396; AAC22396; HI_0737. DR GeneID; 949765; -. DR KEGG; hin:HI0737; -. DR PATRIC; 20190115; VBIHaeInf48452_0773. DR eggNOG; COG0028; LUCA. DR KO; K01652; -. DR OMA; FTYVENQ; -. DR OrthoDB; EOG6Z9B00; -. DR PhylomeDB; O05031; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52518; SSF52518; 2. PE 5: Uncertain; KW Complete proteome; Lyase; Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 265 Putative uncharacterized protein HI_0737. FT /FTId=PRO_0000090814. FT REGION 204 247 Thiamine pyrophosphate binding. FT BINDING 47 47 Thiamine pyrophosphate. {ECO:0000250}. SQ SEQUENCE 265 AA; 28784 MW; 79171AC8A5823144 CRC64; MTGAQLIMAC LKAHHVTTLF GYPGGAIMPT YDALYDAGLD HLLCRNEQGT AMAAIGYARS TGKVGVCIAT SGPGATNLVI GLGDAMMDSI PVVTITGQVA SPLIGTDAFQ EADVLGLSLA CTKHSFIVQS ADVALQGDLI QALNALKQDL DIEPWREQIR NFKAKLDFTY VENQGNRPID PWALLNSLSN RKPNNAIICT DVGQHQMWLV QHILRVARHC GFTVTTMEMT LIETQVRLKI TVKSDRTLDL LVNQLVKLPD VLMVN // ID Y762_HAEIN Reviewed; 226 AA. AC P44050; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein HI_0762; GN OrderedLocusNames=HI_0762; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22429.1; -; Genomic_DNA. DR PIR; E64013; E64013. DR RefSeq; NP_438921.1; NC_000907.1. DR RefSeq; WP_005693159.1; NC_000907.1. DR ProteinModelPortal; P44050; -. DR STRING; 71421.HI0762; -. DR EnsemblBacteria; AAC22429; AAC22429; HI_0762. DR GeneID; 949781; -. DR KEGG; hin:HI0762; -. DR PATRIC; 20190175; VBIHaeInf48452_0801. DR eggNOG; ENOG4108VVQ; Bacteria. DR eggNOG; COG0639; LUCA. DR OMA; GNHDTDS; -. DR OrthoDB; EOG6SNDR2; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 2. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR017056; P-Estase_HI0762_prd. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF036446; Phosphoesterase_HI0762_prd; 1. DR SUPFAM; SSF56300; SSF56300; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 226 Uncharacterized protein HI_0762. FT /FTId=PRO_0000077954. SQ SEQUENCE 226 AA; 26080 MW; 523F961745EE6F1A CRC64; MILFAGDPHG SYDHIYPFIK EQENVALIIL GDLQLTTSDE LDKLAKHCDI WFIHGNHDSK TISAFDSIWG SEWQSRNLHN RVVDIQGTRI AGLGGVFRGQ IWMPPNRPMF FDPIHYCQYS PQEKIWRGGV PLRHRTSIFP SDIEILENQQ ADVLICHEAP KPHPMGFQVI NDLAMKMGVK LVFHGHHHEN FTYRTKYPYK ITNVGFRSLA DAEGNYLLQT IDDREK // ID Y765_HAEIN Reviewed; 282 AA. AC Q57125; O05033; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Putative glycosyltransferase HI_0765; DE EC=2.-.-.-; GN OrderedLocusNames=HI_0765; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 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; L42023; AAC22423.1; -; Genomic_DNA. DR PIR; F64091; F64091. DR RefSeq; NP_438924.2; NC_000907.1. DR STRING; 71421.HI0765; -. DR EnsemblBacteria; AAC22423; AAC22423; HI_0765. DR GeneID; 950810; -. DR KEGG; hin:HI0765; -. DR PATRIC; 20190181; VBIHaeInf48452_0804. DR eggNOG; ENOG4105W1T; Bacteria. DR eggNOG; COG3306; LUCA. DR KO; K07270; -. DR OMA; INIFEDD; -. DR OrthoDB; EOG68Q0TQ; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 282 Putative glycosyltransferase HI_0765. FT /FTId=PRO_0000216242. SQ SEQUENCE 282 AA; 32482 MW; D962E402AA207A18 CRC64; MKISMIFLPH FLYYTVPTFY LFGLLIMHNA AQHNYVISLT TEQKRRKHIT EEFGKQNIPF EFFDAITPDI IEETAKKFNI TLDRSPKAKL SDGEIGCALS HIVLWDLALE NNLNYINIFE DDIHLGENAK ELLEIDYISD DIHVLKLEAN GKMFFKQPKS VKCDRNVYPM TVKQSGCAGY TVTAKGAKYL LELVKNKPLD VAVDSLVFED FLHFKDYKIV QLSPGICVQD FVLHPDNPFE SSLQEGRDRV HGNQRKSSIL EKIKNEFGRV KIKMFGKQVP FK // ID Y787_HAEIN Reviewed; 201 AA. AC P44052; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein HI_0787; GN OrderedLocusNames=HI_0787; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22463.1; -; Genomic_DNA. DR PIR; G64013; G64013. DR RefSeq; NP_438946.1; NC_000907.1. DR RefSeq; WP_010869053.1; NC_000907.1. DR STRING; 71421.HI0787; -. DR EnsemblBacteria; AAC22463; AAC22463; HI_0787. DR GeneID; 949801; -. DR KEGG; hin:HI0787; -. DR PATRIC; 20190225; VBIHaeInf48452_0826. DR eggNOG; ENOG4108W2W; Bacteria. DR eggNOG; ENOG4111IY5; LUCA. DR OMA; VEKMLMH; -. DR OrthoDB; EOG6RVFZW; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 201 Uncharacterized protein HI_0787. FT /FTId=PRO_0000077955. SQ SEQUENCE 201 AA; 23814 MW; BC4BF58FEC14DF96 CRC64; MKYILIHDLP YQEEEIGITE FYDENDLDTE ADIYDRETFG ILLGEYVTGL YLLDDTFIEP VLDNINIPNN VYSTNIFAIH YVAKHILGIK DLDKRLKSGD IELVRELGEV TIGGKEKYFY SFATKYCSHH NPIAFPIYDS YVEQVLLYFN KVDKFSAFKR KDLKNYRKFK EVLIDFQRFN LKELDLYLWL LGKEIFPKSK N // ID Y827_HAEIN Reviewed; 154 AA. AC P44886; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-APR-2016, entry version 96. DE RecName: Full=Uncharacterized acyl-CoA thioester hydrolase HI_0827; DE EC=3.1.2.-; GN OrderedLocusNames=HI_0827; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: Belongs to the acyl coenzyme A hydrolase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HotDog ACOT-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01106}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22485.1; -; Genomic_DNA. DR PIR; A64097; A64097. DR RefSeq; NP_438987.1; NC_000907.1. DR RefSeq; WP_005655643.1; NC_000907.1. DR PDB; 1YLI; X-ray; 1.95 A; A/B=2-154. DR PDB; 3BJK; X-ray; 1.90 A; A/B/C/D/E/F=2-154. DR PDBsum; 1YLI; -. DR PDBsum; 3BJK; -. DR ProteinModelPortal; P44886; -. DR SMR; P44886; 5-151. DR STRING; 71421.HI0827; -. DR EnsemblBacteria; AAC22485; AAC22485; HI_0827. DR GeneID; 949716; -. DR KEGG; hin:HI0827; -. DR PATRIC; 20190309; VBIHaeInf48452_0868. DR eggNOG; ENOG4105NAU; Bacteria. DR eggNOG; COG1607; LUCA. DR KO; K10806; -. DR OMA; VNVEVWV; -. DR OrthoDB; EOG676Z6F; -. DR PhylomeDB; P44886; -. DR BioCyc; RETL1328306-WGS:GSTH-2574-MONOMER; -. DR BRENDA; 3.1.2.20; 2529. DR EvolutionaryTrace; P44886; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR033120; HOTDOG_ACOT. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR006683; Thioestr_dom. DR Pfam; PF03061; 4HBT; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR PROSITE; PS51770; HOTDOG_ACOT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 154 Uncharacterized acyl-CoA thioester FT hydrolase HI_0827. FT /FTId=PRO_0000053822. FT DOMAIN 13 128 HotDog ACOT-type. {ECO:0000255|PROSITE- FT ProRule:PRU01106}. FT STRAND 15 22 {ECO:0000244|PDB:3BJK}. FT HELIX 25 27 {ECO:0000244|PDB:3BJK}. FT STRAND 32 34 {ECO:0000244|PDB:3BJK}. FT HELIX 36 55 {ECO:0000244|PDB:3BJK}. FT STRAND 59 69 {ECO:0000244|PDB:3BJK}. FT STRAND 78 88 {ECO:0000244|PDB:3BJK}. FT STRAND 90 102 {ECO:0000244|PDB:3BJK}. FT STRAND 104 108 {ECO:0000244|PDB:3BJK}. FT STRAND 112 125 {ECO:0000244|PDB:3BJK}. FT HELIX 140 149 {ECO:0000244|PDB:3BJK}. SQ SEQUENCE 154 AA; 16763 MW; FF750B2818DFC1DD CRC64; MSANFTDKNG RQSKGVLLLR TLAMPSDTNA NGDIFGGWIM SQMDMGGAIL AKEIAHGRVV TVAVESMNFI KPISVGDVVC CYGQCLKVGR SSIKIKVEVW VKKVASEPIG ERYCVTDAVF TFVAVDNNGR SRTIPRENNQ ELEKALALIS EQPL // ID Y866_HAEIN Reviewed; 207 AA. AC P44063; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized protein HI_0866; GN OrderedLocusNames=HI_0866; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP SEQUENCE REVISION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. 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; L42023; AAC22527.1; -; Genomic_DNA. DR PIR; I64014; I64014. DR RefSeq; NP_439026.1; NC_000907.1. DR RefSeq; WP_005693214.1; NC_000907.1. DR ProteinModelPortal; P44063; -. DR STRING; 71421.HI0866; -. DR EnsemblBacteria; AAC22527; AAC22527; HI_0866. DR GeneID; 950756; -. DR KEGG; hin:HI0866; -. DR PATRIC; 20190387; VBIHaeInf48452_0907. DR eggNOG; COG3765; LUCA. DR OMA; TEYVNFV; -. DR OrthoDB; EOG6SR8ZM; -. DR PhylomeDB; P44063; -. DR Proteomes; UP000000579; 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 1 207 Uncharacterized protein HI_0866. FT /FTId=PRO_0000077962. FT TRANSMEM 177 197 Helical. {ECO:0000255}. SQ SEQUENCE 207 AA; 23656 MW; E398FC0CB7217455 CRC64; MDKIALKITF SAETPKYAQS VLTEYVNFVS QYSLNQTNQE FKQGFNLRLD ELRFSKEQIE ENLTEEKKVQ VENLTNALDI AKKAGIKDFS RGNNISDSKL ADGTYLFILA EKYLQAQLDI AKNTPVVYPA NYYITDRQLF KLNKLASQLE LVEDVKTYYY LSSPDYPVVK DNPKRSLILA IGFIIGILLP TFFILLGSVI QTNKKQS // ID Y870A_HAEIN Reviewed; 96 AA. AC O86229; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-JAN-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_0870.1; GN OrderedLocusNames=HI_0870.1; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION. RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J., RA Hickey E., Dodson R., Gwinn M.; RL Submitted (MAY-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; L42023; AAC22539.1; -; Genomic_DNA. DR EnsemblBacteria; AAC22539; AAC22539; HI_0870.1. DR Proteomes; UP000000579; 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 96 Uncharacterized protein HI_0870.1. FT /FTId=PRO_0000077965. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. SQ SEQUENCE 96 AA; 11429 MW; 1A0FF09659E11150 CRC64; MVLYFYNKIN RSFGLMILLY FFRSGGLAFR ISELFLIFSI PLFALLINEL SGVNRVLMFF ILVYYISIVF LRRIYVHVVF GVNTFLPYKP IFDSYL // ID Y908_HAEIN Reviewed; 100 AA. AC P44073; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein HI_0908; GN OrderedLocusNames=HI_0908; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22570.1; -; Genomic_DNA. DR PIR; A64016; A64016. DR RefSeq; NP_439068.1; NC_000907.1. DR RefSeq; WP_005655841.1; NC_000907.1. DR STRING; 71421.HI0908; -. DR EnsemblBacteria; AAC22570; AAC22570; HI_0908. DR GeneID; 949910; -. DR KEGG; hin:HI0908; -. DR PATRIC; 20190471; VBIHaeInf48452_0949. DR OMA; TEKQPKI; -. DR OrthoDB; EOG60GRZ1; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR020508; DUF2547. DR Pfam; PF10818; DUF2547; 1. DR ProDom; PD067723; Uncharacterised_HI0908; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein HI_0908. FT /FTId=PRO_0000077973. SQ SEQUENCE 100 AA; 11176 MW; 21C9EAD4BB31A50E CRC64; MISGTVKPNF WSRLLLSIIA IFALPNAQSF ENQNNTENYS SSVSIQQALE TVKVAREVQR QAIPQPSISR QTEKQLKIQP HFFTEALNIS APIRAGPLLI // ID Y912_HAEIN Reviewed; 254 AA. AC P44074; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein HI_0912; GN OrderedLocusNames=HI_0912; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22579.1; -; Genomic_DNA. DR PIR; B64016; B64016. DR RefSeq; NP_439072.1; NC_000907.1. DR RefSeq; WP_005666039.1; NC_000907.1. DR ProteinModelPortal; P44074; -. DR STRING; 71421.HI0912; -. DR EnsemblBacteria; AAC22579; AAC22579; HI_0912. DR GeneID; 950836; -. DR KEGG; hin:HI0912; -. DR PATRIC; 20190479; VBIHaeInf48452_0953. DR eggNOG; ENOG4105DMQ; Bacteria. DR eggNOG; COG0500; LUCA. DR OMA; EKERPMI; -. DR OrthoDB; EOG6MD96P; -. DR PhylomeDB; P44074; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 254 Uncharacterized protein HI_0912. FT /FTId=PRO_0000077974. SQ SEQUENCE 254 AA; 29739 MW; 9C0335171830F7D3 CRC64; MNNKISVYDK DNFFELYQKL RANPISLNEI IEKPTMLSLL PNLKGKKLLD LGCGTGGHLQ LYLERGAAKV IGTDLSEKML EQAEKDLQKC GQFSGRFSLY HLPIEKLAEL PESHFDVITS SFAFHYIENF PTLLSTIHDK LSSNGTLIFS QEHPITTCHK EGERWEKNDK KQQVAYRLNH YREEGKRNRN WFKQPFQTYH RTTATIINNL IHARFQIEQM EEPMLADQPQ WHNEFKDLSH RPPLLFIKAR KVEK // ID Y960_HAEIN Reviewed; 116 AA. AC P44084; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein HI_0960; DE Flags: Precursor; GN OrderedLocusNames=HI_0960; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22628.1; -; Genomic_DNA. DR PIR; C64017; C64017. DR RefSeq; NP_439121.1; NC_000907.1. DR RefSeq; WP_005647993.1; NC_000907.1. DR ProteinModelPortal; P44084; -. DR STRING; 71421.HI0960; -. DR EnsemblBacteria; AAC22628; AAC22628; HI_0960. DR GeneID; 950757; -. DR KEGG; hin:HI0960; -. DR PATRIC; 20190579; VBIHaeInf48452_1002. DR eggNOG; COG5633; LUCA. DR OMA; VNYRLYL; -. DR OrthoDB; EOG6ZWJJ0; -. DR Proteomes; UP000000579; Chromosome. DR InterPro; IPR010824; DUF1425. DR Pfam; PF07233; DUF1425; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 15 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 16 116 Uncharacterized protein HI_0960. FT /FTId=PRO_0000013962. SQ SEQUENCE 116 AA; 13499 MW; 97214FD32CE8C25F CRC64; MKKYFLILAS FMLVACSSSE QNLTYSTKPI LNITSSLSPL IQVETTQKSA VIKNKSQQLL NISYHLYWYD HLGVTQIWEN QQESYSAQFL LKPQEQKSID LTKPTVESKN YRLYLK // ID Y967_HAEIN Reviewed; 34 AA. AC P44086; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAY-2015, entry version 58. DE RecName: Full=Uncharacterized protein HI_0967; GN OrderedLocusNames=HI_0967; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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; L42023; AAC22630.1; -; Genomic_DNA. DR PIR; E64017; E64017. DR RefSeq; NP_439128.1; NC_000907.1. DR RefSeq; WP_005655951.1; NC_000907.1. DR EnsemblBacteria; AAC22630; AAC22630; HI_0967. DR GeneID; 949914; -. DR KEGG; hin:HI0967; -. DR OrthoDB; EOG6BCT2T; -. DR Proteomes; UP000000579; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 34 Uncharacterized protein HI_0967. FT /FTId=PRO_0000077983. SQ SEQUENCE 34 AA; 4090 MW; C3C5FBCD5E99756A CRC64; MQNSSNIFTT DKAANEFSFP DLKNFRYNDR TFLR // ID Y841_HAEIN Reviewed; 585 AA. AC P44898; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 92. DE RecName: Full=Uncharacterized protein HI_0841; GN OrderedLocusNames=HI_0841; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SIMILARITY: To E.coli YejM. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22500.1; -; Genomic_DNA. DR PIR; F64159; F64159. DR RefSeq; NP_439001.1; NC_000907.1. DR RefSeq; WP_005693193.1; NC_000907.1. DR ProteinModelPortal; P44898; -. DR STRING; 71421.HI0841; -. DR EnsemblBacteria; AAC22500; AAC22500; HI_0841. DR GeneID; 949855; -. DR KEGG; hin:HI0841; -. DR PATRIC; 20190337; VBIHaeInf48452_0882. DR eggNOG; ENOG4105E68; Bacteria. DR eggNOG; COG3083; LUCA. DR KO; K07014; -. DR OMA; YAFIIDW; -. DR OrthoDB; EOG61KBCH; -. DR PhylomeDB; P44898; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR000917; Sulfatase_N. DR InterPro; IPR024588; YejM_N. DR Pfam; PF11893; DUF3413; 1. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 585 Uncharacterized protein HI_0841. FT /FTId=PRO_0000169170. SQ SEQUENCE 585 AA; 67738 MW; 246C00BAA7BC7935 CRC64; MKWIKKGTFS GKQYRDDVSR KISWGHWFAF FNIIVAIFIG ARYAFIIDWP DTLAGKLYFF VSLLGHFSFN VFALYLLVVF PLSFIVKNHR TFRGLTVIFS TICTTLLLFD TAVFNRFNLH LSSVVWNLLV NPENGEMSRD WQIFFAPMPI ILLAQMLFSR WSWEKLRSLE RQKWLKGTGI FLTTTFIATH LIYAWADAYL YRPITMQRSN FPLSYPMTAR SFLEKHGFLD GEEYTQKLAQ EGRLDALKID YPKKELTYAP ITHKPNILLV TVSGLRHDAI SNEKMPKLAK FATSSTEFTN HYSTGNSNNA GLIGLFYGLN ANYTDSILSN HTQSVLIEKL RAENYQLGLF SATNFKDSIF RQALFREIKL SSNKTNKPNN ESAVKNLNDF IKAQKTDSPW FAYLDLALEA KNPSDYDRTL QDIDSLLAKA LESTPLENTL VIITSEHGLT FNEMNQKERE NYFGRDEIQV PLLVYWKDLP VGKQNGLSNH ADIFSALMQT VFRVENPLMD YSQGRNLFDL KGDDWVLASN FRWNVVIQPD GTQYHIDRKG NYKKFDKDYI EQSSDRPPLG IFLEAFQLQN FFFEK // ID Y850_HAEIN Reviewed; 144 AA. AC P44060; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein HI_0850; GN OrderedLocusNames=HI_0850; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RseC 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; L42023; AAC22507.1; -; Genomic_DNA. DR PIR; F64014; F64014. DR RefSeq; NP_439010.1; NC_000907.1. DR RefSeq; WP_005670174.1; NC_000907.1. DR STRING; 71421.HI0850; -. DR EnsemblBacteria; AAC22507; AAC22507; HI_0850. DR GeneID; 949863; -. DR KEGG; hin:HI0850; -. DR PATRIC; 20190355; VBIHaeInf48452_0891. DR eggNOG; ENOG4105WMJ; Bacteria. DR eggNOG; COG3086; LUCA. DR KO; K03803; -. DR OMA; GCGSCQA; -. DR OrthoDB; EOG6GBMHX; -. DR PhylomeDB; P44060; -. DR Proteomes; UP000000579; 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; IPR026268; RseC. DR InterPro; IPR007359; SigmaE_reg_RseC_MucC. DR Pfam; PF04246; RseC_MucC; 1. DR PIRSF; PIRSF004923; RseC; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 144 Uncharacterized protein HI_0850. FT /FTId=PRO_0000077960. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. SQ SEQUENCE 144 AA; 15842 MW; 564FC10BDE2CA4BD CRC64; MLRESAVVIS YENGIAKVKC QSQSACGQCA AKNSCGTSSL SELNGKRGEH IFNVETLMPL REGQIVEIGL EEKSMLLSAL LMYVVPLLTL LIVTMLSDYI SDNEILRAIL IFGLTALSFI LVKSYSRKLG QQTEFQPVLL RVLS // ID Y854_HAEIN Reviewed; 253 AA. AC P44061; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized protein HI_0854; GN OrderedLocusNames=HI_0854; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22513.1; -; Genomic_DNA. DR PIR; G64014; G64014. DR RefSeq; NP_439014.1; NC_000907.1. DR RefSeq; WP_005693201.1; NC_000907.1. DR ProteinModelPortal; P44061; -. DR STRING; 71421.HI0854; -. DR EnsemblBacteria; AAC22513; AAC22513; HI_0854. DR GeneID; 949867; -. DR KEGG; hin:HI0854; -. DR PATRIC; 20190363; VBIHaeInf48452_0895. DR eggNOG; ENOG4108WHG; Bacteria. DR eggNOG; COG0748; LUCA. DR KO; K07226; -. DR OMA; NNPHNVE; -. DR OrthoDB; EOG6CVVBS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:InterPro. DR Gene3D; 2.30.110.10; -; 1. DR Gene3D; 3.20.180.10; -; 1. DR InterPro; IPR019595; DUF2470. DR InterPro; IPR026324; Haem_oxygenase_HugZ. DR InterPro; IPR011576; Pyridox_Oxase_FMN-bd. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR Pfam; PF10615; DUF2470; 1. DR Pfam; PF01243; Pyridox_oxidase; 1. DR SUPFAM; SSF50475; SSF50475; 2. DR TIGRFAMs; TIGR04109; heme_ox_HugZ; 1. PE 1: Evidence at protein level; KW Complete proteome; Reference proteome. FT CHAIN 1 253 Uncharacterized protein HI_0854. FT /FTId=PRO_0000077961. SQ SEQUENCE 253 AA; 28840 MW; D76B49B662C5EA10 CRC64; MDFNRIITHM NDHHQDDMAV LCKKFGGEKE ITDVTLVNVD FAGLDFKYNG GKTLRVEFPQ QADAGSIKQV IINLCVENKP VANYDRIKAK IDEFRQEFKS CVLSTLDKDG LPMASYAPII FFDGKYYIYI SAIAEHYENL KRNPNQVEVM FLEDENKAKS IIVRTRLRYK ASARFIPRED PIVEKVLDKL AETMNDVGGI KTIREFTDFD LVELTFGTGR FVRGFGQAYL IDANGEISHI GVKGNPHEKE SDK // ID Y883_HAEIN Reviewed; 456 AA. AC P44917; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Uncharacterized transporter HI_0883; GN OrderedLocusNames=HI_0883; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the sodium:alanine (SAF) symporter 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; L42023; AAC22541.1; -; Genomic_DNA. DR PIR; H64099; H64099. DR RefSeq; NP_439044.1; NC_000907.1. DR RefSeq; WP_005666065.1; NC_000907.1. DR STRING; 71421.HI0883; -. DR EnsemblBacteria; AAC22541; AAC22541; HI_0883. DR GeneID; 949887; -. DR KEGG; hin:HI0883; -. DR PATRIC; 20190423; VBIHaeInf48452_0925. DR eggNOG; ENOG4105BZG; Bacteria. DR eggNOG; COG1115; LUCA. DR KO; K03310; -. DR OMA; AFLHLDM; -. DR OrthoDB; EOG6D2KVD; -. DR PhylomeDB; P44917; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR30330; PTHR30330; 1. DR Pfam; PF01235; Na_Ala_symp; 1. DR PRINTS; PR00175; NAALASMPORT. DR TIGRFAMs; TIGR00835; agcS; 1. DR PROSITE; PS00873; NA_ALANINE_SYMP; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 456 Uncharacterized transporter HI_0883. FT /FTId=PRO_0000161569. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. FT TRANSMEM 305 325 Helical. {ECO:0000255}. FT TRANSMEM 348 368 Helical. {ECO:0000255}. FT TRANSMEM 390 410 Helical. {ECO:0000255}. FT TRANSMEM 414 434 Helical. {ECO:0000255}. SQ SEQUENCE 456 AA; 48827 MW; 69FA3254805DF27A CRC64; MTIESILSAI DSFIWGAPLL ILLSGTGLYL TLRLGFIQIR YLPRALGYLF KKDKGGKGDV SSFAALCTAL AATIGTGNIV GVATAVQAGG PGAIFWMWLV ALLGMATKYA ECLLAVKYRV RDKNGFMAGG PMYYIERGLG IRWLAKLFAL FGVMVAFFGI GTFPQVNAIT HAMQDTFNIP VLVTAIIVTL LVGLIILGGV KRIATASSVI VPFMAILYVT TSLVIILLNI EKVPDAILLI IDSAFDPQAA LGGAVGLTVM KAIQSGVARG IFSNESGLGS APIAAAAAQT REPVRQGLIS MTGTFLDTII VCTMTGIVLV LTGAWNNPEL AGATVTNYAF AQGLGTSIGA TIVTVGLLFF AFTTILGWCY YGERCFVYLV GIRGVKLYRL AYIMLVGLGA FLHLNLIWII ADIVNGLMAF PNLIALIGLR KVIIEETKDY FQRLKINHYD QDEVIK // ID Y977_HAEIN Reviewed; 191 AA. AC P44088; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Probable adenosine monophosphate-protein transferase HI_0977; DE EC=2.7.7.n1; GN OrderedLocusNames=HI_0977; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Probable adenylyltransferase that mediates the addition CC of adenosine 5'-monophosphate (AMP) to specific residues of target CC proteins. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + [protein] = diphosphate + [protein]-AMP. CC -!- SIMILARITY: Belongs to the fic family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 fido domain. {ECO:0000255|PROSITE- CC ProRule:PRU00791}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22637.1; -; Genomic_DNA. DR PIR; G64017; G64017. DR RefSeq; NP_439140.1; NC_000907.1. DR RefSeq; WP_005690872.1; NC_000907.1. DR ProteinModelPortal; P44088; -. DR SMR; P44088; 11-187. DR STRING; 71421.HI0977; -. DR DNASU; 949973; -. DR EnsemblBacteria; AAC22637; AAC22637; HI_0977. DR GeneID; 949973; -. DR KEGG; hin:HI0977; -. DR PATRIC; 20190615; VBIHaeInf48452_1020. DR eggNOG; ENOG4105MZU; Bacteria. DR eggNOG; COG2184; LUCA. DR KO; K04095; -. DR OMA; REQNISK; -. DR OrthoDB; EOG69976Q; -. DR PhylomeDB; P44088; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.3290.10; -; 1. DR InterPro; IPR003812; Fido. DR Pfam; PF02661; Fic; 1. DR SUPFAM; SSF140931; SSF140931; 1. DR PROSITE; PS51459; FIDO; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 191 Probable adenosine monophosphate-protein FT transferase HI_0977. FT /FTId=PRO_0000077987. FT DOMAIN 37 162 Fido. {ECO:0000255|PROSITE- FT ProRule:PRU00791}. FT NP_BIND 67 68 ATP. {ECO:0000250}. FT NP_BIND 112 114 ATP. {ECO:0000250}. FT BINDING 118 118 ATP. {ECO:0000250}. FT BINDING 145 145 ATP. {ECO:0000250}. SQ SEQUENCE 191 AA; 22541 MW; 5C327D09F6D2E93E CRC64; MPPKFWIIII VKKIDQQSLE NAYRLFESGD IHQIEIGSTK GLQQIHHYLF NGLYEFAGKI REQNISKGHF RFANALYLKE ALGKIEQMPE DTFENIINKY VEMNIAHPFL EGNGRSTRIW LDLVLKKHLG KVVNWQNVDK TQYLQAMERS PINDLEIRFL LQANLTDDVN NREIIFKGIE QSYYYEGYEK E // ID YIHI_HAEIN Reviewed; 186 AA. AC P44844; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Der GTPase-activating protein YihI {ECO:0000255|HAMAP-Rule:MF_01058}; GN Name=yihI {ECO:0000255|HAMAP-Rule:MF_01058}; GN OrderedLocusNames=HI_0724; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: A GTPase-activating protein (GAP) that modifies Der/EngA CC GTPase function. May play a role in ribosome biogenesis. CC {ECO:0000255|HAMAP-Rule:MF_01058}. CC -!- SUBUNIT: Interacts with Der. {ECO:0000255|HAMAP-Rule:MF_01058}. CC -!- SIMILARITY: Belongs to the YihI family. {ECO:0000255|HAMAP- CC Rule:MF_01058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22382.1; -; Genomic_DNA. DR PIR; F64157; F64157. DR RefSeq; NP_438882.1; NC_000907.1. DR RefSeq; WP_005693127.1; NC_000907.1. DR STRING; 71421.HI0724; -. DR EnsemblBacteria; AAC22382; AAC22382; HI_0724. DR GeneID; 949751; -. DR KEGG; hin:HI0724; -. DR PATRIC; 20190081; VBIHaeInf48452_0756. DR eggNOG; ENOG4105ZR3; Bacteria. DR eggNOG; COG3078; LUCA. DR KO; K09894; -. DR OMA; ENNECLN; -. DR OrthoDB; EOG615VKS; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR HAMAP; MF_01058; GAP_YihI; 1. DR InterPro; IPR007336; Der_GTPase_activator. DR Pfam; PF04220; YihI; 1. PE 3: Inferred from homology; KW Complete proteome; GTPase activation; Reference proteome; KW Ribosome biogenesis. FT CHAIN 1 186 Der GTPase-activating protein YihI. FT /FTId=PRO_0000209586. SQ SEQUENCE 186 AA; 21538 MW; 0A56B3F59DF8EF8E CRC64; MARKKKTRRI TDIMPIRKAD KKIDITKARS GKKLTCYELD AKAREDKKKR KHKGLASGSR HSAVEEKANK LQNEIKDPKI GSKKKIPLVV EFVNKPEKGQ VIPVIKQVKK QDPMKELENL ENNEILNELL DALDAGKTIS KSDQQFVDEC LDRISELMEE LGIEDEDESE DDLYRTFERM DINQFR // ID YBGC_HAEIN Reviewed; 136 AA. AC P44679; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=Acyl-CoA thioesterase YbgC; DE EC=3.1.2.-; GN Name=ybgC; OrderedLocusNames=HI_0386; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP FUNCTION, MUTAGENESIS OF ASP-18, ACTIVE SITE, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=11959124; DOI=10.1016/S0014-5793(02)02533-4; RA Zhuang Z., Song F., Martin B.M., Dunaway-Mariano D.; RT "The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster RT of Haemophilus influenzae catalyzes acyl-coenzyme A thioester RT hydrolysis."; RL FEBS Lett. 516:161-163(2002). CC -!- FUNCTION: Displays acyl-CoA thioesterase activity with short chain CC aliphatic acyl-CoA thioesters, such as propionyl-CoA and butyryl- CC CoA. Enzyme activity is relatively low, suggesting that the acyl- CC CoA thioesters used in the assays are not the physiological CC substrates. Has no detectable activity with 4-hydroxybenzoyl-CoA, CC lauroyl-CoA (C12:0), arachidoyl-CoA (C20:0) and arachidonoyl-CoA CC (C20:4). {ECO:0000269|PubMed:11959124}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11 mM for propionyl-CoA {ECO:0000269|PubMed:11959124}; CC KM=16 mM for iso-butyryl-CoA {ECO:0000269|PubMed:11959124}; CC KM=24 mM for n-butyryl-CoA {ECO:0000269|PubMed:11959124}; CC KM=20 mM for D,L-beta-hydroxybutyryl-CoA CC {ECO:0000269|PubMed:11959124}; CC Note=Kcat is 0.44 sec(-1) with propionyl-CoA, 0.54 sec(-1) with CC iso-butyryl-CoA and 0.17 sec(-1) with n-butyryl-CoA.; CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase 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; L42023; AAC22044.1; -; Genomic_DNA. DR PIR; H64150; H64150. DR RefSeq; NP_438547.1; NC_000907.1. DR RefSeq; WP_005693784.1; NC_000907.1. DR ProteinModelPortal; P44679; -. DR STRING; 71421.HI0386; -. DR EnsemblBacteria; AAC22044; AAC22044; HI_0386. DR GeneID; 950554; -. DR KEGG; hin:HI0386; -. DR PATRIC; 20189321; VBIHaeInf48452_0404. DR eggNOG; ENOG4107YD3; Bacteria. DR eggNOG; COG0824; LUCA. DR KO; K07107; -. DR OMA; ELGFAQS; -. DR OrthoDB; EOG6JQH7N; -. DR PhylomeDB; P44679; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:InterPro. DR Gene3D; 3.10.129.10; -; 1. DR InterPro; IPR008272; HB-CoA_thioesterase_AS. DR InterPro; IPR029069; HotDog_dom. DR InterPro; IPR006683; Thioestr_dom. DR InterPro; IPR014166; Tol-Pal_acyl-CoA_thioesterase. DR InterPro; IPR006684; YbgC/YbaW. DR Pfam; PF03061; 4HBT; 1. DR PIRSF; PIRSF003230; YbgC; 1. DR SUPFAM; SSF54637; SSF54637; 1. DR TIGRFAMs; TIGR02799; thio_ybgC; 1. DR TIGRFAMs; TIGR00051; TIGR00051; 1. DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 136 Acyl-CoA thioesterase YbgC. FT /FTId=PRO_0000087766. FT ACT_SITE 18 18 {ECO:0000255|PROSITE-ProRule:PRU10041, FT ECO:0000269|PubMed:11959124}. FT MUTAGEN 18 18 D->N: Abolishes enzyme activity. FT {ECO:0000269|PubMed:11959124}. SQ SEQUENCE 136 AA; 15597 MW; E1D5D2E3F800B261 CRC64; MLDNGFSFPV RVYYEDTDAG GVVYHARYLH FFERARTEYL RTLNFTQQTL LEEQQLAFVV KTLAIDYCVA AKLDDLLMVE TEVSEVKGAT ILFEQRLMRN TLMLSKATVK VACVDLGKMK PVAFPKEVKA AFHHLK // ID YIDC_HAEIN Reviewed; 541 AA. AC P44973; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=Membrane protein insertase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Foldase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane integrase YidC {ECO:0000255|HAMAP-Rule:MF_01810}; DE AltName: Full=Membrane protein YidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN Name=yidC {ECO:0000255|HAMAP-Rule:MF_01810}; GN OrderedLocusNames=HI_1001; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(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. {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBUNIT: Interacts with the Sec translocase complex via SecD. CC Specifically interacts with transmembrane segments of nascent CC integral membrane proteins during membrane integration. CC {ECO:0000255|HAMAP-Rule:MF_01810}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01810}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01810}. CC -!- SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01810}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22663.1; -; Genomic_DNA. DR PIR; H64163; H64163. DR RefSeq; NP_439163.1; NC_000907.1. DR RefSeq; WP_005693342.1; NC_000907.1. DR ProteinModelPortal; P44973; -. DR STRING; 71421.HI1001; -. DR DNASU; 949995; -. DR EnsemblBacteria; AAC22663; AAC22663; HI_1001. DR GeneID; 949995; -. DR KEGG; hin:HI1001; -. DR PATRIC; 20190663; VBIHaeInf48452_1044. DR eggNOG; ENOG4105DHW; Bacteria. DR eggNOG; COG0706; LUCA. DR KO; K03217; -. DR OMA; TGPKLQN; -. DR OrthoDB; EOG6X6RF2; -. DR PhylomeDB; P44973; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051205; P:protein insertion into membrane; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR HAMAP; MF_01810; YidC_type1; 1. DR InterPro; IPR019998; Membr_insert_YidC. DR InterPro; IPR028055; Membr_insert_YidC/Oxa1_C. DR InterPro; IPR028053; Membr_insert_YidC_N. DR InterPro; IPR001708; Membrane_insert_OXA1/ALB3/YidC. DR PANTHER; PTHR12428; PTHR12428; 1. DR Pfam; PF02096; 60KD_IMP; 1. DR Pfam; PF14849; YidC_periplas; 1. DR PRINTS; PR00701; 60KDINNERMP. DR PRINTS; PR01900; YIDCPROTEIN. DR TIGRFAMs; TIGR03593; yidC_nterm; 1. DR TIGRFAMs; TIGR03592; yidC_oxa1_cterm; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Chaperone; Complete proteome; KW Membrane; Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 541 Membrane protein insertase YidC. FT /FTId=PRO_0000124716. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 337 357 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 416 436 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 454 474 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. FT TRANSMEM 495 515 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01810}. SQ SEQUENCE 541 AA; 61240 MW; 9406398B334F4EDE CRC64; MDSRRSLLVL ALIFISFLVY QQWQLDKNPP VQTEQTTSIT ATSDVPASSP SNSQAIADSQ TRGRIITLEN DVFRLKIDTL GGDVISSELL KYDAELDSKT PFELLKDTKE HIYIAQSGLI GKNGIDTRSG RAQYQIEGDN FKLAEGQESL SVPLLFEKDG VTYQKIFVLK RGSYDLGVDY KIDNQSGQAI EVEPYGQLKH SIVESSGNVA MPTYTGGAYS SSETNYKKYS FSDMQDNNLS IDTKAGWVAV LQHYFVSAWI PNQDVNNQLY TITDSKNNVA SIGYRGSVVT IPAGSQETIT SSLWTGPKLQ NQMATVANNL DLTVDYGWAW FIAKPLFWLL TFIQGIVSNW GLAIICVTIV VKAILYPLTK AQYTSMAKMR ILQPKMQEMR ERFGDDRQRM SQEMMKLYKE EKVNPLGGCL PILLQMPIFI ALYWTFLEAV ELRHAPFFGW IQDLSAQDPY YILPILMGIS MFLLQKMSPT PVTDPTQQKV MNFMPLVFMF FFLWFPSGLV LYWLVSNLIT IAQQQLIYRG LEKKGLHSRK K // ID YCHF_HAEIN Reviewed; 363 AA. AC P44681; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-NOV-2015, entry version 123. DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000255|HAMAP-Rule:MF_00944}; GN Name=ychF {ECO:0000255|HAMAP-Rule:MF_00944}; Synonyms=engD; GN OrderedLocusNames=HI_0393; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DOMAIN. RX PubMed=12837776; DOI=10.1128/JB.185.14.4031-4037.2003; RA Teplyakov A., Obmolova G., Chu S.Y., Toedt J., Eisenstein E., RA Howard A.J., Gilliland G.L.; RT "Crystal structure of the YchF protein reveals binding sites for GTP RT and nucleic acid."; RL J. Bacteriol. 185:4031-4037(2003). RN [4] RP FUNCTION, AND ATPASE ACTIVITY. RX PubMed=17430889; DOI=10.1074/jbc.M700541200; RA Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., RA Kostrewa D., Kutay U., Kambach C.; RT "Human OLA1 defines an ATPase subfamily in the Obg family of GTP- RT binding proteins."; RL J. Biol. Chem. 282:19928-19937(2007). CC -!- FUNCTION: ATPase that binds to both the 70S ribosome and the 50S CC ribosomal subunit in a nucleotide-independent manner (By CC similarity). Does not hydrolyze GTP. {ECO:0000255|HAMAP- CC Rule:MF_00944, ECO:0000269|PubMed:17430889}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- DOMAIN: Composed of 3 distinct structural domains: the N-terminal CC domain, which has a mononucleotide binding fold typical for the P- CC loop NTPases, followed by a pronounced alpha-helical coiled coil CC domain and the C-terminal domain, which may be involved in RNA CC binding. {ECO:0000269|PubMed:12837776}. CC -!- MASS SPECTROMETRY: Mass=40011; Method=MALDI; Range=2-363; CC Evidence={ECO:0000269|PubMed:10675023}; 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; L42023; AAC22052.1; -; Genomic_DNA. DR PIR; I64150; I64150. DR RefSeq; NP_438555.1; NC_000907.1. DR RefSeq; WP_005693776.1; NC_000907.1. DR PDB; 1JAL; X-ray; 2.40 A; A/B=1-363. DR PDBsum; 1JAL; -. DR ProteinModelPortal; P44681; -. DR SMR; P44681; 1-363. DR STRING; 71421.HI0393; -. DR EnsemblBacteria; AAC22052; AAC22052; HI_0393. DR GeneID; 949492; -. DR KEGG; hin:HI0393; -. DR PATRIC; 20189337; VBIHaeInf48452_0412. DR eggNOG; ENOG4105C3G; Bacteria. DR eggNOG; COG0012; LUCA. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR PhylomeDB; P44681; -. DR BioCyc; RETL1328306-WGS:GSTH-3075-MONOMER; -. DR EvolutionaryTrace; P44681; -. DR Proteomes; UP000000579; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 363 Ribosome-binding ATPase YchF. FT /FTId=PRO_0000201678. FT DOMAIN 3 256 OBG-type G. FT NP_BIND 12 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00944}. FT METAL 16 16 Magnesium. {ECO:0000250}. FT METAL 36 36 Magnesium. {ECO:0000250}. FT STRAND 4 8 {ECO:0000244|PDB:1JAL}. FT HELIX 15 24 {ECO:0000244|PDB:1JAL}. FT STRAND 41 45 {ECO:0000244|PDB:1JAL}. FT HELIX 49 58 {ECO:0000244|PDB:1JAL}. FT STRAND 61 64 {ECO:0000244|PDB:1JAL}. FT STRAND 67 72 {ECO:0000244|PDB:1JAL}. FT HELIX 80 83 {ECO:0000244|PDB:1JAL}. FT HELIX 84 86 {ECO:0000244|PDB:1JAL}. FT HELIX 90 95 {ECO:0000244|PDB:1JAL}. FT STRAND 98 105 {ECO:0000244|PDB:1JAL}. FT HELIX 121 151 {ECO:0000244|PDB:1JAL}. FT TURN 152 154 {ECO:0000244|PDB:1JAL}. FT HELIX 156 173 {ECO:0000244|PDB:1JAL}. FT HELIX 178 180 {ECO:0000244|PDB:1JAL}. FT HELIX 185 191 {ECO:0000244|PDB:1JAL}. FT HELIX 192 194 {ECO:0000244|PDB:1JAL}. FT STRAND 202 207 {ECO:0000244|PDB:1JAL}. FT STRAND 213 215 {ECO:0000244|PDB:1JAL}. FT HELIX 217 228 {ECO:0000244|PDB:1JAL}. FT STRAND 232 236 {ECO:0000244|PDB:1JAL}. FT HELIX 238 243 {ECO:0000244|PDB:1JAL}. FT HELIX 244 246 {ECO:0000244|PDB:1JAL}. FT HELIX 253 256 {ECO:0000244|PDB:1JAL}. FT HELIX 267 276 {ECO:0000244|PDB:1JAL}. FT STRAND 279 285 {ECO:0000244|PDB:1JAL}. FT STRAND 287 296 {ECO:0000244|PDB:1JAL}. FT HELIX 301 306 {ECO:0000244|PDB:1JAL}. FT HELIX 312 315 {ECO:0000244|PDB:1JAL}. FT STRAND 318 322 {ECO:0000244|PDB:1JAL}. FT HELIX 324 329 {ECO:0000244|PDB:1JAL}. FT HELIX 333 338 {ECO:0000244|PDB:1JAL}. FT STRAND 343 345 {ECO:0000244|PDB:1JAL}. FT STRAND 356 361 {ECO:0000244|PDB:1JAL}. SQ SEQUENCE 363 AA; 39751 MW; 08E00CBEF7D0F65E CRC64; MGFKCGIVGL PNVGKSTLFN ALTKAGIEAA NYPFCTIEPN TGVVPMPDPR LDALAEIVKP ERILPTTMEF VDIAGLVAGA SKGEGLGNKF LANIRETDAI GHVVRCFEND DIVHVAGKID PLDDIDTINT ELALADLDSC ERAIQRLQKR AKGGDKEAKF ELSVMEKILP VLENAGMIRS VGLDKEELQA IKSYNFLTLK PTMYIANVNE DGFENNPYLD RVREIAAKEG AVVVPVCAAI ESEIAELDDE EKVEFLQDLG IEEPGLNRVI RAGYALLNLQ TYFTAGVKEV RAWTVSVGAT APKAAAVIHT DFEKGFIRAE VIAYEDFIQF NGENGAKEAG KWRLEGKDYI VQDGDVMHFR FNV // ID ZAPB_HAEIN Reviewed; 72 AA. AC P44812; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=Cell division protein ZapB {ECO:0000255|HAMAP-Rule:MF_01196}; GN Name=zapB {ECO:0000255|HAMAP-Rule:MF_01196}; GN OrderedLocusNames=HI_0668; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 48-52, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=9719565; DOI=10.1002/elps.1150191046; RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., RA Langen H.; RT "Reference map of the low molecular mass proteins of Haemophilus RT influenzae."; RL Electrophoresis 19:1819-1827(1998). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Non-essential, abundant cell division factor that is CC required for proper Z-ring formation. It is recruited early to the CC divisome by direct interaction with FtsZ, stimulating Z-ring CC assembly and thereby promoting cell division earlier in the cell CC cycle. Its recruitment to the Z-ring requires functional FtsA or CC ZipA. {ECO:0000255|HAMAP-Rule:MF_01196}. CC -!- SUBUNIT: Homodimer. The ends of the coiled-coil dimer bind to each CC other, forming polymers. Interacts with FtsZ. {ECO:0000255|HAMAP- CC Rule:MF_01196}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes to the septum at CC mid-cell, in a FtsZ-like pattern. {ECO:0000255|HAMAP- CC Rule:MF_01196}. CC -!- SIMILARITY: Belongs to the ZapB family. {ECO:0000255|HAMAP- CC Rule:MF_01196}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22328.1; -; Genomic_DNA. DR PIR; D64156; D64156. DR RefSeq; NP_438828.1; NC_000907.1. DR RefSeq; WP_005650820.1; NC_000907.1. DR ProteinModelPortal; P44812; -. DR STRING; 71421.HI0668; -. DR EnsemblBacteria; AAC22328; AAC22328; HI_0668. DR GeneID; 949710; -. DR KEGG; hin:HI0668; -. DR PATRIC; 20189953; VBIHaeInf48452_0698. DR eggNOG; ENOG4105N4M; Bacteria. DR eggNOG; COG3074; LUCA. DR KO; K09892; -. DR OMA; GKMEDVQ; -. DR OrthoDB; EOG6P8TT4; -. DR PhylomeDB; P44812; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01196; ZapB; 1. DR InterPro; IPR009252; Cell_div_ZapB. DR Pfam; PF06005; DUF904; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; KW Direct protein sequencing; Reference proteome; Septation. FT CHAIN 1 72 Cell division protein ZapB. FT /FTId=PRO_0000169697. FT COILED 1 71 {ECO:0000255|HAMAP-Rule:MF_01196}. SQ SEQUENCE 72 AA; 8627 MW; C3A9A9FB8CBF8047 CRC64; MSLEILDQLE EKIKQAVETI QLLQLEVEEL KEKNAESQRN IENLQTENEQ LKNEHRNWQE HIRSLLGKFD NV // ID YIDD_HAEIN Reviewed; 86 AA. AC P44972; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Putative membrane protein insertion efficiency factor {ECO:0000255|HAMAP-Rule:MF_00386}; GN OrderedLocusNames=HI_1000; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Could be involved in insertion of integral membrane CC proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00386}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00386}; Cytoplasmic side {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC -!- SIMILARITY: Belongs to the UPF0161 family. {ECO:0000255|HAMAP- CC Rule:MF_00386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22662.1; -; Genomic_DNA. DR PIR; G64163; G64163. DR RefSeq; NP_439162.1; NC_000907.1. DR RefSeq; WP_005647910.1; NC_000907.1. DR STRING; 71421.HI1000; -. DR EnsemblBacteria; AAC22662; AAC22662; HI_1000. DR GeneID; 949902; -. DR KEGG; hin:HI1000; -. DR PATRIC; 20190661; VBIHaeInf48452_1043. DR eggNOG; ENOG4105VAS; Bacteria. DR eggNOG; COG0759; LUCA. DR KO; K08998; -. DR OMA; SEYAVES; -. DR OrthoDB; EOG61ZTN6; -. DR PhylomeDB; P44972; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00386; UPF0161_YidD; 1. DR InterPro; IPR002696; Membr_insert_effic_factor. DR Pfam; PF01809; Haemolytic; 1. DR ProDom; PD004225; DUF37; 1. DR SMART; SM01234; Haemolytic; 1. DR TIGRFAMs; TIGR00278; TIGR00278; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; KW Reference proteome. FT CHAIN 1 86 Putative membrane protein insertion FT efficiency factor. FT /FTId=PRO_0000171828. SQ SEQUENCE 86 AA; 9564 MW; 7AD4F4A5A27C20AB CRC64; MAETHSLGTK ILIKIIRLYQ IMISPFIGAR CRFVPTCSCY GIEALKTHGL LKGGWLTLKR VLKCHPLNAG GFDPVPPKTN NNDEKK // ID YQGF_HAEIN Reviewed; 139 AA. AC P43981; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2016, entry version 99. 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=HI_0305; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=11805338; DOI=10.1073/pnas.012602299; RA Akerley B.J., Rubin E.J., Novick V.L., Amaya K., Judson N., RA Mekalanos J.J.; RT "A genome-scale analysis for identification of genes required for RT growth or survival of Haemophilus influenzae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:966-971(2002). RN [3] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=15044829; DOI=10.1159/000076741; RA Zalacain M., Biswas S., Ingraham K.A., Ambrad J., Bryant A., RA Chalker A.F., Iordanescu S., Fan J., Fan F., Lunsford R.D., RA O'Dwyer K., Palmer L.M., So C., Sylvester D., Volker C., Warren P., RA McDevitt D., Brown J.R., Holmes D.J., Burnham M.K.; RT "A global approach to identify novel broad-spectrum antibacterial RT targets among proteins of unknown function."; RL J. Mol. Microbiol. Biotechnol. 6:109-126(2003). 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 -!- DISRUPTION PHENOTYPE: Controversial; it has been found to be non- CC essential (PubMed:11805338). Has also been found to be essential CC (PubMed:15044829). {ECO:0000269|PubMed:11805338, CC ECO:0000269|PubMed:15044829}. 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; L42023; AAC21970.1; -; Genomic_DNA. DR PIR; H64005; H64005. DR RefSeq; NP_438472.1; NC_000907.1. DR RefSeq; WP_005648994.1; NC_000907.1. DR ProteinModelPortal; P43981; -. DR SMR; P43981; 1-135. DR STRING; 71421.HI0305; -. DR EnsemblBacteria; AAC21970; AAC21970; HI_0305. DR GeneID; 950747; -. DR KEGG; hin:HI0305; -. DR PATRIC; 20189151; VBIHaeInf48452_0322. DR eggNOG; ENOG4107Y66; Bacteria. DR eggNOG; COG0816; LUCA. DR KO; K07447; -. DR OMA; PNWDDIE; -. DR OrthoDB; EOG6N94FV; -. DR PhylomeDB; P43981; -. DR Proteomes; UP000000579; 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 1 139 Putative pre-16S rRNA nuclease. FT /FTId=PRO_0000172071. SQ SEQUENCE 139 AA; 15340 MW; A875112A732AC6B4 CRC64; MGITALAFDF GTKSIGCAIG QSITGTAQAL PAFKAQDGIP NWEAIEKCLK EWKPDVVIVG LPLNMDGTEQ DLTLRARKFA NRLQGRFGVN VHLQDERLTT TQARSEIFER GGFKALKKGK IDGVSACLIL ESWFEYAEY // ID ZNTR_HAEIN Reviewed; 135 AA. AC P45277; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=HTH-type transcriptional regulator ZntR homolog; GN Name=zntR; OrderedLocusNames=HI_1623; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Transcriptional regulator. {ECO:0000250}. CC -!- SIMILARITY: Contains 1 HTH merR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00254}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC23268.1; -; Genomic_DNA. DR RefSeq; NP_439766.1; NC_000907.1. DR RefSeq; WP_005633867.1; NC_000907.1. DR ProteinModelPortal; P45277; -. DR STRING; 71421.HI1623; -. DR EnsemblBacteria; AAC23268; AAC23268; HI_1623. DR GeneID; 950843; -. DR KEGG; hin:HI1623; -. DR PATRIC; 20191983; VBIHaeInf48452_1699. DR eggNOG; ENOG4105W1Y; Bacteria. DR eggNOG; COG0789; LUCA. DR OMA; CAVETIR; -. DR OrthoDB; EOG6NKQXH; -. DR PhylomeDB; P45277; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR000551; MerR-type_HTH_dom. DR Pfam; PF13411; MerR_1; 1. DR PRINTS; PR00040; HTHMERR. DR SMART; SM00422; HTH_MERR; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR PROSITE; PS00552; HTH_MERR_1; 1. DR PROSITE; PS50937; HTH_MERR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 135 HTH-type transcriptional regulator ZntR FT homolog. FT /FTId=PRO_0000098162. FT DOMAIN 1 69 HTH merR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. FT DNA_BIND 4 23 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00254}. SQ SEQUENCE 135 AA; 15636 MW; CE07D848D0BCF19C CRC64; MKIGALAKAL GCTVETIRYY EQQGLIPPPK RTSGNFRQYN EEHLQRLSFI CNCRNLDISL SEIKSLLNLE NASKQQAEEI NRVLDKHIKE VATRIHELAH LRMKLIELRE KTVSNDEDPM KLLLQHSGVK FVRLK // ID ZNUA_HAEIN Reviewed; 337 AA. AC P44526; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=High-affinity zinc uptake system protein ZnuA; DE Flags: Precursor; GN Name=znuA; OrderedLocusNames=HI_0119; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). RN [2] RP PROTEIN SEQUENCE OF 24-32. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=10675023; RX DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4; RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., RA Gray C., Fountoulakis M.; RT "Two-dimensional map of the proteome of Haemophilus influenzae."; RL Electrophoresis 21:411-429(2000). CC -!- FUNCTION: Involved in the high-affinity zinc uptake transport CC system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21794.1; -; Genomic_DNA. DR PIR; D64049; D64049. DR RefSeq; NP_438291.1; NC_000907.1. DR RefSeq; WP_005694411.1; NC_000907.1. DR ProteinModelPortal; P44526; -. DR STRING; 71421.HI0119; -. DR EnsemblBacteria; AAC21794; AAC21794; HI_0119. DR GeneID; 951027; -. DR KEGG; hin:HI0119; -. DR PATRIC; 20188723; VBIHaeInf48452_0123. DR eggNOG; ENOG4105NXV; Bacteria. DR eggNOG; COG4531; LUCA. DR KO; K09815; -. DR OMA; LPGMHLR; -. DR OrthoDB; EOG6PGK2R; -. DR PhylomeDB; P44526; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR GO; GO:0006829; P:zinc II ion transport; IEA:UniProtKB-KW. DR InterPro; IPR006127; ZnuA-like. DR Pfam; PF01297; ZnuA; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Ion transport; KW Metal-binding; Periplasm; Reference proteome; Signal; Transport; Zinc; KW Zinc transport. FT SIGNAL 1 23 {ECO:0000269|PubMed:10675023}. FT CHAIN 24 337 High-affinity zinc uptake system protein FT ZnuA. FT /FTId=PRO_0000031877. FT COMPBIAS 115 163 His-rich. FT METAL 57 57 Zinc. {ECO:0000250}. FT METAL 171 171 Zinc. {ECO:0000250}. FT METAL 235 235 Zinc. {ECO:0000250}. SQ SEQUENCE 337 AA; 37659 MW; 3DBB45AB8F06FFCB CRC64; MKKLLKISAI SAALLSAPMM ANADVLASVK PLGFIVSSIA DGVTGTQVLV PAGASPHDYN LKLSDIQKVK SADLVVWIGE DIDSFLDKPI SQIERKKVIT IADLADVKPL LSKAHHEHFH EDGDHDHDHK HEHKHDHKHD HDHDHDHKHE HKHDHEHHDH DHHEGLTTNW HVWYSPAISK IVAQKVADKL TAQFPDKKAL IAQNLSDFNR TLAEQSEKIT AQLANVKDKG FYVFHDAYGY FNDAYGLKQT GYFTINPLVA PGAKTLAHIK EEIDEHKVNC LFAEPQFTPK VIESLAKNTK VNVGQLDPIG DKVTLGKNSY ATFLQSTADS YMECLAK // ID ZIPA_HAEIN Reviewed; 328 AA. AC P44113; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Cell division protein ZipA {ECO:0000255|HAMAP-Rule:MF_00509}; GN Name=zipA {ECO:0000255|HAMAP-Rule:MF_00509}; GN OrderedLocusNames=HI_1101; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Essential cell division protein that stabilizes the FtsZ CC protofilaments by cross-linking them and that serves as a CC cytoplasmic membrane anchor for the Z ring. Also required for the CC recruitment to the septal ring of downstream cell division CC proteins. {ECO:0000255|HAMAP-Rule:MF_00509}. CC -!- SUBUNIT: Interacts with FtsZ via their C-terminal domains. CC {ECO:0000255|HAMAP-Rule:MF_00509}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00509}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_00509}. Note=Localizes to the Z ring in CC an FtsZ-dependent manner. {ECO:0000255|HAMAP-Rule:MF_00509}. CC -!- SIMILARITY: Belongs to the ZipA family. {ECO:0000255|HAMAP- CC Rule:MF_00509}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22756.1; -; Genomic_DNA. DR PIR; E64020; E64020. DR RefSeq; NP_439258.1; NC_000907.1. DR RefSeq; WP_005693425.1; NC_000907.1. DR ProteinModelPortal; P44113; -. DR STRING; 71421.HI1101; -. DR EnsemblBacteria; AAC22756; AAC22756; HI_1101. DR GeneID; 950071; -. DR KEGG; hin:HI1101; -. DR PATRIC; 20190869; VBIHaeInf48452_1147. DR eggNOG; ENOG4107NPY; Bacteria. DR eggNOG; COG3115; LUCA. DR KO; K03528; -. DR OMA; LPCYGEA; -. DR OrthoDB; EOG6X10VC; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1400.10; -; 1. DR HAMAP; MF_00509; ZipA; 1. DR InterPro; IPR011919; Cell_div_ZipA. DR InterPro; IPR007449; ZipA_FtsZ-bd_C. DR Pfam; PF04354; ZipA_C; 1. DR ProDom; PD035754; ZipA_Fts_Z_bd_C; 1. DR SMART; SM00771; ZipA_C; 1. DR SUPFAM; SSF64383; SSF64383; 1. DR TIGRFAMs; TIGR02205; septum_zipA; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; KW Complete proteome; Membrane; Reference proteome; Septation; KW Transmembrane; Transmembrane helix. FT CHAIN 1 328 Cell division protein ZipA. FT /FTId=PRO_0000214526. FT TOPO_DOM 1 4 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00509}. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00509}. FT TOPO_DOM 26 328 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00509}. SQ SEQUENCE 328 AA; 36766 MW; 73F87008C6FD6A60 CRC64; MDLNTILIIV GIVALVALIV HGLWSNRREK SKYFDKANKF DRTSLTSRSH TQEEMVQPNN ISPNTYVENG HTPIPQPTTE KLPSEAELID YRQSDKSVDD IKISIPNTQP IYDMGNHRSE PIQPTQPQYD MPTANNVASM TLEQLEAQSQ NVGFNGINSS SPELRVQLAE LSHEEHQVDY NLSFNEPKAE TTAHPKQTTG YIQLYLIPKS SEEFNGAKLV QALENLGFIL GKDEMYHRHL DLSVASPVLF SVANLEQPGT FNAYNLAEFN TIGIVLFMQL PSPGNNLANL RMMMRAAHTL AEDLQGVILT EEQEIFDANA EQAYLARV // ID ZNUB_HAEIN Reviewed; 261 AA. AC P44691; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=High-affinity zinc uptake system membrane protein ZnuB; GN Name=znuB; OrderedLocusNames=HI_0407; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Involved in the high-affinity zinc uptake transport CC system. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi- CC pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-3 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22066.1; -; Genomic_DNA. DR PIR; A64066; A64066. DR RefSeq; NP_438569.1; NC_000907.1. DR RefSeq; WP_005693761.1; NC_000907.1. DR ProteinModelPortal; P44691; -. DR STRING; 71421.HI0407; -. DR EnsemblBacteria; AAC22066; AAC22066; HI_0407. DR GeneID; 949507; -. DR KEGG; hin:HI0407; -. DR PATRIC; 20189365; VBIHaeInf48452_0426. DR eggNOG; ENOG4105FAV; Bacteria. DR eggNOG; COG1108; LUCA. DR KO; K09816; -. DR OMA; GVFVVWR; -. DR OrthoDB; EOG6K13RC; -. DR PhylomeDB; P44691; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR GO; GO:0006829; P:zinc II ion transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR001626; ABC_3. DR InterPro; IPR029022; ABC_BtuC-like. DR Pfam; PF00950; ABC-3; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Ion transport; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport; Zinc; Zinc transport. FT CHAIN 1 261 High-affinity zinc uptake system membrane FT protein ZnuB. FT /FTId=PRO_0000171162. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 214 234 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. SQ SEQUENCE 261 AA; 28466 MW; DD2AC8F0DF6CBE96 CRC64; MFEILFPALL TGIVLSLITA PLGVFVVWRK MAYFGDTLSH SALLGVALGI FLQVNPYIAI VVLTLILAIA MVWLESNTQF SIDTLLGIIA HSCLSLGVVT VGLLRNVRVD LMNYLFGDLL AINYTDLIYI GIGVIIVLST LIYFWQSLLS TTVSPELAQV EGINIKKMRF ILMILTALTI ALSMKFVGAL IITSLLIIPA ATARRFARTP ESMVGWAIIM SMLSIIGGLI LSAFYDTAAG PSVVICSAFL FVLSLFKRER L // ID ZAPA_HAEIN Reviewed; 100 AA. AC P44062; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Cell division protein ZapA; DE AltName: Full=Z ring-associated protein ZapA; GN Name=zapA; OrderedLocusNames=HI_0857; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Activator of cell division through the inhibition of CC FtsZ GTPase activity, therefore promoting FtsZ assembly into CC bundles of protofilaments necessary for the formation of the CC division Z ring. It is recruited early at mid-cell but it is not CC essential for cell division (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with FtsZ (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes at CC mid-cell. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ZapA family. 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; L42023; AAC22516.1; -; Genomic_DNA. DR PIR; H64014; H64014. DR RefSeq; NP_439017.1; NC_000907.1. DR RefSeq; WP_005651366.1; NC_000907.1. DR ProteinModelPortal; P44062; -. DR STRING; 71421.HI0857; -. DR EnsemblBacteria; AAC22516; AAC22516; HI_0857. DR GeneID; 950666; -. DR KEGG; hin:HI0857; -. DR PATRIC; 20190369; VBIHaeInf48452_0898. DR eggNOG; COG3027; LUCA. DR KO; K09888; -. DR OMA; LESCIHQ; -. DR OrthoDB; EOG69SKDP; -. DR PhylomeDB; P44062; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR InterPro; IPR007838; Cell_div_ZapA-like. DR Pfam; PF05164; ZapA; 1. DR SUPFAM; SSF102829; SSF102829; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; KW Reference proteome; Septation. FT CHAIN 1 100 Cell division protein ZapA. FT /FTId=PRO_0000169354. FT COILED 21 45 {ECO:0000255}. SQ SEQUENCE 100 AA; 11422 MW; 756D6F5E108C7DAD CRC64; MSLKLVEILV LGQVLRLNVP IEQEELLRQA ARNLDILVSE MKEKTGLIQL DRVLSIVALN LSFELSQEKN KTAKIEEVLR TGIQQLDHSL ENIRVTKEPH // ID ZNUC_HAEIN Reviewed; 268 AA. AC P44692; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Zinc import ATP-binding protein ZnuC {ECO:0000255|HAMAP-Rule:MF_01725}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01725}; GN Name=znuC {ECO:0000255|HAMAP-Rule:MF_01725}; GN OrderedLocusNames=HI_0408; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Part of the ABC transporter complex ZnuABC involved in CC zinc import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01725}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding CC protein (ZnuA). {ECO:0000255|HAMAP-Rule:MF_01725}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01725}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Zinc CC importer (TC 3.A.1.15.5) family. {ECO:0000255|HAMAP- CC Rule:MF_01725}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01725}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC22067.1; -; Genomic_DNA. DR PIR; B64066; B64066. DR RefSeq; NP_438570.1; NC_000907.1. DR RefSeq; WP_005666536.1; NC_000907.1. DR ProteinModelPortal; P44692; -. DR STRING; 71421.HI0408; -. DR PRIDE; P44692; -. DR EnsemblBacteria; AAC22067; AAC22067; HI_0408. DR GeneID; 949513; -. DR KEGG; hin:HI0408; -. DR PATRIC; 20189367; VBIHaeInf48452_0427. DR eggNOG; ENOG4105FDK; Bacteria. DR eggNOG; COG1121; LUCA. DR KO; K09817; -. DR OMA; HVVMAET; -. DR OrthoDB; EOG6VXF80; -. DR PhylomeDB; P44692; -. DR Proteomes; UP000000579; 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:0015633; F:zinc 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; IPR027417; P-loop_NTPase. DR InterPro; IPR017882; ZnuC. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51298; ZNUC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Ion transport; Membrane; Nucleotide-binding; KW Reference proteome; Transport; Zinc; Zinc transport. FT CHAIN 1 268 Zinc import ATP-binding protein ZnuC. FT /FTId=PRO_0000093133. FT DOMAIN 16 231 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01725}. FT NP_BIND 48 55 ATP. {ECO:0000255|HAMAP-Rule:MF_01725}. SQ SEQUENCE 268 AA; 29859 MW; E14DD779752E2709 CRC64; MNITAIRNEQ NQQPLIQLKN INVVFAQKTA LQDINLNIYP NSIITIVGPN GGGKSTLLKT LLKLQTPTSG EVIYSKNVRI GYVPQKIHLD HSLPITVERF LSLKKGIKTQ EISTALEQLS ISHLRKNNMQ KLSGGEMQRV LLARAILNKP NLLVLDEPTQ GVDITGQAEL YQLIHQTQQK LNCAVLMVSH DLHIVMADSK EVLCINQHIC CAGTPDVLSN DPTFMRLWGN QIAQNVGFYT HHHNHHHTLH GDVCGCNSSA VHCQNKDK //